|
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 ... |
83-187 |
3.86e-76 |
|
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: 248.47 E-value: 3.86e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 83 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 162
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 2124423184 163 RNDDIADGNPKLTLGLIWTIILHFQ 187
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
80-198 |
1.63e-73 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 241.47 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 80 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 159
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2124423184 160 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 198
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
79-196 |
4.11e-72 |
|
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: 237.96 E-value: 4.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 79 KDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 158
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 2124423184 159 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 196
Cdd:cd21236 91 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
200-305 |
5.00e-72 |
|
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: 236.46 E-value: 5.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 200 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 279
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 2124423184 280 PEDVDVPQPDEKSIITYVSSLYDAMP 305
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
201-305 |
5.90e-66 |
|
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: 219.19 E-value: 5.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 280
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 2124423184 281 EDVDVPQPDEKSIITYVSSLYDAMP 305
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
80-197 |
3.52e-63 |
|
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: 211.81 E-value: 3.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 80 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 159
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2124423184 160 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 197
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
201-305 |
2.50e-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: 194.43 E-value: 2.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 280
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 2124423184 281 EDVDVPQPDEKSIITYVSSLYDAMP 305
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
199-305 |
1.50e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 178.31 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 199 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 278
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 2124423184 279 DPEDVDVPQPDEKSIITYVSSLYDAMP 305
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
85-188 |
1.21e-50 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 175.65 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 85 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 163
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 2124423184 164 NDDIADGNPKLTLGLIWTIILHFQI 188
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 ... |
75-184 |
1.00e-48 |
|
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: 170.24 E-value: 1.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 75 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 153
Cdd:cd21246 6 IKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLK 85
|
90 100 110
....*....|....*....|....*....|.
gi 2124423184 154 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 184
Cdd:cd21246 86 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
201-301 |
7.38e-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: 161.81 E-value: 7.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 280
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 2124423184 281 EDVDVPQPDEKSIITYVSSLY 301
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
84-412 |
1.24e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 177.44 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 84 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 160
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLFNAII 239
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 240 HRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD----AMPR 306
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidiALHR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 307 VPDVQDGVKANElQLRwQEYRELVLLLLQWIRHHTAAFEERKFPSSFEEIEILWCQFLKFKETE--LPAKEAD-KNRSKG 383
Cdd:COG5069 245 VYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHSLAGQ 322
|
330 340
....*....|....*....|....*....
gi 2124423184 384 IYQSLEgAVQAGQLKVPPGYHPLDVEKEW 412
Cdd:COG5069 323 ILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
75-184 |
2.16e-45 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 160.92 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 75 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLr 153
Cdd:cd21193 6 IRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL- 84
|
90 100 110
....*....|....*....|....*....|.
gi 2124423184 154 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 184
Cdd:cd21193 85 KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
81-188 |
4.18e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.15 E-value: 4.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 81 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 156
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 2124423184 157 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 188
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
201-301 |
5.08e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 5.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 280
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2124423184 281 EDVDVPQPDEKSIITYVSSLY 301
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
81-188 |
1.67e-43 |
|
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: 155.42 E-value: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 81 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 153
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 2124423184 154 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 188
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
75-184 |
3.18e-41 |
|
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: 149.79 E-value: 3.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 75 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 153
Cdd:cd21318 28 IKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 2124423184 154 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 184
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
200-305 |
3.71e-41 |
|
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: 148.62 E-value: 3.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 200 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 279
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 2124423184 280 PEDVDVPQPDEKSIITYVSSLYDAMP 305
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
188-303 |
5.78e-41 |
|
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: 148.28 E-value: 5.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 188 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 267
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423184 268 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 303
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
64-184 |
3.94e-40 |
|
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: 146.35 E-value: 3.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 64 DMDPSRA---IQHEISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRF 139
Cdd:cd21317 7 DNDNSSArlfERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRI 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2124423184 140 HKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 184
Cdd:cd21317 87 HCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
197-301 |
1.49e-38 |
|
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: 141.30 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 197 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 276
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 2124423184 277 LLDPEDVDVPQPDEKSIITYVSSLY 301
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
83-184 |
1.49e-38 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 140.99 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 83 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 161
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 2124423184 162 IRNDDIADGNPKLTLGLIWTIIL 184
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
85-186 |
1.91e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.61 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 85 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 162
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 2124423184 163 RNDDIADGNPKLTLGLIWTIILHF 186
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
81-188 |
2.09e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 140.74 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 81 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 158
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 2124423184 159 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 188
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
197-301 |
5.58e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.81 E-value: 5.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 197 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 276
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 2124423184 277 LLDPEDVDVPQPDEKSIITYVSSLY 301
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
200-301 |
2.97e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 137.30 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 200 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 279
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 2124423184 280 PEDVDVPQPDEKSIITYVSSLY 301
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1381-2012 |
5.55e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 154.32 E-value: 5.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLRRMEE-EERLaeqqraeerERLAAVEAalEKQRQLAEAHAQAKaQAEQeAQELQRRMQEevarreeaavdaqqqkRS 1459
Cdd:COG1196 176 EAERKLEAtEENL---------ERLEDILG--ELERQLEPLERQAE-KAER-YRELKEELKE----------------LE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1460 IQEELQHLRQSsEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1539
Cdd:COG1196 227 AELLLLKLREL-EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1540 RLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEVE 1619
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1620 LQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1699
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1700 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEE 1776
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAA 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1777 ELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAk 1856
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL- 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1857 RQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1936
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1937 LAQLRKASESELE--RQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQaELEAM 2012
Cdd:COG1196 703 EEEERELAEAEEErlEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER-EIEAL 779
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
80-188 |
1.13e-36 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 135.82 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 80 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 158
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 2124423184 159 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 188
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
204-305 |
8.92e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 132.94 E-value: 8.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 204 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 282
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2124423184 283 VDVPQPDEKSIITYVSSLYDAMP 305
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
185-301 |
4.46e-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: 132.10 E-value: 4.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 185 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 264
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423184 265 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 301
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1483-2091 |
4.89e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.78 E-value: 4.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1483 EAAERSRLRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVR 1562
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1563 VKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1642
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1643 VAVAQLreeaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE 1722
Cdd:COG1196 341 ELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1802
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1803 RAEMEVLLASKARAEEESRSTSEKSK----QRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAervlA 1878
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLlaglRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE----Y 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1879 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDT 1958
Cdd:COG1196 566 LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1959 LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 2038
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 2039 EEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQA 2091
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1723-2291 |
5.56e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.78 E-value: 5.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1802
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1803 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERVLAEKLA 1882
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1883 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKgLVEDTLRQR 1962
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1963 RQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 2042
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2043 ARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQEQSM 2117
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2118 LERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQA 2197
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2198 ALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2277
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
570
....*....|....
gi 2124423184 2278 QMEELGKLKARIEA 2291
Cdd:COG1196 765 LERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1356-1943 |
3.00e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 145.46 E-value: 3.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1356 QEYVDLRTRYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQ-------LAEAHAQAKAQ 1427
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1428 AEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTE 1507
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1508 RQRGGAEGELQALRARAE------------------EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEA 1569
Cdd:COG1196 373 ELAEAEEELEELAEELLEalraaaelaaqleeleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1570 AREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLR 1649
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1650 EEAERRAQQQAEAERAREEAERELERWQ-----LKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQ 1724
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1725 AVRQRELAEQELEKQRQLAEGTAQQRLAAEQEliRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRA 1804
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAG--RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1805 EMEVLLASKARAEEESRSTSEKSKQRleaeasrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAI 1884
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1885 GEATRLKTEAEIALKEKEAENERlrrlAEDE-AFQRRRLEEQAAQHkADIEERLAQLRKA 1943
Cdd:COG1196 763 EELERELERLEREIEALGPVNLL----AIEEyEELEERYDFLSEQR-EDLEEARETLEEA 817
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1520-2094 |
6.14e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 144.31 E-value: 6.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1520 LRARAEEAEAQKRQAQEEAERL---RRQVqdETQRKRqaeaelavrVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQ 1596
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1597 AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERW 1676
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1677 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1756
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1757 LIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAS 1836
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1837 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA----AIGEATRLKTEAEIALKEKEAENERLRRLA 1912
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1913 EDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGK----AELEL 1988
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlvaARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1989 ELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2068
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580
....*....|....*....|....*.
gi 2124423184 2069 RAEQESARQLQLAQDAAQKRLQAEEK 2094
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEE 740
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
84-189 |
1.13e-33 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 127.57 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 84 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 160
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHFQIS 189
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
75-184 |
4.59e-33 |
|
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: 127.08 E-value: 4.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 75 ISSLKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 153
Cdd:cd21316 43 IKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 122
|
90 100 110
....*....|....*....|....*....|.
gi 2124423184 154 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 184
Cdd:cd21316 123 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1387-2093 |
6.00e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 142.20 E-value: 6.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1387 EEEERLAEQQRAEERERlaaVEAALEKQRQLAEAHAQAKAQAEQEAQELqRRMQEevARREEAAVDAQQQKRSiqEELQH 1466
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGK---AEEARKAEEAKKKAEDARKAEEARKAEDA-RKAEE--ARKAEDAKRVEIARKA--EDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1467 LRQSSEAEiqaKARQVEAAERSrlrieEEIRVVRlQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1546
Cdd:PTZ00121 1166 AEEARKAE---DAKKAEAARKA-----EEVRKAE-ELRKAEDAR-----KAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1547 DETQRKRQAEAELAVRVKaEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVA--LETAQRSAEVELQSKR 1624
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1625 ASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1704
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1705 EKQKEEAEREARRRGKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1784
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1785 AAAATQKRQELE----AELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEASRFRELAEEAARLRAlAEEAKRQRQ 1860
Cdd:PTZ00121 1469 AKKADEAKKKAEeakkADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAKKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1861 LAEEDAARQRAEAERvlAEKLAAIGEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 1940
Cdd:PTZ00121 1539 AKKAEEKKKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1941 RKASESELERQKGLVEDTLRQRrqveEEILALKVSFEKAAAGKAELELELGRIRS-----NAEDTLRSKEQA--ELEAMR 2013
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAaeeakKAEEDKKKAEEAkkAEEDEK 1688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2014 QRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRL 2089
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
....
gi 2124423184 2090 QAEE 2093
Cdd:PTZ00121 1769 KAEE 1772
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
85-188 |
9.61e-33 |
|
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: 124.32 E-value: 9.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 85 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 162
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 2124423184 163 RNDDIADGNPKLTLGLIWTIILHFQI 188
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
200-298 |
1.54e-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: 123.69 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 200 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 279
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 2124423184 280 PEDVDVPQPDEKSIITYVS 298
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
201-301 |
1.57e-32 |
|
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: 123.67 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 280
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2124423184 281 EDVDVPQPDEKSIITYVSSLY 301
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
85-188 |
1.74e-32 |
|
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: 123.58 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 85 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 163
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 2124423184 164 NDDIADGNPKLTLGLIWTIILHFQI 188
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
188-303 |
2.76e-31 |
|
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: 120.71 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 188 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 267
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423184 268 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 303
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
936-1013 |
3.65e-31 |
|
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: 118.86 E-value: 3.65e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 936 LAWQSLSRDVQLIRSWSLVTFRTMKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSHHYQQLLQS 1013
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
204-305 |
4.04e-31 |
|
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: 119.68 E-value: 4.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 204 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 282
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2124423184 283 VDVPQPDEKSIITYVSSLYDAMP 305
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
204-306 |
1.23e-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: 118.49 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 204 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 281
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 2124423184 282 DVDVPQPDEKSIITYVSSLYDAMPR 306
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
200-298 |
1.42e-30 |
|
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: 118.40 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 200 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 279
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 2124423184 280 PEDVDVPQPDEKSIITYVS 298
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
81-190 |
2.48e-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: 117.68 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 81 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 156
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 2124423184 157 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 190
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
206-301 |
3.42e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 117.06 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 206 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 284
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 2124423184 285 VPQPDEKSIITYVSSLY 301
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
84-186 |
6.60e-30 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 116.43 E-value: 6.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 84 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 160
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHF 186
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1266-1985 |
7.51e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 131.80 E-value: 7.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1266 QDAKRRQEQIQAmvlADSRAVREQLRQEKALLEEIERHGEKVEECQRfAKQYINAIKDYELQlvtyKAQLEPVASPAKKP 1345
Cdd:PTZ00121 1137 EDARKAEEARKA---EDAKRVEIARKAEDARKAEEARKAEDAKKAEA-ARKAEEVRKAEELR----KAEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1346 KVQSGSESViQEYVDLRTryselttltsqyikfiSETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAK 1425
Cdd:PTZ00121 1209 EEERKAEEA-RKAEDAKK----------------AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1426 AQAEQ--EAQELQR----------RMQEEVARREEAAVDAQQQKRSIQ-----EELQHLRQSSEAEIQAKARQVEAAERS 1488
Cdd:PTZ00121 1272 IKAEEarKADELKKaeekkkadeaKKAEEKKKADEAKKKAEEAKKADEakkkaEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1489 RLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE----------AEAQKRQAQEEAERLRRQVQDETQRKRQAEAE 1558
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadeakkkAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1559 LAVRVKAEAEAAREKQRALQALEEFRlQAEEAERRlrqaeAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTL 1638
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKK-----AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1639 QEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlQAEEVAQQKSLAQAEAEKqkeeaerearrr 1718
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK---KAEELKKAEEKKKAEEAK------------ 1570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1719 gKAEEqavrQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1798
Cdd:PTZ00121 1571 -KAEE----DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1799 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRAlAEEAKRQRQLaeedaaRQRAEAERVLA 1878
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-AEEAKKAEEL------KKKEAEEKKKA 1718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1879 EKLAAIGEATRLKteAEIALKEKEAENERLRRLAEDEAFQRRrleeqAAQHKADIEERLAQLRKASESELErqKGLVEDT 1958
Cdd:PTZ00121 1719 EELKKAEEENKIK--AEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVIE--EELDEED 1789
|
730 740
....*....|....*....|....*..
gi 2124423184 1959 LRQRRQVEEEILALKVSFEKAAAGKAE 1985
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1825-2508 |
1.20e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.44 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1825 EKSKQRLEAEAsrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLaaigEATRLKTEAEIALKEKEAE 1904
Cdd:COG1196 199 ERQLEPLERQA----EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1905 NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKglvEDTLRQRRQVEEEILALKVSFEKAAAGKA 1984
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1985 ELELELgrirSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2064
Cdd:COG1196 348 EAEEEL----EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2065 RLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLqqeqsmlERLRGEAEAARRAAEEAEEARERAER 2144
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE-------EAALLEAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2145 EAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAemekhkkfAEQTLRQKA 2224
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA--------AAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2225 QVEQELTTLRLqleETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNT 2304
Cdd:COG1196 569 AKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2305 QRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2384
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2385 ARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQL----EMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIgeklh 2460
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL----- 800
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2124423184 2461 rtelaTQEKVTLVQTLeiqrqqsdhdaERLRQAIAELEREKEKLKQEA 2508
Cdd:COG1196 801 -----SEQREDLEEAR-----------ETLEEAIEEIDRETRERFLET 832
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
186-303 |
4.51e-29 |
|
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: 114.80 E-value: 4.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 186 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 265
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 2124423184 266 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 303
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
204-303 |
2.32e-28 |
|
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: 111.61 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 204 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 282
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 2124423184 283 VDVPQPDEKSIITYVSSLYDA 303
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1527-2515 |
1.34e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 124.17 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1527 AEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAE--AEAAREKQRALQALEEFRLQAE-EAERRLRQAEAERAR 1603
Cdd:NF041483 81 AQIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1604 QVQVA---LETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvavaqlreeaerraqqqaeAERAREEAERELERWQLKA 1680
Cdd:NF041483 161 TESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE--------------------AESARAEAEAILRRARKDA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1681 NEALR-LRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrlAAEQELIR 1759
Cdd:NF041483 221 ERLLNaASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQE---AEEALREARAEAEKVVAE--AKEAAAKQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1760 LRAETEQGEQQRQLLEEELARLQHEAAA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSKQRLEAEA 1835
Cdd:NF041483 296 LASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAKAARTAEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1836 SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVlAEKLAAIG----------------EATRLKTEAEIALK 1899
Cdd:NF041483 376 VLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ-AEQLKGAAkddtkeyraktvelqeEARRLRGEAEQLRA 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1900 EKEAENERLRRLAEDEAFQR-----RRLEEQAAQHKADIE------------------ERLAQLRKASESELERQKGLVE 1956
Cdd:NF041483 455 EAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADelrstataeservrteaiERATTLRRQAEETLERTRAEAE 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1957 dtlRQRRQVEEEILALKVSFEKAA------------AGKAELELELGRIRSNAEDTLRSKEQAELEamrqrqlaaeeeqr 2024
Cdd:NF041483 535 ---RLRAEAEEQAEEVRAAAERAArelreeteraiaARQAEAAEELTRLHTEAEERLTAAEEALAD-------------- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2025 rreaeervqkslaAEEEAARQRKAALEEVERLKAKV-EEARRLRERAEQESAR-QLQLAQDAAQKRLQAEEKAhafavqq 2102
Cdd:NF041483 598 -------------ARAEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAERlRTEAAADASAARAEGENVA------- 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2103 keqelqqtlqqeqsmlERLRGEAEaarraaeeaeeareraereaaqsrrqvEEAERLKQSAEEQAQAQAQAQAAAEKlrK 2182
Cdd:NF041483 658 ----------------VRLRSEAA---------------------------AEAERLKSEAQESADRVRAEAAAAAE--R 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2183 EAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTL-RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEA 2261
Cdd:NF041483 693 VGTEAAEALAAAQEEAARRRREAEETLGSARAEADQEReRAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSA 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2262 ARQRS------------QVEEELFSLRVQMEELGKlKARIEAENRALILR------------DKDNTQRVLQEEAEKMKH 2317
Cdd:NF041483 773 AEQTAqqvrdsvaglqeQAEEEIAGLRSAAEHAAE-RTRTEAQEEADRVRsdayaereraseDANRLRREAQEETEAAKA 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2318 VAEEAarLSVAAQEAARLRELAEEDLAQQRALAEKMLKekmQAVQEATRLKAEA---------ELLQQQKEL---AQEQA 2385
Cdd:NF041483 852 LAERT--VSEAIAEAERLRSDASEYAQRVRTEASDTLA---SAEQDAARTRADAredanrirsDAAAQADRLigeATSEA 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2386 RRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLE-----MSAEAERLKLRVAE-MSRAQARAE---EDAQRFRKQAEEIG 2456
Cdd:NF041483 927 ERLTAEARAEAERLRDEARAEAERVRADAAAQAEqliaeATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEA 1006
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 2457 EKLhRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKS 2515
Cdd:NF041483 1007 ERL-RTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRT 1064
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
188-303 |
2.08e-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: 109.79 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 188 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 267
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423184 268 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 303
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
84-186 |
3.07e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 108.73 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 84 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 160
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHF 186
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1720-2507 |
4.22e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 122.94 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaETEQGEQQRQllEEELARLQHEAAAATQKRQELEAEL 1799
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARK--AEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1800 AKVRAEMEVLLASKARAEEESRSTSEKSKqrleaeASRFRElAEEAARlralAEEAKRQRQLAEEDAARQRAEAERvlAE 1879
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRK------AEELRK-AEDARK----AEAARKAEEERKAEEARKAEDAKK--AE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1880 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ-HKADIEERLAQLRKASESELERQKglvedt 1958
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEK------ 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1959 lrqrRQVEEeilalkvsfekaAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 2038
Cdd:PTZ00121 1302 ----KKADE------------AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2039 EEEAARQRKAALEEVERLKAKVEEARR---LRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQ 2115
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2116 SmlerlrgeaeaARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaQAQAQAAAEKLRKEAEQEAARRAQAE 2195
Cdd:PTZ00121 1446 A-----------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKK-----------KAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2196 QAALRQKQAADAEMEKHKKFAEQTlrQKAQVEQELTTLRLQLEETDHQKSILDEELQrlKAEVTEAARQRSQVEEELFSL 2275
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2276 RVQMEELGKL-KARIEAENRALILRDKDNTQRVLQEEAEKMKhvAEEAARlsvaAQEAARLRELAEEDLAQQRALAEKML 2354
Cdd:PTZ00121 1580 LRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKK----AEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2355 KEKMQAVQEATRLKAEAEllqQQKELAQEqARRLQEDKEQMAQQLEQETQgfqrtlEAERQRQLEMSAEAERLKlrVAEM 2434
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAE---EDKKKAEE-AKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKK--AEEL 1721
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 2435 SRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAE-LEREKEKLKQE 2507
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRME 1795
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
75-188 |
1.08e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 107.92 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 75 ISSLKDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDY 151
Cdd:cd21247 10 IRKLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITF 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 2124423184 152 LRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 188
Cdd:cd21247 90 LKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
188-303 |
1.24e-26 |
|
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: 107.50 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 188 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 267
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423184 268 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 303
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1284-2073 |
1.46e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 120.55 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1284 RAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDY-ELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLR 1362
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELrELELALLVLRLE--ELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1363 TRYSELTTLTSQYIKFISETlrrmeeEERLAEQQraEERERLAAVEAALEKQRQLaeaHAQAKAQAEQEAQELQRRMQEE 1442
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSEL------EEEIEELQ--KELYALANEISRLEQQKQI---LRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1443 VARREEAAVDAQQQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRA 1522
Cdd:TIGR02168 329 ESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1523 RAEEAEAQKRQAQEEAERLRRQVQDetQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAE-- 1600
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREla 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1601 RARQVQVALETAQRSAEVELQSKRASFAEKtaqleRTLQEEHVAVAQLREEAerraqqqaeaerareeaerelERWQLKA 1680
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQ-----SGLSGILGVLSELISVD---------------------EGYEAAI 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1681 NEALRLRLQA----------EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELA------------------ 1732
Cdd:TIGR02168 540 EAALGGRLQAvvvenlnaakKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLgvakdlvkfdpklrkals 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1733 ------------EQELEKQRQL-----------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1777
Cdd:TIGR02168 620 yllggvlvvddlDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1778 LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEASRfRELAEEAARLRALAE 1853
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELTELEAEI-EELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1854 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAeialKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 1933
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1934 EERLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDtLRSK------EQA 2007
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE-LREKlaqlelRLE 932
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 2008 ELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRkaalEEVERLKAKVEEARRLRERAEQE 2073
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR----RRLKRLENKIKELGPVNLAAIEE 994
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
84-189 |
1.64e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.42 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 84 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 160
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHFQIS 189
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1390-2509 |
4.30e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.16 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1390 ERLAEQQRAEERERLAavEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ 1469
Cdd:NF041483 93 ERELRDARAQTQRILQ--EHAEHQARLQAELHTEAVQRRQQLDQELAERRQTVESHVNENVAWAEQLRARTESQARRLLD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1470 SSEAEiqakARQVEAAERSRL-RIEEEirvvrlqlettERQRGGAEGElqalRARAeEAEAQKRQAQEEAERLRRQVQDE 1548
Cdd:NF041483 171 ESRAE----AEQALAAARAEAeRLAEE-----------ARQRLGSEAE----SARA-EAEAILRRARKDAERLLNAASTQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1549 TQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQaeEAERRLRQAEAERARQVQVALETAqrsaevelqSKRASFA 1628
Cdd:NF041483 231 AQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA---------AKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1629 EKT-AQLERTLQEEhvaVAQL-REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEK 1706
Cdd:NF041483 300 ESAnEQRTRTAKEE---IARLvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1707 QKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEELARLQHEa 1785
Cdd:NF041483 377 LTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEARRLRGE- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1786 aaATQKRQELEAELAKVRAEM----------------EVLLASKARAEE-ESRSTSEKSKQRLEA--EASRFRELAE--- 1843
Cdd:NF041483 449 --AEQLRAEAVAEGERIRGEArreavqqieeaartaeELLTKAKADADElRSTATAESERVRTEAieRATTLRRQAEetl 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1844 -----EAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLAEKLA-AIGEATRLKTEAE-------IALKEKEAENERLR 1909
Cdd:NF041483 527 ertraEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEerltaaeEALADARAEAERIR 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1910 RLAEDEAfqrRRLEEQAAqhkadieERLAQLRKASESELERQKGLVEDTLRQRRqVEEEILALKVSFEKAAagkaelelE 1989
Cdd:NF041483 607 REAAEET---ERLRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAAR-AEGENVAVRLRSEAAA--------E 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1990 LGRIRSNAEDTlRSKEQAELEAMRQRqlaaeeeqrrrEAEERVQKSLAAEEEAARQRKaalEEVERLKAKVEEARRLRER 2069
Cdd:NF041483 668 AERLKSEAQES-ADRVRAEAAAAAER-----------VGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQERER 732
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2070 AEQESARQLQlaqdAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQS 2149
Cdd:NF041483 733 AREQSEELLA----SARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAER 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2150 RRQ--VEEAERLKQSAEEQAQAQAQAQAaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAEQTLRQkAQVE 2227
Cdd:NF041483 809 TRTeaQEEADRVRSDAYAERERASEDAN------------------------RLRREAQEETEAAKALAERTVSE-AIAE 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2228 QElttlRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQ------------MEELGKLKARIEAENRA 2295
Cdd:NF041483 864 AE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDaaaqadrligeaTSEAERLTAEARAEAER 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2296 LILRDKDNTQRVLQEEAEKMKHV------------AEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEkmqAVQE 2363
Cdd:NF041483 940 LRDEARAEAERVRADAAAQAEQLiaeatgeaerlrAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTE---AREE 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2364 ATRLKAEA-ELLQQQKELAQEQARRLQEDKEQMAQQL--EQETQGFQRTLEAERQRQLEMSA---EAERLKLR------- 2430
Cdd:NF041483 1017 ADRTLDEArKDANKRRSEAAEQADTLITEAAAEADQLtaKAQEEALRTTTEAEAQADTMVGAarkEAERIVAEatvegns 1096
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2431 VAEMSRAQAR-----AEEDAQRFRKQAEEIG-------EKLH---RTELATQEKVT------LVQTLEIQRQQSDHDAER 2489
Cdd:NF041483 1097 LVEKARTDADellvgARRDATAIRERAEELRdritgeiEELHeraRRESAEQMKSAgercdaLVKAAEEQLAEAEAKAKE 1176
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*.
gi 2124423184 2490 LR--------------------------QAIAELEREKEKLKQEAK 2509
Cdd:NF041483 1177 LVsdanseaskvriaavkkaegllkeaeQKKAELVREAEKIKAEAE 1222
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1447-2271 |
1.53e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.93 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1447 EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE 1526
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1527 aEAQKRQAQEEAERLR-----RQVQD--ETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAE- 1598
Cdd:PTZ00121 1114 -ARKAEEAKKKAEDARkaeeaRKAEDarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEe 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1599 ---AERARQVQVAletaqRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELER 1675
Cdd:PTZ00121 1193 lrkAEDARKAEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1676 WQ--LKANEALRlrlqAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQLAEGtaqqrlaa 1753
Cdd:PTZ00121 1268 RQaaIKAEEARK----ADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADA-------- 1333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1754 eqelIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEmevllASKARAEEESRStsEKSKQRLEA 1833
Cdd:PTZ00121 1334 ----AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-----AAKKKAEEKKKA--DEAKKKAEE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1834 EASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERvlaeklaaigEATRLKTEAEIALKEKEAENERLRRLAE 1913
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK----------KADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1914 DEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEeilaLKVSFEKAAAGKAElelelgri 1993
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAK-------- 1540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1994 rsNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEeaarqrkaaLEEVErlKAKVEEARRLRERAEQE 2073
Cdd:PTZ00121 1541 --KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE---------AKKAE--EARIEEVMKLYEEEKKM 1607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2074 SARQLQLAQDAaqkRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQv 2153
Cdd:PTZ00121 1608 KAEEAKKAEEA---KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA- 1683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2154 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTlrqKAQVEQELTTL 2233
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA---KKDEEEKKKIA 1760
|
810 820 830
....*....|....*....|....*....|....*...
gi 2124423184 2234 RLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2271
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
206-301 |
1.94e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.39 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 206 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 284
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 2124423184 285 VPQPDEKSIITYVSSLY 301
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
88-185 |
2.21e-25 |
|
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: 103.16 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 88 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 163
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 2124423184 164 NDDIADGnPKLTLGLIWTIILH 185
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1380-2520 |
2.42e-25 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 116.85 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1380 SETLRRMEEEE--RLAEQQRAEERERLAAVEAalEKQRQLAEAHAQAKAQAEQ---EAQELQRRMQEEVARREEAAVDAQ 1454
Cdd:NF041483 154 AEQLRARTESQarRLLDESRAEAEQALAAARA--EAERLAEEARQRLGSEAESaraEAEAILRRARKDAERLLNAASTQA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1455 QQKRSIQEELqhlRQSSEAEIQAKARQveAAERSRlrieeeirvvrlqleTTERQRGGAEGELQALRARAEEAEAQKRQA 1534
Cdd:NF041483 232 QEATDHAEQL---RSSTAAESDQARRQ--AAELSR---------------AAEQRMQEAEEALREARAEAEKVVAEAKEA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1535 QeeAERLRRQVQDETQRKRQAEAELAVRV-KAEAEAAREKQRALQALEEFRLQAE----EAERRLRQAEAER-ARQVQVA 1608
Cdd:NF041483 292 A--AKQLASAESANEQRTRTAKEEIARLVgEATKEAEALKAEAEQALADARAEAEklvaEAAEKARTVAAEDtAAQLAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1609 LETAQR-----SAEVELQSKRAS------FAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL--ER 1675
Cdd:NF041483 370 ARTAEEvltkaSEDAKATTRAAAeeaeriRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLrgEA 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1676 WQLKAN---EALRLRLQAEEVAQQKslaqaeaekQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA-EGTAQQRL 1751
Cdd:NF041483 450 EQLRAEavaEGERIRGEARREAVQQ---------IEEAARTAEELLTKAKADADELRSTATAESERVRTEAiERATTLRR 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1752 AAEQELIRLRAE--------TEQGEQQRQLLEEELARLQHEAAAATQKRQ-ELEAELAKVRAEMEVLLASKARAEEESRS 1822
Cdd:NF041483 521 QAEETLERTRAEaerlraeaEEQAEEVRAAAERAARELREETERAIAARQaEAAEELTRLHTEAEERLTAAEEALADARA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1823 TSEKSKQRLEAEASRFRelAEEAARLRAL----AEEAKRQRQLAEEDAARQRAEAERVlaeklaaigeATRLKTEAeial 1898
Cdd:NF041483 601 EAERIRREAAEETERLR--TEAAERIRTLqaqaEQEAERLRTEAAADASAARAEGENV----------AVRLRSEA---- 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1899 kekEAENERLRRLAEDEAfQRRRLEEQAAQhkadieERLAQlrKASESELERQkglvEDTLRQRRQVEEEIlalkvsfek 1978
Cdd:NF041483 665 ---AAEAERLKSEAQESA-DRVRAEAAAAA------ERVGT--EAAEALAAAQ----EEAARRRREAEETL--------- 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1979 aAAGKAELELELGRIRSNAEDTLRSK----EQAELEAMR----QRQLAAEEEQRRREAEERVQKSLA-----AEEEAARQ 2045
Cdd:NF041483 720 -GSARAEADQERERAREQSEELLASArkrvEEAQAEAQRlveeADRRATELVSAAEQTAQQVRDSVAglqeqAEEEIAGL 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2046 RKAALEEVERLKAKV-EEARRLRERAEQESARQlqlAQDAAQKRLQAEEKAHAfavqqkeqelqqtlqqEQSMLERLRGE 2124
Cdd:NF041483 799 RSAAEHAAERTRTEAqEEADRVRSDAYAERERA---SEDANRLRREAQEETEA----------------AKALAERTVSE 859
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2125 AeaarraaeeaeeareraereaaqsrrqVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQA 2204
Cdd:NF041483 860 A---------------------------IAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAA 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2205 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT-EAARQRSQVEEELFSLRVQMEELG 2283
Cdd:NF041483 913 AQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIR 992
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2284 KLKARIEAENRAlilrDKDNTQRVLQEEAEKMKHVAEEAA--RLSVAAQEAARLRELAEEDL------AQQRALAEKMLK 2355
Cdd:NF041483 993 TEAERVKAEAAA----EAERLRTEAREEADRTLDEARKDAnkRRSEAAEQADTLITEAAAEAdqltakAQEEALRTTTEA 1068
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2356 EKMQ------AVQEATRLKAEA-----ELLQQQKELAQE---QARR----LQEDKEQMAQQLEQETQGFQRtlEAERQRQ 2417
Cdd:NF041483 1069 EAQAdtmvgaARKEAERIVAEAtvegnSLVEKARTDADEllvGARRdataIRERAEELRDRITGEIEELHE--RARRESA 1146
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2418 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTelATQEKVTLVQTLEIQRQQSDHDAERLR-QAIAE 2496
Cdd:NF041483 1147 EQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIA--AVKKAEGLLKEAEQKKAELVREAEKIKaEAEAE 1224
|
1210 1220
....*....|....*....|....
gi 2124423184 2497 LEREKEKLKQEAKLLQLKSEEMQT 2520
Cdd:NF041483 1225 AKRTVEEGKRELDVLVRRREDINA 1248
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
188-303 |
3.26e-25 |
|
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: 103.61 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 188 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 267
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423184 268 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 303
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1143-1943 |
4.32e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.92 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1143 AEEVLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1222
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1223 VAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIER 1302
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1303 hgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISET 1382
Cdd:TIGR02168 405 -----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1383 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE-EVARREEAAVDAQQQKR--- 1458
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAALGGRlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1459 -------SIQEELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAE 1525
Cdd:TIGR02168 550 vvvenlnAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1526 EAEAQKRQAQEEAERLRRQVQDETQRKRQAeaeLAVRVKAEAEAAREKQRalQALEEFRLQAEEAERRLRQAEAE--RAR 1603
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLDGDLVRPGG---VITGGSAKTNSSILERR--REIEELEEKIEELEEKIAELEKAlaELR 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1604 QVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehvaVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1683
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1684 LRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAE 1763
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1764 TEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEAEASRFRE 1840
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEELREKLAQLELRLEGLEVRIDN 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1841 LAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIGEATRLkteaeiALKEKEAENERLRRLaedeafqr 1919
Cdd:TIGR02168 941 LQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERYDFL-------- 1005
|
810 820
....*....|....*....|....
gi 2124423184 1920 rrleeqaAQHKADIEERLAQLRKA 1943
Cdd:TIGR02168 1006 -------TAQKEDLTEAKETLEEA 1022
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1764-2646 |
5.64e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 116.01 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1764 TEQGEQQRQLLEEELARLQHEAAAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFREL-- 1841
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1842 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlAEKLAAIGEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 1919
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1920 RRLEEQaaqHKADIEERLAQLRKASESelerqkglvedtlrqrRQVEEeilalkvsfekaaAGKAELELELGRIRsNAED 1999
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2000 TLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQ 2079
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2080 LAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERlrgeaeaarraaeeaeeareraereaaqsRRQVEEAERL 2159
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-----------------------------AKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2160 KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2239
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2240 TDHQksildEELQRLKAEVTEAARQRSQVEEelfslRVQMEELGKlkaRIEAENRALILRDKDNTQRVLQE---EAEKMK 2316
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEEAK 1496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2317 HVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDK 2392
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2393 EQMAQQLEQETQgfqrtleAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVtl 2472
Cdd:PTZ00121 1577 NMALRKAEEAKK-------AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK-- 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2473 vqtleiqrqqsdHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLlqetqalqqsflsEKDTLLQRErfiE 2552
Cdd:PTZ00121 1647 ------------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-------------KAAEALKKE---A 1698
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2553 QEKAKLEQL---FQDEVAKAQKLREEQQRQQKqmeeekqqlvasmeEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLL 2629
Cdd:PTZ00121 1699 EEAKKAEELkkkEAEEKKKAEELKKAEEENKI--------------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
890 900
....*....|....*....|
gi 2124423184 2630 AEENQRLRERLQR---LEEE 2646
Cdd:PTZ00121 1765 EEEKKAEEIRKEKeavIEEE 1784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1719-2415 |
6.34e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 115.62 E-value: 6.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1719 GKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQ----ELIRLRAETEQGEQQRQLleeELARLQHEAAAATQKRQE 1794
Cdd:PTZ00121 1098 GKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEEarkaEDARKAEEARKAEDAKRV---EIARKAEDARKAEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1795 LEAELAK-VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRElAEEAARLRAL--AEEAKRQRQLAEEDAARQRA 1871
Cdd:PTZ00121 1173 EDAKKAEaARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARK-AEDAKKAEAVkkAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1872 EAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAED--EAFQRRRLEEqaAQHKADIEERLAQLRKASESELE 1949
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKK 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1950 RQKGLvedtlrqRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAE-----LEAMRQRQLAAEEEQR 2024
Cdd:PTZ00121 1330 KADAA-------KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkkAEEKKKADEAKKKAEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2025 RREAEERVQKSLAAEEEAARQRKAALE--EVERLKAKVEEARRLRE-RAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQ 2101
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2102 QKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQS--RRQVEEAERLKQSAEEQAQAQAQAQAAAEK 2179
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2180 LRKEAEQEAARRAQAEQAALRQ--KQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSIlDEELQRLKAE 2257
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE-KKKVEQLKKK 1641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2258 VTEAARQRSQVEEELFSLRVQMEELGKL--KARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARL 2335
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2336 RELAEEDLAQQRALAEKMLKEKMQAvQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQlEQETQGFQRTLEAERQ 2415
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-ELDEEDEKRRMEVDKK 1799
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
200-306 |
7.90e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 101.98 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 200 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 276
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 2124423184 277 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 306
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
85-188 |
2.51e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.44 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 85 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 160
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHFQI 188
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
202-301 |
3.17e-24 |
|
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: 99.94 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 202 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 281
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 2124423184 282 D-VDVPQPDEKSIITYVSSLY 301
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
204-304 |
3.51e-24 |
|
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: 99.85 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 204 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 283
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 2124423184 284 DVPQPDEKSIITYVSSLYDAM 304
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
835-901 |
6.08e-24 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 97.72 E-value: 6.08e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 835 QLKPRNpaHPVRGRVPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVVSSSGSEAAVPSVCFLVP 901
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
201-305 |
2.76e-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: 97.17 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 280
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 2124423184 281 EDVDVPQPDEKSIITYVSSLYDAMP 305
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
201-301 |
2.92e-23 |
|
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: 97.11 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 280
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 2124423184 281 EDVDVPQ-PDEKSIITYVSSLY 301
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1723-2561 |
7.93e-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: 108.22 E-value: 7.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1802
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1803 RAEMEVLLASKARAEEESRSTSEkskqrleaeasRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1882
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1883 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrRLEEQAAQHKADIEERLAQLrKASESELERQKGLVEDtlRQR 1962
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEE--LLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1963 RQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAElEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 2042
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE-QALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2043 ARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQ-LAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLErL 2121
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE-I 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2122 RGEAEAARRAAEEAEEARERAEREAAQSRRQVEE-------AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2194
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2195 EQAALRQKQaaDAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEELFS 2274
Cdd:TIGR02168 667 KTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2275 LRVQMEELGKLKARIEAEnralilrdkdntqrvLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKmL 2354
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKE---------------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-L 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2355 KEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLEQETQgfqrtleaerqrqlEMSAEAERLKLRVAE 2433
Cdd:TIGR02168 802 REALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--------------ELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2434 MSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQl 2513
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ- 942
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 2124423184 2514 kseemQTVQQEQLLQETQALQQSFLSEKDTLLQRERfIEQEKAKLEQL 2561
Cdd:TIGR02168 943 -----ERLSEEYSLTLEEAEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1279-2096 |
1.15e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 107.99 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1279 VLADSRAVREQLrqekalleeierhgekveecqrfakqyinaikdyelqlvtykaqlepVASPAKKPKVQSGSESVIQEY 1358
Cdd:NF041483 335 ALADARAEAEKL-----------------------------------------------VAEAAEKARTVAAEDTAAQLA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1359 VDLRTryselttltsqyikfISETLRRMEEEERLAEQQRAEERERLAAvEAALEKQRQLAEAHAQakaqaeqeAQELQRR 1438
Cdd:NF041483 368 KAART---------------AEEVLTKASEDAKATTRAAAEEAERIRR-EAEAEADRLRGEAADQ--------AEQLKGA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1439 MQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE---IQAKAR-----QVEAAERSRLRIEEEIRVVRLQLETT---- 1506
Cdd:NF041483 424 AKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEgerIRGEARreavqQIEEAARTAEELLTKAKADADELRSTatae 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1507 -ERQRGGAEGELQALRARAEEAEAQKRqaqEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRL 1585
Cdd:NF041483 504 sERVRTEAIERATTLRRQAEETLERTR---AEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1586 QAeEAERRLRQAEaERARQVQVALETAQRSAEVELQSKRASFAEKTaqleRTLQEEHVAVAQLREEAERRAQQQAEAERA 1665
Cdd:NF041483 581 HT-EAEERLTAAE-EALADARAEAERIRREAAEETERLRTEAAERI----RTLQAQAEQEAERLRTEAAADASAARAEGE 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1666 REEAERELErwqlKANEALRLRLQAEEVAQQksLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG 1745
Cdd:NF041483 655 NVAVRLRSE----AAAEAERLKSEAQESADR--VRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQ 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1746 TAQQRLAAEQELI---RLRAETEQGEQQRqLLEEELARLQHEAAAATQKRQELEAELAKV--RAEMEV--LLASKARAEE 1818
Cdd:NF041483 729 ERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAE 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1819 ESRSTSEKSKQRLEAEASRFRELA-EEAARLRALA-EEAKRQRQLAEEDAARQRAEAERVLAEklaAIGEATRLKTEAEI 1896
Cdd:NF041483 808 RTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASD 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1897 ALKEKEAENERLRRLAEDEAFQRRrlEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSF 1976
Cdd:NF041483 885 TLASAEQDAARTRADAREDANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1977 EKAAAGKAElelelgRIRSNAEDTLRSKEQAeleAMRQRQLAAEEEQRrreaeervqkslaAEEEAARQRKAALEEVERL 2056
Cdd:NF041483 963 IAEATGEAE------RLRAEAAETVGSAQQH---AERIRTEAERVKAE-------------AAAEAERLRTEAREEADRT 1020
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 2124423184 2057 --KAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAH 2096
Cdd:NF041483 1021 ldEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1058-1622 |
1.21e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1058 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1137
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1138 RSTHGAEEVLKAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVE 1217
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1218 RWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALL 1297
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1298 EEIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyik 1377
Cdd:COG1196 477 AALAE-----------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1378 fisetlrrMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEA----HAQAKAQAEQEAQELQRRMQEEVARREEAAVDA 1453
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1454 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1533
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1534 AQEEAERLRRQvqdETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVA-LETA 1612
Cdd:COG1196 692 ELELEEALLAE---EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEeLERE 768
|
570
....*....|
gi 2124423184 1613 QRSAEVELQS 1622
Cdd:COG1196 769 LERLEREIEA 778
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
201-299 |
3.08e-22 |
|
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: 94.23 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 279
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 2124423184 280 PEDVDVPQPDEKSIITYVSS 299
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
84-189 |
5.68e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.38 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 84 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 160
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHFQIS 189
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
84-189 |
6.11e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 94.38 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 84 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 160
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHFQIS 189
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1883-2666 |
1.31e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.84 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1883 AIGEATRLKTEAEIALKEKeAENERLRRLAEDEAFQRRRLEEQaaqHKADIEERLAQLRKASESELERQKGLVEDTLR-- 1960
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGK-AEEARKAEEAKKKAEDARKAEEA---RKAEDARKAEEARKAEDAKRVEIARKAEDARKae 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1961 QRRQVEEEilalkvsfEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQrqlaaeeeqrrreaeerVQKSLAAEE 2040
Cdd:PTZ00121 1168 EARKAEDA--------KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK-----------------AEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2041 EaarQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAhafavQQKEQELQQTLQQEQSMLER 2120
Cdd:PTZ00121 1223 A---KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-----EEARKADELKKAEEKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2121 LRgeaeaarraaEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALR 2200
Cdd:PTZ00121 1295 AK----------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2201 QKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEEtDHQKSildEELQRLKAEVTEAARQRSQVEEelfslrvqME 2280
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEE-DKKKA---DELKKAAAAKKKADEAKKKAEE--------KK 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2281 ELGKLKARIEAENRAlilrdkdntqrvlqEEAEKMKHVAEEAARLSVAAQEAARLRELAEEdlAQQRALAEKMLKEKMQA 2360
Cdd:PTZ00121 1432 KADEAKKKAEEAKKA--------------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKKADEAKKKAEEA 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2361 VQEATRLKAEAELLQQQKELAQ-EQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAErlKLRVAEMSRaqa 2439
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAK--- 1570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2440 RAEEDAQRFRKQAEEigeklhrteLATQEKVTLVQTLEIQRQQSDHDAERLRQAiaelerEKEKLKQEakllQLKSEEmq 2519
Cdd:PTZ00121 1571 KAEEDKNMALRKAEE---------AKKAEEARIEEVMKLYEEEKKMKAEEAKKA------EEAKIKAE----ELKKAE-- 1629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2520 tvqqeqllqetqalqqsflSEKDTLLQRERFIEQEKAKLEQLFQDE----------VAKAQKLREEQQRQQKQMEEEK-- 2587
Cdd:PTZ00121 1630 -------------------EEKKKVEQLKKKEAEEKKKAEELKKAEeenkikaaeeAKKAEEDKKKAEEAKKAEEDEKka 1690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2588 -QQLVASMEEARQ----RQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQA 2662
Cdd:PTZ00121 1691 aEALKKEAEEAKKaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
....
gi 2124423184 2663 TAVK 2666
Cdd:PTZ00121 1771 EEIR 1774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1583-2459 |
1.85e-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: 103.98 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1583 FRLQAEEAERRLRQAEAERARqVQVALETAQRSAE-VELQSKRAS-FAEKTAQLERTlqEEHVAVAQLREEAERRAQQQA 1660
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDR-LEDILNELERQLKsLERQAEKAErYKELKAELREL--ELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1661 eaerareeaerelerwQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAE-----QE 1735
Cdd:TIGR02168 247 ----------------ELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYAlaneiSR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1736 LEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKAR 1815
Cdd:TIGR02168 300 LEQQKQILR---ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1816 AEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAE 1895
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1896 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELE-----RQKGLVEDTLRQRRQVEEEil 1970
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllknqSGLSGILGVLSELISVDEG-- 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1971 alkvsFEKAaagkaeLELELGrirSNAEDTLRSKEQAELEAmrqrqlaaeeeqrrreaeervqksLAAEEEAARQRKAAL 2050
Cdd:TIGR02168 535 -----YEAA------IEAALG---GRLQAVVVENLNAAKKA------------------------IAFLKQNELGRVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2051 EEV---ERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQ--------AEEKAHAFAvQQKEQELQQTLQQEQSMLE 2119
Cdd:TIGR02168 577 PLDsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvVDDLDNALE-LAKKLRPGYRIVTLDGDLV 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2120 RLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAER-LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAarraqaeqaa 2198
Cdd:TIGR02168 656 RPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAeLEKALAELRKELEELEEELEQLRKELEELS---------- 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2199 lRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRvq 2278
Cdd:TIGR02168 726 -RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-- 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2279 mEELGKLKARIEAENRAL--ILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKE 2356
Cdd:TIGR02168 803 -EALDELRAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2357 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRtLEAERQRQLEMSAEAERLKLRVAEmsR 2436
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEEAE--A 958
|
890 900
....*....|....*....|...
gi 2124423184 2437 AQARAEEDAQRFRKQAEEIGEKL 2459
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1167-1967 |
5.82e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 102.44 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1167 LEATKAALKKLRAQAEAQQpMFDALRDELRGAQE--VGERLQQRHGERDvEVERWRERVAQLLERWQAVLAQTDLrqrEL 1244
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAE-RYKELKAELRELELalLVLRLEELREELE-ELQEELKEAEEELEELTAELQELEE---KL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1245 EQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDY 1324
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1325 ELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTtltsQYIKFISETLRRMEEE-ERLAEQQRAEERER 1403
Cdd:TIGR02168 350 KEELESLEAELE--ELEAELEELESRLEELEEQLETLRSKVAQLE----LQIASLNNEIERLEARlERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1404 LAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR------QSSEAEIQA 1477
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1478 KARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAE----GELQALRARAEEAEAQKRQAQEEAERLRR---------- 1543
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVtflpldsikg 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1544 QVQDETQRKRQAEAELAVRVKAEAEAAREK-QRALQALEEFRLQAEEAERRLRQAEAERARQVQVALE------------ 1610
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvitg 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1611 --TAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRL 1688
Cdd:TIGR02168 664 gsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1689 QAEEVAQQKSLAQAEAEKQkeeaerearrrgkaeeqavrqRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1768
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAE---------------------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1769 QQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEASRFRELAEEAARL 1848
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEELESELEALLNE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1849 RALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAE----NERLRRLAEDEAFQRRRLEE 1924
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALEN 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1925 QAAQHKADIEERLAQLRK----------ASESELERQKGLVEDTLRQRRQVEE 1967
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENkikelgpvnlAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
205-302 |
2.91e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.94 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 205 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 283
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2124423184 284 DVPQPDEKSIITYVSSLYD 302
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
201-301 |
4.15e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 88.17 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 280
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 2124423184 281 EDVDV--PQPDEKSIITYVSSLY 301
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1480-2296 |
9.35e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.21 E-value: 9.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1480 RQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEG-----------ELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1548
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1549 TQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERAR--QVQVALETAQRSAEVELQSKRAS 1626
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1627 FAEKTAQLERtLQEEHVAVAQLREeaerraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKSLAQAEAEK 1706
Cdd:TIGR02168 339 LAELEEKLEE-LKEELESLEAELE-----------------------ELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1707 QKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAA 1786
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1787 AATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEASRFRELAEEAARLRALAEEAKRQR--QLA 1862
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRlqAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1863 EEDAARQRAEAErvlAEKLAAIGEATRLkteAEIALKEKEAENERLRRLAEDEAFQR--RRLEEQAAQHKADIEERLAQL 1940
Cdd:TIGR02168 552 VENLNAAKKAIA---FLKQNELGRVTFL---PLDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLGGV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1941 RKASEselerqkglVEDTLRQRRQVEEEILALKVSFEKAAAG----KAELELELGRI-RSNAEDTLRSK--EQAELEAMR 2013
Cdd:TIGR02168 626 LVVDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTNSSILeRRREIEELEEKieELEEKIAEL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2014 QRQLAAEEEQRRREAEERVQKsLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2093
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQL-RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2094 KAHAfaVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQA 2173
Cdd:TIGR02168 776 ELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2174 QAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQR 2253
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 2124423184 2254 LKAEVteaARQRSQVEEElfsLRVQMEELGKLKARIEAENRAL 2296
Cdd:TIGR02168 934 LEVRI---DNLQERLSEE---YSLTLEEAEALENKIEDDEEEA 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2118-2732 |
1.86e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2118 LERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaqaQAQAAAEKLRKEAEQEAARRAQAEQA 2197
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL-------------AELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2198 ALRQKQAADAEMEKHKKFAEQtlrQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2277
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2278 QMEELgklkARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEK 2357
Cdd:COG1196 366 ALLEA----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2358 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA 2437
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2438 QARAEEDAQRFRKQAEEIGEklhrTELATQEKVTLVQTLEIQRQQSDHDAERL--RQAIAELEREKEKLKQEAKLLQLKS 2515
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALE----AALAAALQNIVVEDDEVAAAAIEYLKAAKagRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2516 EEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERfIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASME 2595
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAAR-LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2596 EARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVKALPNGRDAP 2675
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 2676 DGPATEAEPEHAFDGLRQKVpaQRLQEVGILSTEELQRLVQGRTTVAElaQREDVRR 2732
Cdd:COG1196 757 PEPPDLEELERELERLEREI--EALGPVNLLAIEEYEELEERYDFLSE--QREDLEE 809
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
201-300 |
2.05e-19 |
|
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: 86.38 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 280
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 2124423184 281 ED-VDVPQPDEKSIITYVSSL 300
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
197-302 |
2.87e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 86.15 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 197 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 276
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 2124423184 277 LLDPEDV-DVPQPDEKSIITYVSSLYD 302
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
204-300 |
3.76e-19 |
|
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: 85.45 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 204 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 279
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 2124423184 280 PEDVDVPQPDEKSIITYVSSL 300
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2040-2571 |
1.12e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2040 EEAARQRKAALEEVERLKAKVEEARRLRERAEQEsARQLQLAQDAAQKRLQAEEKAHAfAVQQKEQELQQTLQQEQSMLE 2119
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELE-EAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2120 RLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2199
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2200 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2279
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2280 EELGKLKARIEAENRALILRDKDNTQR--VLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEE--DLAQQRALAEKMLK 2355
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2356 EKMQA--VQEATRLKAEAELLQQQKE--------LAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAE 2425
Cdd:COG1196 546 AALQNivVEDDEVAAAAIEYLKAAKAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2426 RLKLRVAEMSRAQARAEEDAQRFRKQAEEI----GEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREK 2501
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGgsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2502 EKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQLfQDEVAKAQK 2571
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLER 774
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
86-186 |
1.34e-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: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 86 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 161
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 2124423184 162 IRNDDIADGNPKLTLGLIWTIILHF 186
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1374-2012 |
1.69e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.95 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1374 QYIKFISETLRRMEEEERLAEQQR----------AEERERLAAVEAALEKQRQlaeahaqAKAQAEQEAQELQRRMQEEV 1443
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1444 ARREEaavdaqqqkrsIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQAL 1520
Cdd:PRK02224 286 ERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1521 RARAEEaeaqkrqAQEEAERLrrqvqdetqrkrqaEAELavrvkAEAEAAREKQRAlqALEEFRLQAEEAERRLRQAEae 1600
Cdd:PRK02224 355 EERAEE-------LREEAAEL--------------ESEL-----EEAREAVEDRRE--EIEELEEEIEELRERFGDAP-- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1601 rarqvqVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVAVAQlreeaerraqqqaeaerareeaerelerwqlka 1680
Cdd:PRK02224 405 ------VDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEE--------------------------------- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1681 NEALRLRLQAEEVAQQkslaqaeaekqkeeaEREARRRGKAEEQAVRQRELAEqELEKQRqLAEGTAQQRLAAEQELIRL 1760
Cdd:PRK02224 445 AEALLEAGKCPECGQP---------------VEGSPHVETIEEDRERVEELEA-ELEDLE-EEVEEVEERLERAEDLVEA 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1761 RAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLEAEASRFRE 1840
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAE 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1841 LAEEAARLRALAEeakrqrQLAEEDAARQRAEAervLAEKLAAIGEatrLKTEAEIALKEKeaeNERLRRLAEDeaFQRR 1920
Cdd:PRK02224 584 LKERIESLERIRT------LLAAIADAEDEIER---LREKREALAE---LNDERRERLAEK---RERKRELEAE--FDEA 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1921 RLEE------QAAQHKADIEERLAQLRkASESELERQKGLVE------DTLRQRR-QVEEEILALKVSFEKAaagkAELE 1987
Cdd:PRK02224 647 RIEEaredkeRAEEYLEQVEEKLDELR-EERDDLQAEIGAVEneleelEELRERReALENRVEALEALYDEA----EELE 721
|
650 660
....*....|....*....|....*
gi 2124423184 1988 LELGRIRSNaedtLRSKEQAELEAM 2012
Cdd:PRK02224 722 SMYGDLRAE----LRQRNVETLERM 742
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1513-2409 |
2.79e-18 |
|
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: 93.50 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1513 AEGELQALRARAEEAEAQKRQAQEE----AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAE 1588
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAEliidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1589 EAERRLRQAEAERARQVQVAletaqrsAEVELQSKRASFAEKTAQLErtLQEEHVAVAQLREEAERRAQQQAEAERAREE 1668
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEK-------EEEKLAQVLKENKEEEKEKK--LQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1669 AERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQ 1748
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKEL---------KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1749 QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKvRAEMEVLLASKARAEEESRSTSEKSK 1828
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-SIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1829 QRLEAEASRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEiaLKEKEAENERL 1908
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKL-EERSQKESKARSGLKVLLALIKDGVGGRIISAHG--RLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1909 RRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELEL 1988
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1989 ELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2068
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2069 RAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQ 2148
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2149 SRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQ 2228
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2229 ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVL 2308
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2309 QEEAEKMKHVAEEAarlsvaaqeaarLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRL 2388
Cdd:pfam02463 941 LLEEADEKEKEENN------------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
890 900
....*....|....*....|.
gi 2124423184 2389 QEDKEQMAQQLEQETQGFQRT 2409
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSI 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1910-2664 |
2.85e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 93.58 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1910 RLAEDEAFQRRRLEEQAA---QHKADIEERLAQLRKASESeLERQKGLVEDTLRQ----RRQVEeeiLALKVSFEKAAAG 1982
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKETERKLERTREN-LDRLEDILNELERQlkslERQAE---KAERYKELKAELR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1983 KAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRK---AALEEVERLKAK 2059
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2060 VEEARRLRERAEQESAR-QLQLAQDAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEA 2138
Cdd:TIGR02168 304 KQILRERLANLERQLEElEAQLEELESKLDELAEELA---ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2139 RERAEREAAQSRRQVEEA--------ERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEME 2210
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLnneierleARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2211 KHKKFAEQTLRQKaqvEQELTTLRLQLEETDHQKSIL---DEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKA 2287
Cdd:TIGR02168 461 EALEELREELEEA---EQALDAAERELAQLQARLDSLerlQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2288 RIEA---ENRALILRDKDNTQRV---LQEEAEKMKHV----------------AEEAARLSVAAQEAARLRELAE----- 2340
Cdd:TIGR02168 538 AIEAalgGRLQAVVVENLNAAKKaiaFLKQNELGRVTflpldsikgteiqgndREILKNIEGFLGVAKDLVKFDPklrka 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2341 -----------EDLAQQRALAEKMLKEKMQAVQEATRL--------------------KAEAELLQQQKELAQEQARRLQ 2389
Cdd:TIGR02168 618 lsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2390 ---EDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAT 2466
Cdd:TIGR02168 698 kalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2467 QEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDTLLQ 2546
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIES 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2547 RERFIEQEKAKLEQLfQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQE 2626
Cdd:TIGR02168 857 LAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
810 820 830
....*....|....*....|....*....|....*...
gi 2124423184 2627 KLLAEENQRLRERLQRLEEEhraALAHSEEIAASQATA 2664
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEE---AEALENKIEDDEEEA 970
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
87-184 |
4.46e-18 |
|
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: 82.39 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 87 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 162
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 2124423184 163 RNDDI-ADGNPKLTLGLIWTIIL 184
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1379-2091 |
6.47e-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: 92.44 E-value: 6.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1379 ISETLRRMEEEERLAEQQRAEERERLAAVEAALEKqrqLAEAHAQAKAQAEQEAQELQRRMqEEVARREEAAVDAQQQKR 1458
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1459 SIQEELQHLRQSSEAEIQAKARQVEAaersrlrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1532
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdel 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1533 --------QAQEEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQA-LEEFRLQAEEAERRLRQAEAER-- 1601
Cdd:TIGR02169 388 kdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQLAADLsk 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1602 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAerelERWQLKAN 1681
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVG----ERYATAIE 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1682 EALRLRLQA-----EEVAQQK---------------SLAQAEAEKQKEEAEREARRRGKA---------EEQAVR---QR 1729
Cdd:TIGR02169 543 VAAGNRLNNvvvedDAVAKEAiellkrrkagratflPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkYEPAFKyvfGD 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1730 ELAEQELEKQRQL--------------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH 1783
Cdd:TIGR02169 623 TLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEN 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1784 EAAAATQKRQELEAELAKVRAEMEVLLASKARAEE---ESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQ 1860
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1861 LAEEDAARQRAEAERVLAEKLAAIGEATRLKT-EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1939
Cdd:TIGR02169 783 DLEARLSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1940 LRKAsESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKE--QAELEAMRQRQL 2017
Cdd:TIGR02169 863 KEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELSEIEDPKG 941
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 2018 AAEEEQRRREAEERVQKSLAAEEEAARQ----RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQA 2091
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1393-2062 |
7.68e-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: 91.78 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1393 AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQ-HLRQSS 1471
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTeQLEQAK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1472 EAEIQ-AKARQVEAAERSRLriEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQ 1550
Cdd:pfam01576 370 RNKANlEKAKQALESENAEL--QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1551 RKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEVELQSKRASFA 1628
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNslQEQLEEEEEAKRNVERQLSTLQAQLS 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1629 EktaqLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQlKANEALRLRLQAEEVAQQkslaqaeaekqk 1708
Cdd:pfam01576 528 D----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE-KTKNRLQQELDDLLVDLD------------ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1709 eeaerearrrgkaeeqavRQRELAEQELEKQRQLAEGTAQQRLAAEQEL-IRLRAETEQGEQQRQLLEeelarLQHEAAA 1787
Cdd:pfam01576 591 ------------------HQRQLVSNLEKKQKKFDQMLAEEKAISARYAeERDRAEAEAREKETRALS-----LARALEE 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1788 ATQKRQELEAELAKVRAEMEVLLASKARAeEESRSTSEKSKQRLEAEASRFRELAEEA---------ARLR------ALA 1852
Cdd:pfam01576 648 ALEAKEELERTNKQLRAEMEDLVSSKDDV-GKNVHELERSKRALEQQVEEMKTQLEELedelqatedAKLRlevnmqALK 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1853 EEAKRQRQLAEEDA-------ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1925
Cdd:pfam01576 727 AQFERDLQARDEQGeekrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1926 AAQHKADIEE-RLAQ---LRKASESElERQKGLVEDTL----------RQRRQVEEEILALKVSFEKAAAGKAELELELG 1991
Cdd:pfam01576 807 MKDLQRELEEaRASRdeiLAQSKESE-KKLKNLEAELLqlqedlaaseRARRQAQQERDELADEIASGASGKSALQDEKR 885
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1992 RIR---SNAEDTLrSKEQAELEAMRQRQlaaeeeQRRREAEERVQKSLAAEEEAARQRKAALEEVER----LKAKVEE 2062
Cdd:pfam01576 886 RLEariAQLEEEL-EEEQSNTELLNDRL------RKSTLQVEQLTTELAAERSTSQKSESARQQLERqnkeLKAKLQE 956
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1381-1950 |
8.41e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 91.90 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLRRMEEEERLAEQQR------AEERERLAAVEAALEKQRQLAEAHAQAKAQAEQE-AQELQRRMQEEVARREEAAVDA 1453
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1454 QQQKRSIQEELQHLRQ-----------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERqrggaegELQALRA 1522
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAE-------EFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1523 RA----EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA-------------VRVKAE-AEAAREKQRALQALEEFr 1584
Cdd:COG4913 388 EAaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrksniparlLALRDAlAEALGLDEAELPFVGEL- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1585 LQAEEAERRLRQAeAERA----------------------------RQVQVALETAQRSAEVELQSKRASFAEK------ 1630
Cdd:COG4913 467 IEVRPEEERWRGA-IERVlggfaltllvppehyaaalrwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAGKldfkph 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1631 --TAQLERTLQEE--HVAV---AQLREEA----ERRAQQQAEAERAREEAERELERWQL-KANEALRLRLQAEEVAQQKS 1698
Cdd:COG4913 546 pfRAWLEAELGRRfdYVCVdspEELRRHPraitRAGQVKGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1699 LAQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLE 1775
Cdd:COG4913 626 LAEAEERLEAL----------EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1776 EELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEA 1855
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1856 KRQRQLAEEDAARQRAEAERVLAE-KLAAIGEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRRLEEQAAQHKAD 1932
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVAD 850
|
650
....*....|....*...
gi 2124423184 1933 IEERLAQLRKASESELER 1950
Cdd:COG4913 851 LLSKLRRAIREIKERIDP 868
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1383-2103 |
1.38e-17 |
|
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: 91.19 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1383 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVA-----RREEAAVDAQQQK 1457
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYldylkLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1458 RSIQEELQHLRQSSEAE---IQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQA 1534
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEeekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1535 QEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQr 1614
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1615 saEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1694
Cdd:pfam02463 406 --EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1695 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1771
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1772 QLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaeasrfRELAEEAARLRAL 1851
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV------VEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1852 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA 1931
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1932 DIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAED-------TLRSK 2004
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKlkveeekEEKLK 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2005 EQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ---LQLA 2081
Cdd:pfam02463 798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQellLKEE 877
|
730 740
....*....|....*....|..
gi 2124423184 2082 QDAAQKRLQAEEKAHAFAVQQK 2103
Cdd:pfam02463 878 ELEEQKLKDELESKEEKEKEEK 899
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
201-300 |
4.31e-17 |
|
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: 79.90 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 280
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 2124423184 281 ED-VDVPQPDEKSIITYVSSL 300
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
205-302 |
5.94e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.54 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 205 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 283
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2124423184 284 DVPQPDEKSIITYVSSLYD 302
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
203-314 |
1.54e-16 |
|
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: 78.49 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 203 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 282
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 2124423184 283 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 314
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1008-1917 |
1.92e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.43 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1008 QQLLQSLEQGEQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1087
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1088 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTHG----AEEVLKAHEEQLKEAQ 1158
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1159 AVPATL-PELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavlaqt 1237
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1238 dlRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAmvladsravreqlrqekalleEIERHGEKVEECQRFAKQY 1317
Cdd:TIGR02169 390 --YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1318 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESVIQEYVDLRTRYSELTtltsqyiKFISETLRRMEEEERLAEQQR 1397
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVE-------KELSKLQRELAEAEAQARASE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1398 AEERERlAAVEAALEKQ--------RQLAEAHAQAKAQAEQEAQElqrRMQEEVARREEAAVDAQQQKRS---------- 1459
Cdd:TIGR02169 504 ERVRGG-RAVEEVLKASiqgvhgtvAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflp 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1460 ---IQEELQHLRQSSEA--------------EIQAKARQV-------EAAERSRlRIEEEIRVVRLQLETTERQ---RGG 1512
Cdd:TIGR02169 580 lnkMRDERRDLSILSEDgvigfavdlvefdpKYEPAFKYVfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGG 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1513 A-EGELQALRARAEEAEAQKRQAQEEA-ERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEfrlqaeea 1590
Cdd:TIGR02169 659 SrAPRGGILFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ-------- 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1591 errlrqaEAERARQVQVALETAQRSAEVELQSKRASFAE---KTAQLERTLQEEHVAVAQLREEAERraqqqaeaerare 1667
Cdd:TIGR02169 731 -------EEEKLKERLEELEEDLSSLEQEIENVKSELKEleaRIEELEEDLHKLEEALNDLEARLSH------------- 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1668 eaerelERWQLKANEalrLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTA 1747
Cdd:TIGR02169 791 ------SRIPEIQAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1748 QQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKS 1827
Cdd:TIGR02169 862 KKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1828 KQRLE--AEASRFRELAEE----AARLRALAEEAKRQRQLAEEDAARQRAeaervLAEKLAaigeatRLKTEAEiALKEK 1901
Cdd:TIGR02169 941 GEDEEipEEELSLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDE-----LKEKRA------KLEEERK-AILER 1008
|
970
....*....|....*.
gi 2124423184 1902 EAENERLRRLAEDEAF 1917
Cdd:TIGR02169 1009 IEEYEKKKREVFMEAF 1024
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2284-2736 |
2.38e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.91 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2284 KLKARI-EAENRaliLRD-KDNTQRV--LQEEAEK-MKHVAEEAARlsvaAQEAARLRELAEEDLAQQRALAEKMLKEKM 2358
Cdd:COG1196 169 KYKERKeEAERK---LEAtEENLERLedILGELERqLEPLERQAEK----AERYRELKEELKELEAELLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2359 QAVQ-EATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGF----QRTLEAERQRQLEM------SAEAERL 2427
Cdd:COG1196 242 EELEaELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEerrrelEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2428 KLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQE 2507
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2508 AKLLQLKSEEMQtvqqeqllqetqALQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEK 2587
Cdd:COG1196 402 LEELEEAEEALL------------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2588 QQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVKA 2667
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2668 LPNGRDAPDGPATEAEPEHAFDGLRQKVPAQRLQEVGILSTEELQRLV-QGRTTVAELAQREDVRRYLQG 2736
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgAAVDLVASDLREADARYYVLG 619
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1143-1633 |
3.14e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1143 AEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQ--RHGERDVEVERWR 1220
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkKKADELKKAAAAK 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1221 ERVAQLLERWQAVLAQTDLRQRELEqlgrqlryyRESADPLGAWLQDAKRRQEQIQAmvlADSRAVREQLRQEKALLEEI 1300
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEE---------AKKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKKA 1485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1301 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqeyvdlrtRYSELTTLTSQYIKfiS 1380
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA---------KKAEEKKKADELKK--A 1554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQlaeahaQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1460
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE------EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1461 QEELQHLRQ--SSEAEIQAKARQV-EAAERSRLRIEEEIRVVRLQLETTERQRGGAEGElqalrARAEEAEAQKRQAQEE 1537
Cdd:PTZ00121 1629 EEEKKKVEQlkKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-----KKAAEALKKEAEEAKK 1703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1538 AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAER--RLRQAEAERARQVQVALETAQRS 1615
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKiaHLKKEEEKKAEEIRKEKEAVIEE 1783
|
490
....*....|....*...
gi 2124423184 1616 AEVELQSKRASFAEKTAQ 1633
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1399-1943 |
3.57e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.51 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1399 EERERLAAVEAALEKQRQLAEAHAQAkaqaeQEAQElQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRqsseaeIQAK 1478
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEAL-----EDARE-QIELLEPIRELAERYAAARERLAELEYLRAALR------LWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1479 ARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRA--------RAEEAEAQKRQAQEEAERLRRQVQDETQ 1550
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1551 RKRQAE----------AELAVRVKAEAEAAREKQRALQ-ALEEFRLQAEEAERRLRQAEAERArqvqvALETAQRSAEVE 1619
Cdd:COG4913 367 LLAALGlplpasaeefAALRAEAAALLEALEEELEALEeALAEAEAALRDLRRELRELEAEIA-----SLERRKSNIPAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1620 LQSKRASFAEKTAQLERTLQ--EEHVAVAQLReeaerraqqqaeaerareeaerelERWQLKANEAL---RLRL------ 1688
Cdd:COG4913 442 LLALRDALAEALGLDEAELPfvGELIEVRPEE------------------------ERWRGAIERVLggfALTLlvppeh 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1689 --QAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAE 1763
Cdd:COG4913 498 yaAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1764 TEQG---------------------------EQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARA 1816
Cdd:COG4913 578 TRAGqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1817 EEESRSTS--------EKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIG 1885
Cdd:COG4913 658 WDEIDVASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLE 737
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1886 EATRLKTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKA 1943
Cdd:COG4913 738 AAEDLARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEE 788
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1006-1640 |
4.23e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.26 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1006 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLpldkepaRECAQRIAEQQK----AQAEVEGLGK 1080
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEV-------SELEEEIEELQKelyaLANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1081 GVARLSAEAEKVLA-LPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKE--- 1156
Cdd:TIGR02168 303 QKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqle 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1157 --AQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQ-QRHGERDVEVERWRERVAQLLERWQAV 1233
Cdd:TIGR02168 383 tlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1234 LAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMV----------------LADSRAVREQLRQ--EKA 1295
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkallknqsglsgilgvLSELISVDEGYEAaiEAA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1296 L--------------------------------LEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASP-- 1341
Cdd:TIGR02168 543 LggrlqavvvenlnaakkaiaflkqnelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYll 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1342 -------------AKKPKVQSGSESVIQEYVDLRTRYSelttLTSQYIKFISETL---RRMEEEERLAEQQRAEERERLA 1405
Cdd:TIGR02168 623 ggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGV----ITGGSAKTNSSILerrREIEELEEKIEELEEKIAELEK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1406 AVEAALEKQRQLAEAHAQAKAQAEQEAQELqRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAA 1485
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQLSKELTEL----EAEIEELEERLEEA 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1486 ERSRLRIEEEIrvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKA 1565
Cdd:TIGR02168 774 EEELAEAEAEI-------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1566 EAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERArQVQVALETAqRSAEVELQSKRASFAEKTAQLERTLQE 1640
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
206-301 |
4.66e-16 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 77.02 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 206 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 284
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 2124423184 285 VPQPDEKSIITYVSSLY 301
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
203-302 |
6.75e-16 |
|
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: 76.16 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 203 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 282
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 2124423184 283 VDV--PQPDEKSIITYVSSLYD 302
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
203-306 |
1.10e-15 |
|
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: 75.86 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 203 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 282
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 2124423184 283 VDV--PQPDEKSIITYVSSLYDAMPR 306
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1143-2072 |
1.62e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.35 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1143 AEEVLKAHEEQLKEAQAVpatLPELEATKAALKKLRAQAEAqqpmFDALRDELRGAqEVGERLQQrhgerdveverWRER 1222
Cdd:TIGR02169 175 ALEELEEVEENIERLDLI---IDEKRQQLERLRREREKAER----YQALLKEKREY-EGYELLKE-----------KEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1223 VAQLlerwQAVLAQTDLRQRELEQLGRQLRyyrESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIER 1302
Cdd:TIGR02169 236 ERQK----EAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1303 hgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltsqyikfiset 1382
Cdd:TIGR02169 309 ---SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDL-------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1383 LRRMEEEERLAeqqrAEERERLAAVEAALEK-QRQLaeahaqakaqaeQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ 1461
Cdd:TIGR02169 370 RAELEEVDKEF----AETRDELKDYREKLEKlKREI------------NELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1462 EELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEaERL 1541
Cdd:TIGR02169 434 AKINEL----EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER-VRG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1542 RRQVQDETQRKRQAE----AELaVRVKAEAEAARE---KQRALQALEEFRLQAEEAERRLRQAEAERA--------RQVQ 1606
Cdd:TIGR02169 509 GRAVEEVLKASIQGVhgtvAQL-GSVGERYATAIEvaaGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplnkmRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1607 VALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQqqaeaerareeaerelerwqlkaneaLRL 1686
Cdd:TIGR02169 588 RDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGK--------------------------YRM 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1687 RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVR------QRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1760
Cdd:TIGR02169 642 VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERleglkrELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1761 RAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLeaEASRFRE 1840
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA----LNDLEARL--SHSRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1841 LAEEaarLRALAEEAKRQR-QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRrlaedeafqR 1919
Cdd:TIGR02169 796 IQAE---LSKLEEEVSRIEaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK---------K 863
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1920 RRLEEQAAQHKA---DIEERLAQLRKASEsELERQKGLVEdtlRQRRQVEEEILALKVSFEKAAAGKAELELELGRIrsn 1996
Cdd:TIGR02169 864 EELEEELEELEAalrDLESRLGDLKKERD-ELEAQLRELE---RKIEELEAQIEKKRKRLSELKAKLEALEEELSEI--- 936
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1997 aEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ 2072
Cdd:TIGR02169 937 -EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1279-1969 |
2.09e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 83.86 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1279 VLADSRAVREQLRQEKALLEEIERHgekveecQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEY 1358
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKK-------QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1359 VDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERerlaaVEAALEKQRQLAEAHAQAKAQAEQEAQELQRR 1438
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT-----LHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1439 MQEEvarrEEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrLQLETTERQRGGAEGELQ 1518
Cdd:TIGR00618 382 HTLQ----QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE-----LQQRYAELCAAAITCTAQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1519 ALRARaeEAEAQK-RQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAE---RRL 1594
Cdd:TIGR00618 453 CEKLE--KIHLQEsAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltRRM 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1595 RQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEhVAVAQLREEAERRAQQQAEAERAREEAEREle 1674
Cdd:TIGR00618 531 QRGEQTYAQ-----LETSEEDVYHQLTSERKQRASLKEQMQEIQQSF-SILTQCDNRSKEDIPNLQNITVRLQDLTEK-- 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1675 rwQLKANEALRLRLQAEEVAQQkslaqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQ---RL 1751
Cdd:TIGR00618 603 --LSEAEDMLACEQHALLRKLQ-------------------------PEQDLQDVRLHLQQCSQELALKLTALHAlqlTL 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1752 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLAS-KARAEEESRSTSEKSK-- 1828
Cdd:TIGR00618 656 TQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdREFNEIENASSSLGSDla 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1829 QRLEAEA---SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLkteaeiaLKEKEAEN 1905
Cdd:TIGR00618 736 AREDALNqslKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------LKTLEAEI 808
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 1906 ERLRRLAEDEafqRRRLEEQAAQHKADIEERLAQLRKaSESELERQKGLVEDTLRQRRQVEEEI 1969
Cdd:TIGR00618 809 GQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSA-TLGEITHQLLKYEECSKQLAQLTQEQ 868
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1455-2398 |
2.45e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.96 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1455 QQKRSIQEELQHLRQSsEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEA----- 1529
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1530 QKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAR------EKQRALQALEEFRLQAEEAE-----RRLRQAE 1598
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1599 AERARQVQVALETaqrsaEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQaeaerareeaerelerwql 1678
Cdd:TIGR02169 311 AEKERELEDAEER-----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1679 kanEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQEL 1757
Cdd:TIGR02169 367 ---EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1758 IRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAE 1834
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1835 ASRFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLAEKLAAigeatrlktEAEIALKEKEAENER---LRRL 1911
Cdd:TIGR02169 524 HGTVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKM 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1912 AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELeRQKGLVEDTLRQRRQ--------VEEEIlalkvsFEKAAAgk 1983
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLmgkyrmvtLEGEL------FEKSGA-- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1984 aeleLELGRIRSNAEDTLRSKEQAELEAMRQRqlaaeeeqrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEA 2063
Cdd:TIGR02169 655 ----MTGGSRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDEL 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2064 RRLRERAEQE----SARQLQLAQDAAQKRLQAEEkahafaVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEAR 2139
Cdd:TIGR02169 708 SQELSDASRKigeiEKEIEQLEQEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2140 ERAEREAAQSRRQVEEAERLKQsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQT 2219
Cdd:TIGR02169 782 NDLEARLSHSRIPEIQAELSKL----------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2220 LRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEElfsLRVQMEELGKLKARIEaenralILR 2299
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ---LRELERKIEELEAQIE------KKR 916
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2300 DKDNTQRV-LQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQK 2378
Cdd:TIGR02169 917 KRLSELKAkLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKR 995
|
970 980
....*....|....*....|
gi 2124423184 2379 ELAQEQARRLQEDKEQMAQQ 2398
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKK 1015
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
83-182 |
3.19e-15 |
|
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: 74.49 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 83 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 157
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 2124423184 158 KLVNIRNDDIADGNPKLTLGLIWTI 182
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2035-2729 |
3.21e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2035 SLAAEEEAARQRKAALEEVERLKAKVEEARRlRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2114
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK-TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2115 QSMLERLrgeaeaarraaeeaeeareraereaaQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2194
Cdd:PTZ00121 1154 VEIARKA--------------------------EDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2195 EQAALRQKQAADAEMEKHK---KFAEQTlRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVE-- 2269
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAeavKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKka 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2270 EElfslRVQMEELGKLKARIEAENRALILRDKDNTQRvLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRAL 2349
Cdd:PTZ00121 1287 EE----KKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2350 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLEQEtqgfqrtlEAERQRQLEMSAEAErlKL 2429
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKA--------AAAKKKADEAKKKAE--EK 1430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2430 RVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvqtleiQRQQSDHDAERLRQAiAELEREKEKLKQEAK 2509
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK---------KADEAKKKAEEAKKA-DEAKKKAEEAKKKAD 1500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2510 LLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQ----MEE 2585
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEedknMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2586 EKQQLVASMEEAR-----------------QRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2648
Cdd:PTZ00121 1581 RKAEEAKKAEEARieevmklyeeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2649 ---AALAHSEEIAASQA-TAVKALPNGRDAPDGPATEAEPEHAFDGLRQKVPAQ--------RLQEVGILSTEELQRLVQ 2716
Cdd:PTZ00121 1661 ikaAEEAKKAEEDKKKAeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkkkaeelkKAEEENKIKAEEAKKEAE 1740
|
730
....*....|...
gi 2124423184 2717 GRTTVAELAQRED 2729
Cdd:PTZ00121 1741 EDKKKAEEAKKDE 1753
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1184-2094 |
3.27e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 83.30 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1184 QQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQA----------VLAQTDLRQRELEQLGRQLRY 1253
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1254 YRESADPLGAWLQ-DAKRRQEQIQAM--VLADSRAVREQLRQEKALLEeierhgekveecqrfAKqyinaIKDYELQLVT 1330
Cdd:pfam01576 83 RLEEEEERSQQLQnEKKKMQQHIQDLeeQLDEEEAARQKLQLEKVTTE---------------AK-----IKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1331 YKAQlepvasPAKKPKVQSGSESVIQEYVDLRTRYSE----LTTLTSQYIKFISETLRRMEEEE----RLAEQQRAEERE 1402
Cdd:pfam01576 143 LEDQ------NSKLSKERKLLEERISEFTSNLAEEEEkaksLSKLKNKHEAMISDLEERLKKEEkgrqELEKAKRKLEGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1403 RLAAVEAALEKQRQLAEAHAQAkAQAEQEAQELQRRMQEEVARREEaavdAQQQKRSIQEELQHLRQSSEAEIQAKARqv 1482
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRAQL-AKKEEELQAALARLEEETAQKNN----ALKKIRELEAQISELQEDLESERAARNK-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1483 eaAERSRLRIEEEIRVVRLQLETTErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELav 1561
Cdd:pfam01576 290 --AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1562 rvkaeAEAAREKQRALQALEEFRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEktAQLERTLQEE 1641
Cdd:pfam01576 362 -----TEQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1642 HVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAQAEAEKqkeeaerearrrgka 1721
Cdd:pfam01576 434 KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL--------------- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1722 EEQAVRQRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEaelak 1801
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKA----- 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1802 vrAEMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEASRFRE-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAe 1874
Cdd:pfam01576 566 --AAYDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQKKFDQmLAEEKAISARYAEERDRAEAEAREKETRALSLA- 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1875 RVLAEKLAAIGEATR----LKTEAEIALKEKEA------ENERLRRLAEDEAFQ-RRRLEE-----QAAQH-KADIEERL 1937
Cdd:pfam01576 643 RALEEALEAKEELERtnkqLRAEMEDLVSSKDDvgknvhELERSKRALEQQVEEmKTQLEEledelQATEDaKLRLEVNM 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1938 AQLRKASESELERQKGLVEDT----LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAeLEAMR 2013
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEA-VKQLK 801
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2014 QRQLAAEEEQRRREAEERVQKS-LAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQDAAQKRLQA 2091
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRDEiLAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQ 881
|
...
gi 2124423184 2092 EEK 2094
Cdd:pfam01576 882 DEK 884
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4084-4122 |
3.42e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.42e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 4084 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4122
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3506-3544 |
3.77e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.77e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 3506 LLEAQIATGGIIDPVHSHRVPVEVAYQRGYFDEEMNRVL 3544
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
991-1542 |
4.60e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 991 EDRLQAEREYGSCSHHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLrlpldkeparecAQRIAEQQK 1070
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL------------EELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1071 AQAEVEGLGKGVARLSAEAEKVLAlpepspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAH 1150
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEE---------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1151 EEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLErw 1230
Cdd:COG1196 413 LERLERLEE------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1231 qavlAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRqekalLEEIERHGEKVEEC 1310
Cdd:COG1196 485 ----ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-----AALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1311 QRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEE 1389
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1390 ERLAEQQRAEERERLAAVEAALEKQRqLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ 1469
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGS-LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1470 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ-------AQEEAERLR 1542
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELE 794
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1356-1865 |
9.37e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 81.35 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1356 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERL---AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAE--Q 1430
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1431 EAQELQRRMQEEVARREEAavdaQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQR 1510
Cdd:COG4717 133 ELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1511 GGAEGELQALRARAEEAEAQKRQAQEEAERlrrqvQDETQRKRQAEAELAVRVkaeaeaarekqrALQALEEFRLQAEEA 1590
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEA-----AALEERLKEARLLLLIAA------------ALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1591 ERRLRQAEAERARQVQVALETAQRsaevelqsKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAE 1670
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAR--------EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1671 RELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1750
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-----------EDEEELRAALEQAEEYQELKEELEE--LEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1751 LAAEQELIRLRAETEQGEQqrqlLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQR 1830
Cdd:COG4717 411 LEELLGELEELLEALDEEE----LEEELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQE 477
|
490 500 510
....*....|....*....|....*....|....*
gi 2124423184 1831 LEAEASRFRELAEEAARLRALAEEAKRQRQLAEED 1865
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1143-1646 |
9.95e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 9.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1143 AEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpmfDALRDELRGAQEVGERLQQRHGERDVEVErwRER 1222
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAG--LDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1223 VAQllerwQAVLAQTDLRQRELEQLGRQLRYYRESAdplGAWLQDAKRRQEQIQAMvlaDSRAvrEQLRQEKALLE-EIE 1301
Cdd:PRK02224 307 ADA-----EAVEARREELEDRDEELRDRLEECRVAA---QAHNEEAESLREDADDL---EERA--EELREEAAELEsELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1302 RHGEKVEECQrfakqyiNAIKDYELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyikfISE 1381
Cdd:PRK02224 374 EAREAVEDRR-------EEIEELEEEIEELRERFG--DAPVDLGNAEDFLEELREERDELREREAELEAT-------LRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1382 TLRRMEEEERLAEQ-------QRAEERERLAAVEAALEKQRQLAEAHAQAKAQaeqeaqelqrrmQEEVARREEAAVDAQ 1454
Cdd:PRK02224 438 ARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE------------VEEVEERLERAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1455 QQKRsiqeELQHLRQSSEAEIQAKARQVEAAERSRLRIEE-EIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1533
Cdd:PRK02224 506 EAED----RIERLEERREDLEELIAERRETIEEKRERAEElRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1534 AQ--EEAERLRR--QVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEA--ERRLRQAEAERAR---- 1603
Cdd:PRK02224 582 AElkERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERaeey 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2124423184 1604 QVQVALETAQRSAE-VELQSKRASFAEKTAQLERtLQEEHVAVA 1646
Cdd:PRK02224 662 LEQVEEKLDELREErDDLQAEIGAVENELEELEE-LRERREALE 704
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2847-2885 |
1.16e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.16e-14
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 2847 LLEAQIATGGVIDPVHSHRVPVEVAYQRGYFDEEMNRVL 2885
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
80-185 |
1.28e-14 |
|
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: 72.70 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 80 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIAL 149
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423184 150 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 185
Cdd:cd21219 72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3765-3803 |
1.33e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.33e-14
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 3765 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3803
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1101-1854 |
1.33e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 81.17 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1101 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKtislvirSTHGAEEVLKAHEEQLKE-AQAVPATLPELEATKAALKKLRA 1179
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKK-------SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1180 QAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQlgRQLRYYRESAD 1259
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI--KAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1260 PLGAWLQDAKRRQEQI---QAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYElQLVTYKAQLE 1336
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1337 pvaspAKKPKVQSGSesviqeyvdlrtrySELTTLTSQYIKFISETLRRMEEEERL--AEQQRAEERERLAAVEAALEKQ 1414
Cdd:TIGR00618 390 -----TLTQKLQSLC--------------KELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1415 RQ---LAEAHAQ-------AKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEA--EIQAKARQV 1482
Cdd:TIGR00618 451 AQcekLEKIHLQesaqslkEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1483 EAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVR 1562
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1563 VKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1642
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL---QLTLTQERVREHALSIRVLPKELLASRQLALQKMQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1643 VAVAQLREEAER---RAQQQAEAERAREEAERELERWQLkANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArrrg 1719
Cdd:TIGR00618 687 SEKEQLTYWKEMlaqCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE---- 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 kaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQHEAAAATQKRQE 1794
Cdd:TIGR00618 762 --AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRLEE 839
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1795 LEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEE 1854
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
203-304 |
1.94e-14 |
|
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: 72.42 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 203 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 282
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 2124423184 283 -VDVPQPDEKSIITYVSSLYDAM 304
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1399-2094 |
2.02e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 80.78 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1399 EERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR--QSSEAEIQ 1476
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLReaLQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1477 AKARQVEAAERSRLRIEEEIRVVRLQLETTERQrggaegelQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqAE 1556
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ--------EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR-IH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1557 AELAVRvKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALetaqrsaevelqSKRASFAEKTAQLER 1636
Cdd:TIGR00618 314 TELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT------------SIREISCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1637 TLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAlrlRLQAEEVAQQKSLAQAEA--------EKQK 1708
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAELCAAaitctaqcEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1709 EEAEREARRRGKAEEQAVRQRE-LAEQELEKQ----RQLAEGTAQQRLAAEQELIRLRAET------------EQGEQQR 1771
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEqIHLQETRKKavvlARLLELQEEPCPLCGSCIHPNPARQdidnpgpltrrmQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1772 QLLEEELARLQHEAAAATQKRQELEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEaeasrfRELAEEAARLRAL 1851
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQ------DLTEKLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1852 AEEAKRQ-RQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 1930
Cdd:TIGR00618 611 ACEQHALlRKLQPEQDLQDVRLHLQQCSQELAL--KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1931 adiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALkvsfekaAAGKAELelelgrirsNAEDTLRSKEQAELE 2010
Cdd:TIGR00618 689 ---KEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS-------SSLGSDL---------AAREDALNQSLKELM 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2011 AMRQRQLAAEEEQRRREAEERV------QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE-SARQLQLAQD 2083
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIlNLQCETLVQE 829
|
730
....*....|.
gi 2124423184 2084 AAQKRLQAEEK 2094
Cdd:TIGR00618 830 EEQFLSRLEEK 840
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
86-186 |
2.63e-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: 71.56 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 86 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 157
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 2124423184 158 KLVNIRNDDIADGNPKLTLGLIWTIILHF 186
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
201-301 |
2.69e-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: 72.03 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 280
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 2124423184 281 ED-VDVPQPDEKSIITYVSSLY 301
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1116-1584 |
3.38e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1116 LEQVRSLSAIYLEKLKTISLVIRSTHGAEeVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDEL 1195
Cdd:COG4913 254 LEPIRELAERYAAARERLAELEYLRAALR-LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1196 RGA--QEVgERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQE 1273
Cdd:COG4913 333 RGNggDRL-EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1274 QiqamVLADSRAVREQLRQEKALLE---------------EIERH-GEKVEEC--------------------------Q 1311
Cdd:COG4913 412 A----ALRDLRRELRELEAEIASLErrksniparllalrdALAEAlGLDEAELpfvgelievrpeeerwrgaiervlggF 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1312 RF-----------AKQYINAIKDyELQLVTYKAqlEPVASPAKKPKVQSGS--------ESVIQEYVD--LRTRYS---- 1366
Cdd:COG4913 488 ALtllvppehyaaALRWVNRLHL-RGRLVYERV--RTGLPDPERPRLDPDSlagkldfkPHPFRAWLEaeLGRRFDyvcv 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1367 ----ELT------TLTSQyIKFiSETLRRMEEEERL---------AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQ 1427
Cdd:COG4913 565 dspeELRrhpraiTRAGQ-VKG-NGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDA 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1428 AEQEAQELQRRmqEEVARREEAAVDAQQQKRSIQEELQHLRQSSeAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTE 1507
Cdd:COG4913 643 LQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1508 RQRGGAEGELQALRARAEEAEAQKRQAQ-EEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFR 1584
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1107-1972 |
4.03e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 79.73 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1107 SELELTLGKLEQVRslsaiylEKLKTISLVIRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATK--AALKKLRAQAEAQ 1184
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1185 QPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLaQTDLR--QRELEQLGRQLRYYRESadplg 1262
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGelEAEIASLERSIAEKERE----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1263 awLQDAKRRQEQIQAmvladsravreqlrQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPA 1342
Cdd:TIGR02169 317 --LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1343 KKPKvqsgsesviQEYVDLRTRYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHA 1422
Cdd:TIGR02169 381 AETR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1423 QAKAQAEQEAQELQRRMQeevarreeaavDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1502
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLS-----------KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1503 LETTERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDETQRKRQAEaeLAVRVKA------EAEAAREK 1573
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEAIE--LLKRRKAgratflPLNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1574 QRALQALEE-----FRLQAEEAERRLRQAEAERARQVQV--ALETAQR--------SAEVELQSKRA-----SFAEKTAQ 1633
Cdd:TIGR02169 587 RRDLSILSEdgvigFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1634 LERTLQEEHVAVAqlreeaerraqqqaeaerareeaereleRWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEaer 1713
Cdd:TIGR02169 667 LFSRSEPAELQRL----------------------------RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS--- 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1714 earrrgKAEEQAVRQRELAEQELEKQRQLAEG-------TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqhEAA 1786
Cdd:TIGR02169 716 ------RKIGEIEKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EAR 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1787 AATQKRQELEAELAKVRAEmevllaskaRAEEESRSTS-EKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEED 1865
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEE---------VSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1866 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---ERLAQLRK 1942
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIED 938
|
890 900 910
....*....|....*....|....*....|..
gi 2124423184 1943 ASESELE-RQKGLVEDTLRQRRQ-VEEEILAL 1972
Cdd:TIGR02169 939 PKGEDEEiPEEELSLEDVQAELQrVEEEIRAL 970
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1056-1604 |
4.81e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1056 EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISL 1135
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1136 VIRStHGAEEVlkaheEQLKEaqavpatlpELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVE 1215
Cdd:COG4913 331 QIRG-NGGDRL-----EQLER---------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1216 VERWRERVAQllERWQAVLAQTDLRqRELEQLGRQLRYYRESADPLGAWLQDAkrRQEQIQAMVLADSRA--------VR 1287
Cdd:COG4913 396 LEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLAL--RDALAEALGLDEAELpfvgelieVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1288 -EQLRQEKAlleeIER--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsviqey 1358
Cdd:COG4913 471 pEEERWRGA----IERvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG------ 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1359 vdlrtrysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-AVEAALEK--QRQLAEAH------AQ 1423
Cdd:COG4913 539 --------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1424 AKAQAEQEAQELQRRMQEEVARREEAAvDAQQQKRSIQEELQHLRQSSEAEI--QAKARQVEAAERSRLRIEE---EIRV 1498
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAssdDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1499 VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQ 1578
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
570 580
....*....|....*....|....*.
gi 2124423184 1579 ALEEfRLQAEEAERRLRQAEAERARQ 1604
Cdd:COG4913 770 NLEE-RIDALRARLNRAEEELERAMR 794
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1758-2559 |
5.00e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 79.24 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1758 IRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEaEA 1835
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLM-NL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1836 SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEdE 1915
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1916 AFQRRRLEEQAAQHKADIEERLAQLRKASESELERQkglvedtlrQRRQVEEeilalkvsfeKAAAGKAELELELGRIRS 1995
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1996 NAEdtLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2075
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2076 rQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEE 2155
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2156 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRL 2235
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2236 QLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEEL-------GKLKARIEAENRALI--LRDKDNTQR 2306
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdlteklSEAEDMLACEQHALLrkLQPEQDLQD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2307 VLQEEAEKMKHVAEEAARLSVAA--------QEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2378
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQltltqervREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2379 ELAQEQARRLQEDKEQMAQQLEQETQGfqrTLEAERQRQLEMSAEA-ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2457
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAA---REDALNQSLKELMHQArTVLKARTEAHFNNNEEVTAALQTGAELSHLAAE 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2458 KLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQeakLLQLKSEEMQTVQQEQLLQETQALQQsf 2537
Cdd:TIGR00618 787 IQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS---RLEEKSATLGEITHQLLKYEECSKQL-- 861
|
810 820
....*....|....*....|..
gi 2124423184 2538 lsekDTLLQRERFIEQEKAKLE 2559
Cdd:TIGR00618 862 ----AQLTQEQAKIIQLSDKLN 879
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1272-2279 |
9.00e-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: 78.68 E-value: 9.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1272 QEQIQAM--VLADSRAVREQLRQEKALLEEI--------ERHGEKVEECQRFAKQYINAIKDYELQL-----VTYKAQLE 1336
Cdd:pfam01576 46 QEQLQAEteLCAEAEEMRARLAARKQELEEIlhelesrlEEEEERSQQLQNEKKKMQQHIQDLEEQLdeeeaARQKLQLE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1337 PVASPAKKPKVQS-------GSESVIQEYVDLRTRYSELTT--------------LTSQYIKFISETLRRMEEEE----R 1391
Cdd:pfam01576 126 KVTTEAKIKKLEEdillledQNSKLSKERKLLEERISEFTSnlaeeeekakslskLKNKHEAMISDLEERLKKEEkgrqE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1392 LAEQQRAEERERLAAVEAALEKQRQLAEAHAQAkAQAEQEAQELQRRMQEEVARREEAavdaQQQKRSIQEELQHLRQSS 1471
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQL-AKKEEELQAALARLEEETAQKNNA----LKKIRELEAQISELQEDL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1472 EAEIQAKARqveaAERSRLRIEEEIRVVRLQLETTErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQ 1550
Cdd:pfam01576 281 ESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1551 RKRQAEAELAvrvkaeaEAAREKQRALQALEEFRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEk 1630
Cdd:pfam01576 353 KHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1631 tAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAQAEAEKqkee 1710
Cdd:pfam01576 424 -SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL---- 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1711 aerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQ 1790
Cdd:pfam01576 495 -----------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1791 KRQELEAElakvraeMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEASRFRELaeeaarlraLAEEAKRQRQLAEE 1864
Cdd:pfam01576 560 QLEEKAAA-------YDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQKKFDQM---------LAEEKAISARYAEE 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1865 daaRQRAEAERVLAEKLA-----AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ-------RRRLEEQAAQHKAD 1932
Cdd:pfam01576 624 ---RDRAEAEAREKETRAlslarALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNvhelersKRALEQQVEEMKTQ 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1933 IEERLAQLRKASESEL-------------------------ERQKGLVedtlRQRRQVEEEILALKVSFEKAAAGKAELE 1987
Cdd:pfam01576 701 LEELEDELQATEDAKLrlevnmqalkaqferdlqardeqgeEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLE 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1988 LELGRIRSNAEDTLRSKEQAeLEAMRQRQLAAEEEQRRREAEERVQKS-LAAEEEAARQRKAALEEVERLKAKVEEARRL 2066
Cdd:pfam01576 777 LDLKELEAQIDAANKGREEA-VKQLKKLQAQMKDLQRELEEARASRDEiLAQSKESEKKLKNLEAELLQLQEDLAASERA 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2067 RERAEQESAR-QLQLAQDAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSMLERLRGEAEAARR---AAEEAEEARER 2141
Cdd:pfam01576 856 RRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttELAAERSTSQK 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2142 AEREAAQSRRQVEEAeRLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAE---------MEKH 2212
Cdd:pfam01576 936 SESARQQLERQNKEL-KAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEkklkevllqVEDE 1014
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 2213 KKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2279
Cdd:pfam01576 1015 RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
201-298 |
1.24e-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: 69.72 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 276
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 2124423184 277 LLDPEDVDVPQPDEKSIITYVS 298
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2217-2512 |
1.35e-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: 77.86 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2217 EQTLRQKAQVEQELTTLRLQLEETDHQKSIlDEELQRLKAEVTEAARQRSQVEEELFSL--RVQMEELGKLK-------A 2287
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2288 RIEAENRALILRDKDNTQRVLQEEAEKmkhvAEEAARLSVAAQEAARLRELAEEDLAQQR-----------ALAEKMLKE 2356
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEERKR----ELERIRQEEIAMEISRMRELERLQMERQQknervrqeleaARKVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2357 KMQAVQEATRLKAEaELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQlemsAEAERLKLRVAEMSR 2436
Cdd:pfam17380 410 ERQRKIQQQKVEME-QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE----EERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 2437 AQARAEEDAqrfRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRqaIAELEREKEKLKQEAKLLQ 2512
Cdd:pfam17380 485 DRKRAEEQR---RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEMEERRRIQ 555
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
201-301 |
2.05e-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: 69.29 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 280
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 2124423184 281 ED-VDVPQPDEKSIITYVSSLY 301
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
660-838 |
2.54e-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: 72.09 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 660 LYSFVAAATKELMWLSEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEIQNTGDRLLREDHPARPTVESFQ 739
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 740 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDERDQLNEY 819
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 2124423184 820 RGHLSGLARRAKAIVQLKP 838
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1164-1589 |
2.77e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 76.34 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1164 LPELEATKAALKKLRAQAEAqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWR--ERVAQLLERWQAVLAQTDLRQ 1241
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1242 RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQekaLLEEIERHGEKVEECQRFAKQYINAI 1321
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1322 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVI-------QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EE 1390
Cdd:COG4717 223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1391 RLAEQQRAEERERL--AAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKrsIQEELQHLR 1468
Cdd:COG4717 303 EAEELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1469 QSSEAEIQAKARQVEAAErsrlRIEEEIRVVRLQLET---------TERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1539
Cdd:COG4717 381 VEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllgeleellEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1540 RLRRQVQ-----DETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEE 1589
Cdd:COG4717 457 ELEAELEqleedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3099-3137 |
5.91e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 5.91e-13
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 3099 LLEAQAGTGHIIDPATSARLTVDEAVRSGLVGPELHEKL 3137
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
104-183 |
6.24e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.00 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 104 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 175
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 2124423184 176 LGLIWTII 183
Cdd:cd21223 105 LALLWRII 112
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1401-1926 |
9.02e-13 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 75.28 E-value: 9.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1401 RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR 1480
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1481 QVEAAERSRLRIEEEIRVV-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDETQRKRQAEA 1557
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1558 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERT 1637
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1638 LQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARR 1717
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1718 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEA 1797
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1798 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1877
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2124423184 1878 AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1926
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1720-1936 |
1.33e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.87 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1799
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1800 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEASRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1875
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423184 1876 VLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1936
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1416-1836 |
1.51e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 74.39 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1416 QLAEAHAQAKAQAEQEAQELQRRMQEEVARreeaavdaqQQKRSIQEELQHLRQSSEAEiqaKARQVEA-------AERS 1488
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLR---------QEKEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1489 RLRIEEEIRVVRLQLEttERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDETQRKRQaEAELAVRVK-AEA 1567
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1568 EAAREKQRALQALEEFRLQAEEA-ERRLRQAEAERARqvqvaletaqrsaevELQSKRASFAEKTAQLERTLQEEhvava 1646
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1647 qlreeaerraqqqaEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAqaeaekqkeeaerearrrgkaEEQav 1726
Cdd:pfam17380 470 --------------EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI---------------------EEE-- 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1727 RQRELAEQELEkQRQLAEGTAQQRLAAEQElirlraeteqgeQQRQLLEEELARLQHEAAAATQKRQELEAelakvraeM 1806
Cdd:pfam17380 513 RKRKLLEKEME-ERQKAIYEEERRREAEEE------------RRKQQEMEERRRIQEQMRKATEERSRLEA--------M 571
|
410 420 430
....*....|....*....|....*....|
gi 2124423184 1807 EvllaskaRAEEESRSTSEKSKQRLEAEAS 1836
Cdd:pfam17380 572 E-------REREMMRQIVESEKARAEYEAT 594
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1166-1648 |
1.66e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1166 ELEATKAALKKLRAQAEAQQPM------FDALRDELRGAQEVGERLQQRHGERdvEVERWRERVAQLLERWQAVLAQTDL 1239
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1240 RQRELEQLGRQLRyyresadplgawlqDAKRRQEQIqamvladsravreQLRQEKALLEEIERHGEKVEECQRFAKQYIN 1319
Cdd:COG4913 314 LEARLDALREELD--------------ELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1320 AIKDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSELT------------------TLTSQYIKF- 1378
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDLRrelreleaeiaslerrksNIPARLLALr 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1379 --ISETLRRMEEEER-LAE--QQRAEERERLAAVEAALEKQRQ--LAEAHAQAKAQAEQEAQELQRRMQ-EEVARREEAA 1450
Cdd:COG4913 447 daLAEALGLDEAELPfVGEliEVRPEEERWRGAIERVLGGFALtlLVPPEHYAAALRWVNRLHLRGRLVyERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1451 VDAQQQKRSIQEEL------------QHLRQS-------SEAEIQAKARQVEAA-----ERSRLRIEEEIRVVRL----- 1501
Cdd:COG4913 527 ERPRLDPDSLAGKLdfkphpfrawleAELGRRfdyvcvdSPEELRRHPRAITRAgqvkgNGTRHEKDDRRRIRSRyvlgf 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1502 ----QLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR--QVQDETQRKRQAEAELAvRVKAEAEAAREKQR 1575
Cdd:COG4913 607 dnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIA-ELEAELERLDASSD 685
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1576 ALQALEEfrlQAEEAERRLRQAEAERArqvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1648
Cdd:COG4913 686 DLAALEE---QLEELEAELEELEEELD-----ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1720-2520 |
1.90e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQELEKQRQLAEGTAQ-QRLAAEQELIR-----LRAETEQGEQQRQLLEEELARLQHEAAAATQKR- 1792
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQlASLEEELEKLTeeiseLEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKi 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1793 QELEAELAKVRAEMEVLLASKARAEEESRST-SEKSKQRLEAEASRfRELAEEAARLRALAEEAKRQRQlaEEDAARQRA 1871
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLeAEIDKLLAEIEELE-REIEEERKRRDKLTEEYAELKE--ELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1872 EAErvlAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrRRLEEQAAQHKADI---EERLAQLRKASES-- 1946
Cdd:TIGR02169 374 EEV---DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELADLNAAIagiEAKINELEEEKEDka 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1947 -ELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRirsnAEDTLRSKEQAELEAMRQRQLAAEEEQRr 2025
Cdd:TIGR02169 448 lEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE----AEAQARASEERVRGGRAVEEVLKASIQG- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2026 reaeerVQKSLAAEEEAARQRKAALEEV--ERLKAKVEE----ARRLRERAEQESARQL------QLAQDAAQKRLQAEE 2093
Cdd:TIGR02169 523 ------VHGTVAQLGSVGERYATAIEVAagNRLNNVVVEddavAKEAIELLKRRKAGRAtflplnKMRDERRDLSILSED 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2094 KAHAFAV-----QQKEQELQQTLQQEQSMLER---------------LRGEAEAARRAAEEAEEARERAEREAAQSRRQV 2153
Cdd:TIGR02169 597 GVIGFAVdlvefDPKYEPAFKYVFGDTLVVEDieaarrlmgkyrmvtLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2154 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2233
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2234 RLQLEETDHQKSILDEELQRLKAEVteAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEaE 2313
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE-K 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2314 KMKHvaEEAARLSVAAQEAARLRELaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKE 2393
Cdd:TIGR02169 834 EIQE--LQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKERDELEAQLRELERKIE 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2394 QMAQQLEQEtqgfqrtleaeRQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQrfrkqAEEIGEKLHRTELATQEKVtlv 2473
Cdd:TIGR02169 907 ELEAQIEKK-----------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-----EELSLEDVQAELQRVEEEI--- 967
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 2124423184 2474 QTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2520
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
88-189 |
1.95e-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: 66.88 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 88 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 160
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHFQIS 189
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1468-2102 |
2.16e-12 |
|
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: 74.10 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1468 RQSSEAEIQAKARQVEA--AERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1541
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1542 RRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVeLQ 1621
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1622 SKRASFAEKTAQLERTLQEEHVA-VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1700
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1701 QAEAEKQKEEAEREARRRGKAEEQAV-RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEelA 1779
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLENFDERIeRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE--L 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1780 RLQHEAAAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE 1853
Cdd:pfam12128 526 ELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1854 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 1933
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1934 EERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILA-LKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAM 2012
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAyWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2013 RQRQLAAEEEQRRREAEERVQKSLaaeEEAARQRKAALE-----------EVERLKAKVEEARRLRERAEQESARQlqlA 2081
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKI---ERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARL---I 834
|
650 660
....*....|....*....|.
gi 2124423184 2082 QDAAQKRLQAEEKAHAFAVQQ 2102
Cdd:pfam12128 835 ADTKLRRAKLEMERKASEKQQ 855
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3430-3468 |
2.21e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.89 E-value: 2.21e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 3430 LLEAQAATGFLVDPVRNQRLYVHEAVKAGIVGPELHEKL 3468
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
203-302 |
2.32e-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: 66.21 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 203 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 278
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 2124423184 279 DPEDVdVPQPDEKSIITYVSSLYD 302
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
203-303 |
2.93e-12 |
|
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: 65.84 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 203 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 282
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 2124423184 283 VdVPQPDEKSIITYVSSLYDA 303
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1147-1553 |
3.18e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1147 LKAHEEQLKEAQAvpatlpELEATKAALKKLRAQaeaqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQL 1226
Cdd:TIGR02168 679 IEELEEKIEELEE------KIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1227 LERWqavlaqtDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEK 1306
Cdd:TIGR02168 746 EERI-------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1307 VEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpkvqsgsesviqeyvdlrtRYSELTTLTSQYIKFISETLRRM 1386
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIE---------------------------ELSEDIESLAAEIEELEELIEEL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1387 EEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1466
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1467 LRQSSEAEIQAKARQVEAAERSRLRIEEEI-RVVRLQLEtterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1545
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENKIkELGPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLEEAI 1023
|
410
....*....|
gi 2124423184 1546 Q--DETQRKR 1553
Cdd:TIGR02168 1024 EeiDREARER 1033
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1447-2069 |
3.76e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1447 EEAAVDAQQQKRSIQEELQHLRQ--SSEAEIQakaRQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARA 1524
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKfiKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1525 EEAEAQKRQAQEEAERLR------RQVQDETQRKRQAEAELAVRVKaEAEAAREKQRALQALEEFRLQAEEAERRLRQAE 1598
Cdd:PRK03918 238 EEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1599 AERARQVQVALETAQrsaevELQSKRASFAEKTAQLERTLQEehvavaqlreeaerraqqqaeaerareeaERELERWQL 1678
Cdd:PRK03918 317 SRLEEEINGIEERIK-----ELEEKEERLEELKKKLKELEKR-----------------------------LEELEERHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1679 KANEALRLRLQAEEVaqqkslaqaeaekqkeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTAQQRLAAEQELI 1758
Cdd:PRK03918 363 LYEEAKAKKEELERL----------------------------------KKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1759 RLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE-----LAKVRAEMEVLLASKARAEEESRSTsEKSKQRLE- 1832
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKL-RKELRELEk 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1833 --AEASRFRELAEEAARLRALAEEAKrqrQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIA---LKEKEAENER 1907
Cdd:PRK03918 488 vlKKESELIKLKELAEQLKELEEKLK---KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1908 LRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA---------SESELERQKGLVEDTLRQRRQVEEEILALKVSFEK 1978
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1979 AaagKAELElELGRIRSnaEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA 2058
Cdd:PRK03918 645 L---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
650
....*....|.
gi 2124423184 2059 KVEEARRLRER 2069
Cdd:PRK03918 719 ALERVEELREK 729
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4353-4391 |
5.26e-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: 5.26e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 4353 LLEAQACTGGIIDPNTGERFPVTDAVNKGLVDKIMVDRI 4391
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
203-298 |
5.64e-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: 65.10 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 203 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 281
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 2124423184 282 DVDVPQPDEKSIITYVS 298
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3175-3213 |
6.46e-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: 6.46e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 3175 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETSKAL 3213
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1355-1853 |
6.95e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.68 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1355 IQEYVDLRTRYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEahaqakaqaeqeaqE 1434
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLV--------------E 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1435 LQRRMQEEVARREEAAVDAQQQKrsiqeelQHLRQSSEAEIQAKA--RQVEAAERSRLRIEEEIRVVRLQLEtterqrgg 1512
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAAS-------DHLNLVQTALRQQEKieRYQADLEELEERLEEQNEVVEEADE-------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1513 aegelqalraRAEEAEAQKRQAQEEAERLRRQVQD-----ETQRKRQAEAELAVRVKAEAE-----AAREKQRALQALEE 1582
Cdd:PRK04863 377 ----------QQEENEARAEAAEEEVDELKSQLADyqqalDVQQTRAIQYQQAVQALERAKqlcglPDLTADNAEDWLEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1583 FRLQAEEA-------ERRLRQAEAERaRQVQVALETAQR-SAEVElqskRASFAEKTAQLERTLQEEHVAVAQLreeaer 1654
Cdd:PRK04863 447 FQAKEQEAteellslEQKLSVAQAAH-SQFEQAYQLVRKiAGEVS----RSEAWDVARELLRRLREQRHLAEQL------ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1655 raqqqaeaeRAREEAERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQ 1734
Cdd:PRK04863 516 ---------QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD---------------------DEDELEQLQEELEA 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1735 ELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQHEAAAATQKRQELEAELAKvraemevlLA 1811
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------LL 637
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2124423184 1812 SKARAEEESRSTSEKSKQRLEAEASRFREL-AEEAARLRALAE 1853
Cdd:PRK04863 638 ERERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1728-2610 |
7.23e-12 |
|
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: 72.52 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1728 QRELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAe 1805
Cdd:pfam01576 109 EEQLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1806 MEVLLASKARAEEESRSTSEKSKQRLEAEASrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIG 1885
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1886 EATRLktEAEIALKEKEAENERLRRLAEDEafQRRRLEEQ---------------AAQH--KADIEERLAQLRKASESEL 1948
Cdd:pfam01576 265 KIREL--EAQISELQEDLESERAARNKAEK--QRRDLGEElealkteledtldttAAQQelRSKREQEVTELKKALEEET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1949 ERQKGLVEDTLRQRRQVEEEilaLKVSFEKAAAGKAELE---LELGRIRSNAEDTLRSKEQAELEAMRQRQlaaeeeqrr 2025
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQALEE---LTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQAKQDSEHKRK--------- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2026 rEAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR----------QLQLAQDAAQkrlqaEEKA 2095
Cdd:pfam01576 409 -KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesQLQDTQELLQ-----EETR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2096 HAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAE----RLKQSAEEQAQAQA 2171
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEegkkRLQRELEALTQQLE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2172 QAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKF--------------AEQTLRQKAQVEQELT---TLR 2234
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFdqmlaeekaisaryAEERDRAEAEAREKETralSLA 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2235 LQLEETDHQKSILDEELQRLKAE--------------VTEAARQRSQVEEELFSLRVQMEELG-------KLKARIEAEN 2293
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEmedlvsskddvgknVHELERSKRALEQQVEEMKTQLEELEdelqateDAKLRLEVNM 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2294 RALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELA-------EEDLAQQRALAEKMLKEKMQAVQEATR 2366
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKK 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2367 LKAEAELLQQQKE---LAQEQARRLQEDKEQMAQQLEQETQGFQRTLEA----ERQRQLE-----------------MSA 2422
Cdd:pfam01576 803 LQAQMKDLQRELEearASRDEILAQSKESEKKLKNLEAELLQLQEDLAAseraRRQAQQErdeladeiasgasgksaLQD 882
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2423 EAERLKLRVA----EMSRAQARAEEDAQRFRKQAEEIgEKLHrTELATQEkvTLVQTLEIQRQQSDHDAERLRQAIAELE 2498
Cdd:pfam01576 883 EKRRLEARIAqleeELEEEQSNTELLNDRLRKSTLQV-EQLT-TELAAER--STSQKSESARQQLERQNKELKAKLQEME 958
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2499 RE-KEKLKQ-----EAKLLQLksEEMQTVQQEQLLQETQALQQSFLSEKDTLLQrerfIEQEKAKLEQlFQDEVAKAQkl 2572
Cdd:pfam01576 959 GTvKSKFKSsiaalEAKIAQL--EEQLEQESRERQAANKLVRRTEKKLKEVLLQ----VEDERRHADQ-YKDQAEKGN-- 1029
|
970 980 990
....*....|....*....|....*....|....*...
gi 2124423184 2573 reeqqrqqkqmeEEKQQLVASMEEARQRQREAEEGVRR 2610
Cdd:pfam01576 1030 ------------SRMKQLKRQLEEAEEEASRANAARRK 1055
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1391-1853 |
7.25e-12 |
|
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: 72.29 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1391 RLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEqEAQELQRRmQEEVARREEAAVDaqqqkrsiqeelqHLrqs 1470
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMAR-ELEELSAR-ESDLEQDYQAASD-------------HL--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1471 seAEIQAKARQVEAAERSRLRIEEeirvVRLQLETTERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQD--- 1547
Cdd:COG3096 337 --NLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLADyqq 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1548 --ETQRKRQAEAELAVRVKAEAEAAREK-----QRALQALEEFRLQAEEAERRLRQAE------AERARQVQVALETAQR 1614
Cdd:COG3096 404 alDVQQTRAIQYQQAVQALEKARALCGLpdltpENAEDYLAAFRAKEQQATEEVLELEqklsvaDAARRQFEKAYELVCK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1615 -SAEVElqskRASFAEKTAQLERTLQeEHVAVAQlreeaerraqqqaeaerareeaerELERWQLKANEA-LRLRLQAEE 1692
Cdd:COG3096 484 iAGEVE----RSQAWQTARELLRRYR-SQQALAQ------------------------RLQQLRAQLAELeQRLRQQQNA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1693 VAQQKSLaqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1772
Cdd:COG3096 535 ERLLEEF-------------------CQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1773 LLEEElARLQHEAAAATQKRQELEAE----LAKVRAEMEVLLaSKARAEEESRSTSEKSKQRLEAEASRFRELA-EEAAR 1847
Cdd:COG3096 596 ELAAR-APAWLAAQDALERLREQSGEaladSQEVTAAMQQLL-EREREATVERDELAARKQALESQIERLSQPGgAEDPR 673
|
....*.
gi 2124423184 1848 LRALAE 1853
Cdd:COG3096 674 LLALAE 679
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4008-4046 |
9.46e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 9.46e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 4008 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4046
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3841-3879 |
9.46e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 9.46e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 3841 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3879
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2771-2809 |
1.03e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.03e-11
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 2771 LLEAQAASGFLLDPVQNRRLTVNEAVKEGVVGPELHHKL 2809
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1141-1638 |
1.31e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1141 HGAEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELrgAQEVGERLQQRHGERDVEVERWR 1220
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1221 ERVAQLLERWQAVLAQtdLRQ---RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALL 1297
Cdd:COG4913 316 ARLDALREELDELEAQ--IRGnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1298 EEIERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIK 1377
Cdd:COG4913 394 EALEEELEALEEALAEAEA---ALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELP 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1378 FISETLRRMEEEERLaeqQRAEER-------------ERLAAVEAALEKQR-------QLAEAHAQAKAQAEQEAQELQR 1437
Cdd:COG4913 462 FVGELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAG 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1438 RM-----------QEEVARREEAA-VDAQQQ----KRSIQEELQ--------------HLRQ------SSEAEIQAKARQ 1481
Cdd:COG4913 539 KLdfkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRSryvlgfDNRAKLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1482 VEAAERSRLRIEEEIRVVRLQLETTERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDET 1549
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELE 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1550 QRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEVELQSKRASF 1627
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDAL 778
|
570
....*....|.
gi 2124423184 1628 AEKTAQLERTL 1638
Cdd:COG4913 779 RARLNRAEEEL 789
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1720-2017 |
2.21e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.54 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQ-RELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRqllEEELARLQHEAAAATQKR---QEL 1795
Cdd:pfam17380 295 KMEQERLRQeKEEKAREVERRRKLEE-AEKARQAEMDRQAAIYAEQERMAMER---ERELERIRQEERKRELERirqEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1796 EAELAKVRaEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAE---EAARLRALAEEAkRQRQLAEEDAARQRaE 1872
Cdd:pfam17380 371 AMEISRMR-ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-RQREVRRLEEERAR-E 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1873 AERVLAEKLAAIGEATRLKteaeialkEKEAENERLRRLAEDEAFQRRRLEEQ---------AAQHKADIEERlaQLRKA 1943
Cdd:pfam17380 448 MERVRLEEQERQQQVERLR--------QQEEERKRKKLELEKEKRDRKRAEEQrrkilekelEERKQAMIEEE--RKRKL 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1944 SESELE-RQKGLVEDtlRQRRQVEEEilalkvsfekaaaGKAELELElGRIRSNAEDTLRSKEQAELEAM-RQRQL 2017
Cdd:pfam17380 518 LEKEMEeRQKAIYEE--ERRREAEEE-------------RRKQQEME-ERRRIQEQMRKATEERSRLEAMeREREM 577
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1577-2093 |
2.30e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1577 LQALEEFRLQAEEAE---RRLRQAEAERARQVQVALETAQRSAEVE-LQSKRASFAEKTAQLERTLQEEHVAVAQLREEA 1652
Cdd:PRK02224 161 LGKLEEYRERASDARlgvERVLSDQRGSLDQLKAQIEEKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1653 ERRAQQQAEAERAREEAEReLERWQLKANEALRLRLQ-AEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1731
Cdd:PRK02224 241 EVLEEHEERREELETLEAE-IEDLRETIAETEREREElAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1732 AEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLA 1811
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1812 SKARAEEEsRSTSEKSKQRLEAEASRFRE-LAEEAARLRALAEEAKRQRQLAEE----DAARQRAEAERV--LAEKLAAI 1884
Cdd:PRK02224 399 RFGDAPVD-LGNAEDFLEELREERDELRErEAELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1885 GEATRLKTEAEIALKEKEAENERLRRLAEDEAF------QRRRLEEQAAQHKADIEE---RLAQLRKAS---ESELERQK 1952
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDRierleeRREDLEELIAERRETIEEkreRAEELRERAaelEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1953 glvEDTLRQRRQVEEEILALKVSFEKAAAGKAELElELGRIRS------NAEDTL-----RSKEQAELEAMRQRQLaaee 2021
Cdd:PRK02224 558 ---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTllaaiaDAEDEIerlreKREALAELNDERRERL---- 629
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 2022 eqrrreaeervqkslaaeeEAARQRKAALEEvERLKAKVEEARRLRERAEQ------ESARQLQLAQDAAQKRLQAEE 2093
Cdd:PRK02224 630 -------------------AEKRERKRELEA-EFDEARIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVE 687
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1400-1884 |
2.60e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 70.76 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1400 ERERLAAVEAALEKQRQLAEAHAQAKAQaeqeaQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRqssEAEIQAKA 1479
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAE-----QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQ---TALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1480 --RQVEAAERSRLRIEEEIRVVRLQLEtterqrggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRkrqaea 1557
Cdd:PRK04863 350 ieRYQADLEELEERLEEQNEVVEEADE------------------QQEENEARAEAAEEEVDELKSQLADYQQA------ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1558 elavrVKAEAEAAREKQRALQALEEFR-------LQAEEAERRLRQAEAERARQVQVALETAQRsaeVELQSKRASFAEK 1630
Cdd:PRK04863 406 -----LDVQQTRAIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAAHSQFEQ 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1631 TAQLERTLQEEHVAvaqlreeaerraqqqaeaerareeaerelERWQLKANEALR----LRLQAEEVAQQKslaqaeaek 1706
Cdd:PRK04863 478 AYQLVRKIAGEVSR-----------------------------SEAWDVARELLRrlreQRHLAEQLQQLR--------- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1707 qkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgeqQRQLLEEELARLQHEAA 1786
Cdd:PRK04863 520 --------------MRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA---RLESLSESVSEARERRM 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1787 AATQKRQELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAK 1856
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAARAPAWLAAQDALArlreqsgeefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
490 500
....*....|....*....|....*...
gi 2124423184 1857 RQRQLAEEDAARQRAEAERVLAEKLAAI 1884
Cdd:PRK04863 663 RLSQPGGSEDPRLNALAERFGGVLLSEI 690
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1515-2093 |
2.91e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1515 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEA--ER 1592
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1593 RLRQAEAERARQVQVALETA---QRSAEVELQSKRASFAEKTAQLERTLQEehvavaqlreeaerraqqqAEAERAREEA 1669
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------------------LEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1670 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE--REARRRGKAEEQAVRQRELA---EQELEKQRQLAE 1744
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAaelESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1745 GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVR---AEMEVLLA---------- 1811
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqp 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1812 ----SKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAE--EDAARQRAEAERVLAEKLAAIG 1885
Cdd:PRK02224 461 vegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1886 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---------ERLAQLRKASESELERQKGLVE 1956
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1957 ------DTLRQRRqveEEILALKVSFEKAAAGKAELElelgriRSNAEDTLRSKEQaELEAMRQRQlaaeeeqrrreaeE 2030
Cdd:PRK02224 621 lnderrERLAEKR---ERKRELEAEFDEARIEEARED------KERAEEYLEQVEE-KLDELREER-------------D 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 2031 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2093
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1059-1644 |
3.32e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 70.37 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1059 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKL-EQVRSLSAIYLEklktislv 1136
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLsESVSEARERRMA-------- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1137 irsthgaeevLKAHEEQLK-EAQAVPATLPELEATKAALKKLRAQAEaqqpmfdalrDELRGAQEVGERLQQrHGERDVE 1215
Cdd:PRK04863 584 ----------LRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSG----------EEFEDSQDVTEYMQQ-LLERERE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1216 VERWRERVAqllERWQAVLAQTD-LRQRELEQLGRQLRYyresADPLGAWL----------QDA----KRRQEQIQAMVL 1280
Cdd:PRK04863 643 LTVERDELA---ARKQALDEEIErLSQPGGSEDPRLNAL----AERFGGVLlseiyddvslEDApyfsALYGPARHAIVV 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1281 ADSRAVREQLRQEKALLEEI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK----VQS 1349
Cdd:PRK04863 716 PDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRA 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1350 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETL----------------RRMEEEERLAEQQRAEERERLAAVEAALEK 1413
Cdd:PRK04863 794 EREELAERYATLSFDVQKLQRLHQAFSRFIGSHLavafeadpeaelrqlnRRRVELERALADHESQEQQQRSQLEQAKEG 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1414 QRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ--EELQHLRQSSEAEIQAKARQVEAAE----- 1486
Cdd:PRK04863 874 LSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqrd 953
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1487 -RSRLRIEEEIRVVRLQLETTERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDETQRKRQAEAELavrv 1563
Cdd:PRK04863 954 aKQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL---- 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1564 KAEAEAAREK-QRALQALEEFRLQA-EEAERRLRQAEAE------RARQVQVALETAQRSAEVELQS--KRASFAEKTAQ 1633
Cdd:PRK04863 1026 KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDYH 1105
|
650
....*....|.
gi 2124423184 1634 LERTLQEEHVA 1644
Cdd:PRK04863 1106 EMREQVVNAKA 1116
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1824-2661 |
3.39e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.10 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1824 SEKSKQRLEAEASRFRElaeeaARLRALAEEAKRQRQLAEEDaaRQRAEAERVLAEKLAAIgEATRLKTEAEIALKEK-- 1901
Cdd:TIGR02169 170 RKKEKALEELEEVEENI-----ERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKea 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1902 -EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAA 1980
Cdd:TIGR02169 242 iERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1981 AGKAELELELGRIRSNAEDtlrSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQR---KAALEEVERLK 2057
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2058 AKVEE----ARRLRERAEQESARQLQLAQDAA-----QKRLQAEEKAHAFAVQQKEQElqqtlqqeqsmLERLRGEAEAA 2128
Cdd:TIGR02169 399 REINElkreLDRLQEELQRLSEELADLNAAIAgieakINELEEEKEDKALEIKKQEWK-----------LEQLAADLSKY 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2129 RRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAqaqaqaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAE 2208
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV--------------------------------RGGRAVEEV 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2209 MEKHKKFAEQTLRQKAQVEQELTTL-------RLQL----EETDHQKSIldEELQRLKA-EVTEAARQRSQVEEELFSLR 2276
Cdd:TIGR02169 516 LKASIQGVHGTVAQLGSVGERYATAievaagnRLNNvvveDDAVAKEAI--ELLKRRKAgRATFLPLNKMRDERRDLSIL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2277 VQMEELGKLKARIEAENR-----------ALILRDKDNTQRV------------LQEEAEKMKHVAEEAARL-SVAAQEA 2332
Cdd:TIGR02169 594 SEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARRLmgkyrmvtlegeLFEKSGAMTGGSRAPRGGiLFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2333 ARLRELAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQET 2403
Cdd:TIGR02169 674 AELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2404 QGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQS 2483
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2484 DHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQalqqsfLSEKDTLLQRERF-IEQEKAKLEQLF 2562
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD------LESRLGDLKKERDeLEAQLRELERKI 905
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2563 QDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEgvrrkqeelqlleqqrQQQEKLLAEENQRLRERLQR 2642
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE----------------ELSLEDVQAELQRVEEEIRA 969
|
890
....*....|....*....
gi 2124423184 2643 LEEEHRAALAHSEEIAASQ 2661
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRL 988
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2217-2703 |
4.14e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2217 EQTLRQKAQVEQE--LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEElfslRVQMEELGKlkaRIEAENR 2294
Cdd:PTZ00121 1057 EGKAEAKAHVGQDegLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE----ARKAEEAKK---KAEDARK 1129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2295 ALILRDKDNTQRVlqEEAEKmkhvAEEAARLSVA--AQEAARLRELAEEDLAQQRALAEKMLK-EKMQAVQEATRLKAEA 2371
Cdd:PTZ00121 1130 AEEARKAEDARKA--EEARK----AEDAKRVEIArkAEDARKAEEARKAEDAKKAEAARKAEEvRKAEELRKAEDARKAE 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2372 ELLQQQKELAQEQARRLQEDKE-QMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfRK 2450
Cdd:PTZ00121 1204 AARKAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-----AR 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2451 QAEEIG---EKLHRTELATQEKVTLVQTLEIQrqqsdhdAERLRQAiAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLL 2527
Cdd:PTZ00121 1279 KADELKkaeEKKKADEAKKAEEKKKADEAKKK-------AEEAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2528 QETQALQQSFLSEKDTLLQRERfIEQEKAKLEQLFQ--DEVAKAQKLREEQQRQQKQMEEEKQQlVASMEEARQRQREAE 2605
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAE 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2606 EGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRA--ALAHSEEIAASQATAVKALPNGRDAPDGPATEAE 2683
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500
....*....|....*....|
gi 2124423184 2684 PEHAfDGLRQKVPAQRLQEV 2703
Cdd:PTZ00121 1509 KKKA-DEAKKAEEAKKADEA 1527
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1374-2085 |
4.56e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 69.76 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1374 QYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDA 1453
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1454 QQQKRSIQEELQHLRQ---SSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLetteRQRGGA--------EGELQALR 1521
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHF----RSLGSAiskilrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1522 AR----AEEAEAQKRQAQEEAERLRRQVQDetqRKRQAEAELAVRVKA---EAEAAREKQRALQAleefrlQAEEAERRL 1594
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEVEITGlteKASSARSQANSIQS------QLEIIQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1595 RQAEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQeehVAVAQLREEAERRAQQQAEAERAREEAERELE 1674
Cdd:pfam15921 309 RNQNSMYMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLV---LANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1675 RWQLKANEalrLRLQAEevaQQKSLaqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EG 1745
Cdd:pfam15921 385 DLHKREKE---LSLEKE---QNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1746 TAQQRLAAEQ----ELIRLRAETEQGEQQRQLLEEELARLqheaaaaTQKRQELEAELAKVrAEMEVLLASKARAEEESR 1821
Cdd:pfam15921 445 QMERQMAAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1822 STSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLAEKLAAIGEATRL-KTEAE 1895
Cdd:pfam15921 517 AEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLE 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1896 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASESELERQKGL--VEDTLRQRRQVEEEI 1969
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDY 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1970 LALKVSF----EKAAAGKAELELELGRIRSNAE---DTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 2042
Cdd:pfam15921 677 EVLKRNFrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEA 756
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2043 ---ARQRKAALEE-------------VERLKAKVE-EARRLRERAEQESARQLQLAQDAA 2085
Cdd:pfam15921 757 mtnANKEKHFLKEeknklsqelstvaTEKNKMAGElEVLRSQERRLKEKVANMEVALDKA 816
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1398-1884 |
5.15e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.60 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1398 AEERERLaaVEAALEKQRQLAEAHAQaKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKrsiqeelQHLrqsseAEIQA 1477
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQ-LAEEQYRLVEMARELEELSARESDLEQDYQAAS-------DHL-----NLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1478 KARQVEAAERSRLRIEEeirvVRLQLETTERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDetqrKRQAEA 1557
Cdd:COG3096 342 ALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQALD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1558 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVElqskrasfaEKTAQLERT 1637
Cdd:COG3096 407 VQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---------AARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1638 LQeehvAVAQLREEAERRaqqqaeaerareeaerelERWQlKANEALR----LRLQAEEVAQQKSlaqaeaekqkeeaer 1713
Cdd:COG3096 478 YE----LVCKIAGEVERS------------------QAWQ-TARELLRryrsQQALAQRLQQLRA--------------- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1714 earRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQ 1793
Cdd:COG3096 520 ---QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1794 ELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAE 1863
Cdd:COG3096 589 QLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGG 668
|
490 500
....*....|....*....|.
gi 2124423184 1864 EDAARQRAEAERVLAEKLAAI 1884
Cdd:COG3096 669 AEDPRLLALAERLGGVLLSEI 689
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1557-2093 |
5.49e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 69.50 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1557 AELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAE-RARQVQVALETAQRSAEVELQSKRAS--------- 1626
Cdd:COG3899 712 ARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppas 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1627 -FAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAE 1705
Cdd:COG3899 792 aRAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1706 KQKEEAEREARRrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEA 1785
Cdd:COG3899 872 ALAAAAAAAAAA---AALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAA 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1786 AAATQKRQELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEED 1865
Cdd:COG3899 949 AAAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAAL 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1866 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASE 1945
Cdd:COG3899 1016 AAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1946 SELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRR 2025
Cdd:COG3899 1096 ALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAAL 1175
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 2026 REAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2093
Cdd:COG3899 1176 AALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1196-1561 |
6.04e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.60 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1196 RGAQEvgERLQQRHGERDVEVERWR---------ERVAQLLERW-------------QAVLAQTDLRQRELEqlgRQLRY 1253
Cdd:COG3096 780 RAARE--KRLEELRAERDELAEQYAkasfdvqklQRLHQAFSQFvgghlavafapdpEAELAALRQRRSELE---RELAQ 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1254 YRESADPLGAWLQDAKRRQEQI-----QAMVLADsravrEQLRQekaLLEEIERHGEKVEECQRFAKQYINAIkdyelql 1328
Cdd:COG3096 855 HRAQEQQLRQQLDQLKEQLQLLnkllpQANLLAD-----ETLAD---RLEELREELDAAQEAQAFIQQHGKAL------- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1329 vtykAQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltSQYIKFISETLRRM------EEEERLAEQQRAEE-- 1400
Cdd:COG3096 920 ----AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRL----KQQIFALSEVVQRRphfsyeDAVGLLGENSDLNEkl 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1401 RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEevarreeaavdAQQQKRSIQEELQHLrqsseaEIQAKAR 1480
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL------GVQADAE 1052
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1481 QVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDETQRKR 1553
Cdd:COG3096 1053 AEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERR 1132
|
....*...
gi 2124423184 1554 QAEAELAV 1561
Cdd:COG3096 1133 LHRRELAY 1140
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1385-2508 |
6.32e-11 |
|
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: 69.43 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1385 RMEEEERLAEQQRAEERERLAAVEAAL----EKQRQLAEAHA--QAKAQAEQE---------------AQELQRRMQEEV 1443
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNalQEQLQAETElcaeaeemrarlaarKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1444 AR---REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR-QVE--AAERSRLRIEEEIRVVrlqlettERQRGGAEGEL 1517
Cdd:pfam01576 82 SRleeEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKlQLEkvTTEAKIKKLEEDILLL-------EDQNSKLSKER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1518 QALRARAEEAEAQKRQAQEEAERLrrqvqdeTQRKRQAEA---ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRL 1594
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSL-------SKLKNKHEAmisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1595 RQAEAERARQVQvaletaqrSAEVELQSKRASFAEKTAQ---LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAER 1671
Cdd:pfam01576 228 QAQIAELRAQLA--------KKEEELQAALARLEEETAQknnALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1672 ELerwqlkanEALRLRLQ--AEEVAQQKSLAQAEAEKQKEEAerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1749
Cdd:pfam01576 300 EL--------EALKTELEdtLDTTAAQQELRSKREQEVTELK--------KALEEETRSHEAQLQEMRQKHTQALEELTE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1750 RLaaeQELIRLRAETEQGeqqRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLAskaraeeesrSTSEKSKQ 1829
Cdd:pfam01576 364 QL---EQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQA----------RLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1830 RLEAeASRFRELAEEAARLRALAEEAKRQRQLAEEDAarqrAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLR 1909
Cdd:pfam01576 428 RAEL-AEKLSKLQSELESVSSLLNEAEGKNIKLSKDV----SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1910 RLAEDEAFQRRRLEEQAAQHKAdieeRLAQLRKASESELERQKGLVEDtlrqRRQVEEEILALKVSFEKAAAGKAELELE 1989
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQA----QLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1990 LGRIRSNAEDTLrskeqaeLEAMRQRQLAAEEEQRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRER 2069
Cdd:pfam01576 575 KNRLQQELDDLL-------VDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2070 AEQESARQLQLAQDAAQKRLQAEekahafavqqkeqelqqtlqqeqsmLERLRGEAEAARRAAEEAEEARERAEREAAQS 2149
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEM 697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2150 RRQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKKfaeQTLRQKAQVEQE 2229
Cdd:pfam01576 698 KTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQVRELEAE 757
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2230 LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQ 2309
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKN 837
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2310 EEAEKMKHVAEEAARLSVAAQEAARLRELAEEdLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQ 2389
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERDELADE-IASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKST 916
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2390 EDKEQMAQQLEQETQGFQRTLEA----ERQ------RQLEMSAEAE-RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEK 2458
Cdd:pfam01576 917 LQVEQLTTELAAERSTSQKSESArqqlERQnkelkaKLQEMEGTVKsKFKSSIAALEAKIAQLEEQLEQESRERQAANKL 996
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2459 LHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEA 2508
Cdd:pfam01576 997 VRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1167-1874 |
6.73e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.21 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1167 LEATKAALKKLRAQAEaqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWRERV----AQLLERWQAVLAQT----D 1238
Cdd:COG3096 340 QTALRQQEKIERYQED-----LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslkSQLADYQQALDVQQtraiQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1239 LRQ--RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMV------LADSRAVREQLRQEKALLEEIERHGEKVEEC 1310
Cdd:COG3096 415 YQQavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVleleqkLSVADAARRQFEKAYELVCKIAGEVERSQAW 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1311 QRfAKQYINAIKDYELQLvtykAQLEPVAspakkpkvqsgsesviQEYVDLRTRYS---ELTTLTSQYIKFISETLRRME 1387
Cdd:COG3096 495 QT-ARELLRRYRSQQALA----QRLQQLR----------------AQLAELEQRLRqqqNAERLLEEFCQRIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1388 EEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQ---------EAQELQRRMQEEVArreEAAVDAQQQKR 1458
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlAAQDALERLREQSG---EALADSQEVTA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1459 SIQEELQHLRQSSEAEIQAKARqveaaersRLRIEEEIRvvRLQletterQRGGAE-GELQALRAR-------------- 1523
Cdd:COG3096 631 AMQQLLEREREATVERDELAAR--------KQALESQIE--RLS------QPGGAEdPRLLALAERlggvllseiyddvt 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1524 ---AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DETQRKRQaEAELAVRVKAE---------- 1566
Cdd:COG3096 695 ledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVFDAE-ELEDAVVVKLSdrqwrysrfp 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1567 -----AEAAREKQralqaLEEFRLQAEE-----AERRLRQAEAER---------ARQVQVALETaqrSAEVELQSKRASF 1627
Cdd:COG3096 774 evplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvGGHLAVAFAP---DPEAELAALRQRR 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1628 AEKTAQLERTLQEEHVAVAQLREEAERRA-------QQQAEAERAREEAERELERWQLKANEALR-LRLQAEEVAQ-QKS 1698
Cdd:COG3096 846 SELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELREELDAAQEAQAfIQQHGKALAQlEPL 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1699 LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLAAEQELI-RLRAETEQGEQQRQLLEE 1776
Cdd:COG3096 926 VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQAEEARREARE 1005
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1777 ELARLQHEAAAATQKR--------------QELEAELakvrAEMEVLLAskARAEEESRSTSEKSKQRLEAEASRFRELA 1842
Cdd:COG3096 1006 QLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQEL----EELGVQAD--AEAEERARIRRDELHEELSQNRSRRSQLE 1079
|
810 820 830
....*....|....*....|....*....|..
gi 2124423184 1843 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1874
Cdd:COG3096 1080 KQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
81-180 |
7.95e-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: 62.06 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 81 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 152
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 2124423184 153 RHRQVKLVNIRNDDIADGNPKLTLGLIW 180
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
992-1641 |
1.13e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 992 DRLQAEREYgscSHHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRIAEQQKA 1071
Cdd:TIGR02169 201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1072 QAEVEGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVL 1147
Cdd:TIGR02169 257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1148 KAHEEQLKEAQA-----VPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQE------------------VGER 1204
Cdd:TIGR02169 335 LAEIEELEREIEeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREkleklkreinelkreldrLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1205 LQQRHGER---DVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQ---AM 1278
Cdd:TIGR02169 415 LQRLSEELadlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1279 VLADSRAVREQLRQEKALLEEIERHGEKV-------------------------------------EECQRFAKQY---- 1317
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrlnnvvveddavaKEAIELLKRRkagr 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1318 -----INAIK---------------DYELQLVTYKAQLEPVASPAKKpkvqsgsESVIQEYVDLRTRY------------ 1365
Cdd:TIGR02169 575 atflpLNKMRderrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFG-------DTLVVEDIEAARRLmgkyrmvtlege 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1366 ----SELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAEERErLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRmQ 1440
Cdd:TIGR02169 648 lfekSGAMTGGSRAPRGgILFSRSEPAELQRLRERLEGLKRE-LSSLQSELRRIENRLDELSQELSDASRKIGEIEKE-I 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1441 EEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEE------------IRVVRLQLETTER 1508
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlshsrIPEIQAELSKLEE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1509 QRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK---RQAEAELAVRVKAEAEAAREKQRALQALEEfRL 1585
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiEKEIENLNGKKEELEEELEELEAALRDLES-RL 884
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1586 QAEEAERRLRQAEAERARQVQVALETAQRSAEV---ELQSKRASFAEKTAQLERTLQEE 1641
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKrlsELKAKLEALEEELSEIEDPKGED 943
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2200-2402 |
1.25e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2200 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2279
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2280 EEL----------GKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRAL 2349
Cdd:COG4942 107 AELlralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 2350 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQE 2402
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1449-1648 |
3.30e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1449 AAVDAQQQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAE 1528
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1529 AQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF---------RLQAEEAERRLRQAEA 1599
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparreqaeELRADLAELAALRAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124423184 1600 ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1648
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
87-183 |
3.76e-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: 60.28 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 87 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 152
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 2124423184 153 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 183
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1759-2291 |
4.87e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1759 RLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEASRF 1838
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1839 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKE---AENERLRRLA 1912
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1913 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEILALK-------VSFEKA 1979
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1980 AAGKAELELELGRIRSNA---EDTLRSKEQAELEAMRQRQ----------LAAEEEQRRREAEERVQKSLAAEEEAARQR 2046
Cdd:PRK02224 411 EDFLEELREERDELREREaelEATLRTARERVEEAEALLEagkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2047 KAALEE-VERLKAKVEEARRLRERAEQESArqlqLAQDAAQKRLQAEEKAHAfavqqkeqelqqtlqqeqsmLERLRgea 2125
Cdd:PRK02224 491 VEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEKRER--------------------AEELR--- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2126 eaarRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAA 2205
Cdd:PRK02224 544 ----ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2206 DAEMEKHKKFAEQTLRqKAQVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRSQVEEELFSLRVQME 2280
Cdd:PRK02224 620 ELNDERRERLAEKRER-KRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVENELEELEELRE 698
|
570
....*....|.
gi 2124423184 2281 ELGKLKARIEA 2291
Cdd:PRK02224 699 RREALENRVEA 709
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1059-1644 |
5.11e-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: 66.51 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1059 RECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTLGKL-EQVRSLSAIYLEklktislvi 1137
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL----------EELLAELEAQLEELeEQAAEAVEQRSE--------- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1138 rsthgaeevLKAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQqpmfdalrdeLRGAQEVGERLQQRHgERDVEV 1216
Cdd:COG3096 583 ---------LRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEA----------LADSQEVTAAMQQLL-EREREA 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1217 ERWRERVAQllerwqavlaqtdlRQRELEQLGRQLRYYRESADP--------LGAWL----------QDA----KRRQEQ 1274
Cdd:COG3096 643 TVERDELAA--------------RKQALESQIERLSQPGGAEDPrllalaerLGGVLlseiyddvtlEDApyfsALYGPA 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1275 IQAMVLADSRAVREQLRQEKALLEE---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKP 1345
Cdd:COG3096 709 RHAIVVPDLSAVKEQLAGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1346 KVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAAVEAALEKQRQlAEAHAQAK 1425
Cdd:COG3096 789 ELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQ 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1426 AQAEQEAQELQRRMQEEV---------ARREEAAVD---AQQQKRSIQEELQHLRQSSE--AEIQAKARQVEAAERSRLR 1491
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQ 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1492 IEEEIRVVRLQL----ETTER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDETQrkRQAE 1556
Cdd:COG3096 946 AKEQQRRLKQQIfalsEVVQRrphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ--VLAS 1023
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1557 AELAVRVKAE--AEAARE-KQRALQALEEFRLQAEEaERRLRQAEAERARQVQVALETAQRSAEVELQS--KRASFAEKT 1631
Cdd:COG3096 1024 LKSSRDAKQQtlQELEQElEELGVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSlqKRLRKAERD 1102
|
650
....*....|...
gi 2124423184 1632 AQLERTLQEEHVA 1644
Cdd:COG3096 1103 YKQEREQVVQAKA 1115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1723-2374 |
6.46e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1802
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1803 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1882
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1883 AIGEATRLKTEAEIALKEKEAENERLRRlaedeafQRRRLEeqaaQHKADIEERLAQLRKA-------SESEL------- 1948
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEA-------EIASLE----RRKSNIPARLLALRDAlaealglDEAELpfvgeli 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1949 ------ERQKGLVEDTLRQRRQ---VEEEILA------------LKVSFEKAAAGKAE---------------------- 1985
Cdd:COG4913 468 evrpeeERWRGAIERVLGGFALtllVPPEHYAaalrwvnrlhlrGRLVYERVRTGLPDperprldpdslagkldfkphpf 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1986 ---LELELGR----IRSNAEDTLRSKEQAeleAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA 2058
Cdd:COG4913 548 rawLEAELGRrfdyVCVDSPEELRRHPRA---ITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2059 KVEEARRLRERAEQEsarqlqlaQDAAQKRLQAEEKAHAFAVQQKEQELQQTLqqeqsmLERLRGEAEAARRAAEEAEEA 2138
Cdd:COG4913 625 ELAEAEERLEALEAE--------LDALQERREALQRLAEYSWDEIDVASAERE------IAELEAELERLDASSDDLAAL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2139 RERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQ 2218
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2219 TLRQKAQVEQELTTLRLQLEET-------------DHQKSILD-----EELQRLKAEVTEAARQR------SQVEEELFS 2274
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAmrafnrewpaetaDLDADLESlpeylALLDRLEEDGLPEYEERfkellnENSIEFVAD 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2275 LRVQM-EELGKLKARIEAENRalILRDKD-NTQRVLQEEAEKMKHvaEEAARLSVAAQEAARLRELAEEDLAQQRALAEK 2352
Cdd:COG4913 851 LLSKLrRAIREIKERIDPLND--SLKRIPfGPGRYLRLEARPRPD--PEVREFRQELRAVTSGASLFDEELSEARFAALK 926
|
730 740
....*....|....*....|..
gi 2124423184 2353 MLKEKMQAVQEATRLKAEAELL 2374
Cdd:COG4913 927 RLIERLRSEEEESDRRWRARVL 948
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
78-186 |
6.66e-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: 59.52 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 78 LKDERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDY 151
Cdd:cd21222 7 FDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALEL 86
|
90 100 110
....*....|....*....|....*....|....*
gi 2124423184 152 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 186
Cdd:cd21222 87 MEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1762-2323 |
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 2124423184 1762 AETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEASRFR 1839
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1840 E-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIA-----LKEKEAENERLRRLAE 1913
Cdd:PRK03918 266 ErIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieerIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1914 DEAFQRRRLEEQAAQHKA--DIEERLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEILALKvsfekaaAGKAELE 1987
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKIT-------ARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1988 LELGRIRSNAEDTLRSK-----------EQAELEAMRQRQLAAEEeqrrreaeerVQKSLAAEEEAARQRKAALEEVERL 2056
Cdd:PRK03918 419 KEIKELKKAIEELKKAKgkcpvcgreltEEHRKELLEEYTAELKR----------IEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2057 KAKVEEARRLRERAEQESARQLQLAQDAAQKrlqAEEKAHAF-AVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEA 2135
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2136 EEAREraereaaqsrrqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKF 2215
Cdd:PRK03918 566 DELEE-------------ELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2216 AEQTLRQKA--QVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKAR 2288
Cdd:PRK03918 633 EELAETEKRleELRKELEELEKKYSEEEYEELReeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
570 580 590
....*....|....*....|....*....|....*
gi 2124423184 2289 IEAENRALilrdkDNTQRvLQEEAEKMKHVAEEAA 2323
Cdd:PRK03918 713 LEKLEKAL-----ERVEE-LREKVKKYKALLKERA 741
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1775-2507 |
7.65e-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: 65.86 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1775 EEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLR---AL 1851
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIErqlAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1852 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAI-----GEATRLKTEaeiaLKEKEAENERLRRLAEDEAFQRRRLEEQA 1926
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEK----IGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1927 AQHKADIEERLAQLRKaSESELERQKglvedtlRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 2006
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEE-LEREIEEER-------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2007 AELEaMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALE-EVERLKAKVEEARRLRER------AEQESARQLQ 2079
Cdd:TIGR02169 397 LKRE-INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEeEKEDKALEIKKQEWKLEQlaadlsKYEQELYDLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2080 LAQDAAQKRLQA--EEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQ--VEE 2155
Cdd:TIGR02169 476 EEYDRVEKELSKlqRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNnvVVE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2156 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAL---------------------------RQKQAADAE 2208
Cdd:TIGR02169 556 DDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIgfavdlvefdpkyepafkyvfgdtlvvEDIEAARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2209 MEK--------------------HKKFAEQTLRQKAQVEqELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV 2268
Cdd:TIGR02169 636 MGKyrmvtlegelfeksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2269 EEELFSLRVQMEELGKlKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARL-----SVAAQEAARLRELAEEDL 2343
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQ-EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELeedlhKLEEALNDLEARLSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2344 AQQRALAEKMlkEKMQAVQEATRLKAEAELlqQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAE 2423
Cdd:TIGR02169 794 PEIQAELSKL--EEEVSRIEARLREIEQKL--NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2424 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQsdhdaerLRQAIAELEREKEK 2503
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA-------LEEELSEIEDPKGE 942
|
....
gi 2124423184 2504 LKQE 2507
Cdd:TIGR02169 943 DEEI 946
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1412-1633 |
7.79e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.44 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1412 EKQRQLAEAHAQAKAQAEQEAQELQRRM---QEEVARREEAAVDAQQQKRSIQEELQhlrQSSEAEIQAKARQVEAAERS 1488
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQaaeQERLKQLEKERLAAQEQKKQAEEAAK---QAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1489 RLRieeeirvvrlqletterqrggAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDETQRKRQAEAELAVRVKAEA 1567
Cdd:PRK09510 146 KAK---------------------AEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAAAEA 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1568 EAAREKQRALQAleefrlqAEEAErrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1633
Cdd:PRK09510 200 KKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1420-1879 |
1.03e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 65.04 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1420 AHAQAKAQAEQEAQELQRRMQEEVARReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVV 1499
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLAL---AERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1500 RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQA 1579
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1580 LEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQ 1659
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1660 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1739
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1740 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1819
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1820 SRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1879
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1571-1923 |
1.07e-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: 64.76 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1571 REKQRALQALEEFRLQaEEAERRLRqaEAERARQvqvaLETAQRSAEVELQSKRASFAEKtaqlERTLQEEHvavaqlre 1650
Cdd:pfam17380 287 RQQQEKFEKMEQERLR-QEKEEKAR--EVERRRK----LEEAEKARQAEMDRQAAIYAEQ----ERMAMERE-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1651 eaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRrgKAEEQAVRQRE 1730
Cdd:pfam17380 348 --------------------RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1731 LaeQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQ-QRQLLEEELARLQHEAAAATQKRQ-------ELEAELAKV 1802
Cdd:pfam17380 406 I--LEEERQRKIQQ--------QKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1803 RAEMEVLLASKARAEEESRSTSEKskqrlEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLAE 1879
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2124423184 1880 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1923
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1144-1334 |
1.08e-09 |
|
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: 61.69 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1144 EEVLKAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPMFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1223
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1224 AQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADpLGAWLQDAKRRQEQIQamVLADSRAVREQLRQEKALLEEIERH 1303
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|.
gi 2124423184 1304 GEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1334
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1383-1599 |
1.42e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1383 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1462
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1463 ---ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEae 1539
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE-- 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 1540 rlRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF--RLQAEEAERRLRQAEA 1599
Cdd:COG4942 187 --RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAA 246
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1731-1962 |
1.84e-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: 62.94 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1731 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAelakvraemevll 1810
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1811 askARAEEESRSTSEKSKQRLEAEASRfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAervlAEKLAaigEATRL 1890
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1891 KTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE----ERLAQLRKASESELERQKGLVEDTLRQR 1962
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1720-2097 |
2.03e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1799
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELE-AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1800 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAE------EDAARQRAEA 1873
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEeeleqlENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1874 ERVLAEKLAAIGEATRLKTEAEIAL------------------------------KEKEAENERLRRLAEDEAFQRRRLE 1923
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSllsliltiagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1924 EQAAQHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEILALKVSFEKAAAGKAElelelgRIRSNAEDTLR 2002
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2003 SKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQL 2080
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQ 476
|
410
....*....|....*..
gi 2124423184 2081 AQDAAQKRLQAEEKAHA 2097
Cdd:COG4717 477 ELEELKAELRELAEEWA 493
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1719-1962 |
2.82e-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: 62.17 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1719 GKAEEQAVRQRelAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARlQHEAAAATQKRQELEAE 1798
Cdd:TIGR02794 46 GAVAQQANRIQ--QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK-QAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1799 LAKVRAEMEVLLASKARAEeesRSTSEKSKQRLEAEAsrfreLAEEAARLRALAEEAKRQRqlaeEDAARQRAEAER-VL 1877
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEAE---RKAKEEAAKQAEEEA-----KAKAAAEAKKKAEEAKKKA----EAEAKAKAEAEAkAK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1878 AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVED 1957
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQ 270
|
....*
gi 2124423184 1958 TLRQR 1962
Cdd:TIGR02794 271 AIQQN 275
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4429-4467 |
2.99e-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: 2.99e-09
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 4429 FLEVQYLTGGLIEPDVPGRVPLDEALQRGTVDARTAQKL 4467
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1138-1874 |
3.01e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.82 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1138 RSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpmfdaLRDELRGAQEvGERLQQRHGERDVEVE 1217
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1218 RWRERvaqlLERWQAVLAQTDLRQRELEqlgRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVReQLRQEKALL 1297
Cdd:PRK04863 359 ELEER----LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1298 E----EIERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKK-------PKVQSGSESVIQEYVDLRT 1363
Cdd:PRK04863 431 GlpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKiagevsrSEAWDVARELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1364 RYSELTTLTSQYikfisETLRRMEEEERLAEQQRAEERERL-------AAVEAALEKQRQLAEAHAQAKAQA-------E 1429
Cdd:PRK04863 511 LAEQLQQLRMRL-----SELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEArerrmalR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1430 QEAQELQRRMQEEVARREE--AAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTE 1507
Cdd:PRK04863 586 QQLEQLQARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1508 rQRGGAEGE-LQALRAR-----------------AEEAEA---QKRQA--QEEAERLRRQVQDET-------------QR 1551
Cdd:PRK04863 666 -QPGGSEDPrLNALAERfggvllseiyddvsledAPYFSAlygPARHAivVPDLSDAAEQLAGLEdcpedlyliegdpDS 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1552 KRQA-----EAELAVRVK-AEAE--------------AAREKQralqaLEEFRLQAEEAERRLRQAEAERaRQVQVALET 1611
Cdd:PRK04863 745 FDDSvfsveELEKAVVVKiADRQwrysrfpevplfgrAAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQA 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1612 AQR------------SAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlK 1679
Cdd:PRK04863 819 FSRfigshlavafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLA----D 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1680 ANEALRLRLQAEEVAQQkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQ--------------LAE 1744
Cdd:PRK04863 895 RVEEIREQLDEAEEAKR-FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDyQQAQQTQRDAKQqafaltevvqrrahFSY 973
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1745 GTAQQRLAAEQEL-IRLRAETEQGEQQRQLLEEEL--------------ARLQHEAAAATQKRQELEAELAK--VRAEme 1807
Cdd:PRK04863 974 EDAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPAD-- 1051
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1808 vllaskARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1874
Cdd:PRK04863 1052 ------SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
201-303 |
3.06e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.77 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 201 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 279
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 2124423184 280 PEDVDVPQPDEKSIITYVSSLYDA 303
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1751-2604 |
3.53e-09 |
|
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: 63.66 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1751 LAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEkskQR 1830
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELE---SR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1831 LEAEASRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLAE-KLAAIGEATRLKTEAEIAL-KEKEAENERL 1908
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1909 RRL---AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKglvedtlrQRRQVEEEILALKVSFEKAAAGKAE 1985
Cdd:pfam01576 162 SEFtsnLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK--------AKRKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1986 LELELGRirsnAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAE----EEAARQRKAALEEVERLKAKVE 2061
Cdd:pfam01576 234 LRAQLAK----KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESEraarNKAEKQRRDLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2062 EA-------RRLRERAEQESARqlqlaqdaAQKRLQAEEKAHAFAVQQkeqelqqTLQQEQSMLERLRgeaeaarraaee 2134
Cdd:pfam01576 310 DTldttaaqQELRSKREQEVTE--------LKKALEEETRSHEAQLQE-------MRQKHTQALEELT------------ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2135 aeeareraereaaqsrRQVEEAERLKQSaeeqaqaqaqaqaaaeklrkeaeqeaarraqaeqaalrqkqaadaeMEKHKK 2214
Cdd:pfam01576 363 ----------------EQLEQAKRNKAN----------------------------------------------LEKAKQ 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2215 FAEQtlrQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENR 2294
Cdd:pfam01576 381 ALES---ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2295 ALilrDKD---------NTQRVLQEEAEKMKHVAeeaARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEAT 2365
Cdd:pfam01576 458 KL---SKDvsslesqlqDTQELLQEETRQKLNLS---TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2366 RLKAEAELLqqqkELAQEQARRLQEDKEQMAQQLEQETQGFQR---------------TLEAERQRQL------------ 2418
Cdd:pfam01576 532 KLEEDAGTL----EALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrlqqelddlLVDLDHQRQLvsnlekkqkkfd 607
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2419 EMSAEAERLKLRVA-EMSRAQARAEEDAQRFRKQAEEIGEKL-HRTELATQEKVTL----------------VQTLEIQR 2480
Cdd:pfam01576 608 QMLAEEKAISARYAeERDRAEAEAREKETRALSLARALEEALeAKEELERTNKQLRaemedlvsskddvgknVHELERSK 687
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2481 QQSDHDAERLRQAIAELEREKE-----KLKQEAKLLQLKSE---EMQTVQQEQLLQETQALQQsfLSEKDTLLQRERFIE 2552
Cdd:pfam01576 688 RALEQQVEEMKTQLEELEDELQatedaKLRLEVNMQALKAQferDLQARDEQGEEKRRQLVKQ--VRELEAELEDERKQR 765
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 2553 QE----KAKLEQLFQD---EVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREA 2604
Cdd:pfam01576 766 AQavaaKKKLELDLKEleaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI 824
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1367-1582 |
3.71e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 62.58 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1367 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAAVEAAlEKQRQLAEAHAQAKAQ------AEQEAqEL 1435
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAIA-QANREAEEAELEQEREietariAEAEA-EL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1436 QRRMQEEVARREEAAVDAQQQKRsIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqLETTERQRggAEG 1515
Cdd:COG2268 247 AKKKAEERREAETARAEAEAAYE-IAEANAEREVQRQLEIAEREREIELQEKEAEREEAE-------LEADVRKP--AEA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1516 ELQALRARAEeAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEE 1582
Cdd:COG2268 317 EKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDK 382
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1725-2493 |
3.78e-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: 63.43 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1725 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQhEAAAATQK----RQ 1793
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEKieryQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1794 ELEAELAKVRAEMEVLLASkaraeEESRSTSEKSKQRLEAEASRFR-ELAE-----EAARLRALA--------EEAKRQR 1859
Cdd:COG3096 355 DLEELTERLEEQEEVVEEA-----AEQLAEAEARLEAAEEEVDSLKsQLADyqqalDVQQTRAIQyqqavqalEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1860 QL-------AEEDAARQRAEAERVLAEKLAAigeATRLkTEAEIALKEKEAENERLRRLAED----EAFQR-RRLEEQAA 1927
Cdd:COG3096 430 GLpdltpenAEDYLAAFRAKEQQATEEVLEL---EQKL-SVADAARRQFEKAYELVCKIAGEversQAWQTaRELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1928 QHKAdIEERLAQLRkASESELERQkglvedtLRQRRQVEEEILALKVSFEKAAAGKAELELelgrirsnaedtlrskEQA 2007
Cdd:COG3096 506 SQQA-LAQRLQQLR-AQLAELEQR-------LRQQQNAERLLEEFCQRIGQQLDAAEELEE----------------LLA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2008 ELEAMRQRqlaaeeeqrrreaeervqksLAAEEEAARQRKAALE-EVERLKAKVEEarrLRERAEQESARQLQLAQDAAQ 2086
Cdd:COG3096 561 ELEAQLEE--------------------LEEQAAEAVEQRSELRqQLEQLRARIKE---LAARAPAWLAAQDALERLREQ 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2087 krlQAEEKAHAFAVQQkeqelqqtlqQEQSMLERLRGeaeaarraaeeaeeaRERAEREAAQSRRQVE-EAERLKQSAEE 2165
Cdd:COG3096 618 ---SGEALADSQEVTA----------AMQQLLERERE---------------ATVERDELAARKQALEsQIERLSQPGGA 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2166 QAQAQAQAQAAAE------------------------KLRKEAEQEAARRAQAEQAAL-----------RQKQAADA--- 2207
Cdd:COG3096 670 EDPRLLALAERLGgvllseiyddvtledapyfsalygPARHAIVVPDLSAVKEQLAGLedcpedlylieGDPDSFDDsvf 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2208 ---EMEK------------HKKFAEQTLRQKAQVEQELTTLRLQLEETD---HQKSILDEELQRL--------------- 2254
Cdd:COG3096 750 daeELEDavvvklsdrqwrYSRFPEVPLFGRAAREKRLEELRAERDELAeqyAKASFDVQKLQRLhqafsqfvgghlava 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2255 -----KAEVTEAARQRSQVEEELFSLRVQM----EELGKLKARIEAENRAL----ILRDKDNTQRVlqEEAEKMKHVAEE 2321
Cdd:COG3096 830 fapdpEAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLADETLADRL--EELREELDAAQE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2322 AAR-----------------------LSVAAQEAARLRELAEEDLAQQRALAekmLKEKMQ-----AVQEATRLKAEA-- 2371
Cdd:COG3096 908 AQAfiqqhgkalaqleplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFA---LSEVVQrrphfSYEDAVGLLGENsd 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2372 --ELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQrTLEAERQRQLEMSAEAERlklRVAEMS-RAQARAEEDAQRF 2448
Cdd:COG3096 985 lnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ---ELEELGvQADAEAEERARIR 1060
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 2124423184 2449 RKqaeEIGEKLHRTElatQEKVTLVQTLEIQRQQSDHDAERLRQA 2493
Cdd:COG3096 1061 RD---ELHEELSQNR---SRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
564-753 |
4.70e-09 |
|
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: 59.77 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 564 LRYLQDLLAWVEENQRRVDGAEWGVDLPSVEAQLGSHRGLHHSIEEFRAKIERARTDEGQLSPATRGAY---RDCLGRLD 640
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 641 LQYAKLLNSSKGRLRSLE---SLYSFVAAATKELMWLSEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEI 717
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 2124423184 718 QNTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 753
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1393-1591 |
5.40e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.75 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1393 AEQQRAEE-RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREeaavdAQQQKrsiQEELQHLRQSS 1471
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1472 EAEIQAKARQVEAAERSRlRIEEEIRvVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDETQR 1551
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2124423184 1552 KRQAEAELAV-RVKAEAEAAREKQRALQALEEFRLQAEEAE 1591
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1476-1697 |
5.43e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1476 QAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQA 1555
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1556 EAELAVRVKAEAEAAREKQR-ALQALEEFRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1633
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1634 LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQK 1697
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAE 241
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
86-185 |
5.47e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 56.74 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 86 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 160
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILH 185
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4351-4388 |
5.81e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 5.81e-09
10 20 30
....*....|....*....|....*....|....*...
gi 2124423184 4351 QRLLEAQACTGGIIDPNTGERFPVTDAVNKGLVDKIMV 4388
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1518-2043 |
6.18e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 62.95 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1518 QALRARA-EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREkqRALQALEEFRLQAEEAERR--- 1593
Cdd:COG3899 714 RALARGAyAEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLE--RALAARALAALAALRHGNPpas 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1594 ----------LRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAE 1663
Cdd:COG3899 792 arayanlgllLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1664 RAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1743
Cdd:COG3899 872 ALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAA 951
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1744 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSt 1823
Cdd:COG3899 952 AALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAA- 1030
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1824 sekskqRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA 1903
Cdd:COG3899 1031 ------AAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAA 1104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1904 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGK 1983
Cdd:COG3899 1105 LALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLA 1184
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1984 AELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAA 2043
Cdd:COG3899 1185 AAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1755-2604 |
6.23e-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: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1755 QELIRLRAETEQGEQQRQLLEE-----------ELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1823
Cdd:TIGR02169 198 QQLERLRREREKAERYQALLKEkreyegyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1824 SEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAaigEATRLKTEAEIALKEKEA 1903
Cdd:TIGR02169 278 NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1904 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE---SELERQKGLVEDTLRQRRQVEEEILALKVSFEKAA 1980
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1981 AGKAELELEL-----------GRIRSNAEDtlRSKEQAELEAMRQRQlaaeeeqrrrEAEERVQKSLAAEEEAARQRKAA 2049
Cdd:TIGR02169 434 AKINELEEEKedkaleikkqeWKLEQLAAD--LSKYEQELYDLKEEY----------DRVEKELSKLQRELAEAEAQARA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2050 LEEVERLKAKVEEARRLRERAEQESARQL-------QLA-QDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLErL 2121
Cdd:TIGR02169 502 SEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryATAiEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLP-L 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2122 RGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRkeaeqeaarRAQAEQAALRQ 2201
Cdd:TIGR02169 581 NKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYR---------MVTLEGELFEK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2202 KQAADAEMEKHKKFAEQTLRQKAQVEQelttLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEE 2281
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQR----LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2282 LGKlKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLsvaaqeaarlrelaEEDLAQ-QRALAEKMLKEKMQA 2360
Cdd:TIGR02169 728 LEQ-EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL--------------EEDLHKlEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2361 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2440
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2441 AEEDAQRFRKQAEEIGEKlhRTELATQEKVtlvqtLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2520
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKE--RDELEAQLRE-----LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2521 VQQEQllqetqalqqsfLSEKDTLLQRERfIEQEKAKLEQ---LFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEA 2597
Cdd:TIGR02169 946 IPEEE------------LSLEDVQAELQR-VEEEIRALEPvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 2124423184 2598 RQRQREA 2604
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
196-298 |
6.49e-09 |
|
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: 56.71 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 196 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 274
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 2124423184 275 TRLLDPEDVDVPQPDEKSIITYVS 298
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2206-2737 |
7.03e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 62.68 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2206 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKaevtEAARQRSQVEEELFSLRVQMEELGKL 2285
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2286 KARIEAENRALILRDKdntQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELA----------EEDLAQQRALAEKMLK 2355
Cdd:TIGR00618 276 EAVLEETQERINRARK---AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlmkraahvkqQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2356 EKMQAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLEQETQgfqrtlEAERQRQLEMSAEAERLKLRVAEMS 2435
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCK------ELDILQREQATIDTRTSAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2436 RAQARAEEDAQRFRKQAEEigekLHRTELATQEKVTLVQTLEIQrQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKS 2515
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCA----AAITCTAQCEKLEKIHLQESA-QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2516 EEmQTVQQEQLLQETQALQQSFLSEKDTllQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVAsME 2595
Cdd:TIGR00618 501 EE-PCPLCGSCIHPNPARQDIDNPGPLT--RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI-LT 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2596 EARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALaHSEEIAASQATAVKALpngrdap 2675
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL-HLQQCSQELALKLTAL------- 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 2676 dgpateaepehafdglrqkvpaqrlqevgilsTEELQRLVQGRTTVAELAQREDVRRYLQGR 2737
Cdd:TIGR00618 649 --------------------------------HALQLTLTQERVREHALSIRVLPKELLASR 678
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1532-2052 |
7.57e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1532 RQAQEEAERLRRQVQ-----DETQRKRQAEAELAVRVKAEAEAAR--EKQRALQALEEfRLQAEEAERRLRQAEAERARQ 1604
Cdd:COG4913 238 ERAHEALEDAREQIEllepiRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEA-ELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1605 VQVALETAQRSAEVELQSkrasfaEKTAQLERtLQEEhvavaqlreeaerraqqqaeaerareeaereLERWQLKANEAL 1684
Cdd:COG4913 317 RLDALREELDELEAQIRG------NGGDRLEQ-LERE-------------------------------IERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1685 RLRLQAEEVAQQKSLAQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1764
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1765 EQGEQQRQLLEEELARLQHEAAAATQ-KRQELE--AELAKVRAE-------MEVLLASKAR------------------- 1815
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEALGlDEAELPfvGELIEVRPEeerwrgaIERVLGGFALtllvppehyaaalrwvnrl 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1816 ---------------AEEESRSTSEKS-KQRLEAEASRFR-----ELAEEAARLRALAEEA------------------- 1855
Cdd:COG4913 509 hlrgrlvyervrtglPDPERPRLDPDSlAGKLDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgngt 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1856 ----KRQRQLAEE-----DAARQRAEAERVLAEKLAAIGEATRLKTEAEialKEKEAENERLRRLAEDEAFQRRRLEEQA 1926
Cdd:COG4913 589 rhekDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALE---AELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1927 AQHK-ADIEERLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIR---SNAEDTLR 2002
Cdd:COG4913 666 AEREiAELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrlEAAEDLAR 744
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2003 SKEQAELEAMRQRQLaaeeeqrRREAEERVQKSLAAEEEAARQRKAALEE 2052
Cdd:COG4913 745 LELRALLEERFAAAL-------GDAVERELRENLEERIDALRARLNRAEE 787
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1381-1603 |
8.27e-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: 61.01 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLRRMEEEERLAEQQRAEERERLAAVE--AALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQqkr 1458
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1459 siQEELQHlrqssEAEIQAKARQVEAAERSRlrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRQAQEE- 1537
Cdd:TIGR02794 145 --KEEAAK-----QAEEEAKAKAAAEAKKKA-----------------------EEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1538 ---AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERAR 1603
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1383-1997 |
8.47e-09 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 62.13 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1383 LRRMEEEERLAEQQRAEERERLAAVEAA-----LEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQK 1457
Cdd:PRK10246 259 ASRRQQALQQALAAEEKAQPQLAALSLAqparqLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1458 RSIQEELQHLRQSseaeiqakarqveAAERSRLRIEEEirvvrlqletterqrggaegELQALRARAEEAEAQKRQAQEE 1537
Cdd:PRK10246 339 AELQAQQQSLNTW-------------LAEHDRFRQWNN--------------------ELAGWRAQFSQQTSDREQLRQW 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1538 AERLrrqvqDETQRKRQAEAELAVRVKA-EAEAAREKQRALQALEE--FRLQAEEAERRLRQAEAERARQvqvALETAQR 1614
Cdd:PRK10246 386 QQQL-----THAEQKLNALPAITLTLTAdEVAAALAQHAEQRPLRQrlVALHGQIVPQQKRLAQLQVAIQ---NVTQEQT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1615 SAEVELQSKRASFAEKTAQLE--RTLQEEHVAVAQLrEEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEE 1692
Cdd:PRK10246 458 QRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDL-EAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1693 vaQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1772
Cdd:PRK10246 537 --KEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQ-EEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLR 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1773 LLEEELArLQHEAAAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKSKQRLEAEASRFRELAEEAA 1846
Cdd:PRK10246 614 LLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQEAQSWQQRQNELTALQNRIQ 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1847 RLRALAEeakrqrQLAEEDAArqRAEAERVLAEKLAAIGEATrLKTEAEIALKEKEAENERlRRLAE-----DEAFQRRR 1921
Cdd:PRK10246 693 QLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA-QRLQKaqaqfDTALQASV 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1922 LEEQAAQHKADIEE----RLAQLRKASESELERQKGLVEdtlrQRRQVEEEILALKVSFEKAAAGKAELELEL----GRI 1993
Cdd:PRK10246 763 FDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVT----QTAQALAQHQQHRPDGLDLTVTVEQIQQELaqlaQQL 838
|
....
gi 2124423184 1994 RSNA 1997
Cdd:PRK10246 839 RENT 842
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1695-1890 |
1.08e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1695 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1774
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1775 EEELARLQHEAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEE 1854
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 2124423184 1855 AKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1890
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
205-300 |
1.10e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.54 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 205 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 260
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 261 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 300
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1398-1618 |
1.23e-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: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1398 AEERERLAAVEAALEKQRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVARREEAAvdAQQQKRSIQEELQhlRQSSEAEIQ 1476
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEAEAERETEiAIAQANREAEEAELEQEREIETARIAE--AEAELAKKKAEER--REAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1477 AKARQVEAAERSRLRIEEEIRVVRLQLETterqrggaegelqalraRAEEAEAQKRQAQEEAErlrrqvqdetqrkrqae 1556
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQLEIAEREREI-----------------ELQEKEAEREEAELEAD----------------- 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 1557 aelaVRVKAEAEAAREKQRALQALEEFRLQAE-EAERRLRQAEAERA-RQVQVALETAQRSAEV 1618
Cdd:COG2268 310 ----VRKPAEAEKQAAEAEAEAEAEAIRAKGLaEAEGKRALAEAWNKlGDAAILLMLIEKLPEI 369
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1494-1931 |
1.29e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1494 EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DETQRKRQAEAELAvrvkaeaeaar 1571
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELA----------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1572 EKQRALQALEEFRLQAEEAERRLRQAEAErarqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREE 1651
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAE--------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1652 AERRAQQQAEAERAREEAERELERWQLKA--NEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1729
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEErlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1730 ELAEQELEKQRQLAEGTAQQRLaAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEME-- 1807
Cdd:COG4717 295 REKASLGKEAEELQALPALEEL-EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEia 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1808 -VLLASKARAEEESRSTSEKSKQRLEAEAsrfrELAEEAARLRALAEEAKRQRQLAEEDAARQR-AEAERVLAEKLAAIG 1885
Cdd:COG4717 374 aLLAEAGVEDEEELRAALEQAEEYQELKE----ELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2124423184 1886 EATRLKTEAEIALKEKEaENERLRRLAEDEAFQRRRLEEQAAQHKA 1931
Cdd:COG4717 450 ELREELAELEAELEQLE-EDGELAELLQELEELKAELRELAEEWAA 494
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1919-2646 |
1.35e-08 |
|
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: 61.53 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1919 RRRLEEQAA--QHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSN 1996
Cdd:pfam02463 155 RLEIEEEAAgsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1997 AEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2076
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2077 QLQLAQD---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLE-RLRGEAEAARRAAEEAEEARERAEREAAQSRRQ 2152
Cdd:pfam02463 315 KLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEElEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2153 VEEAERLKQSAEEQAQAQAQAQAAAEKLRKeaeqeaarraqaeqaalrqKQAADAEMEKHKKFAEQTLRQKAQVEQELTT 2232
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEE-------------------KKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2233 LRLQLEETDHQKSILDEELQRLKaevtEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEA 2312
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQ----LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2313 EKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAvqeaTRLKAEAELLQQQKELAQEQARRLQEDK 2392
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARK----LRLLIPKLKLPLKSIAVLEIDPILNLAQ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2393 EQMAQQLEQETQGFQRTLEAERQRQLEMSaeaERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTL 2472
Cdd:pfam02463 608 LDKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2473 VQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQalQQSFLSEKDTLLQRERFIE 2552
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ--KIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2553 QEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGvrrkqEELQLLEQQRQQQEKLLAEE 2632
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL-----EEEQLLIEQEEKIKEEELEE 837
|
730
....*....|....
gi 2124423184 2633 NQRLRERLQRLEEE 2646
Cdd:pfam02463 838 LALELKEEQKLEKL 851
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1720-1927 |
1.55e-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: 60.16 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAel 1799
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1800 akvRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1878
Cdd:COG4942 119 ---QPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124423184 1879 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1927
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1401-1870 |
1.60e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.19 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1401 RERLAAVEAALEKQRQLAEAHAqakAQAEQEAQELQRRMQEEVARREEAAVDaqqqkrSIQEELQHLRQSSEAEIqakAR 1480
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYL---ALAERAAAELRGPDQLAWLARLDAEHD------NLRAALRWALAHGDAEL---AL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1481 QVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1560
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1561 VRvkAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1640
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1641 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1720
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1721 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1800
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1801 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1870
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
196-303 |
1.63e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.48 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 196 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 274
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 2124423184 275 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 303
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1304-2093 |
1.95e-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: 61.22 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1304 GEKVEECQ---RFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFis 1380
Cdd:TIGR00606 199 GQKVQEHQmelKYLKQYKEKACEIRDQITSKEAQLE---------SSREIVKSYENELDPLKNRLKEIEHNLSKIMKL-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 etlrrmeEEERLAEQQRAEERERLaaveaalekQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1460
Cdd:TIGR00606 268 -------DNEIKALKSRKKQMEKD---------NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1461 QEELQHLRQSS---EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRgGAEGELQALRARAEEAEAQKRQAQEE 1537
Cdd:TIGR00606 332 NKERRLLNQEKtelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFER-GPFSERQIKNFHTLVIERQEDEAKTA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1538 AERLRRQVQDETQRKRQAEaELAVRVKA-------EAEAAREKQRALQALEEFRLQAEEAERRLRQAEaERARQVQVALE 1610
Cdd:TIGR00606 411 AQLCADLQSKERLKQEQAD-EIRDEKKGlgrtielKKEILEKKQEELKFVIKELQQLEGSSDRILELD-QELRKAERELS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1611 TAQRSAEVELQSKRA-SFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--- 1686
Cdd:TIGR00606 489 KAEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgy 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1687 ---RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE-LAEQELEKQRQLAEGTAQQrlAAEQELIRLRA 1762
Cdd:TIGR00606 569 fpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEsKEEQLSSYEDKLFDVCGSQ--DEESDLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1763 ETEQGEQQRQLLE----------EELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR-- 1830
Cdd:TIGR00606 647 EIEKSSKQRAMLAgatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRrd 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1831 -----LEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA------IGEATRLKTEAEIALK 1899
Cdd:TIGR00606 727 emlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdVTIMERFQMELKDVER 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1900 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD------------IEERLAQLR--KASESELERQKGLVEDTLRQRRQV 1965
Cdd:TIGR00606 807 KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskielnrklIQDQQEQIQhlKSKTNELKSEKLQIGTNLQRRQQF 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1966 EE-------EILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 2038
Cdd:TIGR00606 887 EEqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 2039 EEEAARQRK--------AALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2093
Cdd:TIGR00606 967 GKDDYLKQKetelntvnAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENE 1029
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1538-1994 |
2.01e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.80 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1538 AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQAleefRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1617
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1618 VELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQK 1697
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1698 SLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1777
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1778 LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKR 1857
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1858 QRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERL 1937
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1938 AQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIR 1994
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1384-1645 |
2.02e-08 |
|
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: 59.67 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1384 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQ 1461
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1462 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqletterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1541
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1542 RRQVQDETQR-KRQA-EAELAVRVKAEAEAARE--KQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1617
Cdd:pfam15558 168 KVQENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 2124423184 1618 VELQSKRASFAEKTAQLERTLQEEHVAV 1645
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1789-1940 |
2.14e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 60.27 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1789 TQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEASRFRELAEEAARLRAlaEEAKRQRQLAEEDAAR 1868
Cdd:COG2268 215 AIAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIAE--ANAEREVQRQLEIAER 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1869 QR------AEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 1940
Cdd:COG2268 289 EReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKL 366
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1893-2342 |
2.29e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1893 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEqAAQHKADIEERLAQLRKASEselerqkglVEDTLRQRRQVEEEILAL 1972
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQ---------LLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1973 KVSFEKAAAGKAELElELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEqrrreaeerVQKSLAAEEEAARQRKAALEE 2052
Cdd:COG4717 145 PERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEE---------LQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2053 VERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAA 2132
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2133 EEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAlRQKQAADAEMEKH 2212
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2213 KKFA------EQTLRQKAQVEQELTTLRLQLEETDHQ-KSILDEELQRLKAEVTEAARQR-SQVEEELFSLRVQMEELGK 2284
Cdd:COG4717 374 ALLAeagvedEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEElEELEEELEELEEELEELRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 2285 LKARIEAENRALILRDK-DNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEED 2342
Cdd:COG4717 454 ELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1454-1998 |
2.70e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 60.04 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1454 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEeirvVRLQLE--TTERQRGGAEGELQALRARaeeaEAQK 1531
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1532 RQAQEEAERLRRQVQDETQRKRQAEAELAVrVKAE--------AEAAREKQRALQALEEFRLQAEEAERRLRQAEAERAr 1603
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1604 QVQVALETAqRSAEVELQSKRASFA----EKTAQLERTLQEEHVAVAQLREEAERRAQQQAeaerareeaerelerwQLK 1679
Cdd:pfam05701 191 ATKESLESA-HAAHLEAEEHRIGAAlareQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1680 ANEALRLRLQAEEVAQQKSlaqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQE 1756
Cdd:pfam05701 254 TASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1757 LIRLRAETEQGEQQRQllEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeas 1836
Cdd:pfam05701 318 CLRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA--- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1837 rfrelAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA--ENERLRRLAED 1914
Cdd:pfam05701 390 -----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1915 EAFQR-------------RRLEEQAAQHKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKVSFEKAAA 1981
Cdd:pfam05701 465 EDSPRgvtlsleeyyelsKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKAKE 543
|
570
....*....|....*..
gi 2124423184 1982 GKAELELELGRIRSNAE 1998
Cdd:pfam05701 544 GKLAAEQELRKWRAEHE 560
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
88-182 |
2.84e-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: 54.65 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 88 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 159
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 2124423184 160 VNIRNDDIADGNPKLTLGLIWTI 182
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1089-1582 |
3.23e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1089 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKEaqaVPATLPELE 1168
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1169 ATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERL----QQRHG--ERDVEVERWRERVAQL------LERWQAVLAQ 1236
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLsrleEEINGieERIKELEEKEERLEELkkklkeLEKRLEELEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1237 TDLRQRELEQLGRQLRYYR-----ESADPLGAWLQDAKRRQEQIQ---AMVLADSRAVREQLRQEKALLEEIERHGEKVE 1308
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKkrltgLTPEKLEKELEELEKAKEEIEeeiSKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1309 ECQR---------FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESviqEYVDLRTRYSELTTLTSQYIKFI 1379
Cdd:PRK03918 440 VCGRelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES---ELIKLKELAEQLKELEEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1380 SETLRRMEEE-----ERLAE---QQRAEERE---------RLAAVEAAL-EKQRQLAEAHAQAKAQAEQEAQELQRRMQ- 1440
Cdd:PRK03918 517 LEELEKKAEEyeklkEKLIKlkgEIKSLKKElekleelkkKLAELEKKLdELEEELAELLKELEELGFESVEELEERLKe 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1441 -EEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEE------EIRVVRLQLETTERQRgga 1513
Cdd:PRK03918 597 lEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkysEEEYEELREEYLELSR--- 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1514 egELQALRARAEEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELAVRVKAEAEAAREKQRALQALEE 1582
Cdd:PRK03918 674 --ELAGLRAELEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1203-1510 |
3.63e-08 |
|
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: 60.14 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1203 ERLQQRHGERDVEVERWRervaQLLERWQAvlaqtdlRQRELEqlgRQLRYYRESAdplgawlQDAKRRQEQIQAMVLAD 1282
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1283 SRAVREQLRQEKALLE-----EIERHGEKVEECQRFAKQYINAIKDYELQLV--TYKAQLEPVASPAKKPKVQSGSESVI 1355
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILEEerQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1356 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEaalEKQRQLAEAHAQAKAQAEQEAQEL 1435
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1436 QRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVeAAERSRLRIEEEIRVVRLQLETTERQR 1510
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1732-1940 |
3.95e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1732 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEmevllA 1811
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE-----A 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1812 SKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEEAKrqrQLAEEDAARQRAEAERVlAEKLAAIGEATRLK 1891
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAEAK 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124423184 1892 TEAEIALKEKEAEnerlrrlAEDEAFQRRRLEEQAAQHKADIEERLAQL 1940
Cdd:PRK09510 225 AAAAKAAAEAKAA-------AEKAAAAKAAEKAAAAKAAAEVDDLFGGL 266
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2290-2517 |
5.39e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2290 EAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLS-----VAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEA 2364
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2365 TRLKAEAELLQQQK-ELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE 2443
Cdd:COG4913 319 DALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 2444 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAE-LEREKEKLKQEAKLLQLKSEE 2517
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1270-1648 |
6.10e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1270 RRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQS 1349
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1350 GSESVIQEYVDLRTRYSELTTLtsqyikfiSETLRRMEEEERLAEQQRAEERERL-AAVEAALEKQRQLAEAHAQAKAQA 1428
Cdd:COG4717 140 ELAELPERLEELEERLEELREL--------EEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1429 EQEAQELQRRMQEevARREEAAVDAQQQKRSIQEELQHLRQSSEAE---------------------------------- 1474
Cdd:COG4717 212 EEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllall 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1475 --IQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDETQR 1551
Cdd:COG4717 290 flLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLeLLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1552 KRQAEAELAVRVKAEaEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKT 1631
Cdd:COG4717 370 QEIAALLAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410
....*....|....*..
gi 2124423184 1632 AQLERTLQEEHVAVAQL 1648
Cdd:COG4717 449 EELREELAELEAELEQL 465
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1568-2011 |
7.61e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1568 EAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQ 1647
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1648 LreeaerraqqqaeaERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAeaekqkeeaerearrrgKAEEQAVR 1727
Cdd:COG4717 151 L--------------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATE-----------------EELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1728 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEME 1807
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1808 VLLASKARAEEESRStseKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1887
Cdd:COG4717 280 FLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1888 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR-RQ 1964
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEE 436
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2124423184 1965 VEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEA 2011
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKA 483
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2209-2512 |
8.18e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.88 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2209 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKAR 2288
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2289 IEAENRAL------ILRDKDNTQRVLQEEAEKMKHVAEEAarlsvaaqeaarlRELAEE--DLAQQRALaekmLKEKMQa 2360
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2361 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEaerqrqlemsaeaeRLKLRVAEMSRAQAR 2440
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE--------------ELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 2441 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQ 2512
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1409-1641 |
8.23e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1409 AALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLR--QSSEAEIQAKARQVEAA 1485
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEArAAKDKDAVAAALARVKakKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1486 ERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKA 1565
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1566 EAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEE 1641
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAK-ARKAAQQQANAEPE 670
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2249-2659 |
8.36e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2249 EELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRAL-ILRDKDNTQRVLQEEAEKMKHVAEEAARLSV 2327
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2328 AAQEAARLRELAEEdlaQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQ 2407
Cdd:COG4717 161 LEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2408 RTLEAERQRQLEMSAE----------------------AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2465
Cdd:COG4717 238 AAALEERLKEARLLLLiaaallallglggsllsliltiAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2466 TQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQtvqqeqllqETQALQQSFLSEKDTLL 2545
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---------IAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2546 QRERFIEQEKAKLEQLfqdEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVrrkqeelqlleqqrqqq 2625
Cdd:COG4717 389 AALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL----------------- 448
|
410 420 430
....*....|....*....|....*....|....
gi 2124423184 2626 ekllaeenQRLRERLQRLEEEHRaALAHSEEIAA 2659
Cdd:COG4717 449 --------EELREELAELEAELE-QLEEDGELAE 473
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1380-2095 |
8.53e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1380 SETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKaQAEQEAQELQRRMQEEVARREEAAVDAQQQKRS 1459
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGLPDLTADNAEDWLEEFQAKEQE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1460 IQEELQHLRQS-SEAeiQAKARQVEAAERSRLRIEEEI------RVVRLQLETTERQRGGAEgELQALRARAEEAEaQKR 1532
Cdd:PRK04863 454 ATEELLSLEQKlSVA--QAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAE-QLQQLRMRLSELE-QRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1533 QAQEEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREkqRALQALEEFRLQAEEAERRLRQAEAERARQvqvaleTA 1612
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELE-QLQEELEARLE--SLSESVSEARERRMALRQQLEQLQARIQRL------AA 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1613 QRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERW-QLKANEALRLRLQAE 1691
Cdd:PRK04863 601 RAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLsQPGGSEDPRLNALAE 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1692 EV--------------------------AQQ----KSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1741
Cdd:PRK04863 681 RFggvllseiyddvsledapyfsalygpARHaivvPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVV 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1742 LAEGTAQQRLAAEQELIRL-RAETEQGEQQRQLLEEELARLQHEAAAATQKRQEL--------------------EAELA 1800
Cdd:PRK04863 761 VKIADRQWRYSRFPEVPLFgRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLhqafsrfigshlavafeadpEAELR 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1801 KVRA---EMEVLLASKARAEEESRSTSEKSKQR---LEAEASRFRELAEE--AARLRALAEEAKRQRQlAEEDAARQRAE 1872
Cdd:PRK04863 841 QLNRrrvELERALADHESQEQQQRSQLEQAKEGlsaLNRLLPRLNLLADEtlADRVEEIREQLDEAEE-AKRFVQQHGNA 919
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1873 AERVlaEKLAAI-----GEATRLKTEAEIALKEKEAENERLRRLAedEAFQRRR--LEEQAAQ---HKADIEERLAQLRK 1942
Cdd:PRK04863 920 LAQL--EPIVSVlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALT--EVVQRRAhfSYEDAAEmlaKNSDLNEKLRQRLE 995
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1943 ASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELG----RIRSNAEDTLRSKE---QAELEAMRQR 2015
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvPADSGAEERARARRdelHARLSANRSR 1075
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2016 QlaaeeeqrrreaeERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQLAQD-AAQKRLQAEEK 2094
Cdd:PRK04863 1076 R-------------NQLEKQLTFCEAEMDNLTKKLRKLER---DYHEMREQVVNAKAGWCAVLRLVKDnGVERRLHRREL 1139
|
.
gi 2124423184 2095 A 2095
Cdd:PRK04863 1140 A 1140
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2358-2503 |
8.77e-08 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 58.88 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2358 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQ-QLEQetQGFQRTLEAERQRQLEMSAEAERLK 2428
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARgRLER--QKMHDKAKAEEQRTKLLELQAESAA 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 2429 LRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlRQAIAELEREKEK 2503
Cdd:PTZ00491 711 VESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1812-2083 |
9.12e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.42 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1812 SKARAEEESRSTSEKSKQRLEAEASRF-RELAEEAARLRAlAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1890
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREARHKK-AAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1891 KTEAEIALKEKEAENERLRRLAEDEAfqrrrleEQAAQHKADIEERL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 1968
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAA-------AAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1969 ILALKVsfEKAAAGKAELELElgrIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKA 2048
Cdd:PRK05035 586 IARAKA--KKAAQQAASAEPE---EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 2124423184 2049 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQD 2083
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2322-2519 |
9.28e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 9.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2322 AARLSVAAQEAARLREL------AEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2395
Cdd:COG4942 16 AAQADAAAEAEAELEQLqqeiaeLEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2396 AQQLEQetqgfQRTLEAERQRQLEMSAEAERLKL-----------RVAEMSRAQARA-EEDAQRFRKQAEEIGEKLHRTE 2463
Cdd:COG4942 96 RAELEA-----QKEELAELLRALYRLGRQPPLALllspedfldavRRLQYLKYLAPArREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 2464 LATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQ 2519
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4082-4118 |
9.83e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 9.83e-08
10 20 30
....*....|....*....|....*....|....*..
gi 2124423184 4082 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4118
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1869-2232 |
9.88e-08 |
|
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: 58.60 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1869 QRAEAERVLAEKLAAIgEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasESEL 1948
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1949 ERQKglVEDTLRQRRQVEEEILALKVSFEKaaagkaELE-LELGRIRSNaedtlrSKEQAELEAMRQRQLAAEEEQRRRE 2027
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2028 AEERVQKSLAAEEEAARQRKAALEEVERLKakveEARRLRERaEQESARQLQ-LAQDAAQKRLQAEEKAHAfAVQQKEQE 2106
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEERAR----EMERVRLE-EQERQQQVErLRQQEEERKRKKLELEKE-KRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2107 LQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeklRKEAEQ 2186
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER----------------------RKQQEM 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2124423184 2187 EAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLR-QKAQVEQELTT 2232
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVEsEKARAEYEATT 595
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1422-1636 |
1.03e-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: 57.55 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1422 AQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArqveaAERSRLRIEEEIRvvrl 1501
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQK---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1502 qletterqrggaegelQALRARAEEAEAQKRQAQEEAERlrrQVQDETQRKRQAEAelavRVKAEAEAAREKQRALQALE 1581
Cdd:TIGR02794 120 ----------------QAEEAKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1582 EFRLQAEEAERRLRQ--AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1636
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1240-1621 |
1.16e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1240 RQRELEQLGRQLRYYRESADPLGAWLQDAkrRQEQIQAMVLADsravrEQLRQEkalLEEIERHGEKVEECQRFAKQYIN 1319
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSAL--NRLLPRLNLLAD-----ETLADR---VEEIREQLDEAEEAKRFVQQHGN 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1320 AIkdyelqlvtykAQLEPVAS-----PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF-ISETLRRMEEEERLA 1393
Cdd:PRK04863 919 AL-----------AQLEPIVSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsYEDAAEMLAKNSDLN 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1394 EQQRAeereRLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEevarreeaavdAQQQKRSIQEELQHL--RQSS 1471
Cdd:PRK04863 988 EKLRQ----RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA-----------KRQMLQELKQELQDLgvPADS 1052
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1472 EAEIQAKARqveaaersRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQ 1544
Cdd:PRK04863 1053 GAEERARAR--------RDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVnakagwcAVLRL 1124
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1545 VQDETQRKRQAEAELAVRVKAEAEAAREKqrALQALeefrlqaeeaerRLRQAEAERARQVQVALETAQRsAEVELQ 1621
Cdd:PRK04863 1125 VKDNGVERRLHRRELAYLSADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRLSEDPKR-PERKVQ 1186
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1190-2015 |
1.17e-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: 58.43 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1190 ALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAV-----LAQTDLRQREleQLGRqlryYRESADPLGAW 1264
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnLVQTALRQQE--KIER----YQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1265 LQdakrrqeqIQAMVLADSRAVREQLRQEKALLE-EIERHG-------EKVEECQRFAKQYINAIKDYE-LQLVTYKAQL 1335
Cdd:COG3096 363 LE--------EQEEVVEEAAEQLAEAEARLEAAEeEVDSLKsqladyqQALDVQQTRAIQYQQAVQALEkARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1336 EPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIsETLRRMEEE-ERLAEQQRAEERER-------LAAV 1407
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEvERSQAWQTARELLRryrsqqaLAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1408 EAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAER 1487
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1488 -SRLRIEEEI-RVVRLQLETTERQRGGA---EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVR 1562
Cdd:COG3096 594 iKELAARAPAwLAAQDALERLREQSGEAladSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPR 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1563 VKAEAE---------------------------------------AAREKQRAL--------------QALEEFRLQAEE 1589
Cdd:COG3096 674 LLALAErlggvllseiyddvtledapyfsalygparhaivvpdlsAVKEQLAGLedcpedlyliegdpDSFDDSVFDAEE 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1590 AERRL------RQAEAER----------ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE---EHVAVAqlre 1650
Cdd:COG3096 754 LEDAVvvklsdRQWRYSRfpevplfgraAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgGHLAVA---- 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1651 eaerRAQQQAEAERAREEAERELERWQLKANEAL-RLRLQAEEVAQQKSLAQAEAEKQKEEaerearrrgkAEEQAVRQR 1729
Cdd:COG3096 830 ----FAPDPEAELAALRQRRSELERELAQHRAQEqQLRQQLDQLKEQLQLLNKLLPQANLL----------ADETLADRL 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1730 ELAEQELEKQRQLAEGTAQQRLAAEQ---ELIRLRAETEQGEQQRQLLEEELARLQheaaaatQKRQELEAeLAKVRAEM 1806
Cdd:COG3096 896 EELREELDAAQEAQAFIQQHGKALAQlepLVAVLQSDPEQFEQLQADYLQAKEQQR-------RLKQQIFA-LSEVVQRR 967
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1807 EVLLASKARAE-EESRSTSEKSKQRLEAeasrfrelaeeaarlralAEEAKRQRQLAEEDAARQRAEAERVLAEklaaig 1885
Cdd:COG3096 968 PHFSYEDAVGLlGENSDLNEKLRARLEQ------------------AEEARREAREQLRQAQAQYSQYNQVLAS------ 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1886 eatrLKTEAEIA---LKEKEAENERLRRLAEDEAfqrrrlEEQAAQHKADIEERLAQLRkASESELERQKGLVE---DTL 1959
Cdd:COG3096 1024 ----LKSSRDAKqqtLQELEQELEELGVQADAEA------EERARIRRDELHEELSQNR-SRRSQLEKQLTRCEaemDSL 1092
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1960 RQR-RQVEEEILALKVSFEKAAAGKAELeLELGRiRSNAEDTLRSKEQAELEAMRQR 2015
Cdd:COG3096 1093 QKRlRKAERDYKQEREQVVQAKAGWCAV-LRLAR-DNDVERRLHRRELAYLSADELR 1147
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1729-2101 |
1.28e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1729 RELAEQELEKQR-QLAEGTAQQRLAAEQELIRLRAETEQGEQQrqllEEELARLQHEAAAATQKRQELEAELAKVRAEME 1807
Cdd:COG4717 44 RAMLLERLEKEAdELFKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1808 VLlaSKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1887
Cdd:COG4717 120 KL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1888 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqhKADIEERLAQLRKASESELERQkGLVEDTLRQRRQVEE 1967
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE--AAALEERLKEARLLLLIAAALL-ALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1968 EILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRK 2047
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 2048 AALEEVERLKAKVEEARR--LRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQ 2101
Cdd:COG4717 355 EAEELEEELQLEELEQEIaaLLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1381-1617 |
1.94e-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: 56.47 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1460
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1461 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1540
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1541 LRrqvqdetqRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1617
Cdd:pfam13868 206 LR--------AKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDE 274
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1768-1959 |
1.99e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1768 EQQRQLLEEELAR-LQHEAAAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEASRFR----ELA 1842
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAKAAAaakaKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1843 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE-RVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrr 1921
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA----- 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 2124423184 1922 LEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTL 1959
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1719-1961 |
2.10e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 57.27 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1719 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqheaaaATQKRQEL 1795
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1796 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeasrfrelaEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1875
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1876 VLAEKlaaigeatRLKTEAEIALKEkeaENERLRRLAEDEAFQ-RRRLEEQAAQHKADIEERLAQLRKASESELERQKGL 1954
Cdd:pfam15709 447 AEAEK--------QRQKELEMQLAE---EQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
....*..
gi 2124423184 1955 VEDTLRQ 1961
Cdd:pfam15709 516 AQEQARQ 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1732-1947 |
2.25e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1732 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLA 1811
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1812 SKARAEE---------ESRSTSE--KSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1880
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1881 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESE 1947
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1381-1629 |
2.34e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 56.58 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLRRMEEEERLAEQQRAEERERL--AAVEAALEKQRQ---LAEAHAQAKAQAEQEAQELQRRMqeevarrEEAAVDAQQ 1455
Cdd:pfam15558 88 QVIEKESRWREQAEDQENQRQEKLerARQEAEQRKQCQeqrLKEKEEELQALREQNSLQLQERL-------EEACHKRQL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1456 QKRSIQEELQHLRQSSEAEIQAKARQVE---AAERSRLRIEEEIRVVRLQlettERQRGGAEGELQALRARAEEAEAQKR 1532
Cdd:pfam15558 161 KEREEQKKVQENNLSELLNHQARKVLVDcqaKAEELLRRLSLEQSLQRSQ----ENYEQLVEERHRELREKAQKEEEQFQ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1533 QAQEEAERLRRQvQDETQRKRQAEAELAVRvKAEAEAAREKQRALQALEEFRLQAEEAERRLRQ----AEAERARQVQVA 1608
Cdd:pfam15558 237 RAKWRAEEKEEE-RQEHKEALAELADRKIQ-QARQVAHKTVQDKAQRARELNLEREKNHHILKLkvekEEKCHREGIKEA 314
|
250 260
....*....|....*....|.
gi 2124423184 1609 LETAQRSAEVELQSKRASFAE 1629
Cdd:pfam15558 315 IKKKEQRSEQISREKEATLEE 335
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
81-188 |
2.36e-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: 52.70 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 81 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 153
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423184 154 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 188
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1454-1635 |
2.56e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1454 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqletterqrggaegelqalraraEEAEAQKRQ 1533
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKER---------------------------LAAQEQKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1534 AQeEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAER---ARQVQVALE 1610
Cdd:PRK09510 120 AE-EAAKQAALKQKQAEEAAAKAAAAA-KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAAA 197
|
170 180
....*....|....*....|....*
gi 2124423184 1611 TAQRSAEVELQSKRASFAEKTAQLE 1635
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2223-2648 |
4.13e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.65 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2223 KAQVEQELTTLRLQLEETDHQKSILDEELQRlkaEVTEAARQRSQVEEELFSLRVQMEELGKLKAriEAENRALILRDKD 2302
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2303 NTQ-RVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2377
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2378 ----KELAQEQARRLQEDKEQMaQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEmsraqaraEEDAQRFRKQAE 2453
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2454 EIGEKLHRTElatQEKVTLVQTleiqRQQSDHDAERLRQAIAELE----REKEKLKQEAKLLQLKSEEMQTVQQEQLLQE 2529
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQA----REKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2530 TQALQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEvakaqKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVR 2609
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIE-----NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
410 420 430
....*....|....*....|....*....|....*....
gi 2124423184 2610 RKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2648
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1830-2016 |
4.22e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1830 RLEAEASRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 1905
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1906 ERLRRLAEDEAF----------QRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVS 1975
Cdd:COG4913 302 AELARLEAELERlearldalreELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2124423184 1976 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQ 2016
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1387-1552 |
4.36e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.62 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1387 EEEERLAEQQRAEERERLAAVEAAleKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1466
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1467 LRQSSEAEIQAKARQVEA-AERSRLRIEEEI----RVVRLQLETTERQRGGAEGELQALRARAEEAEAQK------RQAQ 1535
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 2124423184 1536 EEAERLRRQVQDETQRK 1552
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1775-2093 |
4.82e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.03 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1775 EEELARLQHEAAAATQKRQ-ELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE 1853
Cdd:pfam02029 4 EEEAARERRRRAREERRRQkEEEEPSGQVTESVEP--NEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1854 EAKRQRQLAEEDA---------ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN----ERLRRLAEDEAFQRR 1920
Cdd:pfam02029 82 ALERQKEFDPTIAdekesvaerKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnkwsTEVRQAEEEGEEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1921 RLEEQAAQHKADIEERLAQLRKASE---------SELERQKGLVE--------DTLRQRRQVEEEILALKVSFEKAAAGK 1983
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKekkvkyeskVFLDQKRGHPEvksqngeeEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1984 AELELE--LGRIR-SNAEdtlrsKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEaaRQRKAalEEVERLKAKV 2060
Cdd:pfam02029 242 VFLEAEqkLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEE--QRRKQ--EEAERKLREE 312
|
330 340 350
....*....|....*....|....*....|...
gi 2124423184 2061 EEARRLRERAEQESArqlqlaqDAAQKRLQAEE 2093
Cdd:pfam02029 313 EEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2199-2662 |
5.38e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2199 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRSQVEEELF 2273
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2274 SLRVQMEEL-GKLKARIEAENRAL--ILRDKDNTQRVLQEEAEKMKH-VAEEAARLSVAAQEAARLRELAEEDLAQQRAL 2349
Cdd:COG4913 327 ELEAQIRGNgGDRLEQLEREIERLerELEERERRRARLEALLAALGLpLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2350 AEKMLKEKMQAVQEATRLKAEAELLQQQK---ELAQEQARRL----------------------QEDKE-QMAqqLEQET 2403
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDAlaealgldeaelpfvgelievrPEEERwRGA--IERVL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2404 QGFQRTLEAERQRQLEMSAEAERLKLR-------VAEMSRAQARAEEDAQRFrkqAEEIGEKLH------RTELATQEKV 2470
Cdd:COG4913 485 GGFALTLLVPPEHYAAALRWVNRLHLRgrlvyerVRTGLPDPERPRLDPDSL---AGKLDFKPHpfrawlEAELGRRFDY 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2471 TLVQTLEIQRQQS-------------------DHDA---------------ERLRQAIAELEREKEKLKQEAKLLQLKSE 2516
Cdd:COG4913 562 VCVDSPEELRRHPraitragqvkgngtrhekdDRRRirsryvlgfdnraklAALEAELAELEEELAEAEERLEALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2517 EMQTvqqeqLLQETQALQQSFLSEKDTLLQRERfIEQEKAKLEQL--FQDEVAKAQKLREEQQRQQKQMEEEKQQLVASM 2594
Cdd:COG4913 642 ALQE-----RREALQRLAEYSWDEIDVASAERE-IAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEI 715
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 2595 EEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEEnQRLRERLQRLEEEHRAALAHSEEIAASQA 2662
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEERIDALRARL 782
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1485-1610 |
6.46e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 54.67 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1485 AERSRLRIEEEIRVVRLQLETTERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDET---QRKRQAEAELAV 1561
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAALDA 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2124423184 1562 rVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERArQVQVALE 1610
Cdd:COG1566 160 -AQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALA-QAELNLA 206
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2201-2386 |
6.81e-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: 55.80 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2201 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSLRVQME 2280
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2281 ELGKLKARIEaenRAL-ILRDKDNT----QRVLQEEAEKMKHVAE--EAARLSVAAqEAARLREL-AEEDLAQQRALAE- 2351
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIE-EYRALKEAkSNKEDESQRKLEEi 456
|
170 180 190
....*....|....*....|....*....|....*..
gi 2124423184 2352 KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2386
Cdd:pfam05667 457 KELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3763-3798 |
7.18e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 7.18e-07
10 20 30
....*....|....*....|....*....|....*.
gi 2124423184 3763 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3798
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2041-2385 |
7.69e-07 |
|
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: 55.51 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2041 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQDAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2112
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2113 qeqsmLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaAEKLRKEAEQEAARRA 2192
Cdd:pfam17380 362 -----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR------------------KVKILEEERQRKIQQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2193 QAEQAALRQKQAADAEmekhkkfaEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEElqrlkaevtEAARQRSQVEeel 2272
Cdd:pfam17380 419 KVEMEQIRAEQEEARQ--------REVRRLEEERAREMERVRLEEQERQQQVERLRQQ---------EEERKRKKLE--- 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2273 fslrvqMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEK 2352
Cdd:pfam17380 479 ------LEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
330 340 350
....*....|....*....|....*....|....*..
gi 2124423184 2353 MLKEKMQ-AVQEATRLKA---EAELLQQQKELAQEQA 2385
Cdd:pfam17380 553 RIQEQMRkATEERSRLEAmerEREMMRQIVESEKARA 589
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3504-3540 |
9.00e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.86 E-value: 9.00e-07
10 20 30
....*....|....*....|....*....|....*..
gi 2124423184 3504 IRLLEAQIATGGIIDPVHSHRVPVEVAYQRGYFDEEM 3540
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4185-4213 |
9.65e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.09 E-value: 9.65e-07
10 20
....*....|....*....|....*....
gi 2124423184 4185 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4213
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1377-1604 |
9.80e-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: 54.15 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1377 KFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQ 1456
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1457 KRSIQEELQHLRQSSEAEIQAKARQVEAAE---------RSRLRIEEEIRVVRLQLETTERQRggAEGELQALRARAEEA 1527
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQdekaerdelRAKLYQEEQERKERQKEREEAEKK--ARQRQELQQAREEQI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1528 EAQKRQAQEEAER--------------LRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERR 1593
Cdd:pfam13868 246 ELKERRLAEEAEReeeefermlrkqaeDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEA 325
|
250
....*....|.
gi 2124423184 1594 LRQAEAERARQ 1604
Cdd:pfam13868 326 ERRERIEEERQ 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1734-2134 |
9.84e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1734 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH--EAAAATQKRQELEAELAKVRAEMEvlla 1811
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1812 sKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLK 1891
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1892 TEAEIALKEKEAENERLRRL---------------AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVE 1956
Cdd:COG4717 229 LEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1957 DTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQrrreaeerVQKSL 2036
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--------LAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2037 AAEEEAARQRKAALEEVERLKAKVEEA-RRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQ 2115
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410
....*....|....*....
gi 2124423184 2116 SMLERLRGEAEAARRAAEE 2134
Cdd:COG4717 461 ELEQLEEDGELAELLQELE 479
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1388-1572 |
1.06e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1388 EEERLAEQQR--AEERERLaaveAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQ 1465
Cdd:PRK09510 93 QQKQAAEQERlkQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1466 HLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqlettERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqv 1545
Cdd:PRK09510 169 KKAEAEAAKKAAAEAKKKAEAEAAAKAAAE-----------AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA------- 230
|
170 180
....*....|....*....|....*..
gi 2124423184 1546 qdETQRKRQAEAELAVRVKAEAEAARE 1572
Cdd:PRK09510 231 --AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1723-2122 |
1.07e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1800
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1801 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEED--------------- 1865
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1866 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASE 1945
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1946 SELERQKGLVE-DTLRQRRQVEEEILALKVSFEKAAAGKAElelelgRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQR 2024
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2025 RREAEERVQKSLAAEEEAARQRKAALEEveRLKAKVEEARRLRERAEQesarqLQLAQDAAQKRLQAEEKahafavqqke 2104
Cdd:COG4717 419 EELLEALDEEELEEELEELEEELEELEE--ELEELREELAELEAELEQ-----LEEDGELAELLQELEEL---------- 481
|
410
....*....|....*...
gi 2124423184 2105 qelqqtlqqeqsmLERLR 2122
Cdd:COG4717 482 -------------KAELR 486
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1673-2073 |
1.10e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1673 LERWQLKANEA------LRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGT 1746
Cdd:COG4717 104 LEELEAELEELreelekLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1747 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE---------------LAKVRAEMEVLLA 1811
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleaaaleerlkearlLLLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1812 SKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLK 1891
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1892 TEAEIALKEKEAENERLRRLAEDEAFQRRR--LEEQAAQHKADIEERLAQLRKAseSELERQKGLVEDTLRQRRQVEEEI 1969
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEEL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1970 LalkvsfekAAAGKAELELELGRIRSNAEDTlrskeQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAA 2049
Cdd:COG4717 422 L--------EALDEEELEEELEELEEELEEL-----EEELEELREELAELEAELEQLEEDGELAELLQELEELKAELREL 488
|
410 420
....*....|....*....|....
gi 2124423184 2050 LEEVERLKAKVEEARRLRERAEQE 2073
Cdd:COG4717 489 AEEWAALKLALELLEEAREEYREE 512
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1405-1626 |
1.13e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1405 AAVEAALEKQRQ----LAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR 1480
Cdd:TIGR02794 46 GAVAQQANRIQQqkkpAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1481 QVEAAERSRlriEEEIRVVRLQLETTERQrggAEGElqalrARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1560
Cdd:TIGR02794 126 AKQAAEAKA---KAEAEAERKAKEEAAKQ---AEEE-----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1561 vrvKAEAEAAREKQRAlqaleEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRAS 1626
Cdd:TIGR02794 195 ---KAKAEAAKAKAAA-----EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGA 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1394-1573 |
1.20e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1394 EQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRrmqeEVARREEAAVDAQQQKRSIQEELQHLRqsSEA 1473
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1474 EIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAqkrQAQEEAERLRRQVQDETQRKR 1553
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA---ELDEELAELEAELEELEAERE 166
|
170 180
....*....|....*....|
gi 2124423184 1554 QAEAELAVRVKAEAEAAREK 1573
Cdd:COG1579 167 ELAAKIPPELLALYERIRKR 186
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1734-1891 |
1.33e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.02 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1734 QELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqhEAAAATQKRQELEAELAKVRAemevllAS 1812
Cdd:PTZ00491 647 DSLQKSVQLAiEITTKSQEAAARHQAELLEQEARGRLERQKMHDKA-----KAEEQRTKLLELQAESAAVES------SG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1813 KARAEEESRSTSEKSKQRLEAEASRFRelaEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVLAEKLAAIgEATRLK 1891
Cdd:PTZ00491 716 QSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAKAKELADI-EATKFE 791
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2221-2515 |
1.40e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2221 RQKAQVEQELTTLRLQLeeTDHQKSiLDEE-------------LQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKlkA 2287
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQQA-LDVQqtraiqyqqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATE--E 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2288 RIEAENRaliLRDKDNTQRVLQEEAEKMKHVAEEAARlSVAAQEAarlRELaEEDLAQQRALAEKM---------LKEKM 2358
Cdd:PRK04863 458 LLSLEQK---LSVAQAAHSQFEQAYQLVRKIAGEVSR-SEAWDVA---REL-LRRLREQRHLAEQLqqlrmrlseLEQRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2359 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQEtqgfqrtLEAERQRQLEMSAEAERLKLRVAE-MSRA 2437
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARA 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2438 QA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLRQAIAELEREKEKLKQ-----EA 2508
Cdd:PRK04863 603 PAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQpggseDP 673
|
....*..
gi 2124423184 2509 KLLQLKS 2515
Cdd:PRK04863 674 RLNALAE 680
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1524-1640 |
1.51e-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: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1524 AEEAEAQKRQAQEEAERLRRQvqdETQRKRQAEAELAVRVKaEAEAAREKQRAlqaleefRLQAEEAerrLRQAEAERAR 1603
Cdd:COG2268 212 TEIAIAQANREAEEAELEQER---EIETARIAEAEAELAKK-KAEERREAETA-------RAEAEAA---YEIAEANAER 277
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423184 1604 QVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQE 1640
Cdd:COG2268 278 EVQRQLEIAEREREIELQEKEA--EREEAELEADVRK 312
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1758-2063 |
1.51e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.57 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1758 IRLRA-ETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1830
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1831 LEAEASRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlaeklaaigeatrlkteAEIALKEKEAENERLRR 1910
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1911 LAEDEAFQRRrleeqaaqhkadieerlAQLRKASESELERQKGLVEDTLRQRRQVEEEILAlkvsfeKAAAGKAELELEL 1990
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA------RAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 1991 grIRSNAEDTLRSKEQAELEAMRQRQLAAeeeqrrreaeervQKSLAAEEEAARQRKAALE-EVERLKAKVEEA 2063
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKAAQ-------------QQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1847-2657 |
1.80e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1847 RLRALAEEAKRQRQLAEEDAARQRAEAERVLAeklaaiGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRrrleeQA 1926
Cdd:TIGR00618 53 KLPRRSEVIRSLNSLYAAPSEAAFAELEFSLG------TKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGR-----IL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1927 AQHKADIEERLAQLRKASESELERQKGLvedtlrqrRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 2006
Cdd:TIGR00618 122 AAKKSETEEVIHDLLKLDYKTFTRVVLL--------PQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2007 AELEAMRQR-QLAAEEEQRRREAEERVQKSLAAEEEAARqrkaalEEVERLKAKVEEARRLRERAEQESARQLQLAQDAA 2085
Cdd:TIGR00618 194 GKAELLTLRsQLLTLCTPCMPDTYHERKQVLEKELKHLR------EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2086 Q-KRLQAEEKAHAfavqqkeqelqqtlqqeqsmlerlrgeaeaarraaeeaeeARERAEREAAQSRRQVEEAERLKQSAE 2164
Cdd:TIGR00618 268 RiEELRAQEAVLE----------------------------------------ETQERINRARKAAPLAAHIKAVTQIEQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2165 EQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQK--QAADAEMEKHKKFAEQTLRQKAQVEQElTTLRLQLEETDH 2242
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLQQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2243 QKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKdNTQRVLQEEAEKMKHVAEEA 2322
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA-AITCTAQCEKLEKIHLQESA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2323 ARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQedKEQMAQQLEQE 2402
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR--GEQTYAQLETS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2403 TQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIgekLHRTELATQEKVTLVQTLEIQRQQ 2482
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHALLRK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2483 SDHDAERLRQAIAELEREKEKLKQEAKLLQLKSE---EMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLE 2559
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2560 Q---LFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVR-----------RKQEELQLLEQQRQQQ 2625
Cdd:TIGR00618 701 QcqtLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvlkarteahfNNNEEVTAALQTGAEL 780
|
810 820 830
....*....|....*....|....*....|....*...
gi 2124423184 2626 EKLLAEENQRLRER------LQRLEEEHRAALAHSEEI 2657
Cdd:TIGR00618 781 SHLAAEIQFFNRLReedthlLKTLEAEIGQEIPSDEDI 818
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2345-2668 |
1.84e-06 |
|
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: 54.36 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2345 QQRALAEKMLKEKMQavqeatrlKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLEQETQGfqrTLEAERQR-QLEMSA 2422
Cdd:pfam17380 280 HQKAVSERQQQEKFE--------KMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQA---AIYAEQERmAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2423 EAERLKLRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTELATQEKVTLV-QTLEIQRQQSDHDAERLRQaIAELEREK 2501
Cdd:pfam17380 349 ELERIRQEERKRELERIRQEEIAMEISRMRE-----LERLQMERQQKNERVrQELEAARKVKILEEERQRK-IQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2502 EKLKQEAKllQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLE-QLFQDEVAKAQKLR-----EE 2575
Cdd:pfam17380 423 EQIRAEQE--EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLElEKEKRDRKRAEEQRrkileKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2576 QQRQQKQMEEEKQQ---LVASMEEAR------QRQREAEEgvRRKQEELQLLEQQRQQQEKLLAEENQRL------RERL 2640
Cdd:pfam17380 501 LEERKQAMIEEERKrklLEKEMEERQkaiyeeERRREAEE--ERRKQQEMEERRRIQEQMRKATEERSRLeamereREMM 578
|
330 340
....*....|....*....|....*...
gi 2124423184 2641 QRLEEEHRaalAHSEEIAASQATAVKAL 2668
Cdd:pfam17380 579 RQIVESEK---ARAEYEATTPITTIKPI 603
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3968-4005 |
1.88e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 1.88e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2124423184 3968 QKFLEGTSCIAGVFVDSTKERLSVYQAMKKGIIRPGTA 4005
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
48-193 |
2.13e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 50.43 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 48 GWTLRGGSDAALSLGgdmdpsraIQHEISslkdERDRVqkkTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNL 118
Cdd:cd21323 2 GITAIGGTSAISSEG--------TQHSYS----EEEKV---AFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILL 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 119 ISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 193
Cdd:cd21323 67 CKMINLSQPDTIDErainKKKLTPFTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2845-2881 |
2.17e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.17e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2124423184 2845 IRLLEAQIATGGVIDPVHSHRVPVEVAYQRGYFDEEM 2881
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2206-2667 |
2.20e-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: 54.46 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2206 DAEMEKHKKFAEQTLRQKAQVEQELTT--------LRLQLEETDHQKSILDEELQRLKAEV---TEAARQRSQVEEELFS 2274
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2275 LRvqmeeLGKLKARIeaeNRALILRDKDNTQRVLQEEAEKMKHVAEEA-ARLSVAAQEAARLRELAEEDLAQQRaLAEKM 2353
Cdd:pfam12128 444 SR-----LGELKLRL---NQATATPELLLQLENFDERIERAREEQEAAnAEVERLQSELRQARKRRDQASEALR-QASRR 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2354 LKEKMQAVQEATR------------LKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLE 2419
Cdd:pfam12128 515 LEERQSALDELELqlfpqagtllhfLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2420 MSAEAERLKLRVAEMSRA-------QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLR 2491
Cdd:pfam12128 595 WAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALA 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2492 QAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLE-------QLFQD 2564
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRsgakaelKALET 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2565 EVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLE 2644
Cdd:pfam12128 755 WYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLI 834
|
490 500
....*....|....*....|....
gi 2124423184 2645 EEHRAALAHSE-EIAASQATAVKA 2667
Cdd:pfam12128 835 ADTKLRRAKLEmERKASEKQQVRL 858
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
60-194 |
2.34e-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: 50.44 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 60 SLGGDMD-PSRAIQHEISslkderdRVQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDS 129
Cdd:cd21325 5 ALGGTSElSSEGTQHSYS-------EEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 130 LPR----EKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 194
Cdd:cd21325 78 IDErainKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1404-1816 |
2.40e-06 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 54.09 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1404 LAAVEAALEKQRQLAEAHAQAKaqaeqEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE----------- 1472
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVAR-----EDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1473 --------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1544
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1545 VQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKR 1624
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1625 ASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1704
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1705 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1784
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 2124423184 1785 AAAATQKRQELEAELAKVRAEMEVLLASKARA 1816
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1752-1847 |
2.41e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 54.19 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1752 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1831
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 2124423184 1832 EAEASRFrELAEEAAR 1847
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2324-2490 |
2.60e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2324 RLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELAQEQARRLQ-----EDKEQM 2395
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNELQKLEKRLLQkeenlDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2396 AQQLEQETQGFQRTLEAERQRQLEMSAEAERLK-------LRVAEMSRAQAR----------AEEDAQRFRKQAEEIGEk 2458
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKeillekveeeARHEAAVLIKEIEEEAK- 183
|
170 180 190
....*....|....*....|....*....|...
gi 2124423184 2459 lhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2490
Cdd:PRK12704 184 ----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1351-1639 |
2.61e-06 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 53.68 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1351 SESVIQEyvDLRTRYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAAVEAALEKQRQL-----AEAHAQ-A 1424
Cdd:pfam15450 219 AESSLRE--ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1425 KAQAEQE-AQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVE------AAERSRLRIEEEir 1497
Cdd:pfam15450 295 KGQLEESqAGELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1498 VVRLQLETTERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAarekqra 1576
Cdd:pfam15450 373 TLGLKLSEAKKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKA------- 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1577 lqalEEFRLQAeeaerrLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1639
Cdd:pfam15450 446 ----REFEVEA------MRQELAALLSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2326-2604 |
2.68e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 54.07 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2326 SVAAQEAARLRELAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLEqETQG 2405
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLA-AISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2406 FQRTLEAERQRQLEMSAEAERlklrvaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2485
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2486 DAE---RLRQAIAE--LEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSflsekDTLLQRErfiEQEKAKLEQ 2560
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKS-----EAGVAQG---EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2124423184 2561 LFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQR-QREA 2604
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2306-2662 |
2.94e-06 |
|
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: 53.82 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2306 RVLQEEAEKMKHVAEEAARLSVAAQEaaRLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2385
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEE--LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2386 RRLQEDKEQMAQQLEQETQGFQRTLE---AERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2462
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKenkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2463 ELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQ-EAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEK 2541
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2542 DTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEgvrrkqeelqlleQQ 2621
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE-------------DL 473
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2124423184 2622 RQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQA 2662
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1462-1834 |
3.78e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1462 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1541
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1542 RRQVQDETQRKRQAEAELAVRVKA-EAEAAREKQRALQA---LEEFRLQAEEAERRLRQAEAERaRQVQVALETAQ---R 1614
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLEReteLERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEeelR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1615 SAEVELQSKRASFAEKTAQLERtLQEEhvaVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1694
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQ-LQDT---ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1695 QQKSlaqaeaekqkeeaerearrRGKAEEQAVRQR--ELAEQELEKQRQLAEGTAqqRLAAEQELIRLRAETEQGEQQRq 1772
Cdd:pfam07888 265 AQRD-------------------RTQAELHQARLQaaQLTLQLADASLALREGRA--RWAQERETLQQSAEADKDRIEK- 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1773 lLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAE 1834
Cdd:pfam07888 323 -LSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASlrvAQKEKEQLQAE 386
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3173-3209 |
3.80e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.80e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2124423184 3173 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKET 3209
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1362-1495 |
4.38e-06 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 51.52 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1362 RTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQeaqelqR 1437
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEL------L 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1438 RMQEEVARREEAAVDAQQQKRSIQEEL----QHLRQSSEAEIQAKARQVEAA-----ERSRLRIEEE 1495
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKEERENedlnlEQLREKANEE 196
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2208-2645 |
5.13e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2208 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA------EVTEAARQRSQVEEELFSLRVQMEE 2281
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2282 LGKLKARIEAENRALilrdkdntQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAE--EDLAQQRALAEKMLKEKmq 2359
Cdd:PRK03918 312 IEKRLSRLEEEINGI--------EERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2360 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEM 2434
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2435 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKL-KQEAKL 2510
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2511 LQLKSEemqtvqqeqllqetqalqqsfLSEKDTLLQRERFIEQEKAKLEQlfqdEVAKAQKLREEQQRQQKQMEEEKQQL 2590
Cdd:PRK03918 542 KSLKKE---------------------LEKLEELKKKLAELEKKLDELEE----ELAELLKELEELGFESVEELEERLKE 596
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 2591 VASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEE 2645
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1345-1538 |
5.18e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1345 PKVQSGSESVIQEYVDLRTRYSELTTltSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQ- 1423
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1424 -AKAQAEQEAQELQRRMQEEVARREE---AAVDAQQQKRS----IQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEE 1495
Cdd:COG3206 263 pVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAAlraqLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2124423184 1496 IRV---VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1538
Cdd:COG3206 343 LAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1346-1560 |
5.21e-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: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1346 KVQSGSESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHA 1422
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1423 QAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQkrsiQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrvvrlq 1502
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALK------ 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1503 letTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1560
Cdd:COG4942 195 ---AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1723-1947 |
5.45e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1799
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1800 AKVRAEMEVLLASKARAEEESrstsekskQRLEAEAsrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1879
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRA--------QLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1880 klaAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESE 1947
Cdd:COG3206 318 ---LEAELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1008-1547 |
5.54e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1008 QQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIA-EQQKAQAEVEGLGKGVARLS 1086
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCkELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1087 AEAEKVLAlpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRSTHGAEEVLKAHEEQLKEAQAVpaTLPE 1166
Cdd:TIGR00618 421 DLQGQLAH----------AKKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1167 LEATKAALKKLRAQAEAQQPMFDALR---------DELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQT 1237
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1238 DLRQRELEQLGRQLRYYRESADPLGAWLQDAKR---RQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQrfa 1314
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--- 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1315 kQYINAIKDYELQLvTYKAQLEPVASPAKKPKVQsgSESVIQEYVDLRTRYSELTTLTSQyIKFISETLRRMEEEERLAE 1394
Cdd:TIGR00618 643 -LKLTALHALQLTL-TQERVREHALSIRVLPKEL--LASRQLALQKMQSEKEQLTYWKEM-LAQCQTLLRELETHIEEYD 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1395 QQRAEERERLAAVEAALEKQRQLA-----EAHAQAKAQAEQEAQELQRRMQEEVA-----RREEAAVDAQQQKRSIQEEL 1464
Cdd:TIGR00618 718 REFNEIENASSSLGSDLAAREDALnqslkELMHQARTVLKARTEAHFNNNEEVTAalqtgAELSHLAAEIQFFNRLREED 797
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1465 QHLRQSSEAEIQAKARQVEAAersRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1544
Cdd:TIGR00618 798 THLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
...
gi 2124423184 1545 VQD 1547
Cdd:TIGR00618 875 SDK 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2248-2454 |
5.77e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2248 DEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALIlRDKDNTQRVLQEEAEKMKHVAEEAARLSV 2327
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2328 AAQEAARLRELAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2399
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 2400 EQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2454
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1368-1605 |
5.79e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1368 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAAVEAALEKQRQlAEAHAQAKAQAEQEAQELQRrMQEEVAR 1445
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1446 REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRggAEGELQALRAR-A 1524
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1525 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEaAREKQRALQALEEfrlQAEEAERRLRQAEAERARQ 1604
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARE---LYESLLQRLEEARLAEALT 384
|
.
gi 2124423184 1605 V 1605
Cdd:COG3206 385 V 385
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1442-1607 |
5.80e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.84 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1442 EVARR----EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRggaegel 1517
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1518 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEtqrkrqaeaelavrvKAEAEAAREKQRALQALEEfRLQAEEAERRLRQ 1596
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 2124423184 1597 AEAERARQVQV 1607
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1389-1644 |
5.86e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1389 EERLAEQQRaEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE--EVARREEAAVDAQQQKrsiQEELQH 1466
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAElkEELRQSREKHEELEEK---YKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1467 LRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleTTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1546
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIK-------TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1547 DETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEA--ERARQVQVALETAQRSAEvelqSKR 1624
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAllEELRSLQERLNASERKVE----GLG 257
|
250 260
....*....|....*....|
gi 2124423184 1625 ASFAEKTAQLERTLQEEHVA 1644
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQA 277
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1406-1579 |
6.02e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1406 AVEAALEKQRQLAEAHAQAkAQAEQEAQELQRR---MQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQV 1482
Cdd:COG1579 1 AMPEDLRALLDLQELDSEL-DRLEHRLKELPAElaeLEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1483 EAAER--SRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELa 1560
Cdd:COG1579 76 KKYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL- 154
|
170
....*....|....*....
gi 2124423184 1561 vrvKAEAEAAREKQRALQA 1579
Cdd:COG1579 155 ---EAELEELEAEREELAA 170
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1380-1601 |
6.09e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1380 SETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAK----------AQAEQEAQELQRRMQEEVARREEA 1449
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKesvaerkennEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1450 AV----------DAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQA 1519
Cdd:pfam02029 132 ETeirekeyqenKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1520 ---------------------LRARAEEAEAQKrQAQEEAERLRRQVQD------ETQRKRQAEAELAVrvkAEAEAARE 1572
Cdd:pfam02029 212 geeevtklkvttkrrqgglsqSQEREEEAEVFL-EAEQKLEELRRRRQEkeseefEKLRQKQQEAELEL---EELKKKRE 287
|
250 260
....*....|....*....|....*....
gi 2124423184 1573 KQRALQALEEFRLQAEEAERRLRQAEAER 1601
Cdd:pfam02029 288 ERRKLLEEEEQRRKQEEAERKLREEEEKR 316
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2223-2606 |
6.28e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2223 KAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIE--AENRALILR 2299
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEdlRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2300 DKDNtqrvLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQE----ATRLKAEAELLQ 2375
Cdd:PRK02224 273 EREE----LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2376 QQKELAQEQARRLQEDkeqmAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEI 2455
Cdd:PRK02224 349 EDADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2456 GEKLH--RTELAT-QEKVTLVQTL-----------EIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTV 2521
Cdd:PRK02224 425 REREAelEATLRTaRERVEEAEALleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2522 QQEQllqetqalqqsflSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEqqrqqkqmeeeKQQLVASMEEARQRQ 2601
Cdd:PRK02224 505 VEAE-------------DRIERLEERREDLEELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAA 560
|
....*
gi 2124423184 2602 REAEE 2606
Cdd:PRK02224 561 AEAEE 565
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2413-2737 |
6.33e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2413 ERQRQLEMSAEA-ERLKLRVAEMSR------AQARAEEDAQRFRKQAEEI------------GEKLHRTELATQEKVTLV 2473
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERqlksleRQAEKAERYKELKAELRELelallvlrleelREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2474 QTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQtvqqeqllQETQALQQSFLSEKDTLLQRERFIEQ 2553
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE--------QQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2554 EKAKLEQLfQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRkqeeLQLLEQQRQQQEKLLAEEN 2633
Cdd:TIGR02168 328 LESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2634 QRLRERLQRLEEEHRAALAHSEEIAASQATAVKALPNGRDApDGPATEAEPEHAFDGLRQKVPAQRLQEvgilsTEELQR 2713
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE-ELEEELEELQEELERLEEALEELREEL-----EEAEQA 476
|
330 340
....*....|....*....|....
gi 2124423184 2714 LVQGRTTVAELAQREDVRRYLQGR 2737
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQEN 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2200-2663 |
6.34e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2200 RQKQAADAEMEKHkkfaEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfslrvqm 2279
Cdd:PRK02224 234 ETRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2280 eELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAA----QEAARLRELAEEDLAQQRALAEKM-- 2353
Cdd:PRK02224 303 -GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddleERAEELREEAAELESELEEAREAVed 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2354 -------LKEKMQAVQEA--------TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE---------------QET 2403
Cdd:PRK02224 382 rreeieeLEEEIEELRERfgdapvdlGNAEDFLEELREERDELREREAELEATLRTARERVEeaealleagkcpecgQPV 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2404 QGFQR--TLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE------DAQRFRKQAEEIGEKLHRTELATQEKVTLVQT 2475
Cdd:PRK02224 462 EGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2476 LEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQlksEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERfieqek 2555
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN---SKLAELKERIESLERIRTLLAAIADAEDEIERLR------ 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2556 AKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQqlvASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLA----- 2630
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDE---ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGavene 689
|
490 500 510
....*....|....*....|....*....|....
gi 2124423184 2631 -EENQRLRERLQRLEEEHRAALAHSEEIAASQAT 2663
Cdd:PRK02224 690 lEELEELRERREALENRVEALEALYDEAEELESM 723
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
196-303 |
6.52e-06 |
|
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: 48.26 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 196 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 274
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 2124423184 275 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 303
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1454-1640 |
6.98e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1454 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETT--ERQRGGAEGELQALRARAEEAEAQK 1531
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKllLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1532 RQAQEEAERLRRQVQD-----ETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEfrlQAEEAERRLRQAEAERARQVQ 1606
Cdd:COG3206 243 AALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA---QIAALRAQLQQEAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|....
gi 2124423184 1607 VALETAQRSAEvELQSKRASFAEKTAQLERTLQE 1640
Cdd:COG3206 320 AELEALQAREA-SLQAQLAQLEARLAELPELEAE 352
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2005-2521 |
7.30e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 52.45 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2005 EQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA------ARQRKAALEEVERLKAKVEEARRLRERAEQESARQL 2078
Cdd:pfam07111 63 QQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmeldalAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQREL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2079 QLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVE---- 2154
Cdd:pfam07111 143 EEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTlves 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2155 --------------------EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA-EMEKHK 2213
Cdd:pfam07111 223 lrkyvgeqvppevhsqtwelERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSlEPEFPK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2214 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR-----------SQVEEELFSLR-VQMEE 2281
Cdd:pfam07111 303 KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQailqralqdkaAEVEVERMSAKgLQMEL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2282 LGKLKARIEAENRA--------LILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKM 2353
Cdd:pfam07111 383 SRAQEARRRQQQQTasaeeqlkFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLR 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2354 LK-----------------EKMQAVQEATRLKAE----AELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRT--- 2409
Cdd:pfam07111 463 QEscpppppappvdadlslELEQLREERNRLDAElqlsAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESlas 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2410 ----LEAERQRQLEMSAEAERLKLRVAEMSRA-----QARAEEDAQRFRKQAEEIGEKLHRTEL---------------A 2465
Cdd:pfam07111 543 vgqqLEVARQGQQESTEEAASLRQELTQQQEIygqalQEKVAEVETRLREQLSDTKRRLNEARReqakavvslrqiqhrA 622
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2466 TQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKE----KLKQEAKLLQLKSEEMQTV 2521
Cdd:pfam07111 623 TQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNlmlaTLQQEGLLSRYKQQRLLAV 682
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1137-1696 |
8.23e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.50 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1137 IRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAAL--KKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGER-- 1212
Cdd:PRK10246 250 TRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRar 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1213 --------------------------------DVEVERWRERVAQL------LERWQAVLAqTDLRQRE----------- 1243
Cdd:PRK10246 330 irhhaakqsaelqaqqqslntwlaehdrfrqwNNELAGWRAQFSQQtsdreqLRQWQQQLT-HAEQKLNalpaitltlta 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1244 ------LEQLGRQlRYYRESADPLGAWLQDAKRRQEQIQAMVladSRAVREQLRQEKALLEEIERHGEKVEE-------C 1310
Cdd:PRK10246 409 devaaaLAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQVAI---QNVTQEQTQRNAALNEMRQRYKEKTQQladvktiC 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1311 QRFAKqyinaIKDyelqLVTYKAQLEPvASPAkkPKVQSGSESVIQEYVDLRtryselttltsqyikfISETLRRMEEEE 1390
Cdd:PRK10246 485 EQEAR-----IKD----LEAQRAQLQA-GQPC--PLCGSTSHPAVEAYQALE----------------PGVNQSRLDALE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1391 RLAEQQRAEERERLAAVEaALEKQRQLAEAHAQAKAQAEQ----EAQEL------QRRMQEEVARREEAAVDAQQQKRSI 1460
Cdd:PRK10246 537 KEVKKLGEEGAALRGQLD-ALTKQLQRDESEAQSLRQEEQaltqQWQAVcaslniTLQPQDDIQPWLDAQEEHERQLRLL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1461 QEelQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEEIRVVRLQLEtterqrggAEGELQA-LRARAEEAeAQKRQAQEEA 1538
Cdd:PRK10246 616 SQ--RHELQGQIAAHNQQIIQYQQQiEQRQQQLLTALAGYALTLP--------QEDEEASwLATRQQEA-QSWQQRQNEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1539 ERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQaEAERARQVQVALETAqrsaev 1618
Cdd:PRK10246 685 TALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVL-EAQRLQKAQAQFDTA------ 757
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1619 eLQSKRasFAEKTAQLERTLQEEhvAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQ 1696
Cdd:PRK10246 758 -LQASV--FDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQE 830
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2311-2470 |
8.31e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.80 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2311 EAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2390
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2391 DKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2470
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1383-1863 |
8.65e-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: 52.05 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1383 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAeahaQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1462
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1463 ELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIR--VVRLQLET-------TERQRGGAEGELQALRARAEEA 1527
Cdd:pfam05557 133 ELEELQERLDllkakaSEAEQLRQNLEKQQSSLAEAEQRIKelEFEIQSQEqdseivkNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1528 EAQKRQAQEEAERLRRQVQDETQRKRQAEaelavrvKAEAEAAR---EKQRALQALEEFRLQAEEAERRLRQAEAERARQ 1604
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLEREE-------KYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1605 VQValetaqRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL-----ERWQLK 1679
Cdd:pfam05557 286 EQL------QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkERDGYR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1680 AN-EALRLRLQAEEVAQQKSLAQAEAE----KQKEEAEREARRRGKAEEQAVRQRELA---EQELEKQRQlAEGTAQQRL 1751
Cdd:pfam05557 360 AIlESYDKELTMSNYSPQLLERIEEAEdmtqKMQAHNEEMEAQLSVAEEELGGYKQQAqtlERELQALRQ-QESLADPSY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1752 AAE------QELIRLRAETEQGEQQRQLLEEELAR--------------LQHEAAAATQKRQELEAELAKVRAEMEvlla 1811
Cdd:pfam05557 439 SKEevdslrRKLETLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIE---- 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1812 skaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEA-KRQRQLAE 1863
Cdd:pfam05557 515 ---RLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAeLKNQRLKE 564
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
992-1544 |
8.70e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 992 DRLQAEREYGSCSHHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLRLPLDK---EPARECAQRIAE 1067
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLRRELDDrnmEVQRLEALLKAM 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1068 QQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTLGKLEQVrslsaiyLEKLKTISLVIRSTHGAEEVL 1147
Cdd:pfam15921 439 KSECQGQMERQMAAIQGKNESLEKV----------SSLTAQLESTKEMLRKV-------VEELTAKKMTLESSERTVSDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1148 KAHEEQLKEAqavpatlpeLEATKAALKKLRAQAEAQQPMFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRERVA 1224
Cdd:pfam15921 502 TASLQEKERA---------IEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1225 QLLE-------RWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALL 1297
Cdd:pfam15921 573 NMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIK 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1298 EEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyik 1377
Cdd:pfam15921 653 QERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN---- 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1378 fiseTLRRMEEEERlaeqqraeererlAAVEAALEKQRQLAEAHAQAKAqaeqeaqelqrrMQEEVARREEAAVDAQQQK 1457
Cdd:pfam15921 714 ----TLKSMEGSDG-------------HAMKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNANKEK 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1458 RSIQEELQHLRQssEAEIQAKARQVEAAERSRLRIEEEirvvRLQLETTERQRGGAEGELQAlrarAEEAEAQKRQAQEE 1537
Cdd:pfam15921 765 HFLKEEKNKLSQ--ELSTVATEKNKMAGELEVLRSQER----RLKEKVANMEVALDKASLQF----AECQDIIQRQEQES 834
|
....*..
gi 2124423184 1538 AeRLRRQ 1544
Cdd:pfam15921 835 V-RLKLQ 840
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1404-1498 |
9.05e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 52.26 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1404 LAAVEAALEKQRQLAEAHAQAKAQAEQEAqelqRRMQEEVARREEAAVDAQQQKRSIQEELQHLR-QSSEAEIQAKARQV 1482
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 2124423184 1483 EAAERSRLRI---EEEIRV 1498
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1517-1791 |
1.04e-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: 51.30 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1517 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQAleefrlQAEEAERRLRQ 1596
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQ------ELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1597 AEAERARqvqvaletaqrsAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERW 1676
Cdd:COG4942 88 LEKEIAE------------LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1677 QLKANEALRLRLQAEEVAQQKSLAQaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEgtaqqrlaAEQE 1756
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALL--------------------AELEEERAALEALKAERQKLLAR--------LEKE 207
|
250 260 270
....*....|....*....|....*....|....*
gi 2124423184 1757 LIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1791
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1393-1836 |
1.10e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.45 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1393 AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1472
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1473 AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1552
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1553 RQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1632
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1633 QLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE 1712
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1713 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKR 1792
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2124423184 1793 QELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAS 1836
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALAS 527
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2288-2453 |
1.10e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.41 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2288 RIEAENRALILRDKdntqRVLQEEAEKMKHVAE-----EAARLSVAAQEAARLRELAEEDLAQQ--RALAEKMLKEKMQA 2360
Cdd:COG2268 199 RDARIAEAEAERET----EIAIAQANREAEEAEleqerEIETARIAEAEAELAKKKAEERREAEtaRAEAEAAYEIAEAN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2361 VQEATRLKAEAELLQQQKELAqeQARRLQEDKEQMAQQLEQetqgfqrtLEAERQRQLEmSAEAErlklrvAEMSRAQAR 2440
Cdd:COG2268 275 AEREVQRQLEIAEREREIELQ--EKEAEREEAELEADVRKP--------AEAEKQAAEA-EAEAE------AEAIRAKGL 337
|
170
....*....|...
gi 2124423184 2441 AEedAQRFRKQAE 2453
Cdd:COG2268 338 AE--AEGKRALAE 348
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3392-3427 |
1.13e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.13e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2124423184 3392 LLQGSGCLAGIYLEESKEKVTIYEAMRRGLLRPSTA 3427
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3970-4008 |
1.28e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.28e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 3970 FLEGTSCIAGVFVDSTKERLSVYQAMKKGIIRPGTAFEL 4008
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
83-182 |
1.30e-05 |
|
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: 47.27 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 83 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 158
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 2124423184 159 LVNIRNDDIADGNPKLTLGLIWTI 182
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3392-3430 |
1.36e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.36e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 3392 LLQGSGCLAGIYLEESKEKVTIYEAMRRGLLRPSTATVL 3430
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2319-2770 |
1.41e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 51.51 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2319 AEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2398
Cdd:COG4995 10 LAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2399 LEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEI 2478
Cdd:COG4995 90 LAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2479 QRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKL 2558
Cdd:COG4995 170 LALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2559 EQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRE 2638
Cdd:COG4995 250 LAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2639 RLQRLEEEHRAALAHSEEIAASQATAVKALPNGRDAPDGPATEAEPEHAFDGLRQKVPAQRLQEVGILSTEELQRLVQGR 2718
Cdd:COG4995 330 LALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLL 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 2719 TTVAELAQREDVRRYLQGRSSIAGLLLKP--ANEKLSIYTALRRQLLSPGTALI 2770
Cdd:COG4995 410 RLLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1384-1557 |
1.43e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1384 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAE----QEAQELQRRMQEEVARreEAAVDAQQQKRS 1459
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEerqrQEEEERKQRLQLQAAQ--ERARQQQEEFRR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1460 IQEELQHLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEae 1539
Cdd:pfam15709 431 KLQELQRKKQQEEAE--------RAEAEKQRQKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE-- 496
|
170
....*....|....*...
gi 2124423184 1540 rlRRQVQDETQRKRQAEA 1557
Cdd:pfam15709 497 --RRQKEEEAARLALEEA 512
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
663-753 |
1.46e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.55 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 663 FVAAATKELMWLSEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEIQNTGDRLLREDHPARPTVESFQAAL 742
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEEL 82
|
90
....*....|.
gi 2124423184 743 QTQWSWMLQLC 753
Cdd:smart00150 83 NERWEELKELA 93
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1720-1936 |
1.48e-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: 51.76 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQE 1794
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEESRAVTKELTTLAQGLDA 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1795 LEAELAKV-------RAEMEVLLasKARAEEESRSTSEKSKQRLEAEASRF----RELAEEAARLRALAEEAKRQRQLAE 1863
Cdd:NF012221 1632 LDSQATYAgesgdqwRNPFAGGL--LDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAGVAQGEQNQANAE 1709
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1864 EDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1936
Cdd:NF012221 1710 QDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESDKPNR 1782
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2299-2454 |
1.49e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2299 RDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2375
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 2376 QQKELAQEQARRLQEDKEqmaQQLEQETQgfqrtLEAERQRQLEMsAEAERLKLRvAEMSRAQARAEEDAQRFRKQAEE 2454
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQ---RQKELEMQ-----LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLEAEERRQKEEE 503
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1311-1642 |
1.50e-05 |
|
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: 51.55 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1311 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRY-SELTTLTSQyikfiSETLRRMEEE 1389
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1390 ERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQ----------ELQRRMQE-EVARREEAAVDAQQQKR 1458
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyktlELEIAESDvEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1459 SIQEELQHLRQSSEAEiQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEA----EAQKRQA 1534
Cdd:NF033838 201 RDEEKIKQAKAKVESK-KAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGvlgePATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1535 QEEAERLRRQVQDET-------QRKRQAEAELAV-RVKAEAEAAREKQR---ALQALEEFRLQAEEAERRLRQAEA---- 1599
Cdd:NF033838 280 ENDAKSSDSSVGEETlpspslkPEKKVAEAEKKVeEAKKKAKDQKEEDRrnyPTNTYKTLELEIAESDVKVKEAELelvk 359
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2124423184 1600 ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1642
Cdd:NF033838 360 EEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1729-2451 |
1.52e-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: 51.66 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1729 RELAEQELEKQRQLAEGTAQQRLAAE---QELIRLRAETEQGEQQRQLLEEELARLQHEA--AAATQKRQELEAELAKVR 1803
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHFRSlgSAISKILRELDTEISYLK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1804 AEM----EVLLASKARAEEESRSTSEKSKQRLEAEASR----FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1875
Cdd:pfam15921 238 GRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLISEheveITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1876 VLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErlaQLRKASESELERQKGLV 1955
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD---QLQKLLADLHKREKELS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1956 EDTLRQRRQVEEEIlalkvsfekaaaGKAeleLELGRIRSNAEDtlRSKEQAELEAMRQrqlaaeeeqrrrEAEERVQKS 2035
Cdd:pfam15921 395 LEKEQNKRLWDRDT------------GNS---ITIDHLRRELDD--RNMEVQRLEALLK------------AMKSECQGQ 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2036 LAAEEEAARQRKAALEEVERLKAKVEEARR-LRERAEQESARQLQLAqdaAQKRLQAEEKAhafAVQQKEQELQQTLQQE 2114
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMTLE---SSERTVSDLTA---SLQEKERAIEATNAEI 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2115 QSMLERLRgeaeaarraaeeaeeareraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLrkeaeqeaaRRAQA 2194
Cdd:pfam15921 520 TKLRSRVD----------------------------LKLQELQHLKNEGDHLRNVQTECEALKLQM---------AEKDK 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2195 EQAALRQKQAADAEM-EKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV----E 2269
Cdd:pfam15921 563 VIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagS 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2270 EELFSLRVQMEELGKLKARIEAENRAL--ILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQ---EAAR--LRELAEED 2342
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQselEQTRntLKSMEGSD 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2343 -------LAQQRALAEK-----MLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRT 2409
Cdd:pfam15921 723 ghamkvaMGMQKQITAKrgqidALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 2124423184 2410 leaeRQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2451
Cdd:pfam15921 803 ----KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2293-2665 |
1.63e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2293 NRALILRDKDNTQRvlQEEAEKMKHVAEEAARLSVAAQEAARLRElAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2367
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEELSA-RESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2368 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGF--QRTLEAERQRQLEMSAEAERLkLRVAE 2433
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2434 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQL 2513
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2514 KSEEMQtvqqeqllqetqalqqsflsekdtlLQRERFIEQEKAKLEQLFQdEVAKAQKLREEQQRQQKQMEEEKQQLVAS 2593
Cdd:COG3096 505 RSQQAL-------------------------AQRLQQLRAQLAELEQRLR-QQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 2594 MEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQR------LRERLQRLEEEHRAALAHSEEIAASQATAV 2665
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTAAMQQLL 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1559-1807 |
1.90e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1559 LAVRVKAEAEAAREKQRALQALEEfRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTL 1638
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1639 QEEHVAVAQLREEAERRAQQQAEAerareeaerelerWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR 1718
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRAL-------------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1719 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlaaeqeliRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1798
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERA--------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*....
gi 2124423184 1799 LAKVRAEME 1807
Cdd:COG4942 229 IARLEAEAA 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1418-1633 |
2.03e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1418 AEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERsrlRIEEEIR 1497
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1498 VVRLQLETTERQrGGAEGELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDETQRKRQAEA 1557
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1558 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1633
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
60-193 |
2.06e-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: 47.31 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 60 SLGGDMDPSRA-IQHEISslkderdRVQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDS 129
Cdd:cd21324 5 AIGGTSEQSSAgTQHSYS-------EEEKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDT 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 130 LPR----EKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 193
Cdd:cd21324 78 IDErtinKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1811-2010 |
2.13e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1811 ASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLAEKLAAIGEATRL 1890
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1891 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIL 1970
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2124423184 1971 ALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 2010
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1504-1641 |
2.33e-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: 49.84 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1504 ETTERQRGGAEGELQALRARAEEAEAQKRQAQEeaerlrRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF 1583
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK------QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1584 RLQAEEAERRlRQAEAERARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1641
Cdd:TIGR02794 124 AKAKQAAEAK-AKAEAEAERK---AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEA 177
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
81-189 |
2.49e-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: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 81 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 151
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 2124423184 152 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 189
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1415-1542 |
2.56e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1415 RQLAEAHAQAKAQ-----AEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSR 1489
Cdd:COG1566 79 TDLQAALAQAEAQlaaaeAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAAL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1490 LRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1542
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2199-2501 |
2.63e-05 |
|
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: 50.07 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2199 LRQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQksildeeLQRLKAEVTEAARQRSQVEEELFSLRVQ 2278
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2279 MEELGKLKARIEAENRALILRDKDNTQRVLQEEAEkmkhvaeeaarlsVAAQEAARLRELAEEDLAQQRALAEKM-LKEK 2357
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2358 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLEQETQGFQRT---LEAERQRQLEMSAEAERLKLRVAEM 2434
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 2435 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLRqaiAELEREK 2501
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLK---EELQRER 384
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1394-1617 |
2.78e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 49.98 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1394 EQQRAEERERLAAveaalEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE---ELQHLRQS 1470
Cdd:PRK07735 3 PEKDLEDLKKEAA-----RRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAakaKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1471 SEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE-----AEAQKRQAQEEAERLRRQV 1545
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAaakakAAALAKQKREGTEEVTEEE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 1546 QDETQRKRQAEAELAVRVKAeaeAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1617
Cdd:PRK07735 158 EETDKEKAKAKAAAAAKAKA---AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQG 226
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1689-1865 |
2.79e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1689 QAEEVAQQKslaQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1764
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1765 EQGEQQRQLLEEELArlQHEAAAATQKRQELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRfr 1839
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA-- 236
|
170 180
....*....|....*....|....*.
gi 2124423184 1840 elAEEAARLRALAEEAKRQRQLAEED 1865
Cdd:PRK09510 237 --AAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
48-183 |
2.81e-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: 46.89 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 48 GWTLRGGSDAALSLGgdmdpsraIQHeisSLKDErdrvQKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNL 118
Cdd:cd21292 2 GIDAKGGTSEASSEG--------TTH---SYSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILL 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 119 ISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 183
Cdd:cd21292 67 CKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1215-1455 |
2.92e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.25 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1215 EVERWRERVAQLLERWQAVLAQTDLRQREL------EQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVRE 1288
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFdptiadEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1289 QLRQ-----EKALLEEIERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEPVASPAK---------KPKVQSGSESV 1354
Cdd:pfam02029 140 YQENkwsteVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVfldqkrghpEVKSQNGEEEV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1355 IQEYVDLRTRYSELTTL--TSQYIKFISETLRRMEEEERLAEQQRAEERERL------AAVEAAL-----EKQRQLAEAH 1421
Cdd:pfam02029 217 TKLKVTTKRRQGGLSQSqeREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLrqkqqeAELELEElkkkrEERRKLLEEE 296
|
250 260 270
....*....|....*....|....*....|....*...
gi 2124423184 1422 AQAKAQAEQEAQ----ELQRRMQEEVARREEAAVDAQQ 1455
Cdd:pfam02029 297 EQRRKQEEAERKlreeEEKRRMKEEIERRRAEAAEKRQ 334
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2199-2728 |
2.96e-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: 50.74 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2199 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILdeelqRLKAEVTEAARQRSQVEEELFSLRVQ 2278
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2279 MEELGKLKARIEA--ENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAA---RLRELAEE---DLAQQRALA 2350
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2351 EKMLKEKMQAVQEATRLKAEAELlQQQKELAQEQARRLQEDKEQMAQQLEQETQ-----------GFQRTLEAERQ---- 2415
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDL-QGQLAHAKKQQELQQRYAELCAAAITCTAQceklekihlqeSAQSLKEREQQlqtk 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2416 -----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERL 2490
Cdd:TIGR00618 479 eqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2491 RQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQeqllqetqaLQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQ 2570
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN---------ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2571 KLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEE-----------NQRLRER 2639
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQltywkemlaqcQTLLREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2640 LQRLEEEHR-------AALAHSEEIAASQATAVKALPNGRDAPDGPATEAEPEHAFDGLRQKVPAQRLQEVGILSTEELQ 2712
Cdd:TIGR00618 710 ETHIEEYDRefneienASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQF 789
|
570
....*....|....*.
gi 2124423184 2713 RLVQGRTTVAELAQRE 2728
Cdd:TIGR00618 790 FNRLREEDTHLLKTLE 805
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1390-1875 |
3.05e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.04 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1390 ERLAEQQRAEERERlAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ 1469
Cdd:COG3064 2 QEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1470 SSEAEIQAKARQVeAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDET 1549
Cdd:COG3064 81 EAEKAAAEAEKKA-AAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1550 QRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAE 1629
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1630 KTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKE 1709
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1710 EAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAAT 1789
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1790 QKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQ 1869
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLAD 479
|
....*.
gi 2124423184 1870 RAEAER 1875
Cdd:COG3064 480 LLLLGG 485
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1723-2509 |
3.15e-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: 50.49 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR-----LQHEAAAATQKRQELEA 1797
Cdd:pfam05483 98 EAELKQKENKLQENRKIIE-AQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1798 ElakvraemevllaskaraEEESRSTSEKSKQRLEAEASRFRELAEEAARLR-----ALAEEAKRQRQLaEEDAARQRAE 1872
Cdd:pfam05483 177 E------------------REETRQVYMDLNNNIEKMILAFEELRVQAENARlemhfKLKEDHEKIQHL-EEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1873 AERVLAEKLAAIGEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRRLEeQAAQHKADIEERLAQLRKASESELERQK 1952
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESR---DKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1953 GLVED---TLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEeqrrreae 2029
Cdd:pfam05483 314 ALEEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME-------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2030 erVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQDAAQKRLQAEEK-AHAFAVQqkeqe 2106
Cdd:pfam05483 386 --LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeIHDLEIQ----- 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2107 lqqtlqqeqsmlerlrgeaeaarraaeeaeearerAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQ 2186
Cdd:pfam05483 459 -----------------------------------LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2187 EAARRAQAEQAALRQKQaadaEMEKHKKFAEQTLRQKAQVEQELTTLRLQLE--------ETDHQKSILD---EELQRLK 2255
Cdd:pfam05483 504 LTQEASDMTLELKKHQE----DIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqKGDEVKCKLDkseENARSIE 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2256 AEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALilrDKDNTQRVLQEEAEKMKhVAEEAARLSVAAQEAARL 2335
Cdd:pfam05483 580 YEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL---KKKGSAENKQLNAYEIK-VNKLELELASAKQKFEEI 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2336 RELAEEDLAQQRALAEKMLKEkmqaVQEATRLKAEAELLQQQKELaqeqarRLQEDKEQMAQQLEQETQGFQRTLEaERQ 2415
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEE----VEKAKAIADEAVKLQKEIDK------RCQHKIAEMVALMEKHKHQYDKIIE-ERD 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2416 RQLEMSAEAERlklrvaEMSRAQARAEEDAQRFRkqaeeigeklhrtelatQEKVTLVQTLEIQRQqsdhdaerlrqaia 2495
Cdd:pfam05483 725 SELGLYKNKEQ------EQSSAKAALEIELSNIK-----------------AELLSLKKQLEIEKE-------------- 767
|
810
....*....|....
gi 2124423184 2496 elerEKEKLKQEAK 2509
Cdd:pfam05483 768 ----EKEKLKMEAK 777
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1144-1860 |
3.30e-05 |
|
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: 50.14 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1144 EEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpmfdaLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1222
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1223 VAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESAdplGAWLQDAKRRQEQIQAMVladsRAVREQLRQEKALLEEIER 1302
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRKQL----SKTQEELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1303 H-GEKV------EECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELTTLTSQY 1375
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1376 IKFISETLRRMEEEE-RLAEQQRAEERERLAAVEaalEKQRQLAEAHAQAKAQAEQEAQeLQRRMQEEVARREEAAVDAq 1454
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDKAAEVEVERMSA- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1455 qqkRSIQEELQhlrQSSEAEIQAKARQVEAAERSRLrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQA 1534
Cdd:pfam07111 376 ---KGLQMELS---RAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1535 QEEAER--LRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF--RLQAEEAERRLRQAEAERARQVQVALE 1610
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVAQQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1611 TAQrsaevELQSKRASFAEKTAQLERTLQEEhvavaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRlqa 1690
Cdd:pfam07111 529 LEQ-----ELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR--- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1691 EEVAQQKSLAQAEAEKQKEEAEREARrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE-----QELIRLRAETE 1765
Cdd:pfam07111 566 QELTQQQEIYGQALQEKVAEVETRLR-----EQLSDTKRRLNEARREQAKAVVSLRQIQHRATQekernQELRRLQDEAR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1766 QGEQQR-----QLLEEE----LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRL 1831
Cdd:pfam07111 641 KEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSL 720
|
730 740
....*....|....*....|....*....
gi 2124423184 1832 EAEASRFRELAEEAARLRALAEEAKRQRQ 1860
Cdd:pfam07111 721 TVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1360-1640 |
3.63e-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: 49.89 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1360 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLaEAHAQAKAQAEQEAQELQRRM 1439
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1440 QEEVARREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGE 1516
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1517 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEA 1590
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1591 --ERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQE 1640
Cdd:pfam07888 316 dkDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1677-2095 |
3.75e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.91 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1677 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1756
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1757 LIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAS 1836
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1837 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEA 1916
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1917 FQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSN 1996
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1997 AEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2076
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 2124423184 2077 QLQLAQDAAQKRLQAEEKA 2095
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1380-1862 |
3.97e-05 |
|
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: 50.14 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1380 SETLRRMEEEERLAEQQRAEE--RERLAAVEAALEKQRQLAEA-----HAQAKAQAEQEAQELQRR-MQEEVARREEAAV 1451
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAEllRKQLSKTQEELEAQVTLVESlrkyvGEQVPPEVHSQTWELERQeLLDTMQHLQEDRA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1452 DAQQQKRSIQ---EELQHLRQSSEAEIQAKARQVEAAE-------RSRL-RIEEEIRVVRLQLETTERQRggaEGELQAL 1520
Cdd:pfam07111 260 DLQATVELLQvrvQSLTHMLALQEEELTRKIQPSDSLEpefpkkcRSLLnRWREKVFALMVQLKAQDLEH---RDSVKQL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1521 RARAEEAEAQKRQAQEEAERLRRQVQDETqrkrqaeAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAeAE 1600
Cdd:pfam07111 337 RGQVAELQEQVTSQSQEQAILQRALQDKA-------AEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFV-VN 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1601 RARQVQVALETA-----QRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELER 1675
Cdd:pfam07111 409 AMSSTQIWLETTmtrveQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLRE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1676 WQLKANEALRL-------------------RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL 1736
Cdd:pfam07111 489 ERNRLDAELQLsahliqqevgrareqgeaeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1737 EKQRQLAeGTAQQRLAAEQElIRLRAETEQGEQQRQLLEEELAR-------LQHEAAAATQKRQELEaelakvraemevl 1809
Cdd:pfam07111 569 TQQQEIY-GQALQEKVAEVE-TRLREQLSDTKRRLNEARREQAKavvslrqIQHRATQEKERNQELR------------- 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1810 laskaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLA 1862
Cdd:pfam07111 634 -----RLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLA 681
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1465-1753 |
3.99e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.95 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1465 QHLRQSsEAEIQAKARQVEAAERSRLRIEEeirvvrlqletteRQrggaegelqalrARAEeaeaqkRQAQEEAERLRRQ 1544
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA-------------RQ------------ARLE------REKAAREARHKKA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1545 VQDETQRKRQAEAELAVRVKAeAEAAREKQRALQALEEFRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVEL--- 1620
Cdd:PRK05035 477 AEARAAKDKDAVAAALARVKA-KKAAATQPIVIKAGARPDNSAVIAAREARKAQArARQAEKQAAAAADPKKAAVAAaia 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1621 --QSKRASFAEKTAQLERTLQEEHVAVAQlREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1698
Cdd:PRK05035 556 raKAKKAAQQAANAEAEEEVDPKKAAVAA-AIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQAN 634
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1699 LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1753
Cdd:PRK05035 635 AEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1448-1654 |
4.09e-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: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1448 EAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRieeeirvvrlqletTERQRGGAEGELQALRARAEEA 1527
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK--------------ELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1528 EAQKRQAQEEAErlrrqvQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERrlrQAEAERArqvqv 1607
Cdd:TIGR02794 115 EEKQKQAEEAKA------KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK---KAEAEAK----- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2124423184 1608 ALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAER 1654
Cdd:TIGR02794 181 AKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2318-2520 |
4.27e-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: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2318 VAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2397
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2398 QLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQTLE 2477
Cdd:TIGR02794 128 QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AAKA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2124423184 2478 IQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2520
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2320-2661 |
4.31e-05 |
|
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: 49.97 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2320 EEAARLSVAAQEAARLRELAEEDLAQQRALAEKMlKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2399
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLE-ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2400 EQETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQ 2474
Cdd:pfam02463 239 IDLLQELLRDEQEEIEsskqeIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2475 TLEIQRQQSDHDAERLRQAIAELEREKeKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQE 2554
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2555 KAKLEQLFQdEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQ 2634
Cdd:pfam02463 397 LELKSEEEK-EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|....*..
gi 2124423184 2635 RLRERLQRLEEEHRAALAHSEEIAASQ 2661
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKE 502
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1719-1841 |
4.42e-05 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1719 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQH-----EAAAATQKR 1792
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 1793 QELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEASRFREL 1841
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4178-4206 |
4.59e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.59e-05
10 20
....*....|....*....|....*....
gi 2124423184 4178 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4206
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1166-1636 |
4.61e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1166 ELEATKAALKKLRAQAEAQQPMFDALRDELrgaqevgERLQQRHGERDVEVERWRERVAQLLERWQAVlaqtDLRQRELE 1245
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKEL-------EEVLREINEISSELPELREELEKLEKEVKEL----EELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1246 QLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVladsravrEQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYE 1325
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEI--------EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1326 LQLVTYKAQLEPVASPAKK-PKVQSGSESVIQEYVDLRTRYSELTTltsqYIKFISETLRRMEEEERLAEQQRAEERERL 1404
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKElEEKEERLEELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1405 AAVEAALEKqrqlaeahaqAKAQAEQEAQELQRR---MQEEVARREEAAVDAQQQK-------RSIQEE--LQHLRQSSE 1472
Cdd:PRK03918 390 EKELEELEK----------AKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1473 --AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEgELQALRAR-----AEEAEAQKRQAQEEAERLR--- 1542
Cdd:PRK03918 460 elKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKlkkynLEELEKKAEEYEKLKEKLIklk 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1543 ---RQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQA-EEAERRLRQAE--------AERARQVQVALE 1610
Cdd:PRK03918 539 geiKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEpfyneyleLKDAEKELEREE 618
|
490 500
....*....|....*....|....*.
gi 2124423184 1611 TAQRSAEVELQSKRASFAEKTAQLER 1636
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEE 644
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1573-2472 |
4.89e-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: 49.73 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1573 KQRALQALEEFRLQAEEAERRLRQAEAERARQ----------VQVALETAQ--RSAEVELQSKRASFAEKTA-QLERTLQ 1639
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQkfylrqsvidLQTKLQEMQmeRDAMADIRRRESQSQEDLRnQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1640 EEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlkanEALRLRLQAEEVAQQKslaqaeAEKQKEEAEREARRRG 1719
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ-------EIRSILVDFEEASGKK------IYEHDSMSTMHFRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRqrelaeqELEKQRQLAEGtaqQRLAAEQELIRLRAETEQG-----EQQRQLLEEELARLQHEAAAATQKRQE 1794
Cdd:pfam15921 220 SAISKILR-------ELDTEISYLKG---RIFPVEDQLEALKSESQNKielllQQHQDRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1795 LEAELAKVRAEMEVLlaskaraEEESRSTSE---KSKQRLEAEASRFRELAEEAARL-RALAEEAKRQRQLAEEDAARQR 1870
Cdd:pfam15921 290 ARSQANSIQSQLEII-------QEQARNQNSmymRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSELTEAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1871 AEAERVLAEKLAAIGEATRL-----KTEAEIALkEKEaENER--------------LRRLAEDEAFQRRRLEEQAAQHKA 1931
Cdd:pfam15921 363 TERDQFSQESGNLDDQLQKLladlhKREKELSL-EKE-QNKRlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1932 D----IEERLAQLRKASESeLERQKGL---VEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTlrsk 2004
Cdd:pfam15921 441 EcqgqMERQMAAIQGKNES-LEKVSSLtaqLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT---- 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2005 eQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEV-ERLKAKVEEARRL-RERAEQESARQL---Q 2079
Cdd:pfam15921 516 -NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKViEILRQQIENMTQLvGQHGRTAGAMQVekaQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2080 LAQDAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSMLE----RLRGEAEAARRAAEEAEEARERAEREAAQSRRQV-- 2153
Cdd:pfam15921 595 LEKEINDRRLELQEFK---ILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELns 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2154 --EEAERLKQSAEEQAQAQAQAQAAAeklrKEAEQEAARRAQAEQAALRQKQAADAE-MEKHKKFAEQTLRQKAQV---E 2227
Cdd:pfam15921 672 lsEDYEVLKRNFRNKSEEMETTTNKL----KMQLKSAQSELEQTRNTLKSMEGSDGHaMKVAMGMQKQITAKRGQIdalQ 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2228 QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEaenralILRDKDNTQrv 2307
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME------VALDKASLQ-- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2308 LQEEAEKMKHVAEEAARLSVaaQEAARLRELAEEDLAQQRALAEKMLKEkmqavQEATRLKAEAELLQQQKELAQEQARR 2387
Cdd:pfam15921 820 FAECQDIIQRQEQESVRLKL--QHTLDVKELQGPGYTSNSSMKPRLLQP-----ASFTRTHSNVPSSQSTASFLSHHSRK 892
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2388 ---LQEDKEQMAQQLEQETQ---GFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLhr 2461
Cdd:pfam15921 893 tnaLKEDPTRDLKQLLQELRsviNEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKS-- 970
|
970
....*....|.
gi 2124423184 2462 TELATQEKVTL 2472
Cdd:pfam15921 971 SETCSREPVLL 981
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1836-2082 |
4.99e-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: 49.51 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1836 SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDE 1915
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1916 AFQRRRLEEQAAQHKADIEE------RLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELE 1989
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1990 LGRIRSnaedtlrSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEE--AARQRKAALEE-VERLKAKVEEARRL 2066
Cdd:pfam07888 194 FQELRN-------SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrSLQERLNASERkVEGLGEELSSMAAQ 266
|
250
....*....|....*..
gi 2124423184 2067 RERAEQESAR-QLQLAQ 2082
Cdd:pfam07888 267 RDRTQAELHQaRLQAAQ 283
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1720-1935 |
5.06e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1791
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1792 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE--EAKRQRQLAEEDAARQ 1869
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARakAKKAAQQAASAEPEEQ 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1870 RAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 1935
Cdd:PRK05035 607 VAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2040-2513 |
5.11e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2040 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEekahAFAVQQKEQELQQTLQQEQSMLE 2119
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ----LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2120 RLRgeaeaarraaeeaeeareraereaaQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2199
Cdd:COG4717 150 ELE-------------------------ERLEELRELEE--------------------ELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2200 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA-EVTEAARQRSQVEEELFSLRVQ 2278
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2279 MEELGKLKARI------EAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEK 2352
Cdd:COG4717 265 GGSLLSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2353 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQrtlEAERQRQLEMSAEAERLKLRVA 2432
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE---LKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2433 EMSRAQARAEEDAQRFRKQAEEIGEKL--HRTELATQEkvtlvqtLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKL 2510
Cdd:COG4717 422 LEALDEEELEEELEELEEELEELEEELeeLREELAELE-------AELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
...
gi 2124423184 2511 LQL 2513
Cdd:COG4717 495 LKL 497
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2290-2407 |
5.31e-05 |
|
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: 48.34 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2290 EAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEaarlRELAEEDLAQQRALAE--KMLKEKMQavQEATRL 2367
Cdd:cd16269 180 EAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----RELEQKLEDQERSYEEhlRQLKEKME--EERENL 253
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2124423184 2368 KAEAELLQQQKElaQEQARRLQEDKEQMAQQLEQETQGFQ 2407
Cdd:cd16269 254 LKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1521-1696 |
5.40e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1521 RARAEEAEAQ------KRQAQEEAerlRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQralQALEEFRLQAEEAER-- 1592
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1593 -RLRQAEAERARQVQVA----LETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERARE 1667
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKA 490
|
170 180 190
....*....|....*....|....*....|....
gi 2124423184 1668 EAERelERWQLKANEALRLRL-----QAEEVAQQ 1696
Cdd:pfam15709 491 RLEA--EERRQKEEEAARLALeeamkQAQEQARQ 522
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1445-1798 |
5.49e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1445 RREEAAVDAQQQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARA 1524
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1525 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQ 1604
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1605 VQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1684
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1685 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1764
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 2124423184 1765 EQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1798
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1723-2044 |
5.63e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1802
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1803 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1882
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1883 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR 1962
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1963 RQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 2042
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
..
gi 2124423184 2043 AR 2044
Cdd:COG4372 368 AD 369
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
85-186 |
5.76e-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: 45.49 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 85 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 160
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHF 186
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2201-2409 |
5.87e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2201 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAAR--QRSQVEEELFSLRVQ 2278
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalYRSGGSVSYLDVLLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2279 MEELGKLKARIEAENRaLILRDKD--NTQRVLQEEAEKMKHVAEEA-ARLSVAAQEAARLRELAEEDLAQQRALAEKMLK 2355
Cdd:COG3883 111 SESFSDFLDRLSALSK-IADADADllEELKADKAELEAKKAELEAKlAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 2356 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRT 2409
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1384-1603 |
6.08e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.82 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1384 RRMEEEERLAEQQRAEER--ERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ 1461
Cdd:PRK07735 29 KHGAEISKLEEENREKEKalPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1462 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1541
Cdd:PRK07735 109 AKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1542 RRQVQDETQR-KRQAEAELAVRVKAEAeAAREKQRALQ----ALEEFRLQAEEAERRLRQAEAERAR 1603
Cdd:PRK07735 189 GEGTEEVTEEeKAKAKAKAAAAAKAKA-AALAKQKASQgngdSGDEDAKAKAIAAAKAKAAAAARAK 254
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1393-1554 |
6.31e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 49.13 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1393 AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1472
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1473 AEIQAKARQVEAAERSRLRIEEEirvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDETQRK 1552
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 2124423184 1553 RQ 1554
Cdd:PRK12678 216 EE 217
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1840-2075 |
6.48e-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: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1840 ELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRlaedeafQR 1919
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1920 RRLEEQAAQHKADIEERLAQLRKASESE----LERQKGlVEDTLRQRRQVEEEILALKVSFEKAAAGKAELElelgRIRS 1995
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPplalLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLAELA----ALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1996 NAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2075
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2305-2605 |
6.82e-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: 48.38 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2305 QRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2384
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2385 ARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEM--SRAQARAEEDAQRFRKQAEEIGEKLHRT 2462
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEkaEREEEREAEREEIEEEKEREIARLRAQQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2463 ELATQEKVTLvQTLEIQRQQSDHDAERLRQAIAELEReKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKD 2542
Cdd:pfam13868 194 EKAQDEKAER-DELRAKLYQEEQERKERQKEREEAEK-KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 2543 TLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAE 2605
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEE 334
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1727-1951 |
7.34e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.38 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1727 RQRELAEQELEKQRQLAEGTAQQRLAAEQEL---------IRLRAETEQGEqqRQLLEEELARLQHEAAAATQKRQELEA 1797
Cdd:pfam00038 47 RLYSLYEKEIEDLRRQLDTLTVERARLQLELdnlrlaaedFRQKYEDELNL--RTSAENDLVGLRKDLDEATLARVDLEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1798 elaKVRAEMEVLLASKARAEEESRSTSEKSKQR---LEAEASRFRELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEA 1873
Cdd:pfam00038 125 ---KIESLKEELAFLKKNHEEEVRELQAQVSDTqvnVEMDAARKLDLTSALAEIRAQYEEiAAKNREEAEEWYQSKLEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1874 ERVLAEKLAAIGEATRLKTEAEIALKEKEAENERL--------RRLAEDEAfqrrRLEEQAAQHKADIEERLAQLRKASE 1945
Cdd:pfam00038 202 QQAAARNGDALRSAKEEITELRRTIQSLEIELQSLkkqkasleRQLAETEE----RYELQLADYQELISELEAELQETRQ 277
|
....*.
gi 2124423184 1946 sELERQ 1951
Cdd:pfam00038 278 -EMARQ 282
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3839-3875 |
8.28e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 8.28e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2124423184 3839 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3875
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1723-1989 |
8.37e-05 |
|
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: 48.53 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQH-------EAAAATQKRQEL 1795
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1796 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEASRFR-ELAEEAARLRALAEEAKRQRQLAEEDAARQRaeae 1874
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEARNQLR---- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1875 rvlaEKLAAIGEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAAqhKADIEERLAQLRKA---SESELERQ 1951
Cdd:pfam19220 273 ----DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA--RAELEERAEMLTKAlaaKDAALERA 344
|
250 260 270
....*....|....*....|....*....|....*....
gi 2124423184 1952 KGLVEDTLRQRRQVEEEILALKVSFEKAAAG-KAELELE 1989
Cdd:pfam19220 345 EERIASLSDRIAELTKRFEVERAALEQANRRlKEELQRE 383
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1379-1584 |
9.54e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.74 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1379 ISETLRRMEEEERLAEQQRAEERERLAAVEAALekqrqlaeahAQAKAQAEQEAQELqRRMQEEVARREEAAVDAQQQKR 1458
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQAL----------AQVIANQKRLERQL-EELEAEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1459 siqeelQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1532
Cdd:COG1842 83 ------EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKvneals 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1533 -----QAQEEAERLRRQVqDETQRKRQAEAELAVR--VKAEAEAAREKQRALQALEEFR 1584
Cdd:COG1842 157 gidsdDATSALERMEEKI-EEMEARAEAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1569-1872 |
9.85e-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: 47.99 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1569 AAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEEHVAVAQL 1648
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEERE-QKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1649 REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQ 1728
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1729 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAatQKRQELEAELAKVRAEMEV 1808
Cdd:pfam13868 188 RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE--LKERRLAEEAEREEEEFER 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 1809 LLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1872
Cdd:pfam13868 266 MLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1394-1495 |
9.98e-05 |
|
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: 47.57 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1394 EQQRAEERERLAAVEAALEKQRQLAEAHAQAkaqaeqEAQELQRRMQEEVARREEaaVDAQQQKRSIQEELQHLRQSSEA 1473
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKA------EAAEQERKLLEEQQRELE--QKLEDQERSYEEHLRQLKEKMEE 248
|
90 100
....*....|....*....|..
gi 2124423184 1474 EIQAKARQVEAAERSRLRIEEE 1495
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEA 270
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1232-1491 |
1.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1232 AVLAQTDLR---QRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVE 1308
Cdd:COG4942 14 AAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1309 ECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESVIQEYvdlrtRYSELTTLTSQYIKFISETLRRMEE 1388
Cdd:COG4942 94 ELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1389 EERLAEQQRAEERERLAAVEAALEKQRqlaeahaQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR 1468
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|...
gi 2124423184 1469 QSSEAEIQAKARQVEAAERSRLR 1491
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKGKLP 256
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1243-1558 |
1.03e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 48.78 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1243 ELEQLGR---QLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQL----RQEKALLEEIERHGEKV-------- 1307
Cdd:PLN03188 892 EITQLNRlvqQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFLEEELaslmHEHKLLKEKYENHPEVLrtkielkr 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1308 --EECQRFAKQY--------INAIKDYELQLVTYkaqLEPVASPAKKpkvqsgSESVIQ-EYVDLRTRYSELTTLT---- 1372
Cdd:PLN03188 972 vqDELEHYRNFYdmgerevlLEEIQDLRSQLQYY---IDSSLPSARK------RNSLLKlTYSCEPSQAPPLNTIPestd 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1373 -SQYIKFISETLRRMEEEER---LAEQQRAEererLAAVEAALEKQRQLAEAH---AQAKAQAEQEAQELQRRMQEEVAR 1445
Cdd:PLN03188 1043 eSPEKKLEQERLRWTEAESKwisLAEELRTE----LDASRALAEKQKHELDTEkrcAEELKEAMQMAMEGHARMLEQYAD 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1446 REEAAVDAQQQKRSIQEELQHLRQsseAEIQAKARQVE-------AAERSRLRIEEEIRVVRLQLETTERQ---RGGAE- 1514
Cdd:PLN03188 1119 LEEKHIQLLARHRRIQEGIDDVKK---AAARAGVRGAEskfinalAAEISALKVEREKERRYLRDENKSLQaqlRDTAEa 1195
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1515 ----GELQALRARAEEA--EAQKR--QAQEEA-------ERLRRQVQDETQRKRQAEAE 1558
Cdd:PLN03188 1196 vqaaGELLVRLKEAEEAltVAQKRamDAEQEAaeaykqiDKLKRKHENEISTLNQLVAE 1254
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1886-2520 |
1.04e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 48.67 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1886 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQV 1965
Cdd:NF041483 23 EMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRPAYDGADIGYQAEQLLRNAQIQADQLRADAERELRDARAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1966 EEEIlaLKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQ----------AELEAMRQRQLAAEEEQRRREAEERVQKS 2035
Cdd:NF041483 103 TQRI--LQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQtveshvnenvAWAEQLRARTESQARRLLDESRAEAEQAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2036 LAAEEEA------ARQRKAALEEVERLKAK--VEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQEL 2107
Cdd:NF041483 181 AAARAEAerlaeeARQRLGSEAESARAEAEaiLRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2108 QQTLQQEQSMLERLR-----GEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRK 2182
Cdd:NF041483 261 RAAEQRMQEAEEALRearaeAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2183 EAEQEAARRAQAEQAALRQKQAAdAEMEKHKKFAEQTLrQKAQVEQELTTlRLQLEETDHQKSILDEELQRLKAEVTEAA 2262
Cdd:NF041483 341 AEAEKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVL-TKASEDAKATT-RAAAEEAERIRREAEAEADRLRGEAADQA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2263 RQ-RSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAAR-----LSVAAQEAARLR 2336
Cdd:NF041483 418 EQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARtaeelLTKAKADADELR 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2337 ELAEEDLAQQRALA-EKMLKEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQ 2415
Cdd:NF041483 498 STATAESERVRTEAiERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQAEAA 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2416 RQLE-MSAEAERlKLRVAEMSRAQARAEedAQRFRKQAEEIGEKLhRTELAtqEKVTLVQtleiqrQQSDHDAERLR--- 2491
Cdd:NF041483 575 EELTrLHTEAEE-RLTAAEEALADARAE--AERIRREAAEETERL-RTEAA--ERIRTLQ------AQAEQEAERLRtea 642
|
650 660 670
....*....|....*....|....*....|....*.
gi 2124423184 2492 -----QAIAELEREKEKLKQEA--KLLQLKSEEMQT 2520
Cdd:NF041483 643 aadasAARAEGENVAVRLRSEAaaEAERLKSEAQES 678
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1376-1616 |
1.05e-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: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1376 IKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQ 1455
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1456 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALR-------AraeEAE 1528
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKaeleaakA---ELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1529 AQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVA 1608
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
....*...
gi 2124423184 1609 LETAQRSA 1616
Cdd:COG3883 255 AGAAAGSA 262
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1128-1635 |
1.05e-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: 48.68 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1128 EKLKTISLVIRSTHGAeevLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQ-QPMFDALRDELRGAQEvgeRLQ 1206
Cdd:pfam12128 251 NTLESAELRLSHLHFG---YKSDETLIASRQE------ERQETSAELNQLLRTLDDQwKEKRDELNGELSAADA---AVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1207 QRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAV 1286
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1287 REQLRQEKAL-LEEIERHGEKVEECQRFA-KQYINAIKDYELQLvtykaqlepvASPAKKPKVQSGSESVIQEyvdlrtr 1364
Cdd:pfam12128 399 LAKIREARDRqLAVAEDDLQALESELREQlEAGKLEFNEEEYRL----------KSRLGELKLRLNQATATPE------- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1365 yseltTLTSQYIKfiSETLRRMEEEErlaeQQRAEERERLAAVEAALEKQRQLA-EAHAQAKAQAEQEAQELQRRMQEEV 1443
Cdd:pfam12128 462 -----LLLQLENF--DERIERAREEQ----EAANAEVERLQSELRQARKRRDQAsEALRQASRRLEERQSALDELELQLF 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1444 AR--------REEAAVDAQQQKRSIQEELQH-------------------------LRQ-------SSEAEIQAKARQVE 1483
Cdd:pfam12128 531 PQagtllhflRKEAPDWEQSIGKVISPELLHrtdldpevwdgsvggelnlygvkldLKRidvpewaASEEELRERLDKAE 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1484 AA---ERSRL-RIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRrqvqdeTQRKRQAEAEl 1559
Cdd:pfam12128 611 EAlqsAREKQaAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAL------AERKDSANER- 683
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1560 avRVKAEAEAAREKQRALQALEEFRLQAEEAerrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1635
Cdd:pfam12128 684 --LNSLEAQLKQLDKKHQAWLEEQKEQKREA----RTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE 753
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1866-2097 |
1.15e-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: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1866 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE 1945
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1946 SELERQKGLVEDTLRQR-RQVEEEILALKVSFEKAAAGKAELEL--ELGRIRSNAEDTLRsKEQAELEAMRQRQLAAeee 2022
Cdd:COG4942 97 AELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELR-ADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 2023 qrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHA 2097
Cdd:COG4942 173 ----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2312-2497 |
1.19e-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: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2312 AEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELaqEQARRLQED 2391
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAEL--ERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2392 KEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2471
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*.
gi 2124423184 2472 LVQTLEIQRQQSDHDAERLRQAIAEL 2497
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERA 792
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1821-1969 |
1.22e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1821 RSTSEKSKQRLEAEASRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 1899
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 1900 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 1969
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1400-1621 |
1.28e-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: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1400 ERERLAAVEAALEKQRQLAEAHAQAKAQAEQ---EAQELQRRMQEEVarreeaavdaqqqkRSIQEELQHLRQSSEAEIQ 1476
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQlrtELQELEAQQQEEA--------------ESSREQLQELEEQLATERS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1477 AKarqvEAAERSRLRIEEEIRVVRLQLETTERQRggaegelqalraraeeaEAQKRQAQEEAERLRRQVQDETQRKRQaE 1556
Cdd:pfam09787 108 AR----REAEAELERLQEELRYLEEELRRSKATL-----------------QSRIKDREAEIEKLRNQLTSKSQSSSS-Q 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1557 AELAVRVKAEAEAAREKQRALQALEEFR----LQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQ 1621
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKnslvLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLR 234
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1445-1576 |
1.31e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.74 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1445 RREEAAVD-AQQQKRSIQEELQHLRQSS--EAEIQAKARQVEAAERSRLRIEEEI-RVVRLQletteRQRGGAEGELQAL 1520
Cdd:COG1566 79 TDLQAALAqAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDEA 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1521 RARAEEAEAQKRQAQEEAERLRRQVQDETQrKRQAEAELavrvkAEAEAAREKQRA 1576
Cdd:COG1566 154 RAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQAEL 203
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1983-2459 |
1.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1983 KAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERvQKSLAAEEEAARQRKAALEEVERLKAKVEE 2062
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2063 ARRLRERAEQESARqlqlaqdaaQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERA 2142
Cdd:COG4717 134 LEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2143 EREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKK-------- 2214
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2215 ----FAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAArqrsqveEELFSLRVQMEELGKLKARIE 2290
Cdd:COG4717 285 llalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2291 -AENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLkekmqAVQEATRLKA 2369
Cdd:COG4717 358 eLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2370 EAELLQQQKELAQEQARRLQEDKEQMAQQLEQ-ETQGFQRTLEAERQRQL----EMSAEAERLKLRVAEMSRAQARAEED 2444
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKaelrELAEEWAALKLALELLEEAREEYREE 512
|
490
....*....|....*.
gi 2124423184 2445 AQ-RFRKQAEEIGEKL 2459
Cdd:COG4717 513 RLpPVLERASEYFSRL 528
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2226-2606 |
1.41e-04 |
|
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: 48.18 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2226 VEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKL-KARIEAENRALILRDKDNT 2304
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLlDEKKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2305 QRVLQEEAEKMKHVAEEAARLSVAAQEAARLR------ELAEEDL--AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2376
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEvedlktELEKEKLknIELTAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2377 -------QKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEaERQRQLEMSAE-AERLKLRVAEMSRAQARAEEDAQRF 2448
Cdd:pfam05483 521 diinckkQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD-EVKCKLDKSEEnARSIEYEVLKKEKQMKILENKCNNL 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2449 RKQAEEIG---EKLHRTELATQEKVTL----VQTLEIQRQQSDHDAERLRQAIAEL------EREKEKLKQEAKLLQLKS 2515
Cdd:pfam05483 600 KKQIENKNkniEELHQENKALKKKGSAenkqLNAYEIKVNKLELELASAKQKFEEIidnyqkEIEDKKISEEKLLEEVEK 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2516 EEMQTVQQEQLLQETQALQQSFLSEKDTLL-----QRERFIEQEKAKL---EQLFQDEVAKAQKLREEQQRQQKQMEEEK 2587
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHKIAEMVALMekhkhQYDKIIEERDSELglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
|
410
....*....|....*....
gi 2124423184 2588 QQLVASMEEARQRQREAEE 2606
Cdd:pfam05483 760 KQLEIEKEEKEKLKMEAKE 778
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4008-4042 |
1.41e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.41e-04
10 20 30
....*....|....*....|....*....|....*
gi 2124423184 4008 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4042
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1725-2093 |
1.44e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1725 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--HEAAAATQKRQELEA 1797
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1798 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAsRFRELAEEAARLRAlaEEAKRQRQLaeeDAARQRAEAERvl 1877
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKS--QLADYQQAL---DVQQTRAIQYQ-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1878 aEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA--DIEERLAQLRKASESELERqkglv 1955
Cdd:PRK04863 418 -QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahSQFEQAYQLVRKIAGEVSR----- 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1956 EDTLRQRRQVEEEILALKVSFEKAAAGKAELElELGRirsnaedtlRSKEQAELEAMRQRqlaaeeeqrrreAEERVQKS 2035
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHLAEQLQQLRMRLS-ELEQ---------RLRQQQRAERLLAE------------FCKRLGKN 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 2036 LAAEEEAARQRKAALEEVERLKAKVEEArrlRERAEQESARQLQLAQDAAQKRLQAEE 2093
Cdd:PRK04863 550 LDDEDELEQLQEELEARLESLSESVSEA---RERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1470-1683 |
1.44e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1470 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1547
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1548 -ETQRKRQAEAELAV------------RVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAErARQVQVALETAQR 1614
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1615 saevELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1683
Cdd:COG3883 172 ----ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2217-2474 |
1.46e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2217 EQTLR---QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRS------QVEEELFSLRVQmeeLGKLKA 2287
Cdd:PRK11281 66 EQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLESRLAQTLDQ---LQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2288 RIEAENRALIlrdkdnTQRVLQEEAEkmkhvaeeaARLSVAAQEAARLRELAEEDLAQQRALAEKmLKEKMQAVQEATrl 2367
Cdd:PRK11281 143 DLAEYNSQLV------SLQTQPERAQ---------AALYANSQRLQQIRNLLKGGKVGGKALRPS-QRVLLQAEQALL-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2368 kaEAELLQQQKELA-----QE--QARRlqEDKEQMAQQLEQETQGFQrtlEAERQRQLEMSAEAerlklrVAEMSRAQAR 2440
Cdd:PRK11281 205 --NAQNDLQRKSLEgntqlQDllQKQR--DYLTARIQRLEHQLQLLQ---EAINSKRLTLSEKT------VQEAQSQDEA 271
|
250 260 270
....*....|....*....|....*....|....*
gi 2124423184 2441 AEEDAQRFRKQAEEIGEKLHRTEL-ATQEKVTLVQ 2474
Cdd:PRK11281 272 ARIQANPLVAQELEINLQLSQRLLkATEKLNTLTQ 306
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1393-1507 |
1.48e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1393 AEQQRAEERERLAAVEAALEKQRQLAEAHAQ---AKAQAEQEAQELQRRM---------QEEVARREEAAVDAQQQKRSI 1460
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlaaAQAQLDLAQRELERYQalykkgavsQQELDEARAALDAAQAQLEAA 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2124423184 1461 QEELQHLRQSSEAEiqakaRQVEAAERSRLRIEEEIRVVRLQLETTE 1507
Cdd:COG1566 168 QAQLAQAQAGLREE-----EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1414-1547 |
1.49e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1414 QRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSRLRI 1492
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1493 EEEIRVVRLQLETTERQRGGaegelqalRARAEEAEAQKRQAQEEAERLRRQVQD 1547
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLRE--------EEELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3802-3838 |
1.70e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.70e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2124423184 3802 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPAEEA 3838
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2243-2661 |
1.73e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2243 QKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALilrdKDNTQRVLQEEA--EKMKHVAE 2320
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA----SDHLNLVQTALRqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2321 EAARLSVAAQEAARLRELAEEDLAQQRALAEkmlkekmQAVQEATRLKA------EAELLQQQKELAQEQARRLQEDKEQ 2394
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAE-------AAEEEVDELKSqladyqQALDVQQTRAIQYQQAVQALERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2395 MAQ--QLEQET-QGFQRTLEAERQRQLEMSAEAERlKLRVAEMSRAQAraEEDAQRFRKQAEEIGEklhrtELATQEKVT 2471
Cdd:PRK04863 429 LCGlpDLTADNaEDWLEEFQAKEQEATEELLSLEQ-KLSVAQAAHSQF--EQAYQLVRKIAGEVSR-----SEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2472 LVQTLEIQRQQSDHdAERLRQAIAELEREkekLKQEAKLLQLKSEEMQtvqqeqllqetqALQQSFLSEKDTllqrERFI 2551
Cdd:PRK04863 501 LLRRLREQRHLAEQ-LQQLRMRLSELEQR---LRQQQRAERLLAEFCK------------RLGKNLDDEDEL----EQLQ 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2552 EQEKAKLEQLfQDEVAKAQKLREEQQRQQKQMeeekQQLVASMEEARQRQREAEEGVRRKQEELQLLEqqrqqqekllaE 2631
Cdd:PRK04863 561 EELEARLESL-SESVSEARERRMALRQQLEQL----QARIQRLAARAPAWLAAQDALARLREQSGEEF-----------E 624
|
410 420 430
....*....|....*....|....*....|
gi 2124423184 2632 ENQRLRERLQRLEEEHRAALAHSEEIAASQ 2661
Cdd:PRK04863 625 DSQDVTEYMQQLLERERELTVERDELAARK 654
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1423-1579 |
1.92e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 47.03 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1423 QAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAER---------SRLRIE 1493
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAqlaqaqidlARRRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1494 EEIRVV-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ-VQDETQRKRQAEAELAvrvKAEAEAAR 1571
Cdd:pfam00529 133 APIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSeLSGAQLQIAEAEAELK---LAKLDLER 209
|
....*...
gi 2124423184 1572 EKQRALQA 1579
Cdd:pfam00529 210 TEIRAPVD 217
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4317-4350 |
1.93e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.93e-04
10 20 30
....*....|....*....|....*....|....
gi 2124423184 4317 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4350
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1743-2239 |
1.95e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.93 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1743 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV----------RAEMEVLLAS 1812
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1813 KARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT 1892
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1893 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILAL 1972
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1973 KVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEE 2052
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2053 VERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAA 2132
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2133 EEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2212
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 2124423184 2213 KKFAEQTLRQKAQVEQELTTLRLQLEE 2239
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
223-300 |
1.98e-04 |
|
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: 43.45 E-value: 1.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 223 DNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 300
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1756-2069 |
2.07e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.43 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1756 ELIRLRAETEQGEQQ--RQLLEEELARLQHEAAAATQKRQeLEAELAKVRA---EMEVLLASKARAEEESRSTSEKSKQR 1830
Cdd:pfam05557 3 ELIESKARLSQLQNEkkQMELEHKRARIELEKKASALKRQ-LDRESDRNQElqkRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1831 LEAEASRFRELAEEAARLRALAE----------EAKRQRQLAEEDAARQRAEAERV---LAEKLAAIGEATRLKTEAEIA 1897
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREvisclknelsELRRQIQRAELELQSTNSELEELqerLDLLKAKASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1898 LKEKEAENERLRRLAedeafQRRRLEEQAAQHKADIEERLAQLRKAsESELERQKGLVE---DTLRQRRQVEEEILALKV 1974
Cdd:pfam05557 162 QSSLAEAEQRIKELE-----FEIQSQEQDSEIVKNSKSELARIPEL-EKELERLREHNKhlnENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1975 S---FEKAAAGKAELELELGRIRS----------NAEDTLRSKE--QAELEAMRQRQLAAEEE----QRRREAEERVQKS 2035
Cdd:pfam05557 236 KlerEEKYREEAATLELEKEKLEQelqswvklaqDTGLNLRSPEdlSRRIEQLQQREIVLKEEnsslTSSARQLEKARRE 315
|
330 340 350
....*....|....*....|....*....|....
gi 2124423184 2036 LaaEEEAARQRKAALEEVERLKAKVEEARRLRER 2069
Cdd:pfam05557 316 L--EQELAQYLKKIEDLNKKLKRHKALVRRLQRR 347
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3726-3762 |
2.23e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.23e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2124423184 3726 RYLYGTGCVAGVYVPGSRQTLTIYQALKKGLLSAEVA 3762
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1384-1554 |
2.25e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.59 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1384 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQlAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1463
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARA-AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1464 LQHLRQSSEAEIQAKARQVEAAERSRLRieeeiRVVRLQLETTERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRR 1543
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRR 230
|
170
....*....|.
gi 2124423184 1544 QVQDETQRKRQ 1554
Cdd:PRK12678 231 RRRDRRDARGD 241
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1381-1570 |
2.37e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLRRMEEEERLAEQQRAEERERLAAVEAALekqrqlaeAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1460
Cdd:PRK05035 524 EARKAQARARQAEKQAAAAADPKKAAVAAAI--------ARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1461 QEELQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEEIRVVRLQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAE 1539
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE 670
|
170 180 190
....*....|....*....|....*....|.
gi 2124423184 1540 rlrrqvQDETQRKRQAEAELAvRVKAEAEAA 1570
Cdd:PRK05035 671 ------EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1527-1647 |
2.47e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1527 AEAQKRQAQEEAERLRRQVQDETQRKRQAEaELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQ 1606
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423184 1607 VALETAQRSAEVElqSKRASFAEKTAQLERTLQEEHVAVAQ 1647
Cdd:PRK09510 140 KAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKK 178
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1720-1879 |
2.48e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.59 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQHEAAAATQKRQELEA 1797
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1798 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1873
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....*.
gi 2124423184 1874 ERVLAE 1879
Cdd:COG1842 207 EDELAA 212
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2205-2446 |
2.56e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2205 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfslRVQMEELGK 2284
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2285 LkARIEAENRALIlrdkDNTQRVLQEEaekmkHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMlkekmqavQEA 2364
Cdd:COG3883 91 R-ARALYRSGGSV----SYLDVLLGSE-----SFSDFLDRLSALSKIADADADLLEELKADKAELEAKK--------AEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2365 TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQEtqgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEED 2444
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE----EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
..
gi 2124423184 2445 AQ 2446
Cdd:COG3883 229 AA 230
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2041-2653 |
2.57e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2041 EAARQRKAALEEV----ERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEqs 2116
Cdd:COG4913 245 EDAREQIELLEPIrelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR-- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2117 mlERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVE-EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEqeaarraqae 2195
Cdd:COG4913 323 --EELDELEAQIRGNGGDRLEQLEREIERLERELEERErRRARLEALLAALGLPLPASAEEFAALRAEAA---------- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2196 qaalRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRsqvEEEL--- 2272
Cdd:COG4913 391 ----ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD---EAELpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2273 -------------------------FSLRVQMEELGKLKARIEAENRALILRdkdnTQRVLQEEAEKMKHVAEE---AAR 2324
Cdd:COG4913 464 gelievrpeeerwrgaiervlggfaLTLLVPPEHYAAALRWVNRLHLRGRLV----YERVRTGLPDPERPRLDPdslAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2325 LSVAAQEAarlRELAEEDLAQQRALA----EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE 2400
Cdd:COG4913 540 LDFKPHPF---RAWLEAELGRRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2401 QETQGFQRTLEAERQRQLEMSAEAERL--KLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtlVQTLEI 2478
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD----LAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2479 QRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFlsekDTLLQRERFIEQEKAKL 2558
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVERELR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2559 EQLfQDEVAKAQKLREEQQrqqkqmeeekQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEEN-QRLR 2637
Cdd:COG4913 769 ENL-EERIDALRARLNRAE----------EELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYeERFK 837
|
650
....*....|....*.
gi 2124423184 2638 ERLQRLEEEHRAALAH 2653
Cdd:COG4913 838 ELLNENSIEFVADLLS 853
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2214-2668 |
2.74e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2214 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAEN 2293
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2294 RALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2373
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2374 LQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2453
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2454 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQAL 2533
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2534 QQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQE 2613
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 2614 ELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVKAL 2668
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2202-2417 |
2.74e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2202 KQAADAEMEKH----KKFAE---QTLRQ-KAQVEQELTTLRLQLEETDH---------QKSILDEELQRLKAEVTEAARQ 2264
Cdd:NF012221 1549 KHAKQDDAAQNaladKERAEadrQRLEQeKQQQLAAISGSQSQLESTDQnaletngqaQRDAILEESRAVTKELTTLAQG 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2265 RSQVEEElfslRVQMEELGKlKARIEAENRAL--ILRDKDNTQRVLQE--EAEKMKHVAEEA-ARLSVAAQEAA-----R 2334
Cdd:NF012221 1629 LDALDSQ----ATYAGESGD-QWRNPFAGGLLdrVQEQLDDAKKISGKqlADAKQRHVDNQQkVKDAVAKSEAGvaqgeQ 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2335 LRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKeqmAQQLEQETQGFQRTLEAER 2414
Cdd:NF012221 1704 NQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENK---ANQAQADAKGAKQDESDKP 1780
|
...
gi 2124423184 2415 QRQ 2417
Cdd:NF012221 1781 NRQ 1783
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1454-1605 |
2.82e-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: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1454 QQQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEG--ELQALRARAEEAE 1528
Cdd:COG1579 23 EHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1529 AQKRQAQEEAERLRRQVQdetqrkrQAEAELAvrvKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQV 1605
Cdd:COG1579 103 RRISDLEDEILELMERIE-------ELEEELA---ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2238-2520 |
2.91e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2238 EETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDntqrvLQEEAEKMKH 2317
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS-----KRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2318 VAEeaarlsvaaqeaaRLRELAEEdlaqqralaEKMLKEKmqaVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2397
Cdd:PRK03918 264 LEE-------------RIEELKKE---------IEELEEK---VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2398 qLEQETQGFQRTL-EAErqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFrkqaEEIGEKLHRTElatqekvtlvqtl 2476
Cdd:PRK03918 319 -LEEEINGIEERIkELE-----EKEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELE------------- 375
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2124423184 2477 EIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2520
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1719-1866 |
3.10e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1719 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQHEAAAATQKRQELEA 1797
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1798 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEASRF-RELAEEAARLRALAEEAKRQRQLAEEDA 1866
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLEH 506
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3430-3463 |
3.28e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.28e-04
10 20 30
....*....|....*....|....*....|....
gi 2124423184 3430 LLEAQAATGFLVDPVRNQRLYVHEAVKAGIVGPE 3463
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1435-2068 |
3.33e-04 |
|
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: 47.02 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1435 LQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAE 1514
Cdd:pfam05483 79 LYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1515 gELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELavRVKAEaeaarekqralQALEEFRLQAEEAERRL 1594
Cdd:pfam05483 159 -LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL--RVQAE-----------NARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1595 RQAEAERARQV-----QVALETAQrSAEVELQSKRASFaektaqlerTLQEEHVAVAQLREEAERRAQQQAEAERAREEA 1669
Cdd:pfam05483 225 QHLEEEYKKEIndkekQVSLLLIQ-ITEKENKMKDLTF---------LLEESRDKANQLEEKTKLQDENLKELIEKKDHL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1670 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegTAQQ 1749
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR----TEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1750 RLaaeqelirlraetEQGEQQRQLLEEELARLQHEAAAATQ----KRQELEaELAKVRAEMEVLLASKARAEEESRSTSE 1825
Cdd:pfam05483 371 RL-------------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1826 KSKQRLEAEASRFRELAEEAARLRALaeEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLkteaeialkekeaEN 1905
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL-------------EN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1906 ERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEILALKVS 1975
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1976 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKsLAAEEEAARQR--------- 2046
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKfeeiidnyq 660
|
650 660 670
....*....|....*....|....*....|..
gi 2124423184 2047 ----------KAALEEVERLKAKVEEARRLRE 2068
Cdd:pfam05483 661 keiedkkiseEKLLEEVEKAKAIADEAVKLQK 692
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1382-1621 |
3.36e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 46.57 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1382 TLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQ-EAQELQRRMQEEVARRE------EAAVDAQ 1454
Cdd:COG1538 84 DLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQaRAQLAQAEAQLAQARNAlalllgLPPPAPL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1455 QQKRSIQEELQHLRQSSEAEIQAKAR--QVEAAERSRLRIEEEIRVVRLQL----------ETTERQRGGAEGELQ---- 1518
Cdd:COG1538 164 DLPDPLPPLPPLPPSLPGLPSEALERrpDLRAAEAQLEAAEAEIGVARAAFlpslslsasyGYSSSDDLFSGGSDTwsvg 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1519 -----------ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQ-ALEEFR-- 1584
Cdd:COG1538 244 lslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAEEALElARARYRag 323
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2124423184 1585 ----LQAEEAERRLRQAEAERarqvqVALETAQRSAEVELQ 1621
Cdd:COG1538 324 laslLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1720-1913 |
3.56e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1799
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1800 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1879
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 2124423184 1880 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAE 1913
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2040-2573 |
3.56e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2040 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHA--FAVQQKEQELQQTLQQEQSM 2117
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALrlWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2118 LERLRGEAEAARRAAEEAEEARERAEREAAQS-RRQVEEAER----LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRA 2192
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEReierLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2193 QAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRsqvEEEL 2272
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD---EAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2273 ----------------------------FSLRVQMEELGKLKARIEAENRALILRdkdnTQRVLQEEAEKMKHVAEE--- 2321
Cdd:COG4913 461 pfvgelievrpeeerwrgaiervlggfaLTLLVPPEHYAAALRWVNRLHLRGRLV----YERVRTGLPDPERPRLDPdsl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2322 AARLSVAAQEAarlRELAEEDLAQQRALA----EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2397
Cdd:COG4913 537 AGKLDFKPHPF---RAWLEAELGRRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2398 QLEQETQGFQRTLEAERQRQLEMSAEAERL--KLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtlVQT 2475
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD----LAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2476 LEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFlsekDTLLQRERFIEQEK 2555
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVER 765
|
570
....*....|....*...
gi 2124423184 2556 AKLEQLfQDEVAKAQKLR 2573
Cdd:COG4913 766 ELRENL-EERIDALRARL 782
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1405-1602 |
3.63e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 46.18 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1405 AAVEAALEKQRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVAR--REEAAVD-AQQQKRSIQEELQHLRQSSEAEIQAKAR 1480
Cdd:COG1538 4 ELIERALANNPDLRAARARvEAARAQLRQARAGLLPSQELDLggKRRARIEaAKAQAEAAEADLRAARLDLAAEVAQAYF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1481 QVEAAERSRLRIEEEIRVVRLQLETTERQR---GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEA 1557
Cdd:COG1538 84 DLLAAQEQLALAEENLALAEELLELARARYeagLASRLDVLQAEAQLAQARAQLAQAEAQLAQARNALALLLGLPPPAPL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2124423184 1558 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERA 1602
Cdd:COG1538 164 DLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAEAEIG 208
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2337-2461 |
3.85e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.65 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2337 ELAEEDLAQQRALAEKML---KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAE 2413
Cdd:cd16269 170 EVLQEFLQSKEAEAEAILqadQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEE 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2124423184 2414 RQRQLEmsaEAERLklrVAEMSRAQARAEEdaQRFRKQAEEIGEKLHR 2461
Cdd:cd16269 250 RENLLK---EQERA---LESKLKEQEALLE--EGFKEQAELLQEEIRS 289
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2220-2560 |
4.01e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2220 LRQKAQVEQ---ELTTLRLQLEEtdhQKSILDEelqrLKAEVTEAARQRSQVEEELFSLRVQMEELgkLKARIEAENRAL 2296
Cdd:PRK04863 344 LRQQEKIERyqaDLEELEERLEE---QNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLADY--QQALDVQQTRAI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2297 ILRdkdNTQRVLqEEAEKMKHVAEEAARLSVAAQEAARlrelAEEDLAQQRALaekMLKEKMQAVQEATRLKAEA-ELLQ 2375
Cdd:PRK04863 415 QYQ---QAVQAL-ERAKQLCGLPDLTADNAEDWLEEFQ----AKEQEATEELL---SLEQKLSVAQAAHSQFEQAyQLVR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2376 Q-----QKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEmsAEAERLKLRVAEMSRAQARAEEDAQRFRK 2450
Cdd:PRK04863 484 KiagevSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2451 QAEEigeklhRTELATQEKVTLVQTLEIQRQQsdhdAERLRQAIAELE-REKEKLKQEAKLLQLKSEEMQTVQQEQLLQE 2529
Cdd:PRK04863 562 ELEA------RLESLSESVSEARERRMALRQQ----LEQLQARIQRLAaRAPAWLAAQDALARLREQSGEEFEDSQDVTE 631
|
330 340 350
....*....|....*....|....*....|....*
gi 2124423184 2530 TQALQQ----SFLSEKDTLLQRERFIEQEKAKLEQ 2560
Cdd:PRK04863 632 YMQQLLererELTVERDELAARKQALDEEIERLSQ 666
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3136-3172 |
4.03e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.03e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2124423184 3136 KLLSAEKAVTGYKDPYSGKSVSLFQALKKGLIPKEQG 3172
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2199-2560 |
4.65e-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: 46.76 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2199 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTT---LRLQLEET--DHQKSILDEELQRLKAEVTEAARQRSQVEEELF 2273
Cdd:pfam12128 451 LRLNQATATPELLLQLENFDERIERAREEQEAANaevERLQSELRqaRKRRDQASEALRQASRRLEERQSALDELELQLF 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2274 S--------LRVQM----EELGKLKARieaenrALILRDKDNTQRVLQEEAEKMK------HVAEEAARLSVAAQEAARL 2335
Cdd:pfam12128 531 PqagtllhfLRKEApdweQSIGKVISP------ELLHRTDLDPEVWDGSVGGELNlygvklDLKRIDVPEWAASEEELRE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2336 R-ELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEaER 2414
Cdd:pfam12128 605 RlDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ER 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2415 QRQLEmsAEAERLKLRVAEMSRAQAR--AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQ 2492
Cdd:pfam12128 684 LNSLE--AQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLA 761
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 2493 AIAELEREKEKLKQEAKLLQLKSEEMQtVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQ 2560
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIERIA-VRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ 828
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1710-1873 |
4.81e-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: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1710 EAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQElirlrAETEQGEQQRQL-LEEELARLQHEAAAA 1788
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA-----YEIAEANAEREVqRQLEIAEREREIELQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1789 TQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEedAA 1867
Cdd:COG2268 296 EKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IA 370
|
....*.
gi 2124423184 1868 RQRAEA 1873
Cdd:COG2268 371 EAAAKP 376
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1407-1606 |
4.91e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1407 VEAALEKQRQL----AEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQV 1482
Cdd:PRK12678 52 IAAIKEARGGGaaaaAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1483 EAAERSRLRieeeirvvrlqleTTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElavr 1562
Cdd:PRK12678 132 ERGEAARRG-------------AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRRE---- 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423184 1563 vkaeaEAAREKQRALQaleefRLQAEEAERRLRQAEAERARQVQ 1606
Cdd:PRK12678 195 -----ERGRDGDDRDR-----RDRREQGDRREERGRRDGGDRRG 228
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2733-2771 |
5.11e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.39 E-value: 5.11e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 2733 YLQGRSSIAGLLLKPANEKLSIYTALRRQLLSPGTALIL 2771
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1408-1908 |
5.16e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.59 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1408 EAALEKQRQLAEAhAQAKAQAEQeAQELQRRMQEeVARREEAAVDAQQQKRSIQE---ELQHLRQSSEAEiqakarqvea 1484
Cdd:PRK10929 25 EKQITQELEQAKA-AKTPAQAEI-VEALQSALNW-LEERKGSLERAKQYQQVIDNfpkLSAELRQQLNNE---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1485 aersrlriEEEIRVVRLQLETterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRrQVQDETQRKRQAEAElAVRVK 1564
Cdd:PRK10929 92 --------RDEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAR-EISDSLSQLPQQQTE-ARRQL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1565 AEAEaarekqRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSA--EVELQSKRASFAEK-TAQLERTLQee 1641
Cdd:PRK10929 154 NEIE------RRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARLRSELAKKrSQQLDAYLQ-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1642 hvavaqlreeaerraqqqaeaerareeaerelerwqlkaneALRLRLQAEevaqqkslaqaeaekqkeeaerearrrgka 1721
Cdd:PRK10929 226 -----------------------------------------ALRNQLNSQ------------------------------ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1722 eeqavRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQHEAAAATQK-RQELEA--- 1797
Cdd:PRK10929 235 -----RQRE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlre 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1798 ---ELAKVRAEMEVLLASKARAEEESRStsekskQRLEAEASRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRAE 1872
Cdd:PRK10929 308 qsqWLGVSNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAE 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1873 AERVLAEKLAA---------------IGEATRLK---TEAEIALKE-KEAENERL 1908
Cdd:PRK10929 377 QNRILDAQLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2279-2446 |
5.22e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.61 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2279 MEELGKLKARIEAENRALILRDKdntqRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKM 2358
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQK----KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2359 QAVQEATR-LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRvAEMSRA 2437
Cdd:TIGR02794 125 KAKQAAEAkAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK-AEAAKA 203
|
....*....
gi 2124423184 2438 QARAEEDAQ 2446
Cdd:TIGR02794 204 KAAAEAAAK 212
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1383-1572 |
5.44e-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: 46.15 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1383 LRRMEEEERLAEQQRAEERERLAAVEAA-LEKQRQLAEAHAqakaqaEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ 1461
Cdd:pfam05262 203 LKERESQEDAKRAQQLKEELDKKQIDADkAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1462 EELQHLRQSSEAEIQAKARQVEAAERsrlrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRqaQEEAERL 1541
Cdd:pfam05262 277 ENQKREIEKAQIEIKKNDEEALKAKD-------------------------HKAFDLKQESKASEKEAEDK--ELEAQKK 329
|
170 180 190
....*....|....*....|....*....|..
gi 2124423184 1542 RRQVQDETQR-KRQAEAElavrVKAEAEAARE 1572
Cdd:pfam05262 330 REPVAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3059-3096 |
5.46e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.46e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2124423184 3059 RQALRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVA 3096
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1829-1943 |
5.56e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.48 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1829 QRLEAEASRFRELAEEAARLRALAEEAKRQRQlaeedaarqraeAERVLAEKLAAIGEATRLKTEAEIA-LKEKEAENER 1907
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQ------------QELVALEGLAAELEEKQQELEAQLEqLQEKAAETSQ 212
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2124423184 1908 LRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA 1943
Cdd:PRK11448 213 ERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKA 247
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1412-1543 |
5.88e-04 |
|
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: 43.49 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1412 EKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL--RQSSEAEIQAKARQVEAAERSR 1489
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 1490 LRIEEEIRVVRLQLETTERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1543
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1454-1623 |
5.89e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1454 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRL-------RIE-EEIRVVRLQLETTerqrgGAEGELQAlRARAE 1525
Cdd:PTZ00491 647 DSLQKSVQLAIEITTKSQEAAARHQAELLEQEARGRLerqkmhdKAKaEEQRTKLLELQAE-----SAAVESSG-QSRAE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1526 -EAEAQKRQAQEEAErlrrqVQdetQRKRQAEAElavRVKAEAEAAREKQRALQALEEFRLQAE---EAERRLRQAEAER 1601
Cdd:PTZ00491 721 aLAEAEARLIEAEAE-----VE---QAELRAKAL---RIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATK 789
|
170 180
....*....|....*....|....*.
gi 2124423184 1602 ARQVQVAL--ET--AQRSAEVELQSK 1623
Cdd:PTZ00491 790 FERIVEALgrETliAIARAGPELQAK 815
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1145-1789 |
6.12e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1145 EVLKAHEEQLKEAQAVPATLPE-LEATKAALKKLRAQAE-AQQPMFDALRDELRGAQEVGERLQQRHGERDVEV------ 1216
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNnIEKMILAFEELRVQAEnARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliq 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1217 ---------------ERWRERVAQLLERwqavlaqTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLA 1281
Cdd:pfam05483 249 itekenkmkdltfllEESRDKANQLEEK-------TKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1282 DSRAVREQLRQEKALLEEIERHGE--------------KVEECQRFAKQYINAIKDyELQLVTYKAQlepvaspakkpKV 1347
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAahsfvvtefeattcSLEELLRTEQQRLEKNED-QLKIITMELQ-----------KK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1348 QSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETlrrmEEEERLAEQQRAEERErLAAVEAALEKQRQLAEAHAQAKAQ 1427
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK----KQFEKIAEELKGKEQE-LIFLLQAREKEIHDLEIQLTAIKT 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1428 AEQ----EAQELQRRMQEEVARREEaaVDAQQQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRlrieEEIRVVRlQL 1503
Cdd:pfam05483 465 SEEhylkEVEDLKTELEKEKLKNIE--LTAHCDKLLL-ENKELTQEASDMTLELKKHQEDIINCKK----QEERMLK-QI 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1504 ETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEef 1583
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH-- 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1584 rlQAEEAERRLRQAEAERARqvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLreeaerraqqqaeae 1663
Cdd:pfam05483 615 --QENKALKKKGSAENKQLN----AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL--------------- 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1664 rareeaERELERWQLKANEALRLRLQAEEVAQQKslaqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1743
Cdd:pfam05483 674 ------LEEVEKAKAIADEAVKLQKEIDKRCQHK-----------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2124423184 1744 EGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAAT 1789
Cdd:pfam05483 737 QSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2199-2606 |
6.22e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2199 LRQKQAadaEMEKHKKFAEQTLR--QKAQVEQELTTLRLQLE------------ETDHQKSILDEELQRLKAEVTEAARQ 2264
Cdd:pfam05483 101 LKQKEN---KLQENRKIIEAQRKaiQELQFENEKVSLKLEEEiqenkdlikennATRHLCNLLKETCARSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2265 RSQVEEELFSLRVQMEE--LGKLKARIEAENRALILRDKdntqrvLQEEAEKMKHVAEEAARlsvaaqeaarlrelAEED 2342
Cdd:pfam05483 178 REETRQVYMDLNNNIEKmiLAFEELRVQAENARLEMHFK------LKEDHEKIQHLEEEYKK--------------EIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2343 LAQQRALAEKMLKEKMQAVQEATRLkaeaellqqqkelaqeqarrLQEDKEQmAQQLEQETQGFQRTLEAERQRQLEMSA 2422
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFL--------------------LEESRDK-ANQLEEKTKLQDENLKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2423 EAERLKLRVAEMSRAQARAEEDAQRFRK-----------QAEEIGEKLHRTELATQEKVTLVQTLE----IQRQQSDHDA 2487
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAKAAHSFVVTEFEATTCSLEellrTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2488 ERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVqqeqllqetqalqQSFLSEKDTLLqrerfieQEKAKLEQLFQDEVA 2567
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEEL-------------KKILAEDEKLL-------DEKKQFEKIAEELKG 436
|
410 420 430
....*....|....*....|....*....|....*....
gi 2124423184 2568 KAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEE 2606
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2154-2501 |
6.33e-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: 45.29 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2154 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKhkkfAEQTLRQKAQVEQELTTL 2233
Cdd:pfam13868 3 ENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEE----EEKEEERKEERKRYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2234 RLQLEETDHQKSILDEELQRLKAEVTEAARQrsqveeelfslrVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEAE 2313
Cdd:pfam13868 79 EEQIEEREQKRQEEYEEKLQEREQMDEIVER------------IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2314 KMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRAlAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2393
Cdd:pfam13868 147 KEEEREEDERILEYLKEKAEREEEREAEREEIEEE-KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2394 QMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE----DAQRFRKQAEEIGEKLHRTELATQEK 2469
Cdd:pfam13868 226 EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEieqeEAEKRRMKRLEHRRELEKQIEEREEQ 305
|
330 340 350
....*....|....*....|....*....|..
gi 2124423184 2470 VTLVQTLEIQRQQSDHDAERLRQAIAELEREK 2501
Cdd:pfam13868 306 RAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1108-1324 |
6.43e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1108 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAALkklraqaEAQQPM 1187
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1188 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLlerwqavlaqtdlrQRELEQLGRQLRYYRESADPLGAWLQD 1267
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1268 AKRRQEQIQAMVladsRAVREQLRQE-KALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1324
Cdd:COG4913 753 ERFAAALGDAVE----RELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1525-1604 |
6.52e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.10 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1525 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAEL------AVRVKAEAEAAREKQRALQA-LEEFRLQAEEAERRLRQA 1597
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAeaqqqeLVALEGLAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 2124423184 1598 EAERARQ 1604
Cdd:PRK11448 218 RKEITDQ 224
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
421-1370 |
6.66e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 421 EREKQLRSEFERLERLQRIVSKLqmeaglcEEQLNqadallqsdvRLLAAGKAPQRAGEVERDLDKADsmIRLLFNDVQT 500
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNEL-------ERQLK----------SLERQAEKAERYKELKAELRELE--LALLVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 501 LKDGRhpqgeqmyrrvyrlhERLVAIRTEYNLRLKAGVAAPVTQVTQVTlQSTQRRPELEDSTLRYLQDLLAWVEENQRr 580
Cdd:TIGR02168 237 LREEL---------------EELQEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELYALANEISR- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 581 vdgaewgvdlpsveaqlgshrgLHHSIEEFRAKIERARTDEGQLSpatrgAYRDCLGRLDLQYAKLLNSSKGRLRSLESL 660
Cdd:TIGR02168 300 ----------------------LEQQKQILRERLANLERQLEELE-----AQLEELESKLDELAEELAELEEKLEELKEE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 661 YSFVAAATKELMWL---SEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEIQNTGDRLLREDHPARPTVES 737
Cdd:TIGR02168 353 LESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 738 FQ-AALQTQwswmlqlcccIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKytcdrsitVTRLEDLLQDAQDERDQL 816
Cdd:TIGR02168 433 AElKELQAE----------LEELEEELEELQEELERLEEALEELREELEEAEQA--------LDAAERELAQLQARLDSL 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 817 NEYRGHLSGLARRAKAIvqLKPRNPAHPVRGRVPLLAVCD--YKQVEVTVHKGDECQLVGPAQPSHWKVVSSSgSEAAVP 894
Cdd:TIGR02168 495 ERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVDegYEAAIEAALGGRLQAVVVENLNAAKKAIAFL-KQNELG 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 895 SVCFLVPPPNQEAQEAITRLEA-QHQALVTLWHQLHVDMKSllawqSLSRDVQLIRSWSLVTfrtmkpEEQRQALRSLEL 973
Cdd:TIGR02168 572 RVTFLPLDSIKGTEIQGNDREIlKNIEGFLGVAKDLVKFDP-----KLRKALSYLLGGVLVV------DDLDNALELAKK 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 974 HYQAFLRDSQD----------AGGFGPED--RLQAEREYGSCSHHYQQLLQSLEQGEQeesrcqrcisELKDIRLQLEAC 1041
Cdd:TIGR02168 641 LRPGYRIVTLDgdlvrpggviTGGSAKTNssILERRREIEELEEKIEELEEKIAELEK----------ALAELRKELEEL 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1042 ETRTVHRLRLPLDKEpaRECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRS 1121
Cdd:TIGR02168 711 EEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIAQLSKELTE-------------LEAEIEELEERLEEAEE 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1122 LSAIYLEKLKTISLVIRsthGAEEVLKAHEEQLKEAQAVPATLPELEATKA-ALKKLRAQAEAQQPMFDALRDELRGAQE 1200
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNEEAANLReRLESLERRIAATERRLEDLEEQIEELSE 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1201 VGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLgawLQDAKRRQEQIQAMVL 1280
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL---RRELEELREKLAQLEL 929
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1281 ADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakkpkvqsgSESVIQEYVD 1360
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV------------NLAAIEEYEE 997
|
970
....*....|
gi 2124423184 1361 LRTRYSELTT 1370
Cdd:TIGR02168 998 LKERYDFLTA 1007
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1760-2014 |
6.77e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1760 LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAemevlLASKARAEEEsrstsekskqrLEAEasrfR 1839
Cdd:COG0497 156 LLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEA-----AALQPGEEEE-----------LEEE----R 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1840 ELAEEAARLRALAEEAkrQRQLAEED--AARQRAEAERVLaEKLAAIGE-----ATRLkTEAEIALKEKEAEnerLRRLA 1912
Cdd:COG0497 216 RRLSNAEKLREALQEA--LEALSGGEggALDLLGQALRAL-ERLAEYDPslaelAERL-ESALIELEEAASE---LRRYL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1913 EDEAFQRRRLEEqaaqhkadIEERLAQLRKaseselerqkglvedtLRQRRQVE-EEILALkvsfekaaagKAELELELG 1991
Cdd:COG0497 289 DSLEFDPERLEE--------VEERLALLRR----------------LARKYGVTvEELLAY----------AEELRAELA 334
|
250 260
....*....|....*....|...
gi 2124423184 1992 RIrSNAEDTLRSKEQAELEAMRQ 2014
Cdd:COG0497 335 EL-ENSDERLEELEAELAEAEAE 356
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4427-4464 |
6.92e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 6.92e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2124423184 4427 QRFLEVQYLTGGLIEPDVPGRVPLDEALQRGTVDARTA 4464
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1405-1612 |
7.10e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1405 AAVEAALEKQRQLAEAHAQAKAQAEQEAQELQ--RRMQEEVARREEAAVDAQQQKRSIQE-----------ELQHLRQSS 1471
Cdd:PHA03247 1150 STVDAAVRAHGVLADAVAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARlgalgaaaadlAVAVRRENP 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1472 EAE------IQAKARQVEAAERSRLRIEEEIRVVrLQLETTERQRGGAEGELQAL-------RARAEEAEAQkrqAQEEA 1538
Cdd:PHA03247 1230 QAEgdraalLEAAARAVTAAREGLAACEGEFGGL-LHAEGSAGDPSPSGRALQELgkvvgatRRRADELEAA---AADLA 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1539 ERLRRQVQDETQRKRQAEAELAV-RVKAEAEAAREKQRALQAL--------EEFRLQAEeaerrlrQAEAERARQVQVAL 1609
Cdd:PHA03247 1306 EKMAARRARASRERWAADVEAALdRVENRAEFDAVELRRLQALaathgynpRDFRKRAE-------QALAANAKTATLAL 1378
|
...
gi 2124423184 1610 ETA 1612
Cdd:PHA03247 1379 EAA 1381
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1417-1596 |
7.20e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.23 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1417 LAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKarqveaaersrlrieeei 1496
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1497 rvvrlQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQR-----KRQAEAELAV---RVKAEAE 1568
Cdd:COG3524 222 -----LIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARltgasGGDSLASLLAeyeRLELERE 296
|
170 180
....*....|....*....|....*....
gi 2124423184 1569 -AAREKQRALQALEEFRLqaeEAERRLRQ 1596
Cdd:COG3524 297 fAEKAYTSALAALEQARI---EAARQQRY 322
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2203-2422 |
7.34e-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: 45.13 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2203 QAADAEMEKHKKFAEQTLRQKAQVEQEL------------TTLRLQLEETDHQKSILDEELQRLKAEV----TEAARQRS 2266
Cdd:pfam09787 3 ESAKQELADYKQKAARILQSKEKLIASLkegsgvegldssTALTLELEELRQERDLLREEIQKLRGQIqqlrTELQELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2267 QVEEELFSLRvqmEELGKLKARIEAENRAliLRDKDNTQRVLQEEaekMKHVAEEAARLSVAAQEAARLRELAEEDLAQQ 2346
Cdd:pfam09787 83 QQQEEAESSR---EQLQELEEQLATERSA--RREAEAELERLQEE---LRYLEEELRRSKATLQSRIKDREAEIEKLRNQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 2347 raLAEKMLKEKMQAVQEAtRLKAEAELLQQQkelaQEQARRLQEDKEQMAQQLEQ-ETQGFQRTLEAERQRQLEMSA 2422
Cdd:pfam09787 155 --LTSKSQSSSSQSELEN-RLHQLTETLIQK----QTMLEALSTEKNSLVLQLERmEQQIKELQGEGSNGTSINMEG 224
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1747-2093 |
7.40e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1747 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAA----TQKRQELEAELAKVRAEME----VLLASKARAEE 1818
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEErlaeLEAKRQAEEEAREAKAEAEqraaELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1819 ESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA 1894
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKaeeaKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1895 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKV 1974
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1975 SFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVE 2054
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 2124423184 2055 RLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2093
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALA 359
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1387-1648 |
8.55e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1387 EEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEE-------VARREEAAVDAQQQKRS 1459
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafldrTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1460 IQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEI--RVVRLQLETTE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1536
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1537 EAERLRRQV-QDETQRKRQAEAELAVRVKAEAEAAREK---QRALQALEEFRLQAEEAERRLRQaeAERARQVQVALETA 1612
Cdd:pfam02029 165 EAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRghpEVKSQNGEEEVTKLKVTTKRRQG--GLSQSQEREEEAEV 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 2124423184 1613 QRSAEVELQSKRASFAEKTAQ-LERTLQEEHVAVAQL 1648
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKESEeFEKLRQKQQEAELEL 279
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2314-2489 |
8.97e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 45.24 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2314 KMKHvAEEAARLSV--AAQEAARLRELAEEDLAQQRALAEKMLKEK-----MQAVQEAT--RLKAEAELLQQQKELAQEQ 2384
Cdd:PRK00106 25 KMKS-AKEAAELTLlnAEQEAVNLRGKAERDAEHIKKTAKRESKALkkellLEAKEEARkyREEIEQEFKSERQELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2385 ARRLQE------------DKEQMAQQLEQETQGFQRTLEaERQRQLEMSAEAERLKL-RVAEMSRAQARAEEDAQRFRKQ 2451
Cdd:PRK00106 104 SRLTERatsldrkdenlsSKEKTLESKEQSLTDKSKHID-EREEQVEKLEEQKKAELeRVAALSQAEAREIILAETENKL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423184 2452 AEEIGEKLHRTELATQEKVT------LVQTLeiQRQQSDHDAER 2489
Cdd:PRK00106 183 THEIATRIREAEREVKDRSDkmakdlLAQAM--QRLAGEYVTEQ 224
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1720-1955 |
9.05e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.82 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQ-RQLLEEELARLqHEAAAATQKRQEleae 1798
Cdd:pfam05911 10 KVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKI-HDVVLKKTKEWE---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1799 laKVRAEMEVLLAskaraeeesrstsEKSKQRLEAEasrfrelAEEAARLRALAEEAKRQRQLAEEdaaRQRAEAE-RVL 1877
Cdd:pfam05911 85 --KIKAELEAKLV-------------ETEQELLRAA-------AENDALSRSLQERENLLMKLSEE---KSQAEAEiEAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1878 AEKL-AAIGEATRLKTEAEIALKEKEAENErlrrlaEDEaFQRRRLEEQAAQHKADIeERLAQLrkasESELERQKGLV 1955
Cdd:pfam05911 140 KSRLeSCEKEINSLKYELHVLSKELEIRNE------EKN-MSRRSADAAHKQHLESV-KKIAKL----EAECQRLRGLV 206
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2216-2469 |
9.21e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2216 AEQTLRQKAQVEQELTTLRLQLEETDHQK----------SILDEELQRLKAEVT-EAARQRSQVEEELFSLRVQMEELGK 2284
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLiRGATEGLCVHSLSKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2285 LKARIEAENRALI-LRDKDNTQRVLQEEAEKMK-HVAEEAARLSVAAQEAARLRELAEE--------------------- 2341
Cdd:PLN02939 238 LKDDIQFLKAELIeVAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPLQYDcwwekvenlqdlldratnqve 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2342 ----DLAQQRALAEK--MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTL----E 2411
Cdd:PLN02939 318 kaalVLDQNQDLRDKvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLsklkE 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 2412 AERQRQLEMSAEA------ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2469
Cdd:PLN02939 398 ESKKRSLEHPADDmpsefwSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGK 461
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1394-1501 |
9.45e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1394 EQQRAEERERLAAVEAALE-----------KQRQLAEAHAQAKAQAEQEAQELQRRMQEEVA------RREEAAVDAQQQ 1456
Cdd:PRK00409 526 EELERELEQKAEEAEALLKeaeklkeeleeKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADeiikelRQLQKGGYASVK 605
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2124423184 1457 KRSIQEELQHLRQSSEAEIQAKARQVEAAErsRLRIEEEIRVVRL 1501
Cdd:PRK00409 606 AHELIEARKRLNKANEKKEKKKKKQKEKQE--ELKVGDEVKYLSL 648
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1362-1648 |
9.76e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1362 RTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE 1441
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1442 EVARREEAavdaQQQKRSIQEELQHLRQsseaeiqakarQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALR 1521
Cdd:COG4372 92 AQAELAQA----QEELESLQEEAEELQE-----------ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1522 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAER 1601
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2124423184 1602 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1648
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1018-1648 |
9.80e-04 |
|
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: 45.73 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1018 EQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPE 1097
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1098 PSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAALKKL 1177
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1178 RAQAEAQQPMFDALRDELRGAQE-------VGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQ 1250
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1251 LRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQR---FAKQYINAIKDYELQ 1327
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRakvVEGILKDTELTKLKE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1328 LVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERlaEQQRAEERERLAAV 1407
Cdd:pfam02463 640 SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK--KEQREKEELKKLKL 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1408 EAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEA------AVDAQQQKRSIQEELQHLRQSSEAEIQAKARQ 1481
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeekeeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1482 VEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ--AQEEAERLRRQVQDETQRKRQAEAEL 1559
Cdd:pfam02463 798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklAEEELERLEEEITKEELLQELLLKEE 877
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1560 AVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1639
Cdd:pfam02463 878 ELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
|
....*....
gi 2124423184 1640 EEHVAVAQL 1648
Cdd:pfam02463 958 EEERNKRLL 966
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2220-2517 |
1.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2220 LRQKAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIeaenralil 2298
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2299 RDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2378
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2379 ELAQEQARRLQEDKEQMA--QQLEQETQGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIG 2456
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILelEGYEMDYNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2457 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLRQAIAELEREKEKL 2504
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 2124423184 2505 KQEAKllQLKSEE 2517
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3727-3765 |
1.11e-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: 1.11e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2124423184 3727 YLYGTGCVAGVYVPGSRQTLTIYQALKKGLLSAEVARLL 3765
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2234-2464 |
1.11e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2234 RLQLEETDHQKSildEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRAlilrdkdntqrvlQEEAE 2313
Cdd:PRK09510 66 RQQQQQKSAKRA---EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA-------------KQAAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2314 KMKHVAEEAARLSVAAQEAARLRELAEEDLAQQrALAEKMLKEKMQAVQeatrlKAEAEllqQQKELAQEQARRLQEDKE 2393
Cdd:PRK09510 130 KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKKKAEAEAAK-----KAAAE---AKKKAEAEAAAKAAAEAK 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423184 2394 QMAQQleqetqgfqrtlEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2464
Cdd:PRK09510 201 KKAEA------------EAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1191-1559 |
1.11e-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: 44.89 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1191 LRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLgrqLRYYRESADPLGAWLQDAKR 1270
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1271 RQEQIQAMVLADSRAVREQLRQEKALLEEI----ERHGEKVEECQRF---AKQYINAIKDYELQLVTYKAQLEPVASPAK 1343
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIktltQRVLERETELERMkerAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1344 K--PKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISETLRRMEEEERLAEQQRAeERERLAAVEAALEKQRQLAEAH 1421
Cdd:pfam07888 189 SlsKEFQELRNSLAQRDTQVLQLQDTITTLTQK----LTTAHRKEAENEALLEELRS-LQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1422 AQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEiRVVRL 1501
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE-RMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1502 QLETT-ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAEL 1559
Cdd:pfam07888 343 KLEVElGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2305-2483 |
1.19e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2305 QRVLQEEAEKMkhvaeEAARLsvAAQEAARLRELAEE--DLAQQRALAEKMLKE---KMQAVQEATRLKAEAELLQQQKE 2379
Cdd:PRK10929 109 QEILQVSSQLL-----EKSRQ--AQQEQDRAREISDSlsQLPQQQTEARRQLNEierRLQTLGTPNTPLAQAQLTALQAE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2380 LA-------------------QEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQA 2439
Cdd:PRK10929 182 SAalkalvdelelaqlsannrQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIV 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2124423184 2440 RA----EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQS 2483
Cdd:PRK10929 262 AQfkinRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQS 309
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1260-1460 |
1.28e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1260 PLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRfakqyinAIKDYELQLVTYKAQL-EPV 1338
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASR-------KLRETQNTLNQLNKQIdELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1339 ASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLT-------SQ-------YIKFISE----------------TLRRMEE 1388
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQlilsgeeSQrgerilaYFGYLNQarqetiaelkqtreelAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1389 EERLAEQQ----------------RAEERERLAAVEAALEK-QRQLAE--------------AHAQAKAQAEQEAQELQR 1437
Cdd:PRK11637 190 EEKQSQQKtllyeqqaqqqkleqaRNERKKTLTGLESSLQKdQQQLSElranesrlrdsiarAEREAKARAEREAREAAR 269
|
250 260
....*....|....*....|....
gi 2124423184 1438 -RMQEEVARREEAAVDAQQQKRSI 1460
Cdd:PRK11637 270 vRDKQKQAKRKGSTYKPTESERSL 293
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1720-1887 |
1.31e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLEEELARLQHEAAAATQKRQELEAE 1798
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLLELQAESAAVESSGQSRAEALAEAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1799 LAKVRAEMEVLLAS-KARAEE-ESRSTSEKSKQRLEAEASRFRELAEEaarlralaeEAKRQRQLAEEDAARQRAEAERV 1876
Cdd:PTZ00491 727 ARLIEAEAEVEQAElRAKALRiEAEAELEKLRKRQELELEYEQAQNEL---------EIAKAKELADIEATKFERIVEAL 797
|
170
....*....|.
gi 2124423184 1877 LAEKLAAIGEA 1887
Cdd:PTZ00491 798 GRETLIAIARA 808
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1144-1967 |
1.33e-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: 45.04 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1144 EEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDE-LRGAQEVGERLQQRHGERDVEVERWRER 1222
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1223 VAQLLERWQAvlAQTDLRQRELEQLGRQLRYYREsadplgawlqdAKRRQEQIQAMvlaDSRAVREQLRQEKALLEE--- 1299
Cdd:TIGR00606 324 CQRELEKLNK--ERRLLNQEKTELLVEQGRLQLQ-----------ADRHQEHIRAR---DSLIQSLATRLELDGFERgpf 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1300 IER-----HGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK--VQSGSESVIQEYVDLRTRYSELTTLT 1372
Cdd:TIGR00606 388 SERqiknfHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGrtIELKKEILEKKQEELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1373 --SQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREeaa 1450
Cdd:TIGR00606 468 gsSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK--- 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1451 VDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRI---EEEIRVVRLQLETTERQRGGAEGELQALRARAEEA 1527
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1528 E-----AQKRQAQE-EAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREK-------QRALQALEEFRLQAEEAERRL 1594
Cdd:TIGR00606 625 EdklfdVCGSQDEEsDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1595 RQAEAE-RARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL 1673
Cdd:TIGR00606 705 RLAPDKlKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1674 ERWQLKANEALRLRLQAEEVaqQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1753
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDV--ERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1754 EQELIRLRAETEQ---GEQQRQLLEEELARLQHEA----AAATQKRQE---LEAELAKVRAEMEVLLASK----ARAEEE 1819
Cdd:TIGR00606 863 KSKTNELKSEKLQigtNLQRRQQFEEQLVELSTEVqsliREIKDAKEQdspLETFLEKDQQEKEELISSKetsnKKAQDK 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1820 SRSTSEKSKQRLEAEASRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAE------AERVLAEKLa 1882
Cdd:TIGR00606 943 VNDIKEKVKNIHGYMKDIENKIQDgkddylkqketELNTVNAQLEECEKHQEKINEDMRLMRQDidtqkiQERWLQDNL- 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1883 aigeaTRLKTEAEIalkeKEAENERLRRLAedEAFQRRRLEEQAAQHKadIEERLAQLRKASESELERQKGLVEDTLRQR 1962
Cdd:TIGR00606 1022 -----TLRKRENEL----KEVEEELKQHLK--EMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFK 1088
|
....*
gi 2124423184 1963 RQVEE 1967
Cdd:TIGR00606 1089 KELRE 1093
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2219-2573 |
1.34e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 45.05 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2219 TLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT-EAARQRSQVEEELFSlrvqmEELGKLKARIEAENRAL- 2296
Cdd:pfam13166 94 IQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLdECWKKIKRKKNSALS-----EALNGFKYEANFKSRLLr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2297 -ILRDKDNTQRVLQEEAEKmkhvAEEAARLSVAAQEAARLRE-LAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2374
Cdd:pfam13166 169 eIEKDNFNAGVLLSDEDRK----AALATVFSDNKPEIAPLTFnVIDFDALEKAEILIQKVIGKSSAIEELIKNPDLADWV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2375 QQQKELAQE--------QARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEA-ERLKLRVAEMSRAQArAEEDA 2445
Cdd:pfam13166 245 EQGLELHKAhldtcpfcGQPLPAERKAALEAHFDDEFTEFQNRLQKLIEKVESAISSLlAQLPAVSDLASLLSA-FELDV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2446 QRFRKQAEEIGEKLHrtelatqekvTLVQTLEIQRQQSDHDAErLRQAIAELEREKEKLKQEAKLLQlKSEEMQTVQQEQ 2525
Cdd:pfam13166 324 EDIESEAEVLNSQLD----------GLRRALEAKRKDPFKSIE-LDSVDAKIESINDLVASINELIA-KHNEITDNFEEE 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 2526 LLQETQALQQSFLSEKDTLLQRE----RFIEQEKAKLEQLFQDEVAKAQKLR 2573
Cdd:pfam13166 392 KNKAKKKLRLHLVEEFKSEIDEYkdkyAGLEKAINSLEKEIKNLEAEIKKLR 443
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1724-2666 |
1.39e-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: 45.04 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1724 QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAeLAKVR 1803
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1804 AEMEVLLAS-KARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAA-------RQRAEAER 1875
Cdd:TIGR00606 279 KQMEKDNSElELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTellveqgRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1876 VLAEKLAAIGEATRLKTEAEIALKEKEAENERlrRLAEDEAFQRRRLEEQA---AQHKADIEERLAQLRKASESELERQK 1952
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSER--QIKNFHTLVIERQEDEAktaAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1953 GLVEDTLRQRRQVEEEILALKVSFEK----AAAGKAELELELGRIRSNAEDTLrSKEQAELEAMRQRQLAAEEEQRRREA 2028
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKElqqlEGSSDRILELDQELRKAERELSK-AEKNSLTETLKKEVKSLQNEKADLDR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2029 EErvqKSLAAEEEAARQRKAALEEVERL-KAKVEEARRLRERAEQESARQLQLAQDAAQKRlQAEEKAHAFAVQQKEqel 2107
Cdd:TIGR00606 516 KL---RKLDQEMEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKSKEINQ--- 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2108 qqtlqqeqsMLERLRgeaeaarraaeeaeeARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAeklrkeaeqe 2187
Cdd:TIGR00606 589 ---------TRDRLA---------------KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS---------- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2188 aarraqaeqaalrqkQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ 2267
Cdd:TIGR00606 635 ---------------QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2268 VEEELFSLRVQMEELGKLKARIEAEnRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSvaaqeaarlRELAEE--DLAQ 2345
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKR-RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN---------RDIQRLknDIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2346 QralaEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEA 2424
Cdd:TIGR00606 770 Q----ETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKI 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2425 ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLeiqrQQSDHDAERLRQAIAELEREKEKL 2504
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV----QSLIREIKDAKEQDSPLETFLEKD 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2505 KQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTllqrERFIEQEKAKLEQLFQDEVAKaqklreeqqrqqkqme 2584
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI----ENKIQDGKDDYLKQKETELNT---------------- 981
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2585 eekqqLVASMEEARQRQREAEEGVRrkqeeLQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATA 2664
Cdd:TIGR00606 982 -----VNAQLEECEKHQEKINEDMR-----LMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQ 1051
|
..
gi 2124423184 2665 VK 2666
Cdd:TIGR00606 1052 MK 1053
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1779-1906 |
1.43e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 44.01 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1779 ARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKqrlEAEASRfrelaEEAARLRALAEEA-KR 1857
Cdd:PRK06991 146 AWSQAQADAARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAA---AAPAAD-----DAEAKKRAIIAAAlER 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1858 QRQLAEEDAARQRA--EAERVLAEKLAAI--GEATRLKTEAEIALKEKEAENE 1906
Cdd:PRK06991 218 ARKKKEELAAQGAGpkNTEGVSAAVQAQIdaAEARRKRLAEQRDAPDDANADG 270
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1411-1589 |
1.47e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1411 LEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEvaRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKarQVEAAERSRL 1490
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKE--EQLDARAEKL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1491 RIEEEirvvrlQLETTERqrggaegelqALRARAEEAEAQKRQAQEEAERLrrqvqdETQRKRQAEAELAVRVKAEAEaa 1570
Cdd:PRK12705 101 DNLEN------QLEEREK----------ALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180
....*....|....*....|
gi 2124423184 1571 REK-QRALQALEEFRLQAEE 1589
Cdd:PRK12705 157 EEKaQRVKKIEEEADLEAER 176
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1723-1866 |
1.49e-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: 44.61 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1802
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1803 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDA 1866
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1644-2099 |
1.51e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.01 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1644 AVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEE 1723
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1724 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVR 1803
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1804 AEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1883
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1884 IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRR 1963
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1964 QVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAA 2043
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 2044 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFA 2099
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2210-2561 |
1.51e-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: 45.01 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2210 EKHKKFAEQTLRQKAQVEQ---ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLK 2286
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEKlnnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2287 ARI-EAENRALILRD-KDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQqralAEKMLKEKMQAVQEa 2364
Cdd:TIGR04523 218 SQIsELKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ----NNKKIKELEKQLNQ- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2365 trLKAEAELLQQQKE---------LAQEQARRLQEDKEQMAQ------QLEQETQGFQRTLEAERQRQLEMSAEAERLKL 2429
Cdd:TIGR04523 293 --LKSEISDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2430 RVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAK 2509
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 2510 LLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQL 2561
Cdd:TIGR04523 451 VKELIIKNLDN-TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
80-183 |
1.56e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.66 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 80 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 137
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2124423184 138 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 183
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1759-1970 |
1.58e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1759 RLRAETEQGEQQRQLLEEELARLQHEAAAAtqkrqelEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEAEAsrf 1838
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA-------EAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARA--- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1839 rELAEEAARLRALAEEAKRQRQ-LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEA- 1916
Cdd:COG3206 234 -ELAEAEARLAALRAQLGSGPDaLPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAq 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1917 ---FQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEdtLRQRRQVEEEIL 1970
Cdd:COG3206 313 rilASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR--LEREVEVARELY 367
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1514-1648 |
1.62e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1514 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDetqRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERR 1593
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1594 LRQAEAERARQ-VQVALETAQRSAEVELQSK----RASFAEKTAQLERTLQEEHVAVAQL 1648
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1730-1951 |
1.68e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1730 ELAEQELEKQRQLAEGTAQqrlAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEV 1808
Cdd:pfam09787 3 ESAKQELADYKQKAARILQ---SKEKLIASLKeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1809 LLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARL----RALAEEAKRQRQLAEEDAARQRAEAERVlaeklaai 1884
Cdd:pfam09787 80 LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLqeelRYLEEELRRSKATLQSRIKDREAEIEKL-------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1885 geATRLKTEAEIALKEKEAENeRLRRLAEDEAFQRRRLEEQAAQHKADI--EERLAQLRKASESELERQ 1951
Cdd:pfam09787 152 --RNQLTSKSQSSSSQSELEN-RLHQLTETLIQKQTMLEALSTEKNSLVlqLERMEQQIKELQGEGSNG 217
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1410-1581 |
1.69e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1410 ALEKQRQLA--------EAHAQAKAQA-EQEAQ-ELQR-RMQEEVARREEAAVDAQQQKRSiqEELQHLRQS-SEAEIQA 1477
Cdd:PTZ00491 648 SLQKSVQLAieittksqEAAARHQAELlEQEARgRLERqKMHDKAKAEEQRTKLLELQAES--AAVESSGQSrAEALAEA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1478 KARQVEAaersrlrieeeirvvrlqletterqrggaEGELQALRARAEeaeaqkrqaqeeAERLRRQVQDETQRKRQaEA 1557
Cdd:PTZ00491 726 EARLIEA-----------------------------EAEVEQAELRAK------------ALRIEAEAELEKLRKRQ-EL 763
|
170 180
....*....|....*....|....
gi 2124423184 1558 ELAVRvKAEAEAAREKQRALQALE 1581
Cdd:PTZ00491 764 ELEYE-QAQNELEIAKAKELADIE 786
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3099-3132 |
1.71e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 1.71e-03
10 20 30
....*....|....*....|....*....|....
gi 2124423184 3099 LLEAQAGTGHIIDPATSARLTVDEAVRSGLVGPE 3132
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2359-2454 |
1.72e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2359 QAVQEA-TRLKAEAELLQQQK---ELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEA------ERQRQL-EMSAEAERL 2427
Cdd:PRK11637 166 QARQETiAELKQTREELAAQKaelEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGlesslqKDQQQLsELRANESRL 245
|
90 100 110
....*....|....*....|....*....|.
gi 2124423184 2428 KLRVAEMSR-AQARAEE---DAQRFRKQAEE 2454
Cdd:PRK11637 246 RDSIARAEReAKARAERearEAARVRDKQKQ 276
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1008-1433 |
1.76e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1008 QQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1087
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1088 EAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTislvirsthgAEEVLKAHEEQLKEAQAVPATLPEL 1167
Cdd:COG4717 178 ELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEE----------AQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1168 EATKAALKKLRAQA-----EAQQPMFDALRDELRGAQEVGERLQQRHGERDVeveRWRERVAQLLERWQAVLAQTDLRQR 1242
Cdd:COG4717 243 ERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1243 ELEQLGRQLRYYRE-SADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQE-KALLEEIerHGEKVEECQRFAKQYiNA 1320
Cdd:COG4717 320 ELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAEA--GVEDEEELRAALEQA-EE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1321 IKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISET---LRRMEEEERLAE--Q 1395
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeaeLEQLEEDGELAEllQ 476
|
410 420 430
....*....|....*....|....*....|....*...
gi 2124423184 1396 QRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQ 1433
Cdd:COG4717 477 ELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1394-1497 |
1.77e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 43.63 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1394 EQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAqelqrRMQEEVARREEAAVDAQQQKRS-IQEELQHLRQSSE 1472
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARAAARAAASAAA-----AAAEASAAAAPAADDAEAKKRAiIAAALERARKKKE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423184 1473 ----------------AEIQAkarQVEAAERSRLRIEEEIR 1497
Cdd:PRK06991 224 elaaqgagpkntegvsAAVQA---QIDAAEARRKRLAEQRD 261
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1517-1616 |
1.80e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.08 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1517 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEtQRKRQAEAElAVRVKAEAEAAREKQRALQALEefrlqaEEAERR 1593
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 2124423184 1594 LRQAEAERARQVQVALETAQRSA 1616
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1855-2076 |
1.84e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1855 AKRQRQLAEEDAARQRAEAERvlaeklaaigEATRLKTEAEIALKEkeaENERLRRLAEDEAFQRRR-LEEQaaqhkadi 1933
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKK----------EAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNeLQKL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1934 EERLAQlrkaSESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAaagKAELElelgrirsnaedTLRSKEQAELEAMr 2013
Cdd:PRK12704 88 EKRLLQ----KEENLDRKLELLEKREEELEKKEKELEQKQQELEKK---EEELE------------ELIEEQLQELERI- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 2014 qrqlaaeeeqrrreaeervqKSLAAEEeaARQRkaALEEVERlKAKVEEARRLR---ERAEQESAR 2076
Cdd:PRK12704 148 --------------------SGLTAEE--AKEI--LLEKVEE-EARHEAAVLIKeieEEAKEEADK 188
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1452-1639 |
1.93e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.76 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1452 DAQQQKRSiqeELQHLRQSSEAEIQAKARQVEAA--ERSRLRIE-----EEIRVVRLQLETTERQRGGAEGELQALRARA 1524
Cdd:pfam00038 36 ELRQKKGA---EPSRLYSLYEKEIEDLRRQLDTLtvERARLQLEldnlrLAAEDFRQKYEDELNLRTSAENDLVGLRKDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1525 EEAEAQKRQAQEEAERL------RRQVQDETQRKRQAEAELAVRVkAEAEAAReKQRALQALEEFRLQAEE-AERRLRQA 1597
Cdd:pfam00038 113 DEATLARVDLEAKIESLkeelafLKKNHEEEVRELQAQVSDTQVN-VEMDAAR-KLDLTSALAEIRAQYEEiAAKNREEA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2124423184 1598 EAerarQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQ 1639
Cdd:pfam00038 191 EE----WYQSKLEELQQAAARNGDALRSA-KEEITELRRTIQ 227
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1066-1635 |
1.97e-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: 44.35 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1066 AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLeqvrslsaiyLEKLKTISLVIRSTHGAEE 1145
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRN----------QELQKRIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1146 VLKAHEEQLKEAQAVPATLPELEATKAALkklraQAEAQQpMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQ 1225
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1226 LLERWQAV---LAQTDLRQREL---EQLGRQLRYYRESADPLGAWLQDAKRRQEQIqamvlADSRAVREQLRQEKALLEE 1299
Cdd:pfam05557 144 LKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI-----PELEKELERLREHNKHLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1300 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASpakkpKVQSGsESVIQEY-VDLRTRyselTTLTSQYIKF 1378
Cdd:pfam05557 219 NIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ-----ELQSW-VKLAQDTgLNLRSP----EDLSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1379 ISETLRRMEEEERLAEQQRAEERErlaaveaalekQRQLAEAHAQAKAQAEQEAQELQRrmQEEVARReeaavdAQQQKR 1458
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKA-----------RRELEQELAQYLKKIEDLNKKLKR--HKALVRR------LQRRVL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1459 SIQEELQHLRQ---------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGG-------AEGELQALRA 1522
Cdd:pfam05557 350 LLTKERDGYRAilesydkelTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGykqqaqtLERELQALRQ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1523 RAEEAEAQkrQAQEEAERLRRQVQD---ETQRKRQAEAELAVRV-----KAEAEAAREKQRALQ---ALEEFRLQAEEAE 1591
Cdd:pfam05557 430 QESLADPS--YSKEEVDSLRRKLETlelERQRLREQKNELEMELerrclQGDYDPKKTKVLHLSmnpAAEAYQQRKNQLE 507
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2124423184 1592 RrlRQAEAERAR----QVQVALETAQRSAEVELQSKRASFAEKTAQLE 1635
Cdd:pfam05557 508 K--LQAEIERLKrllkKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2150-2507 |
2.07e-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: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2150 RRQVEEAERLKQSAEEQAQAQAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAeQTLRQKAQVEQE 2229
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEE---------------------------KYKELSASSEELSEEKD-ALLAQRAAHEAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2230 LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRAL--ILRDKDNTQRV 2307
Cdd:pfam07888 131 IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQRDTQVLQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2308 LQEEAEKMKHVAEEAARlSVAAQEAAR--LRELAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKELAQ--- 2382
Cdd:pfam07888 211 LQDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQAAQltl 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2383 ---EQARRLQEDKEQMAqqleQETQGFQRTLEAERQRQLEMSAEAERLKLRVaemsraqarAEEDAQRfrkqaeeigEKL 2459
Cdd:pfam07888 287 qlaDASLALREGRARWA----QERETLQQSAEADKDRIEKLSAELQRLEERL---------QEERMER---------EKL 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2124423184 2460 hRTELATQEKVTLVQTLEIQRQQSDhdaerLRQAIAELEREKEKLKQE 2507
Cdd:pfam07888 345 -EVELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAE 386
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1674-2157 |
2.08e-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: 44.35 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1674 ERWQLKANEALRLRLQAEEVAQQKSLAQ--AEAEKQKEEAER---------------EARRRGKAEEQAVRQRELAEQEL 1736
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKriRLLEKREAEAEEalreqaelnrlkkkyLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1737 EKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLE----------EELARLQHEAAAATQKRQELEAELAKVRAEM 1806
Cdd:pfam05557 108 CLKNELSE-LRRQIQRAELELQSTNSELEELQERLDLLKakaseaeqlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1807 EVLLASKarAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLAEKLA- 1882
Cdd:pfam05557 187 EIVKNSK--SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSw 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1883 -AIGEATRLKTEAEIALKEK--EAENERLRRLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASESE---LERQKGLVE 1956
Cdd:pfam05557 265 vKLAQDTGLNLRSPEDLSRRieQLQQREIVLKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRHKALVR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1957 DTLRQRRQVEEEILALKV---SFEKAAAGKAELELELGRIRSNAEdtLRSKEQAELEAMR-QRQLAAEEEQRRREAEERV 2032
Cdd:pfam05557 343 RLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEEAED--MTQKMQAHNEEMEaQLSVAEEELGGYKQQAQTL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2033 QKSLAA--EEEAARQRKAALEEVERLKAKVEEAR----RLRERAEQESAR--QLQLAQDAAQKR---LQAEEKAHAFAVQ 2101
Cdd:pfam05557 421 ERELQAlrQQESLADPSYSKEEVDSLRRKLETLElerqRLREQKNELEMEleRRCLQGDYDPKKtkvLHLSMNPAAEAYQ 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 2102 QKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAE 2157
Cdd:pfam05557 501 QRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAE 556
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1468-1940 |
2.10e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1468 RQSSEAEIQAKARQVEAAERSRLRIEEEIRVvRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1547
Cdd:COG3064 7 EKAAEAAAQERLEQAEAEKRAAAEAEQKAKE-EAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1548 ETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASF 1627
Cdd:COG3064 86 AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1628 AEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQ 1707
Cdd:COG3064 166 AAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1708 KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAA 1787
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1788 ATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAA 1867
Cdd:COG3064 326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRL 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1868 RQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 1940
Cdd:COG3064 406 DLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1426-1795 |
2.15e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1426 AQAEQEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQl 1503
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRqkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1504 ETTERQRggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKqralqalEEF 1583
Cdd:pfam02029 81 EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWST-------EVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1584 RLQAEEAERRLRQAEAERA-RQVQVALETAQRSAEVELQSKRASfaEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEA 1662
Cdd:pfam02029 151 QAEEEGEEEEDKSEEAEEVpTENFAKEEVKDEKIKKEKKVKYES--KVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1663 ERAREEAERELERWQLKANEALrlrlqaeevaqqkslaqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQl 1742
Cdd:pfam02029 229 GLSQSQEREEEAEVFLEAEQKL-------------------------------------EELRRRRQEKESEEFEKLRQ- 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1743 aegtAQQRLAAEQELI--------RLRAETEQG----EQQRQLLEEELARLQHEA-----AAATQKRQEL 1795
Cdd:pfam02029 271 ----KQQEAELELEELkkkreerrKLLEEEEQRrkqeEAERKLREEEEKRRMKEEierrrAEAAEKRQKL 336
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1720-1972 |
2.16e-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: 43.75 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQ--ELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELE 1796
Cdd:pfam13868 67 RKEERKRYRQELEEQieEREQKRQEEyEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1797 AE--------LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEE--AARLRALAEEAKRQRQLAEEDA 1866
Cdd:pfam13868 147 KEeereederILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQEEQERKERQKEREE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1867 ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN--ERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQL 1940
Cdd:pfam13868 227 AEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAEKRRMKRLEHRRElekqIEEREEQR 306
|
250 260 270
....*....|....*....|....*....|..
gi 2124423184 1941 RKASESELERQKGLVEDTLRQRRQVEEEILAL 1972
Cdd:pfam13868 307 AAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2299-2452 |
2.18e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2299 RDKDNTQRVLQE---EAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQ 2375
Cdd:PRK12705 30 RLAKEAERILQEaqkEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREE-ERLVQKEEQLDARAEKLDNLENQLE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 2376 QQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQA 2452
Cdd:PRK12705 109 EREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2808-2844 |
2.19e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.19e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2124423184 2808 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVRDHG 2844
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1144-1432 |
2.19e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1144 EEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEvgERLQQRhgERDVEVERWRE-- 1221
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQE--EIAMEISRMREle 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1222 -----------RVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYREsadplgawlQDAKRRQEQIQAMVLADSRAVREQL 1290
Cdd:pfam17380 382 rlqmerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA---------EQEEARQREVRRLEEERAREMERVR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1291 RQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEyvdlRTRYSELTT 1370
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE----KEMEERQKA 528
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1371 LTSQYIKFISETLRR----MEEEERLAEQQR--AEERERLAAVEAALEKQRQLAEAHaqaKAQAEQEA 1432
Cdd:pfam17380 529 IYEEERRREAEEERRkqqeMEERRRIQEQMRkaTEERSRLEAMEREREMMRQIVESE---KARAEYEA 593
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1720-2158 |
2.21e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgeQQRQLLEEELARLQHEAAAATQKRQELEAEL 1799
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQ--RAAELAAEAAKKLAEAEKAAAEAEKKAAAEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1800 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1879
Cdd:COG3064 98 AKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1880 KLAA-IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDT 1958
Cdd:COG3064 178 AAAAlVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1959 LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 2038
Cdd:COG3064 258 GVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2039 EEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSML 2118
Cdd:COG3064 338 EAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASA 417
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2124423184 2119 ERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAER 2158
Cdd:COG3064 418 VELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTG 457
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2200-2400 |
2.22e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2200 RQKQAADAEMEKHKKFAEQTLRQK-AQVEQELTTLRLQLEETDHQKSILDEELQRlKAEVTEAARQRS-QVEEELFSLRV 2277
Cdd:COG2268 201 ARIAEAEAERETEIAIAQANREAEeAELEQEREIETARIAEAEAELAKKKAEERR-EAETARAEAEAAyEIAEANAEREV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2278 QME-ELGKLKARIEAEnralilrdkdnTQRVLQEEAEKMKHVAEEAArlsvAAQEAARLRELAEEDLAQQRALAEKmlke 2356
Cdd:COG2268 280 QRQlEIAEREREIELQ-----------EKEAEREEAELEADVRKPAE----AEKQAAEAEAEAEAEAIRAKGLAEA---- 340
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423184 2357 kmqavqEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE 2400
Cdd:COG2268 341 ------EGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLE 378
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2320-2517 |
2.23e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2320 EEAARLSVAAQEAARLRelAEEDLAQQRALAEkmLKEKmQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2399
Cdd:PRK05035 465 EKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2400 EQETQGFQRTLEAERQR-----------QLEMSAEAERLKLRV-AEMSRAQAR-AEEDAQRFRKQAEEIGEKLHRTELAT 2466
Cdd:PRK05035 540 AAAADPKKAAVAAAIARakakkaaqqaaNAEAEEEVDPKKAAVaAAIARAKAKkAAQQAASAEPEEQVAEVDPKKAAVAA 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2124423184 2467 QEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEE 2517
Cdd:PRK05035 620 AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE 670
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1384-1465 |
2.29e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.53 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1384 RRMEEEERLAEQQRAEERERLAAVEA-ALEKQRQLAEAHAQAK---AQAEQEAQELQRR-----MQEEVARREEAAVDAQ 1454
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKLAAEalaeaQAEAQASKEKARREIE 111
|
90
....*....|.
gi 2124423184 1455 QQKRSIQEELQ 1465
Cdd:PRK07353 112 QQKQAALAQLE 122
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1223-1500 |
2.29e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1223 VAQLLERWQAVLAQTDLRQRELEQLGRQlryyresadplgawLQDAKRRQEQIQAMVLADSRAVREQLRQ--EKALLEEI 1300
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQ--------------LAQAPAKLRQAQAELEALKDDNDEETREtlSTLSLRQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1301 ERhgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSelTTLTSQyiKFIS 1380
Cdd:PRK11281 127 ES---RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLR-RMEEEERLAEQQRAEERERLAA---VEAALEKQRQLAEAHAQakaQAEQEAQELQ------RRMQ-EEVARREEA 1449
Cdd:PRK11281 191 PSQRvLLQAEQALLNAQNDLQRKSLEGntqLQDLLQKQRDYLTARIQ---RLEHQLQLLQeainskRLTLsEKTVQEAQS 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1450 AVDAQQQKRS--IQEELQHLRQSSEAEIQAKAR-------------QVEAAERSRLRIEEEIRVVR 1500
Cdd:PRK11281 268 QDEAARIQANplVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQISVLK 333
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1360-1632 |
2.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1360 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAE---QEAQELQ 1436
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1437 RRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSS----------EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETT 1506
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRkqleaqiaelQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1507 ERQRggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQ 1586
Cdd:COG4372 177 SEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2124423184 1587 AEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1632
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1381-1494 |
2.49e-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: 41.56 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLRRMEEEERLAEQQRA-EERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQEL-QRRMQEEVARREEAAVDAQQQKR 1458
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423184 1459 SIQEELQHLRQSSEAeiqAKARQVEAAERSRLRIEE 1494
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAERQRQEREK 123
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
1384-1540 |
2.52e-03 |
|
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.
Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 43.73 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1384 RRMEEEERLAEQQRAE---ERERLAAVEAALEKQRQLAEAHAQA---KAQA-EQEAQELQRRMQEEVARREE-------- 1448
Cdd:pfam05914 165 KQAEEEEKHAELLYDQkrlERDRRALELAKLEEECRRAVNAATKnfnQALAaEQAERRRLEKRQEQEDNLAEiynhltsd 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1449 -------AAVDAQQQKRSIQEELQHLRQSSEAEIQaKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALR 1521
Cdd:pfam05914 245 lltenpeVAQSSLGPHRVIPDRWKGMSPEQLKEIR-KEQEQQREEKERRREEEKQRDAEWDRQRLELARAALLLEREQQR 323
|
170 180
....*....|....*....|...
gi 2124423184 1522 ARAEEAEAQ----KRQAQEEAER 1540
Cdd:pfam05914 324 LRRELRRQLdeenLQLAQEQKAR 346
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2362-2440 |
2.55e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 43.55 E-value: 2.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 2362 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLEQETQgfqrTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2440
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQAK----ALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
81-189 |
2.57e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.13 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 81 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 151
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 2124423184 152 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 189
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2731-2768 |
2.58e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.58e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2124423184 2731 RRYLQGRSSIAGLLLKPANEKLSIYTALRRQLLSPGTA 2768
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
92-182 |
2.60e-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: 40.75 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 92 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 164
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 2124423184 165 DDIADGNPKLTLGLIWTI 182
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2771-2804 |
2.71e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.71e-03
10 20 30
....*....|....*....|....*....|....
gi 2124423184 2771 LLEAQAASGFLLDPVQNRRLTVNEAVKEGVVGPE 2804
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1249-1461 |
2.79e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1249 RQLRYYRESADPLGAWLQDAKRRQEQiqamVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINA---IKDYE 1325
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRK----ELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAraeLAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1326 LQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSEL-TTLTSQYIKF------ISETLRRMEEEERLAEQQRA 1398
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsARYTPNHPDVialraqIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1399 EERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEE-------VARREEAAVDAQQQKRSIQ 1461
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelyeslLQRLEEARLAEALTVGNVR 389
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2216-2394 |
2.86e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2216 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR--SQVEEELFSLRVQMEELgklKARIEAEN 2293
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAEL---SARYTPNH 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2294 RALilrdkdntQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2373
Cdd:COG3206 291 PDV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
170 180
....*....|....*....|.
gi 2124423184 2374 LQQQKELAQEQARRLQEDKEQ 2394
Cdd:COG3206 363 ARELYESLLQRLEEARLAEAL 383
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1162-1605 |
3.10e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.74 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1162 ATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQ 1241
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1242 RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAI 1321
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1322 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEER 1401
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1402 ERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQ 1481
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1482 VEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAV 1561
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2124423184 1562 RVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQV 1605
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1393-1465 |
3.23e-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: 40.88 E-value: 3.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1393 AEQQRAEERERLAAVEAALEKQRQLAEA-HAQAKAQAEQEAQELQRRMQEEVAR-REEAAVDAQQQKRSIQEELQ 1465
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEiIEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQEKEKALAELR 116
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2214-2381 |
3.28e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.30 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2214 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKSILDEElqrlkAEVTEAARQRSQVEEELFSLRVQMEELgklkARIEAEN 2293
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAAL----RSYLSPN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2294 RALIlrdkdntqRVLQEEAEKMKH-VAEEAARLSVAAQEAARLRELAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEA 2371
Cdd:COG3524 248 SPQV--------RQLRRRIAALEKqIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEA 316
|
170
....*....|
gi 2124423184 2372 EllQQQKELA 2381
Cdd:COG3524 317 A--RQQRYLA 324
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2199-2463 |
3.38e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2199 LRQKQAADAEMEKHKK-----FAE-QTLRQK-AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2271
Cdd:COG1340 14 EEKIEELREEIEELKEkrdelNEElKELAEKrDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2272 LFSLRVQMEELG-------KLKARIEA-------------ENRALILRDKDntqrvLQEEAEKMKHVAEEAARLSVAAQE 2331
Cdd:COG1340 94 LDELRKELAELNkaggsidKLRKEIERlewrqqtevlspeEEKELVEKIKE-----LEKELEKAKKALEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2332 AARLRELAEEDLAQQRALAEKM--LKEKMQAV-QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLeqetqgfqr 2408
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL--------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 2409 tleaerqRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTE 2463
Cdd:COG1340 240 -------RELRKELKKLRKKQRALKREKEKEELEE-------KAEEIFEKLKKGE 280
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1737-2010 |
3.38e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 43.31 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1737 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQL-----LEEELARLqheaaaaTQKRQELEAELAKVRAEMEV 1808
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQYdsnrrLGERIQDI-------TFWKSELEKELEELDEEIEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1809 LLASKARAEEESRSTSEK---SKQRLEAEASRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAAR 1868
Cdd:pfam03148 76 LLEEKRRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1869 QRAEAErvLAEKLAAIG---EATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLR 1941
Cdd:pfam03148 154 HKLEKD--LSDKKEALEideKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSIL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1942 KASESELERQKGLVEDTLRQRrqVEEeilalkvsFEKAaagKAELELELGRIRSNAEDTlrSKEQAELE 2010
Cdd:pfam03148 232 EQTANDLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTLQEIAEL--EKNIEALE 285
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1736-2103 |
3.49e-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: 43.35 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1736 LEKQRQLAE-GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAElaKVRAEMEVLLASKA 1814
Cdd:pfam07888 9 LEEESHGEEgGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE--RQRRELESRVAELK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1815 RAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRAlAEEAKRQRQLAEEDAArqRAEAERVLaeklaaigeatrlktea 1894
Cdd:pfam07888 87 EELRQSREKHEELEEKYKELSASSEELSEEKDALLA-QRAAHEARIRELEEDI--KTLTQRVL----------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1895 eialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKV 1974
Cdd:pfam07888 147 -----ERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS-KEFQELRNSLAQRDTQVLQLQDTITTLTQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1975 SFEKAAAGKAELELELGRIRSNAE-------------------DTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKS 2035
Cdd:pfam07888 221 KLTTAHRKEAENEALLEELRSLQErlnaserkveglgeelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRA 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 2036 LAAEEEAARQRKAALE---------EVERLKAKVEEARRLRERAEQESARQ--LQLAQDAAQKRLQAEEKAhAFAVQQK 2103
Cdd:pfam07888 301 RWAQERETLQQSAEADkdrieklsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQK 378
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1394-1510 |
3.61e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1394 EQQRAEERERLAAVEAALEKQRQLAEAhaQAKAQAEQEAQELQRRMQEEVARREEAavdaqqQKRSIQEELQHLRQSSEA 1473
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAKEKAIEAE--RAKAEAAEAEQELLREKQKEEEQMMEA------QERSYQEHVKQLIEKMEA 254
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423184 1474 EIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQR 1510
Cdd:pfam02841 255 EREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1411-1557 |
3.66e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.00 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1411 LEKQRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEA----- 1484
Cdd:pfam13904 47 LKLERQPLEAYENwLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAesask 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1485 --AERSRLRIEEEIRVVRLQLETTERQRggaegelqalraraeeaeaQKRQAQEEAERLRRQVQDETQRKRQAEA 1557
Cdd:pfam13904 127 slAKPERKVSQEEAKEVLQEWERKKLEQ-------------------QQRKREEEQREQLKKEEEEQERKQLAEK 182
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1460-1831 |
3.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1460 IQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1539
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1540 RLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQAlEEFRLQAEEAERRLRQAEAERARQVQvalETAQRSAEVE 1619
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELE-SLQEEAEELQEELEELQK-ERQDLEQQRKQLEAQIAELQSEIAER---EEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1620 LQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1699
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1700 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1779
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 1780 RLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL 1831
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1720-1875 |
3.70e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 42.66 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1720 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQelEAEL 1799
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRR--NEEL 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1800 AKvRAEMEVLLASKARAEEESRSTSEKskqrlEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER 1875
Cdd:pfam12037 129 LR-KQEESVAKQEAMRIQAQRRQTEEH-----EAELRRETERAKAEAEAEARAKEERENEDLNLEQ-LREKANEER 197
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1461-1647 |
3.80e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.95 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1461 QEELQHLRQSSEAEIQakarqveaaersrlRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1540
Cdd:pfam15665 13 EAEIQALKEAHEEEIQ--------------QILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1541 LRRQVQDetqRKRQAEAELAVRVKAEAEAAREKQRALQA-LEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSaeve 1619
Cdd:pfam15665 79 YKRRVEE---RELKAEAEHRQRVVELSREVEEAKRAFEEkLESFEQLQAQFEQEKRKALEELRAKHRQEIQELLTT---- 151
|
170 180
....*....|....*....|....*...
gi 2124423184 1620 LQSKRASFAEKTAQLERTLQEEHVAVAQ 1647
Cdd:pfam15665 152 QRAQSASSLAEQEKLEELHKAELESLRK 179
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2362-2509 |
3.85e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2362 QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAErlklrvaeMSRAQARA 2441
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA--------AAAAKAKA 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423184 2442 EEDAQRFR---KQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSdhdAERLRQAIAELErEKEKLKQEAK 2509
Cdd:PRK09510 150 EAEAKRAAaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK---AAAEAKKKAEAE-AKKKAAAEAK 216
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1731-2016 |
3.92e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1731 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLL 1810
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1811 ASKARAEeesrsTSEKSKQRLEAE--ASRFRELAEEAARLRALAEEAKRqrqlaeedaarqraeAERVLAeKLAAIGEAt 1888
Cdd:PRK11637 110 ASIAKLE-----QQQAAQERLLAAqlDAAFRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1889 RLKTEAEialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVedtlrqrrqveee 1968
Cdd:PRK11637 168 RQETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 1969 ilALKVSFEKAAAGKAELELELGRIRSN-AEDTLRSKEQAELEA-----MRQRQ 2016
Cdd:PRK11637 223 --GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarVRDKQ 274
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2368-2509 |
3.99e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2368 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQgfQRTLEAERQRQLEMSAEAErlklrvAEMSRAQARAEEDAQR 2447
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK--QRAAEQARQKELEQRAAAE------KAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423184 2448 fRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAK 2509
Cdd:TIGR02794 118 -QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1468-1603 |
4.03e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1468 RQSSEAEIQAKARQVEA-AERSRLRIE-EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR--- 1542
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvla 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423184 1543 -------RQVQDETQRKRQAEAELAVRVKAEAEAAREK-QRALQALEEFRLQAEEAERRLRQAEAERAR 1603
Cdd:pfam00529 134 piggisrESLVTAGALVAQAQANLLATVAQLDQIYVQItQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3062-3099 |
4.15e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 37.69 E-value: 4.15e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2124423184 3062 LRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVAVAL 3099
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1384-1791 |
4.16e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1384 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAK-AQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1462
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1463 ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1542
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1543 RQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQS 1622
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1623 KRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQA 1702
Cdd:COG3064 264 LAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1703 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1782
Cdd:COG3064 344 LAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
....*....
gi 2124423184 1783 HEAAAATQK 1791
Cdd:COG3064 424 LALAGAAGA 432
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1379-1480 |
4.25e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.67 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1379 ISETLRR----MEEEE-RL---AEQQRAEER----ERLAAVEAAlEKQRQLAEAHAQAKAqAEQEAQELQRRMQEE--VA 1444
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLliaEQHQKVVEKeaetERKRAVIEA-EKDAEVAKIQMQQKI-MEKEAEKKISEIEDEmhLA 237
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2124423184 1445 rREEAAVDAQQQKRSIQEELQHLRQSSE----AEIQAKAR 1480
Cdd:cd03406 238 -REKARADAEYYRALREAEANKLKLTPEylelKKYQAIAN 276
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1728-1821 |
4.26e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.29 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1728 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEME 1807
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 2124423184 1808 VLLASKARAEEESR 1821
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2199-2420 |
4.37e-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: 42.60 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2199 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ-VEEELFSLRV 2277
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2278 QMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEK 2357
Cdd:pfam13868 199 EKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQ 278
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 2358 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEM 2420
Cdd:pfam13868 279 EEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1768-1972 |
4.55e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1768 EQQRQLLEeeLARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAsrfRELAEEAAR 1847
Cdd:COG1579 4 EDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLELEI---EEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1848 LRALAEEAKRQRQLA-----EEDAARQRAEAERVLAEklaaigeatrlkteaeiALKEKEAENERLRRLAEDEAFQRRRL 1922
Cdd:COG1579 78 YEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILE-----------------LMERIEELEEELAELEAELAELEAEL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1923 EEQaaqhKADIEERLAQLRKASESELERQKGLVEdtlrqrrQVEEEILAL 1972
Cdd:COG1579 141 EEK----KAELDEELAELEAELEELEAEREELAA-------KIPPELLAL 179
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2200-2507 |
4.64e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2200 RQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2279
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2280 EELGKLKARIEAENRAlilrdkDNTQRvlqeeaekmkhvaeeaaRLSVAAQEAARLRELAEEDLAQQRALAEKMLKeKMQ 2359
Cdd:pfam15905 132 LELTRVNELLKAKFSE------DGTQK-----------------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2360 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRqLEMSAEAERLKLRVAEMSRAQA 2439
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 2440 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQE 2507
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| HPtr |
COG2198 |
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms]; |
1721-2500 |
4.98e-03 |
|
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
Pssm-ID: 441800 [Multi-domain] Cd Length: 871 Bit Score: 43.11 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1721 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1800
Cdd:COG2198 11 LLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLLELLLLLLLLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1801 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1880
Cdd:COG2198 91 LLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1881 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLR 1960
Cdd:COG2198 171 LLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1961 QRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEE 2040
Cdd:COG2198 251 LLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2041 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLER 2120
Cdd:COG2198 331 LLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2121 LRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALR 2200
Cdd:COG2198 411 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLL 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2201 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQME 2280
Cdd:COG2198 491 LLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGL 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2281 ELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQA 2360
Cdd:COG2198 571 LLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLL 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2361 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2440
Cdd:COG2198 651 LLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLL 730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 2441 AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQR----------------QQSDHDAERLRQAIAELERE 2500
Cdd:COG2198 731 LLLLLLLLLLLLLLLAAAAAAAASPAAPALPVLDLEALRRlggdpellrellelflEELPELLAELRQALAAGDLE 806
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1833-2343 |
5.01e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.31 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1833 AEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLa 1912
Cdd:COG3899 752 AEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEA- 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1913 edeafQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGR 1992
Cdd:COG3899 831 -----RALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1993 IRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ 2072
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2073 ESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQ 2152
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAA 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2153 VEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAemekhkkfaeqtLRQKAQVEQELTT 2232
Cdd:COG3899 1066 AALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAAL------------AALALAAAARAAA 1133
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2233 LRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEA 2312
Cdd:COG3899 1134 ALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALA 1213
|
490 500 510
....*....|....*....|....*....|.
gi 2124423184 2313 EKMKHVAEEAARLSVAAQEAARLRELAEEDL 2343
Cdd:COG3899 1214 LLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1381-1487 |
5.12e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1381 ETLRRMEEEERLAEQQRAEERErlAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARRE---EAAVDAQQQK 1457
Cdd:PRK09510 122 EAAKQAALKQKQAEEAAAKAAA--AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaeaEAAAKAAAEA 199
|
90 100 110
....*....|....*....|....*....|
gi 2124423184 1458 RSIQEELQHLRQSSEAEIQAKARQVEAAER 1487
Cdd:PRK09510 200 KKKAEAEAKKKAAAEAKKKAAAEAKAAAAK 229
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1394-1636 |
5.19e-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: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1394 EQQRAEERERLaaVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEA 1473
Cdd:pfam05667 238 EEYRKRKRTKL--LKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1474 EIQAKARQVEAAERsRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLrrqvQDETQRKR 1553
Cdd:pfam05667 316 TSSPPTKVETEEEL-QQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEEL----EKQYKVKK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1554 QAEAELA------VRVKAEAEAAREKQRALQAL-EEFRLQAEEAERRLRQAEAERARQVQVALETAQ------RSAEVEL 1620
Cdd:pfam05667 391 KTLDLLPdaeeniAKLQALVDASAQRLVELAGQwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKelrekiKEVAEEA 470
|
250
....*....|....*.
gi 2124423184 1621 QSKRASFAEKTAQLER 1636
Cdd:pfam05667 471 KQKEELYKQLVAEYER 486
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1517-1606 |
5.21e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1517 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELavrvKAEAEaarekQRALQALEEFRLQAEEAERRLRQ 1596
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90
....*....|
gi 2124423184 1597 AEAERARQVQ 1606
Cdd:PRK00409 596 LQKGGYASVK 605
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
1743-1886 |
5.27e-03 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 42.48 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1743 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS 1822
Cdd:COG4191 1 ALRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 1823 TSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGE 1886
Cdd:COG4191 81 LLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGE 144
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1719-1879 |
5.32e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.59 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1719 GKAEEQAVRQRELAEQELEKQRQLA---EGTAQQRL-AAEQELIR-LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQ 1793
Cdd:pfam04012 42 RQALAQTIARQKQLERRLEQQTEQAkklEEKAQAALtKGNEELAReALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1794 ELEAELAKVRAEMEVLLA--SKARAEEESRSTSEKSK-QRLEAEASRFRE-LAEEAARLRALAEEAKRQRQLAE-EDAAR 1868
Cdd:pfam04012 122 ALETKIQQLKAKKNLLKArlKAAKAQEAVQTSLGSLStSSATDSFERIEEkIEEREARADAAAELASAVDLDAKlEQAGI 201
|
170
....*....|.
gi 2124423184 1869 QRAEAERVLAE 1879
Cdd:pfam04012 202 QMEVSEDVLAR 212
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1552-1786 |
5.41e-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: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1552 KRQAEAELAVRVKAEaeaaREKQRALQAleEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEkt 1631
Cdd:pfam15709 327 KREQEKASRDRLRAE----RAEMRRLEV--ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1632 aqlERTLQEEHVAVAQLREEAERraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKSLAqaeaekqkeea 1711
Cdd:pfam15709 399 ---ERQRQEEEERKQRLQLQAAQ-------------------ERARQQQEEFRRKLQELQRKKQQEEAE----------- 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423184 1712 erearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAA 1786
Cdd:pfam15709 446 --------RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1721-1969 |
5.60e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 42.33 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1721 AEEQAVRQRELAEQELEKQRQLAEGTAQ---------QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1791
Cdd:pfam15558 90 IEKESRWREQAEDQENQRQEKLERARQEaeqrkqcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1792 RQELEAELAKVRAeMEVLLASKARAEEESRSTS-EKSKQRLEAEASRFRELAEEAARLRALAEEAKRQR-QLAEEDAARQ 1869
Cdd:pfam15558 170 QENNLSELLNHQA-RKVLVDCQAKAEELLRRLSlEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRaKWRAEEKEEE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1870 RAEAERVLAEKLAAIGEATRLKTEAEIALK---------EKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQL 1940
Cdd:pfam15558 249 RQEHKEALAELADRKIQQARQVAHKTVQDKaqrarelnlEREKNHHILKLKVEKEEKCHREGIKEAIKKK---EQRSEQI 325
|
250 260
....*....|....*....|....*....
gi 2124423184 1941 RKASESELERQKGLVEDTLRQRRQVEEEI 1969
Cdd:pfam15558 326 SREKEATLEEARKTARASFHMREKVREET 354
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2220-2644 |
5.65e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2220 LRQKAQVEQELTTLRLQLEETDHQKSILDEELQR----LKAEVTEAARQRSQVEEELFSLRVQMEelgKLKARIEAENRA 2295
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlvlANSELTEARTERDQFSQESGNLDDQLQ---KLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2296 LILrDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELaeedLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQ 2375
Cdd:pfam15921 393 LSL-EKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEAL----LKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2376 QQKELAQEQARRLQED---KEQMAQQLEQETQGFQRTLEaERQRQLEMS-AEAERLKLRV-AEMSRAQARAEEDAQRFRK 2450
Cdd:pfam15921 468 AQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQ-EKERAIEATnAEITKLRSRVdLKLQELQHLKNEGDHLRNV 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2451 QAEEIGEKLhrtELATQEKVtlvqtLEIQRQQSDHDAERLRQ---AIAELEREKEKLKQEAKLLQLKSEEMQTvqqeqll 2527
Cdd:pfam15921 547 QTECEALKL---QMAEKDKV-----IEILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRRLELQEFKI------- 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2528 qetqaLQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREaeeg 2607
Cdd:pfam15921 612 -----LKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---- 682
|
410 420 430
....*....|....*....|....*....|....*..
gi 2124423184 2608 VRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLE 2644
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1358-1648 |
5.66e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1358 YVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEErERLAAV-------EAALEKQRQLAEAHAQAKAQAEQ 1430
Cdd:PRK10811 484 YSVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQ-PALATFampdvppAPTPAEPAAPVVAAAPKAAAATP 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1431 EAQ-----------------ELQRRMQEEVARREEAAVDAQQQKRsiqeelqhlrqsseaeiqaKARQVEAAERSRLRIE 1493
Cdd:PRK10811 563 PAQpgllsrffgalkalfsgGEETKPQEQPAPKAEAKPERQQDRR-------------------KPRQNNRRDRNERRDT 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1494 EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAvrvKAEAEAarek 1573
Cdd:PRK10811 624 RDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQA---QQEAKA---- 696
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423184 1574 qralQALEEFRLQAEEAERRLRQAEAERA-RQV--QVALETAQrSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1648
Cdd:PRK10811 697 ----LNVEEQSVQETEQEERVQQVQPRRKqRQLnqKVRIEQSV-AEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPL 769
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2303-2606 |
5.74e-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: 43.02 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2303 NTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRElaeEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQQK--- 2378
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRL---EKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKSIDikk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2379 --ELAQEQARRLQEDKEQMAQQLEQETqGFQRTLEAERQRQLEMSAEAERLKLRVAEM--SRAQARAEEDAQRFRKQAEE 2454
Cdd:COG5185 310 atESLEEQLAAAEAEQELEESKRETET-GIQNLTAEIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSFKDTIES 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2455 IGEKLH--RTELATQEKVtLVQTLEIQRQQSDHDAERLRQAIAELEREkekLKQEAKLLQLKSEEMQTVQQEQLLQETQA 2532
Cdd:COG5185 389 TKESLDeiPQNQRGYAQE-ILATLEDTLKAADRQIEELQRQIEQATSS---NEEVSKLLNELISELNKVMREADEESQSR 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 2533 LQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEE 2606
Cdd:COG5185 465 LEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHI 538
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2201-2474 |
5.87e-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: 42.21 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2201 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFS-L 2275
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREeI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2276 RVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARlsvAAQEAARLRELAEEDLAQQRALAEKMLK 2355
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE---KEREIARLRAQQEKAQDEKAERDELRAK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2356 EKMQAVQEATRLKAEAEL---LQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLE--AERQRQLEMSAEAERLK-- 2428
Cdd:pfam13868 210 LYQEEQERKERQKEREEAekkARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRkqAEDEEIEQEEAEKRRMKrl 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2124423184 2429 -----LRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2474
Cdd:pfam13868 290 ehrreLEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1279-1588 |
5.99e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1279 VLADSRAVREQLRQEkalLEEIE-----RHGEKVEECQ-------------RFAKQYINAIKDYELQLVTYKAQLEPVAS 1340
Cdd:PRK10929 17 AYAATAPDEKQITQE---LEQAKaaktpAQAEIVEALQsalnwleerkgslERAKQYQQVIDNFPKLSAELRQQLNNERD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1341 PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAAVEAALEKQRQLA 1418
Cdd:PRK10929 94 EPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1419 EAHAQAKAQAeqeaqelqrrMQEEVARReEAAVDaqqqkrsiQEELQHLRQSSEAEIqakAR-QVEAAERSRLRIEEEIR 1497
Cdd:PRK10929 168 TPLAQAQLTA----------LQAESAAL-KALVD--------ELELAQLSANNRQEL---ARlRSELAKKRSQQLDAYLQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1498 VVRLQLeTTERQRggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAEL---AVRVKAEA----EAA 1570
Cdd:PRK10929 226 ALRNQL-NSQRQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAA 292
|
330
....*....|....*...
gi 2124423184 1571 REKQRALQALEEFRLQAE 1588
Cdd:PRK10929 293 SQTLQVRQALNTLREQSQ 310
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2333-2508 |
6.11e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2333 ARLRELAEEDLAQQRALAEkmLKEKmqAVQEATRLkaeAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEA 2412
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTD--LKER--ESQEDAKR---AQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2413 ERQRQLEMSAEAERLKLRVA-----EMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDhDA 2487
Cdd:pfam05262 257 AKNLPKPADTSSPKEDKQVAenqkrEIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP-VA 334
|
170 180
....*....|....*....|.
gi 2124423184 2488 ERLRQAIAELEREKEKLKQEA 2508
Cdd:pfam05262 335 EDLQKTKPQVEAQPTSLNEDA 355
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2200-2610 |
6.22e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2200 RQKQAADAEMEKHKKFAEQTLRqkaqvEQELTTLRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2277
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLD-----EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2278 QMEE-------LGKLKARIEAENRALILRDKDNTQRVLQEEAEKMK----------HVAEEAARLS-VAAQEAARLRELA 2339
Cdd:pfam01576 167 NLAEeeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAeLRAQLAKKEEELQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2340 E-----EDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE--QETQGFQRTLEA 2412
Cdd:pfam01576 247 AalarlEEETAQKNNALKKIRELEAQISE---LQEDLESERAARNKAEKQRRDLGEELEALKTELEdtLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2413 ERQRQLEM-----SAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELA----TQEKVTLVQTLEIQRQQS 2483
Cdd:pfam01576 324 KREQEVTElkkalEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQAleseNAELQAELRTLQQAKQDS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2484 DHDAERLRQAIAEL-------EREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQ-----QSFLSEKDTLLQRE--- 2548
Cdd:pfam01576 404 EHKRKKLEGQLQELqarlsesERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKdvsslESQLQDTQELLQEEtrq 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2549 --------RFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQL------VASMEEARQR-QREAEEGV----- 2608
Cdd:pfam01576 484 klnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLeedagtLEALEEGKKRlQRELEALTqqlee 563
|
490
....*....|....
gi 2124423184 2609 ------------RR 2610
Cdd:pfam01576 564 kaaaydklektkNR 577
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2313-2407 |
6.23e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.89 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2313 EKMKHVAEEAARLSVAAQEAARLRELAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2386
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 2124423184 2387 RLQEDKEQMAQQLEQETQGFQ 2407
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1723-1888 |
6.54e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1723 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1802
Cdd:COG3883 115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1803 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1882
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
....*.
gi 2124423184 1883 AIGEAT 1888
Cdd:COG3883 275 GAAAAS 280
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2311-2446 |
6.54e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2311 EAEKMK-HVAEEAAR---LSVAAQEAARlrELAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQKELAQEQAR 2386
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 2387 RLQEdkeqmaqqLEQETQgfQRTLEAERQRQLeMSAEAERLKLRVAEMSR----AQARAEEDAQ 2446
Cdd:PTZ00491 761 QELE--------LEYEQA--QNELEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2199-2363 |
6.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2199 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQ 2278
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2279 mEELGKLKARIEAENRALILRDKDnTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKM 2358
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 2124423184 2359 QAVQE 2363
Cdd:COG1579 167 ELAAK 171
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1373-1925 |
6.73e-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: 42.73 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1373 SQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKqrqLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVD 1452
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS---YEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1453 AQQQ-KRSIQEELQHLRQS----------SEAEIQAKARQVEAAERSrlrIEEEIRVVRLQLETTERQRGGAEGELQALR 1521
Cdd:TIGR00606 660 GATAvYSQFITQLTDENQSccpvcqrvfqTEAELQEFISDLQSKLRL---APDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1522 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVrVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAEr 1601
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGT-IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK- 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1602 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHvavaqlreeaerraqqqaeaerareeaERELERWQLKAN 1681
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ---------------------------QEQIQHLKSKTN 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1682 EALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLR 1761
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1762 AETEQGEQQRQLLEEELarlqhEAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRST-----SEKSKQRLEAEAS 1836
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKI-----QDGKDDYLKQK-ETELNTVNAQLEECEKHQEKINEDMRLMrqdidTQKIQERWLQDNL 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1837 RFRELAEEaarLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGeatrlKTEAEIALKEKEAENERLRRLAEDEA 1916
Cdd:TIGR00606 1022 TLRKRENE---LKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIK-----RNHVLALGRQKGYEKEIKHFKKELRE 1093
|
....*....
gi 2124423184 1917 FQRRRLEEQ 1925
Cdd:TIGR00606 1094 PQFRDAEEK 1102
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2280-2397 |
7.10e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2280 EELGKLKARIEAENRALILRDKDNTQrvLQEEaekmkhVAEEAARLSVAAQEAARLRELAEEdLAQQRALAEKMLKEKMQ 2359
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQDS------VANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2360 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ 2397
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAK 173
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1395-1589 |
7.22e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.27 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1395 QQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE 1474
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1475 IQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEA-ERLRRQVQDETQRKR 1553
Cdd:PRK07735 156 EEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAkQKASQGNGDSGDEDA 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 2124423184 1554 QAEAELAVRVKAEAeAAREKQRALQALEEFRLQAEE 1589
Cdd:PRK07735 236 KAKAIAAAKAKAAA-AARAKTKGAEGKKEEEPKQEE 270
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1721-1821 |
7.68e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1721 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1800
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 2124423184 1801 KvRAEMEVLLaskarAEEESR 1821
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1430-1569 |
7.73e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1430 QEAQELQRRMqEEVARREEAAVDAQQQkrSIQEELQHLRQSsEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQ 1509
Cdd:COG0542 411 EELDELERRL-EQLEIEKEALKKEQDE--ASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK 486
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423184 1510 RGGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDETQRKRQAEAELAVRVKAEAEA 1569
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1826-1974 |
7.75e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1826 KSKQRLEAEASRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LAEKLAAigEATRLKTE 1893
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1894 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALK 1973
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
.
gi 2124423184 1974 V 1974
Cdd:PRK12705 181 I 181
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
85-187 |
7.83e-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: 39.59 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 85 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 160
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 2124423184 161 NIRNDDIADGNPKLTLGLIWTIILHFQ 187
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1268-1596 |
7.95e-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: 42.15 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1268 AKRRQEQIQAMvLADSRAVREQLRQE-KALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVaspakkpk 1346
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELK---DKYRELRKTLLANRFSYGPAIDEL-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1347 vqsgsESVIQEYVDLRTRYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQ-RQLAEAHAQAK 1425
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1426 AQ--------AEQEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLRQSSEAEIQAKA----------RQVEAAE 1486
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKKyveknlpeieDYLEHAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1487 RSRLRIEEEIRVV----RLQLETTERQRgGAEGELQALRARAEEAE---AQKRQAQEEaerLRRQVQDETQRKRQAEAEL 1559
Cdd:pfam06160 305 EQNKELKEELERVqqsyTLNENELERVR-GLEKQLEELEKRYDEIVerlEEKEVAYSE---LQEELEEILEQLEEIEEEQ 380
|
330 340 350
....*....|....*....|....*....|....*..
gi 2124423184 1560 AVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQ 1596
Cdd:pfam06160 381 EEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1570-1624 |
8.31e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423184 1570 AREKQRALQaleefRLQAEEAERRlRQAEAERARQVQVALETAQRS-AEVELQSKR 1624
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1451-1597 |
8.72e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1451 VDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrlrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQ 1530
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 1531 KRQAQEEAERLRRQVQdetqrkrQAEAElavrvkaeaEAAREKQRALQALEEFRLqaEEAERR------LRQA 1597
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1390-1636 |
8.89e-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: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1390 ERLAEQQRAEERERLAAVEaALEKQRQlaeahaqakaQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRq 1469
Cdd:pfam10174 453 ERLKEQREREDRERLEELE-SLKKENK----------DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK- 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1470 SSEAEIQA-------------KARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQK----- 1531
Cdd:pfam10174 521 SLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKndkdk 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1532 ----------RQAQEEAERLR--RQVQDETQRKRQAEAELAVRVK-AEAEAAREKQRA--LQALEEFRLQAEEAERRLRQ 1596
Cdd:pfam10174 601 kiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDATKARLSS 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423184 1597 AE--------------AERARQVQVALETAQRS------------AEVEL-QSKRASFAEKTAQLER 1636
Cdd:pfam10174 681 TQqslaekdghltnlrAERRKQLEEILEMKQEAllaaisekdaniALLELsSSKKKKTQEEVMALKR 747
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2323-2464 |
9.43e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 2323 ARLSVAAQEAARlrELAEEDLAQQRALAEKmLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQE-DKEQMAQQLEQ 2401
Cdd:COG1566 74 ARLDPTDLQAAL--AQAEAQLAAAEAQLAR-LEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlYKKGAVSQQEL 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423184 2402 ETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQArAEEDAQRFRKQAEEIGEKLHRTEL 2464
Cdd:COG1566 151 DEA--RAALDAAQAQLEAAQAQLAQAQAGLREEEELAA-AQAQVAQAEAALAQAELNLARTTI 210
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1768-1970 |
9.48e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.89 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1768 EQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAA- 1846
Cdd:cd00176 18 EKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1847 RLRALAEEAKRQRQLAEEDAARQRAEAervlAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEdeafQRRRLEEQA 1926
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADDLEQWLEE----KEAALASEDLGKDLESVEELLKKHKELEEELEAHEP----RLKSLNELA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423184 1927 AQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIL 1970
Cdd:cd00176 170 EELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4323-4353 |
9.49e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.49e-03
10 20 30
....*....|....*....|....*....|.
gi 2124423184 4323 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4353
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1552-1925 |
9.80e-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: 42.31 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1552 KRQAEAELAVRVKAEAEAAREKqralqaleefrLQAEEAERRLRQAEAERArqvqvaLETAQRSAEVELQSKRASFAEKT 1631
Cdd:NF033838 108 KEKSEAELTSKTKKELDAAFEQ-----------FKKDTLEPGKKVAEATKK------VEEAEKKAKDQKEEDRRNYPTNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1632 AQ-LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERwqlKANEALRL------RLQAEEvaqqkslaqaea 1704
Cdd:NF033838 171 YKtLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVES---KKAEATRLekiktdREKAEE------------ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1705 ekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLRAETEQGEQ---------QRQL 1773
Cdd:NF033838 236 ---------EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPdkKENDAKSSDSSVGEEtlpspslkpEKKV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1774 LEEELARLQHEAAAATQKRQ-----------ELEAELA----KVR-AEMEVLLASKARAEEEsrstsEKSKQRLEAEASR 1837
Cdd:NF033838 307 AEAEKKVEEAKKKAKDQKEEdrrnyptntykTLELEIAesdvKVKeAELELVKEEAKEPRNE-----EKIKQAKAKVESK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1838 frelAEEAARLralaEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAF 1917
Cdd:NF033838 382 ----KAEATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQAE 453
|
410
....*....|
gi 2124423184 1918 Q--RRRLEEQ 1925
Cdd:NF033838 454 EdyARRSEEE 463
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1389-1487 |
9.91e-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: 39.77 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 1389 EERLAEQQRAEERERLAAVEAALEKQRQLAEAHA-------QAKAQAEQEAQELQRRMQEEVARREEAAvdaqqqKRSIQ 1461
Cdd:COG0711 33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARAeaaeiiaEARKEAEAIAEEAKAEAEAEAERIIAQA------EAEIE 106
|
90 100
....*....|....*....|....*.
gi 2124423184 1462 EELQHLRQSSEAEIQAKArqVEAAER 1487
Cdd:COG0711 107 QERAKALAELRAEVADLA--VAIAEK 130
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
88-300 |
9.93e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 42.24 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 88 KTFTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---SLPREKGR-------MRFHKLQNVQIALDYLRHRQV 157
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 158 KLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMVEGY---QGLRCDNFTS 227
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGLKGdkeEGIRSFGDPA 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423184 228 SWRDGRLFNAIIHRHKPMLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPdEKSIITYVSSL 300
Cdd:COG5069 532 GSVSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP-RLDVLTFIESL 609
|
|
| |
