|
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 ... |
68-172 |
3.84e-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: 3.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 68 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 147
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1920237952 148 RNDDIADGNPKLTLGLIWTIILHFQ 172
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
65-183 |
9.77e-74 |
|
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: 242.24 E-value: 9.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 65 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 144
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237952 145 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 183
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
57-181 |
4.08e-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: 4.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 57 ERAVIRIADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDY 136
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDY 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1920237952 137 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 181
Cdd:cd21236 84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
185-290 |
8.96e-70 |
|
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: 230.29 E-value: 8.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 185 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 264
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1920237952 265 PEDVDVPQPDEKSIITYVSSLYDAMP 290
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
186-290 |
4.01e-64 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 213.79 E-value: 4.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 265
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1920237952 266 EDVDVPQPDEKSIITYVSSLYDAMP 290
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
65-182 |
3.79e-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: 3.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 65 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 144
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1920237952 145 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 182
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
186-290 |
1.44e-56 |
|
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: 192.51 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 265
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1920237952 266 EDVDVPQPDEKSIITYVSSLYDAMP 290
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
70-173 |
1.20e-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: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 70 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 148
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1920237952 149 NDDIADGNPKLTLGLIWTIILHFQI 173
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
184-290 |
6.67e-50 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 173.30 E-value: 6.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 184 DMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 263
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1920237952 264 DPEDVDVPQPDEKSIITYVSSLYDAMP 290
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
57-169 |
9.49e-49 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 170.63 E-value: 9.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 57 ERAVIR-IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIAL 134
Cdd:cd21246 2 ERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237952 135 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 169
Cdd:cd21246 82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
64-397 |
6.60e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 175.13 E-value: 6.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 64 ADERDRVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHR 140
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 141 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGCQ-GLRCDNFTTSWRDGRL 219
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 220 FNAIIHRHKPTLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD--- 287
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkid 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 288 -AMPRVPDVQDGVKANElQLRwQEYRELVLLLLQWIRAHTAGFEERRFPSSFEEIEILWCQFLKFKETE--LPAKEAD-K 363
Cdd:COG5069 240 iALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlH 317
|
330 340 350
....*....|....*....|....*....|....
gi 1920237952 364 NRSKGIYQSLEgAVQAGQLKVPPGYHPLDVEKEW 397
Cdd:COG5069 318 SLAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
186-286 |
6.70e-45 |
|
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: 159.11 E-value: 6.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 265
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1920237952 266 EDVDVPQPDEKSIITYVSSLY 286
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
57-169 |
1.13e-44 |
|
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: 158.61 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 57 ERAVIR-IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIAL 134
Cdd:cd21193 2 EKGRIRaLQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237952 135 DYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 169
Cdd:cd21193 82 AFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
66-173 |
3.49e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 157.15 E-value: 3.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 66 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 141
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1920237952 142 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 173
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
66-173 |
1.12e-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: 155.81 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 66 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 138
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237952 139 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 173
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
186-286 |
4.65e-43 |
|
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: 153.71 E-value: 4.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 265
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237952 266 EDVDVPQPDEKSIITYVSSLY 286
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
185-290 |
5.88e-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: 147.85 E-value: 5.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 185 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 264
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1920237952 265 PEDVDVPQPDEKSIITYVSSLYDAMP 290
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
63-169 |
1.45e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 147.86 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 63 IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQ 141
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQR 110
|
90 100
....*....|....*....|....*...
gi 1920237952 142 VKLVNIRNDDIADGNPKLTLGLIWTIIL 169
Cdd:cd21318 111 VHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
173-288 |
8.69e-40 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 144.81 E-value: 8.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 173 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 252
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237952 253 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 288
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
57-169 |
2.07e-39 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 144.43 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 57 ERAVIR-IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIAL 134
Cdd:cd21317 17 ERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKAL 96
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237952 135 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 169
Cdd:cd21317 97 QFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
68-169 |
1.13e-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: 141.37 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 68 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 146
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1920237952 147 IRNDDIADGNPKLTLGLIWTIIL 169
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
66-173 |
1.66e-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: 141.12 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 66 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 143
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1920237952 144 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 173
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
70-171 |
1.90e-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: 1.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 70 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 147
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1920237952 148 RNDDIADGNPKLTLGLIWTIILHF 171
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1329-1904 |
1.21e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 156.25 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1329 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEErERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1408
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-AELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1409 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQA 1488
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1489 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1568
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1569 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaEAERARAEAERELERWQLK 1648
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL--------AGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1649 ANEALRLRLQAeevAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR 1728
Cdd:COG1196 536 YEAALEAALAA---ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1729 LRAETEQGEqqrqLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1808
Cdd:COG1196 613 ARYYVLGDT----LLGRTLVAARLEAALRR--AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1809 ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 1888
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570
....*....|....*.
gi 1920237952 1889 RLLEEQAAQHKADIEA 1904
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
182-286 |
2.08e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 138.27 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 182 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 261
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1920237952 262 LLDPEDVDVPQPDEKSIITYVSSLY 286
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
182-286 |
4.50e-37 |
|
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: 137.06 E-value: 4.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 182 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 261
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1920237952 262 LLDPEDVDVPQPDEKSIITYVSSLY 286
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1357-2062 |
9.25e-37 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 154.91 E-value: 9.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1357 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiqEELQHL 1436
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA--EDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1437 RQSSEAEIQAKARQVEAAERSRlRIEEEIRVVRLQlEATERQRGGAEGELQALRaRAEEAeaqkRQAQEEAERLRRQVQD 1516
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDAR-KAEAARKAEEER-KAEEARKAEDAKKAEAVK-KAEEA----KKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1517 ETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF 1596
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKA----DELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1597 AEKTAQ-LERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAlrlRLQAEEVAQQKSLTQaeaek 1675
Cdd:PTZ00121 1327 AKKKADaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA---KKKAEEKKKADEAKK----- 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1676 qkeeaerearrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQLLE-----EELAR 1749
Cdd:PTZ00121 1399 -------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEeakkaEEAKK 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1750 LQREAAAATQKRRELE----AELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEAGRFRELAEEAARLRAlAEEAK 1825
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEeakkADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1826 RQRQLAEEDAVRQRAEAERvlAEKLAAISEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 1905
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1906 LAQLRKASESELERQKGLVEDTLRQRrqveEEILALKGSFEKAAAGKAELELELGRIRGT-----AEDTLRSKEQA--EQ 1978
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAAeeakkAEEDKKKAEEAkkAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1979 EAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQESARQLQLAQEAA 2054
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
....*...
gi 1920237952 2055 QKRLQAEE 2062
Cdd:PTZ00121 1765 EEEKKAEE 1772
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
65-173 |
9.93e-37 |
|
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: 9.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 65 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 143
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1920237952 144 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 173
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1362-1963 |
1.85e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.40 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1362 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAEReAQGLQrrmqeevarreevaveAQEQKRSIQEELQHLRQSs 1440
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAER-YRELK----------------EELKELEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1441 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQR 1520
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1521 KRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEAELQSEHASFAEKT 1600
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1601 AQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEA 1680
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1681 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR------LRAETEQGEQQRQLLEEELARLQREA 1754
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavavlIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1755 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1834
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1835 AVRQRAEAERVLAEKLAA--ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKA 1912
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 1913 SESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 1963
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
185-286 |
1.18e-35 |
|
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: 132.68 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 185 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 264
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1920237952 265 PEDVDVPQPDEKSIITYVSSLY 286
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1489-2089 |
3.92e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.16 E-value: 3.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1489 LRARAEEAEAQKRQAQEEAERL---RRQVqdETQR---KRQAE-AELALRVQAEAEAaREKQRALQALEELRLQAEEAER 1561
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLeplERQAEkAERYRELKEELKE-LEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1562 RLRQAEAERARqvqvaLETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERE 1641
Cdd:COG1196 247 ELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYEL--LAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1642 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1721
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---------AELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1722 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1801
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1802 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA----AISEATRLKTEAEIALKEKEAENERL 1877
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1878 RRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELEL 1957
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1958 ELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2037
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2038 RAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLER 2089
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
189-290 |
1.23e-34 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 129.47 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 189 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 267
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237952 268 VDVPQPDEKSIITYVSSLYDAMP 290
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
170-286 |
1.55e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 130.56 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 170 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQA 249
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237952 250 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 286
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1692-2260 |
2.80e-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: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1692 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1771
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1772 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLA 1851
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1852 AISEATRLKTEAEIALKEKEAENERLRRlaedEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQR 1931
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1932 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEA 2011
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2012 ARQRKAALEEVERLKAKVEEAR---RLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQE 2083
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAAlaaALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2084 QSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2163
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2164 EQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2243
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 1920237952 2244 LRVQMEELGKLKARIEA 2260
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
69-174 |
8.93e-34 |
|
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: 127.95 E-value: 8.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 145
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILHFQIS 174
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
57-169 |
5.49e-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: 5.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 57 ERAVIR-IADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIAL 134
Cdd:cd21316 39 ERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKAL 118
|
90 100 110
....*....|....*....|....*....|....*
gi 1920237952 135 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 169
Cdd:cd21316 119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
70-173 |
7.20e-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: 124.71 E-value: 7.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 70 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 147
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1920237952 148 RNDDIADGNPKLTLGLIWTIILHFQI 173
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
70-173 |
1.73e-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: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 70 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 148
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1920237952 149 NDDIADGNPKLTLGLIWTIILHFQI 173
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
186-286 |
5.68e-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: 122.13 E-value: 5.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 265
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1920237952 266 EDVDVPQPDEKSIITYVSSLY 286
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
185-283 |
4.50e-31 |
|
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: 119.45 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 185 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 264
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1920237952 265 PEDVDVPQPDEKSIITYVS 283
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1350-1954 |
1.15e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.50 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1350 ETLRRMEEEERLAEQQRAE------------ERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1417
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEavkkaeeakkdaEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1418 V--AVEAQ--EQKRSIQEELQHLRQSSEAEiQAKARQVEA---AERSRLRIEEEirvvRLQLEATERQRGGAEGELQALR 1490
Cdd:PTZ00121 1289 KkkADEAKkaEEKKKADEAKKKAEEAKKAD-EAKKKAEEAkkkADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAE 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1491 ARAEEAEAQKRQAQEEAERLRRQVQ-----DETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRlQAEEAERRLRQ 1565
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEekkkaDEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1566 A--------EAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLR--EEATRRAQQQAEAERAR 1635
Cdd:PTZ00121 1443 AkkadeakkKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1636 AEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKQKEEAEREARRRgKAEEqavrQRELAEQELEKQRQLAEGT 1715
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKK----AEEKKKADELKKAEELKKAEEKKKAEEAK-KAEE----DKNMALRKAEEAKKAEEAR 1593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1716 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1795
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1796 SKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEedaVRQRAEAERVLAEKLAAISEATRLKteAEIALKEKEAENE 1875
Cdd:PTZ00121 1674 KKKAEEAK----KAEEDEKKAAEALKKEAEEAKKAEE---LKKKEAEEKKKAEELKKAEEENKIK--AEEAKKEAEEDKK 1744
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1876 RLRRLAEDEAFQRRLleeqaAQHKADIEARLAQLRKASESELErqKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAE 1954
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKI-----AHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
173-288 |
1.61e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.40 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 173 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 252
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237952 253 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 288
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
185-283 |
1.67e-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: 118.01 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 185 MTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 264
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1920237952 265 PEDVDVPQPDEKSIITYVS 283
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1350-1982 |
1.70e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.11 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1350 ETLRRMEEEERLAEQQRAEERERLAEVEAALE--KQRQLAEAHAQAKAQAEREAQGLQR----------RMQEEVARREE 1417
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKaedakkaeavKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1418 VAVEAQEQKRSIQ-EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRlQLEATERQRGGAEGELQALRAR-AEE 1495
Cdd:PTZ00121 1241 EAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKkADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1496 AEAQKRQAQEEAERLRRQVQdETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAERRlrqaeAERARQV 1574
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAKKK-----AEEKKKA 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1575 QVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARaeaerelerwqlKANEALR 1654
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE------------EAKKAEE 1461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1655 LRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQElIRLRAETE 1734
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE-AKKADEAK 1540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1735 QGEQQR---QLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaEAGRFRELA 1811
Cdd:PTZ00121 1541 KAEEKKkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAK 1619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1812 EEAARLRALAEEAKRQRQLAEEDA--------VRQRAEAERVLAEKLAAISEATrlKTEAEIALKEKEAENERLRRLAED 1883
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKKE 1697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1884 EAFQRRLleEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVeEEILALKGSFEKAAAGKAELELELGRIR 1963
Cdd:PTZ00121 1698 AEEAKKA--EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
650
....*....|....*....
gi 1920237952 1964 GTAEDTLRSKEQAEQEAAR 1982
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRR 1793
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
189-290 |
1.81e-30 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 117.75 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 189 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 267
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1920237952 268 VDVPQPDEKSIITYVSSLYDAMP 290
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
66-175 |
2.49e-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: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 66 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 141
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1920237952 142 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 175
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
905-982 |
4.20e-30 |
|
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: 115.78 E-value: 4.20e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 905 LAWQSLGRDMQLIRSWSLATFRTLKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSRHYQQLLQS 982
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
69-171 |
5.96e-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: 5.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 145
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILHF 171
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1759-2470 |
1.29e-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: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1759 QKRRELEAELAKVRAEMEvllaskaRAEEEsrsTSEKSKQ--RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedav 1836
Cdd:COG1196 172 ERKEEAERKLEATEENLE-------RLEDI---LGELERQlePLERQA----EKAERYRELKEELKELEAELLLLK---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1837 RQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadiEARLAQLRKASESE 1916
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL------LAELARLEQDIARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1917 LERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRRE 1996
Cdd:COG1196 308 EERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1997 AEERVQKSLAAEEEAARQRKAALEEVERLKAkvEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQEL 2076
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2077 QQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2156
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2157 AARRAQAEQAALRQKQAAdaemekhkqfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRgq 2236
Cdd:COG1196 542 AALAAALQNIVVEDDEVA----------AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR-- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2237 vEEELFSLRVQMEELGklkarieaenRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2316
Cdd:COG1196 610 -EADARYYVLGDTLLG----------RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2317 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERL 2396
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2397 RLRVAEMSRAQARAEEDARRFRK-------QAEDIGERLyrTELATQekvmlVQTLETQRqqsdrdaERLREAIAELEHE 2469
Cdd:COG1196 759 PPDLEELERELERLEREIEALGPvnllaieEYEELEERY--DFLSEQ-----REDLEEAR-------ETLEEAIEEIDRE 824
|
.
gi 1920237952 2470 K 2470
Cdd:COG1196 825 T 825
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
189-291 |
3.12e-29 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 114.64 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 189 EKLLL-WSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 266
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1920237952 267 DVDVPQPDEKSIITYVSSLYDAMPR 291
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
191-286 |
3.46e-29 |
|
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: 113.98 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 191 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 269
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1920237952 270 VPQPDEKSIITYVSSLY 286
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
171-288 |
3.58e-28 |
|
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: 112.10 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 171 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAF 250
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237952 251 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 288
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1205-1823 |
3.80e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 3.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1205 QTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVpLANSQAVREQLRQEKALLED-IERHGEKveecqrfa 1283
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELeLEEAQAE-------- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1284 kqyinaikdyELQLVTYKAQLEPVASPAKkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAE 1363
Cdd:COG1196 290 ----------EYELLAELARLEQDIARLE--------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1364 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqglqrrmqeEVARREEVAVEAQEQKRSIQEELQHLRQSSEAE 1443
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL---------EALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1444 IQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRqvQDETQRKRQ 1523
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA--RLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1524 AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE----K 1599
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflplD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1600 TAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEE 1679
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1680 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1759
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 1760 KRRELEAELAKVRAEMEvllaskaraEEESRSTSEKSKQRLEAEAGRF--------RELAEEAARLRALAEE 1823
Cdd:COG1196 741 LLEEEELLEEEALEELP---------EPPDLEELERELERLEREIEALgpvnllaiEEYEELEERYDFLSEQ 803
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1519-2234 |
4.28e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1519 QRKRQAEAELAlrvQAEAEAAR--------EKQralqaLEELRLQAEEAERRLRQAEAERARQVQVALetaqrsaeAELQ 1590
Cdd:COG1196 172 ERKEEAERKLE---ATEENLERledilgelERQ-----LEPLERQAEKAERYRELKEELKELEAELLL--------LKLR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1591 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkanEALRLRLQAEEvaqqksltq 1670
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAEL--------------------------EELRLELEELE--------- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1671 aeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1750
Cdd:COG1196 281 ------------------LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1751 QREAAAATQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1830
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1831 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLR 1910
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1911 KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEE 1990
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1991 ERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2070
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2071 QKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLR 2150
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2151 KEAEQEAARRAQAEQAALRQKQAADAEMEKHKqfAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLK-- 2224
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELER--LEREIEALGPVnllaIEEYEELEERYDFLSEQREDLEEARETLEea 817
|
730
....*....|.
gi 1920237952 2225 -AEVTEAARQR 2234
Cdd:COG1196 818 iEEIDRETRER 828
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
69-171 |
3.02e-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: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 145
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILHF 171
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1733-2623 |
9.62e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.79 E-value: 9.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1733 TEQGEQQRQLLEEELARLQREAAAATqkRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1810
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1811 AEEAARlralAEEAKRQrqlAEEdaVRQRAEAERvlAEKLAAISEATRLKTE--AEIALKEKEAENERLRRLAEDeafQR 1888
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAED---AK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1889 RLLEEQAAqhkadIEARLA-QLRKASESelerqkglvedtlrqrRQVEEeilalkgsfekaaAGKAELELELGRIRgTAE 1967
Cdd:PTZ00121 1177 KAEAARKA-----EEVRKAeELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAE 1221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1968 DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQL 2047
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKA 1298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2048 QLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERlrseaeaarraaeeaeaareraereaaqsRRQVEEAER 2127
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-----------------------------AKKAAEAAK 1349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2128 LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQaLRQKAQVEQELTALRLQLE 2207
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAE 1428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2208 ETDHQksildEELQRLKAEVTEAARQRGQVEEelfslRVQMEELGKlkaRIEAENRALVLRDKDSAQRLLQE---EAEKM 2284
Cdd:PTZ00121 1429 EKKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEEA 1495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2285 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2360
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2361 KeQMAQQLAQETQgfqktlETERQRQLEMSAEAERLRLRVAEmsraQARAEEDARrfrKQAEDIGErlyrtelaTQEKVM 2440
Cdd:PTZ00121 1576 K-NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAK---IKAEELKK--------AEEEKK 1633
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2441 LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsflsekdslLQRErci 2520
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-------------LKKE--- 1697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2521 EQEKAKLEQL---FQDEVAKAQALREEQQRQQQqmqqekqqlaaSMEEARRRQHE----AEEgVRRQQEELQRLAQQQQQ 2593
Cdd:PTZ00121 1698 AEEAKKAEELkkkEAEEKKKAEELKKAEEENKI-----------KAEEAKKEAEEdkkkAEE-AKKDEEEKKKIAHLKKE 1765
|
890 900 910
....*....|....*....|....*....|....
gi 1920237952 2594 QEKLLAEENQR----LRERLQHLEEERRAALARS 2623
Cdd:PTZ00121 1766 EEKKAEEIRKEkeavIEEELDEEDEKRRMEVDKK 1799
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
189-288 |
1.13e-26 |
|
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: 106.99 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 189 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 267
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1920237952 268 VDVPQPDEKSIITYVSSLYDA 288
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
173-288 |
1.66e-26 |
|
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: 107.09 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 173 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 252
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237952 253 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 288
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
69-174 |
1.75e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.04 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 145
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILHFQIS 174
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
173-288 |
8.35e-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: 105.19 E-value: 8.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 173 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 252
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237952 253 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 288
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1899-2627 |
1.10e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 118.32 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1899 KADIEARLAQLRKASESELERQKGLVEDTlRQRRQVEEEilalKGSFE---KAAAGKAELELELGRIRGTAEDTLRSKE- 1974
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDN-RADEATEEA----FGKAEeakKTETGKAEEARKAEEAKKKAEDARKAEEa 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1975 -QAE-----QEAARQRQLAAEEERRRREAEERVQKSLAAEE----EAARQ----RKAA----LEEVERLKA--KVEEARR 2034
Cdd:PTZ00121 1134 rKAEdarkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDakkaEAARKaeevRKAEelrkAEDARKAEAarKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2035 LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAERE 2114
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2115 AAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA--EMEKHKQFAEQALRQK 2192
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2193 AQVEQELTALRLQLEETDHQksildEELQRLKAEVTEAARQRGQVEEElfslrvqmeelgKLKARiEAENRALVLRDKDS 2272
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAA------------KKKAD-EAKKKAEEKKKADE 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2273 AQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQlAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2350
Cdd:PTZ00121 1436 AKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKK-ADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2351 QEqARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQA--RAEEDARRFRKQAEDigerL 2428
Cdd:PTZ00121 1513 DE-AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-KAEEKKKAEEakKAEEDKNMALRKAEE----A 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2429 YRTELATQEKVM-LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFL 2507
Cdd:PTZ00121 1587 KKAEEARIEEVMkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2508 SEKDsllqrerciEQEKAKLEQLFQDEVAKAQAlrEEQQRQQQQMQQEKQQLAASMEEARRRQHE---AEEGVRRQQEEL 2584
Cdd:PTZ00121 1667 AKKA---------EEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAKKAEELKKKEAEEKKKAEElkkAEEENKIKAEEA 1735
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1920237952 2585 QRLAQQ-QQQQEKLLAEENQrlRERLQHL--EEERRAALARSEEIA 2627
Cdd:PTZ00121 1736 KKEAEEdKKKAEEAKKDEEE--KKKIAHLkkEEEKKAEEIRKEKEA 1779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1425-2227 |
1.55e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.55 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1425 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEaEAQKRQAQ 1504
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE-ARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1505 EEAERLR-----RQVQD--ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE----AERARQ 1573
Cdd:PTZ00121 1122 KKAEDARkaeeaRKAEDarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEelrkAEDARK 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1574 VQVAletaqRSAEAELQSEHASFAEKTAQLERTLKEEHVAvvQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1653
Cdd:PTZ00121 1202 AEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1654 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQLAEGTAQQrlaAEQEliRLRAET 1733
Cdd:PTZ00121 1275 EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKK---AEEA--KKAAEA 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1734 EQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEmEVLLA--SKARAEEESRSTSEKSKQrlEAEAGRFRELA 1811
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKAdeAKKKAEEDKKKADELKKA--AAAKKKADEAK 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1812 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 1891
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1892 EEQAAQHKADiEARLAQLRKASEsELERQKglvedtlrQRRQVEEeilaLKGSFEKAAAGKAELELELGRirgtAEDTlR 1971
Cdd:PTZ00121 1504 KAAEAKKKAD-EAKKAEEAKKAD-EAKKAE--------EAKKADE----AKKAEEKKKADELKKAEELKK----AEEK-K 1564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1972 SKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRlrerAEQESARQLQLaq 2051
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK----AEEEKKKVEQL-- 1638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2052 eaaqKRLQAEEKAHAFAVQQKEQELQQTLqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQs 2131
Cdd:PTZ00121 1639 ----KKKEAEEKKKAEELKKAEEENKIKA-------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE- 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2132 aeeQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADaemEKHKQFAEQALRQKAQVEQELTALRLQLEETDH 2211
Cdd:PTZ00121 1707 ---LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
810
....*....|....*.
gi 1920237952 2212 QKSILDEELQRLKAEV 2227
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEV 1796
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
62-173 |
1.62e-25 |
|
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: 104.45 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 62 RIADERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 138
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLK 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237952 139 HR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 173
Cdd:cd21247 92 TKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
73-170 |
2.20e-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: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 73 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 148
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1920237952 149 NDDIADGnPKLTLGLIWTIILH 170
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
70-173 |
2.38e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.44 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 70 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 145
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILHFQI 173
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
173-288 |
2.46e-24 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 100.92 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 173 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSV 252
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237952 253 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 288
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1362-2573 |
3.37e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 113.00 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1362 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAEREAQGLQRRMQ--EEVARREEvAVEAQEQKRSIQEELQHLRQ 1438
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAELHTEAVQRRQQldQELAERRQ-TVESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1439 SSEA-----EIQAKARQVEAAERSRlrieeeirVVRLQLEAteRQRGGAEGElqalRARAEeAEAQKRQAQEEAERLRRQ 1513
Cdd:NF041483 162 ESQArrlldESRAEAEQALAAARAE--------AERLAEEA--RQRLGSEAE----SARAE-AEAILRRARKDAERLLNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1514 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQaeEAERRLRQAEAERARQVQVALETA-QRSAEAELQSE 1592
Cdd:NF041483 227 ASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAaKQLASAESANE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1593 hasfaektaQLERTLKEEhvaVVQLREEATRRAQQQAEAERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQA 1671
Cdd:NF041483 305 ---------QRTRTAKEE---IARLVGEATKEAEALKAEAEQALADARAEAEKLVaEAAEKARTVAAEDTAAQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1672 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEELARL 1750
Cdd:NF041483 373 AEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEARRL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1751 QREAAaatQKRRELEAELAKVRAEmevllaskARAEeesrstsekSKQRLEAEAGRFRELAEEAarlRALAEEAKRQrql 1830
Cdd:NF041483 446 RGEAE---QLRAEAVAEGERIRGE--------ARRE---------AVQQIEEAARTAEELLTKA---KADADELRST--- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1831 aeedavrQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA-QHKADIEARLAQL 1909
Cdd:NF041483 500 -------ATAESERVRTE---AIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAArELREETERAIAAR 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1910 RKASESELERQKGLVEdtlrQRRQVEEEilALKGSFEKAAAGKAELELELGRIRGTAEDTLRS-KEQAEQEAARQRqlaa 1988
Cdd:NF041483 570 QAEAAEELTRLHTEAE----ERLTAAEE--ALADARAEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLR---- 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1989 eeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLR-------ERAEQESARQLQLAQ-EAAQKRLQ 2059
Cdd:NF041483 640 -----TEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQEsADRVRaeaaaaaERVGTEAAEALAAAQeEAARRRRE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2060 AEE---KAHAFAVQQKEQELQQTLQQEQSVLERLrseaeaarraaeeaeaareraEREAAQSRRQVEEAERlkqsaeeqa 2136
Cdd:NF041483 715 AEEtlgSARAEADQERERAREQSEELLASARKRV---------------------EEAQAEAQRLVEEADR--------- 764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2137 qaqaqaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-DHQKSI 2215
Cdd:NF041483 765 --------------------------------RATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAaERTRTE 812
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2216 LDEELQRLKAEvteAARQRGQVEEELFSLRVQ-MEELGKLKARIEAEnralVLRDKDSAQRLLQEEAEKMKQVAEEAA-R 2293
Cdd:NF041483 813 AQEEADRVRSD---AYAERERASEDANRLRREaQEETEAAKALAERT----VSEAIAEAERLRSDASEYAQRVRTEASdT 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2294 LSVAAQEAARLRQLAEEDLAQQRALA---EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAq 2370
Cdd:NF041483 886 LASAEQDAARTRADAREDANRIRSDAaaqADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIA- 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2371 etqgfqktleterqrqlEMSAEAERLRLRVAE-MSRAQARAE---EDARRFRKQAEDIGERLyRTELATQEKVMLVQTLE 2446
Cdd:NF041483 965 -----------------EATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEAERL-RTEAREEADRTLDEARK 1026
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2447 TQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLL----QETQALQQSFLSEKDSLLQRERcieq 2522
Cdd:NF041483 1027 DANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVgaarKEAERIVAEATVEGNSLVEKAR---- 1102
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 2523 ekAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLaasMEEARRRQHEA 2573
Cdd:NF041483 1103 --TDADELLVGARRDATAIRERAEELRDRITGEIEEL---HERARRESAEQ 1148
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
191-286 |
6.38e-24 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 99.15 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 191 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 269
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1920237952 270 VPQPDEKSIITYVSSLY 286
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
185-291 |
7.05e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 99.28 E-value: 7.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 185 MTAKEKLLLWSQRMVEGC-QGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 261
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1920237952 262 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 291
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1399-2259 |
9.94e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 111.30 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1399 REAQGLQRRMQEEVARREEVAVEAQEQKRSIQ------EELQHLR-QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1471
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKaELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1472 LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1551
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1552 LRLQAEEAERRLrqaeaerarqvqvaletaqrsaeAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaea 1631
Cdd:TIGR02168 335 LAEELAELEEKL-----------------------EELKEELESLEAELEELEAELEELESRLEELEEQLE--------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1632 eraraeaerelerwQLKANEALRLRLQAEEVAQQKSLTQAEaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQL 1711
Cdd:TIGR02168 383 --------------TLRSKVAQLELQIASLNNEIERLEARL-------------------ERLEDRRERLQQEIEELLKK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1712 AEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS 1791
Cdd:TIGR02168 430 LE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1792 TSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaeEDAVRQRAEAERVLAEKLAAiSEATRLKTEAEIALKE 1869
Cdd:TIGR02168 508 VKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL---QAVVVENLNAAKKAIAFLKQ-NELGRVTFLPLDSIKG 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1870 KEAENERLRRLAEDEAFQRRL--LEEQAAQHKADIEARLAQLRKASEselerqkglVEDTLRQRRQVEEEIL-------- 1939
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAkdLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRivtldgdl 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1940 -----ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerRRREAEERVQKSLAAEEEAARQ 2014
Cdd:TIGR02168 655 vrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK-------ELEELEEELEQLRKELEELSRQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2015 RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLERLRSEA 2094
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2095 EAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAA 2174
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2175 DAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK---AEVTEAARQRGQVEEELFSLRVQMEEL 2251
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLQERLSEEYSLTLEEAEALENKIED 965
|
....*...
gi 1920237952 2252 GKLKARIE 2259
Cdd:TIGR02168 966 DEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1325-2061 |
6.43e-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: 108.61 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1325 QEYVDLRTRYSELS-TLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAL--------EKQRQLAEA------ 1389
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeelrlevsELEEEIEELqkelya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1390 HAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE------ELQHLRQSSEAEIQAKARQVEAAERSRLRIEE 1463
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElaeelaELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1464 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQ 1543
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI--EELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1544 RALQALEELRLQAEEAERRLRQAEAERarqvqvaletaqRSAEAELQsEHASFAEKTAQLERTLKEEHVAVVQLREEAtr 1623
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQAL------------DAAERELA-QLQARLDSLERLQENLEGFSEGVKALLKNQ-- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1624 raQQQAEAERARAEAERELERWQLKANEALRLRLQA---EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1700
Cdd:TIGR02168 516 --SGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1701 AEQELEKQRQLA---EGTAQQRLAAEQELIRLR-AETEQG--EQQRQLLEEELA------------RLQREAAAATQKRR 1762
Cdd:TIGR02168 594 LKNIEGFLGVAKdlvKFDPKLRKALSYLLGGVLvVDDLDNalELAKKLRPGYRIvtldgdlvrpggVITGGSAKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1763 ELEAELAKVRAEMEvLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA 1842
Cdd:TIGR02168 674 ERRREIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1843 ERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED-----EAFQRRLLEEQAAQHKADIEARLAQLRKAS-ESE 1916
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeelKALREALDELRAELTLLNEEAANLRERLESlERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1917 LERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRRE 1996
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 1997 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERA--EQESARQLQLAQEAAQKRLQAE 2061
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYslTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1717-2509 |
7.61e-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: 108.61 E-value: 7.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1717 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtQKRRELEAELAKVRAEmevLLASKARAEEESRSTSEKS 1796
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKA-ERYKELKAELRELELA---LLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1797 KQRLEAEagrFRELAEEAARLRALAEEAKRQRQLAEEDAvrqrAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENER 1876
Cdd:TIGR02168 248 LKEAEEE---LEELTAELQELEEKLEELRLEVSELEEEI----EELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1877 LRRLAEDEAFQRRLLEEQAAQHKADIEaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFekaaagkAELE 1956
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-------AQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1957 LELGRIRGTAEDTLRSKEQAEQEAARQRQ-LAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL 2035
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2036 RERAEQESARQLQLAQE--AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2113
Cdd:TIGR02168 473 AEQALDAAERELAQLQArlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2114 EAAQSRRQVEEAerLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAaDAEMEKHKQFAeqaLRQKA 2193
Cdd:TIGR02168 553 ENLNAAKKAIAF--LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF-DPKLRKALSYL---LGGVL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2194 QVEQELTALRLQlEETDHQKSI--LDEELQRLKAEVTEAARQRGQVeeeLFSLRVQMEELGKLKARIEAENRAL--VLRD 2269
Cdd:TIGR02168 627 VVDDLDNALELA-KKLRPGYRIvtLDGDLVRPGGVITGGSAKTNSS---ILERRREIEELEEKIEELEEKIAELekALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2270 KDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE-----------KMQAVQEATRLKA 2338
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieeleerLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2339 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRAQARAEEDARRFR 2418
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE----DLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2419 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTvRQEQLLQE 2498
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVR 937
|
810
....*....|.
gi 1920237952 2499 TQALQQSFLSE 2509
Cdd:TIGR02168 938 IDNLQERLSEE 948
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
187-286 |
9.82e-23 |
|
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: 95.71 E-value: 9.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 187 AKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 266
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1920237952 267 D-VDVPQPDEKSIITYVSSLY 286
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1888-2529 |
1.22e-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: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1888 RRLLEEQA--AQHKADIEARLAQLRKASE---------SELERQKglveDTLRQRRQVEEEILALKGSFEKAaagkaELE 1956
Cdd:COG1196 158 RAIIEEAAgiSKYKERKEEAERKLEATEEnlerledilGELERQL----EPLERQAEKAERYRELKEELKEL-----EAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1957 LELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2036
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2037 ERAEQESARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqsvlERLRSEAEAARRAAEEAEAARERAEREAA 2116
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELE-----------------------EELEELEEELEEAEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2117 QSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2196
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2197 QELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAenrALVLRDKDSAQRL 2276
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG---VKAALLLAGLRGL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2277 LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2356
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2357 LQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQ 2436
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2437 EKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQR 2516
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
650
....*....|...
gi 1920237952 2517 ERcIEQEKAKLEQ 2529
Cdd:COG1196 763 EE-LERELERLER 774
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1353-2064 |
1.39e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 107.60 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1353 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQE 1431
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIAR---LVGEATKEAEALKA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1432 ELQHLRQSSEAEiqAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGElQALRARAEEAEAQKRQAQEEAERLR 1511
Cdd:NF041483 331 EAEQALADARAE--AEKLVAEAAEKARTVAAED--------TAAQLAKAARTAE-EVLTKASEDAKATTRAAAEEAERIR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1512 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRAlqalEELRLQaEEAeRRLRqAEAERARqvqvaletaqrsaeaelqs 1591
Cdd:NF041483 400 REAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLR------------------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1592 ehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELErwqlkANEALRLRLQAEEVAqqKSLTQA 1671
Cdd:NF041483 454 -----AEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTA-----TAESERVRTEAIERA--TTLRRQ 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1672 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAETEQ----GEQQRQLLEEE 1746
Cdd:NF041483 522 AEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEErltaAEEALADARAE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1747 LARLQREAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALA 1821
Cdd:NF041483 602 AERIRREAAEETERLRTEAAErirtlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEA------AAEAERLKSEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1822 EE-AKRQRQLAEEDAVRQRAEAERVLAeklAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrllEEQAAQHKA 1900
Cdd:NF041483 676 QEsADRVRAEAAAAAERVGTEAAEALA---AAQEEAARRRREAEETLGSARAEADQERERAREQS------EELLASARK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1901 DIEARLAQLRKASESELERQKGLV---EDTLRQRR--------QVEEEILALKGSFEKAAA-GKAELELELGRIRGtaeD 1968
Cdd:NF041483 747 RVEEAQAEAQRLVEEADRRATELVsaaEQTAQQVRdsvaglqeQAEEEIAGLRSAAEHAAErTRTEAQEEADRVRS---D 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1969 TLRSKEQAEQEAARQRQlaaeeerrrreaeERVQKSLAAEEEAARQRKAALEEVERLKAKVEE-ARRLRERAeqeSARQL 2047
Cdd:NF041483 824 AYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEA---SDTLA 887
|
730
....*....|....*..
gi 1920237952 2048 QLAQEAAQKRLQAEEKA 2064
Cdd:NF041483 888 SAEQDAARTRADAREDA 904
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
189-289 |
1.72e-22 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 94.84 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 189 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 268
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1920237952 269 DVPQPDEKSIITYVSSLYDAM 289
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
186-284 |
2.09e-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: 94.61 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 264
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1920237952 265 PEDVDVPQPDEKSIITYVSS 284
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1696-2466 |
2.28e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.06 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1696 RQRELAEQELEKQRQLAEgtaqqrlaAEQELIRLRAETeqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEM 1775
Cdd:TIGR02168 207 RQAEKAERYKELKAELRE--------LELALLVLRLEE---------LREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1776 EVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1855
Cdd:TIGR02168 270 EELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1856 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQH---KADIEARLAQLRKASeSELERQKGLVEDTLRQRR 1932
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIASLN-NEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1933 QVEEEILALKGSFEKAAagKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRrreaeervQKSLAAEEEAA 2012
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA--------LDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2013 RQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQK 2072
Cdd:TIGR02168 488 QARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLKQ 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2073 EQELQQTLQQEQSVLER-LRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE-------AERLKQSAEEQAQAQAQAQA 2144
Cdd:TIGR02168 568 NELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRI 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2145 AAEKLRKEAEQEAARRAQAEQAALRQKQaaDAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLK 2224
Cdd:TIGR02168 648 VTLDGDLVRPGGVITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2225 AEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ----- 2299
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE-IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrea 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2300 ------------EAARLRQLAEEDLAQQRALAEKML----KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQ 2363
Cdd:TIGR02168 805 ldelraeltllnEEAANLRERLESLERRIAATERRLedleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2364 MAQQLAQ---ETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDigerLYRTELATQEKvm 2440
Cdd:TIGR02168 885 LEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE----EYSLTLEEAEA-- 958
|
810 820
....*....|....*....|....*.
gi 1920237952 2441 LVQTLETQRQQSDRDAERLREAIAEL 2466
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1349-2065 |
2.85e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 106.83 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1349 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAEREAQGLQRRMQEEVAR-REEV 1418
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1419 AVEAQEQKRSIQEELQHLRqsSEAEiQAKARQVEAAERSRLRIEEEIRVVRLQLE-ATERQRGGAEGELQALRARAEE-- 1495
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1496 --AEAQKRQAQEEAERLRRQVQDETQRKRQAEAE--LALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR-QAEAER 1570
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLRTEAAEriRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRsEAAAEA 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1571 ARQVQVALETAQRsaeaeLQSEHASFAEKTAQlertlkeehvavvqlreeatrraqqqaeaeraraeaerelerwqlKAN 1650
Cdd:NF041483 669 ERLKSEAQESADR-----VRAEAAAAAERVGT---------------------------------------------EAA 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1651 EALrlrlqaeevaqqksltqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI--- 1727
Cdd:NF041483 699 EAL----------------------------------AAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasa 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1728 RLRAETEQGEQQRqLLEEELARLQREAAAATQKRRELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAE 1803
Cdd:NF041483 745 RKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSD 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1804 AGRFRELA-EEAARLRALA-EEAKRQRQLAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEIALKEKEAENERLRRLA 1881
Cdd:NF041483 824 AYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADA 900
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1882 EDEAFQRRllEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAElelelgR 1961
Cdd:NF041483 901 REDANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------R 972
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1962 IRGTAEDTLRSkeqAEQEAARQRQLAAEEERRrreaeervqkslaAEEEAARQRKAALEEVERL--KAKVEEARRLRERA 2039
Cdd:NF041483 973 LRAEAAETVGS---AQQHAERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAA 1036
|
730 740
....*....|....*....|....*.
gi 1920237952 2040 EQESARQLQLAQEAAQKRLQAEEKAH 2065
Cdd:NF041483 1037 EQADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
186-286 |
2.99e-22 |
|
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: 94.41 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 265
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1920237952 266 EDVDVPQ-PDEKSIITYVSSLY 286
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2003-2618 |
4.51e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2003 KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQ 2082
Cdd:COG1196 203 EPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2083 EQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQ 2162
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2163 AEQAALRQKQAADAEMEKHKQFAEQALRQkaqvEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2242
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2243 SLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2322
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2323 LKEKMQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRV 2400
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2401 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2480
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2481 QLKSEEMQTVRQEQLLQETQALQQsflsekdsLLQRERCIEQEKAKLEQlfqdevakaqalreeqqrqqqqmqqekqqlA 2560
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAE--------EEEERELAEAEEERLEE------------------------------E 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 2561 ASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA 2618
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1800-2615 |
6.18e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1800 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAVR------------QRAEAERVLAEKLAAISEATRlKTEAE 1864
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1865 IALKEKEAENERLRRLAEDEAFQRRLLEEQAAQhKADIEARLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEILAL 1941
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1942 KGSFEKAAAGKAELELELgrirgtaEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2021
Cdd:TIGR02168 308 RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2022 VERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ-QKEQELQQTLQQEQSVLERLRSEAEAAR 2098
Cdd:TIGR02168 381 LETLRSKVAQLELqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2099 RAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQaeqaaLRQKQAADAEM 2178
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-----LSELISVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2179 EKHKQFAEQALRQKAQVEQELTALRLQleetDHQKsilDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARI 2258
Cdd:TIGR02168 536 EAAIEAALGGRLQAVVVENLNAAKKAI----AFLK---QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2259 EAENRA-----------LVLRDKDSAQRLLQEEAEKMKQVAEEAARLS---VAAQEAARLRQLAeedLAQQRALAEkmLK 2324
Cdd:TIGR02168 609 KFDPKLrkalsyllggvLVVDDLDNALELAKKLRPGYRIVTLDGDLVRpggVITGGSAKTNSSI---LERRREIEE--LE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2325 EKMQAVQEAtrlkaEAELLQQQKELAQEQarrlqedkeqmaQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMS 2404
Cdd:TIGR02168 684 EKIEELEEK-----IAELEKALAELRKEL------------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2405 RAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS 2484
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2485 EEMQTvRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASME 2564
Cdd:TIGR02168 827 ESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELR 904
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 2565 EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2615
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
69-174 |
6.38e-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: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 145
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILHFQIS 174
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1027-1591 |
6.61e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.02 E-value: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1027 ARECAQRITEQQKAQAEVDGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1106
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1107 RSTQEAEEVLRAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVE 1186
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1187 RWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL 1266
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1267 EDIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLtsqyir 1346
Cdd:COG1196 477 AALAE-----------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1347 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA----HAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1422
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1423 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1502
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1503 AQEEAERLRRQvqdETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVA-LETA 1581
Cdd:COG1196 692 ELELEEALLAE---EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEeLERE 768
|
570
....*....|
gi 1920237952 1582 QRSAEAELQS 1591
Cdd:COG1196 769 LERLEREIEA 778
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
186-290 |
7.17e-22 |
|
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: 93.32 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGcQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 265
Cdd:cd21245 3 KAIKALLNWVQRRTRK-YGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1920237952 266 EDVDVPQPDEKSIITYVSSLYDAMP 290
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
69-174 |
7.41e-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: 94.00 E-value: 7.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 69 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 145
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILHFQIS 174
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1496-2630 |
9.17e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 101.83 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1496 AEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE--AEAAREKQRALQALEELRLQAE-EAERRLRQAEAERAR 1572
Cdd:NF041483 81 AQIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1573 QVQVA---LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVvqlREEATRRAQQQAEAERARAEAERELERWQLKA 1649
Cdd:NF041483 161 TESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESA---RAEAEAILRRARKDAERLLNAASTQAQEATDH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1650 NEALRLRLQAE-EVAQQKSltqaeaekqkeeaereaRRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrlAAEQELIR 1728
Cdd:NF041483 238 AEQLRSSTAAEsDQARRQA-----------------AELSRAAEQRMQE---AEEALREARAEAEKVVAE--AKEAAAKQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1729 LRAETEQGEQQRQLLEEELARLQREAAA-ATQKRRELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSKQRLEAEA 1804
Cdd:NF041483 296 LASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAKAARTAEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1805 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAI---------------SEATRLKTEAEIALKE 1869
Cdd:NF041483 376 VLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEQLRAE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1870 KEAENERLRRLAEDEAFQR-----RLLEEQAAQHKADIEarlaQLRKASESELERQKG-LVEDTLRQRRQVEEeilALKG 1943
Cdd:NF041483 456 AVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADAD----ELRSTATAESERVRTeAIERATTLRRQAEE---TLER 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1944 SFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ------LAAEEERRRREAEERVQKSLAAEEEAARQRKA 2017
Cdd:NF041483 529 TRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQaeaaeeLTRLHTEAEERLTAAEEALADARAEAERIRRE 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2018 ALEEVERLKAKV-EEARRLRERAEQESARqlqLAQEAAQKRLQAEEKAHAFAVqqkeqelqqtlqqeqsvleRLRSEAEa 2096
Cdd:NF041483 609 AAEETERLRTEAaERIRTLQAQAEQEAER---LRTEAAADASAARAEGENVAV-------------------RLRSEAA- 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2097 arraaeeaeaareraereaaqsrrqvEEAERLKqsaeeqaqaqAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaada 2176
Cdd:NF041483 666 --------------------------AEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEALAAAQ---- 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2177 emekhkqfaEQALRQKAQVEQELTALRLQLEEtdhqksildeelqrlkaevtEAARQRGQVEEELFSLRVQMEELGKLKA 2256
Cdd:NF041483 706 ---------EEAARRRREAEETLGSARAEADQ--------------------ERERAREQSEELLASARKRVEEAQAEAQ 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2257 RI--EAENRA--LVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA-RLRQLAEEDLAQQRALAekmLKEKMQAVQ 2331
Cdd:NF041483 757 RLveEADRRAteLVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAeRTRTEAQEEADRVRSDA---YAERERASE 833
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2332 EATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLemsAEAERlrlrvaEMSRAQARAE 2411
Cdd:NF041483 834 DANRLRREA---QEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTL---ASAEQ------DAARTRADAR 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2412 EDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREaiaelehEKDKLKQEAQLLQLKSEEMQTVR 2491
Cdd:NF041483 902 EDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERV-------RADAAAQAEQLIAEATGEAERLR 974
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2492 QEQLLQETQALQQSflsekdsllqrerciEQEKAKLEQLFQDEVAKAQALReeqqrqqqqmqqekqqlAASMEEARRRQH 2571
Cdd:NF041483 975 AEAAETVGSAQQHA---------------ERIRTEAERVKAEAAAEAERLR-----------------TEAREEADRTLD 1022
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 2572 EAeegvrrQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPSR 2630
Cdd:NF041483 1023 EA------RKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTM 1075
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1108-1912 |
1.28e-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: 101.29 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1108 STQEAEEVLRAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1187
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1188 WRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLE 1267
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1268 DIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQyirf 1347
Cdd:TIGR02168 401 EIER-----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE---- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1348 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQE-EVARREEVAVEAQ--- 1423
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAAlgg 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1424 -------EQKRSIQEELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR 1490
Cdd:TIGR02168 546 rlqavvvENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1491 ARAEEAEAQKRQAQEEAERLR-------------------RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEE 1551
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1552 LRLQAEEAERRLRQAEAERARQVqvaleTAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaea 1631
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE----- 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1632 eraraeaerelerwQLKANEALRLRLQAeEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELaEQELEKQRQL 1711
Cdd:TIGR02168 776 --------------ELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL-ERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1712 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAE---EE 1788
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrelEE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1789 SRSTSEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAVRQRAEAERvLAEKLAAISEATRLkteaeiAL 1867
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AI 992
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1920237952 1868 KEKEAENERLRRLaedeafqrrlleeqaAQHKADIEARLAQLRKA 1912
Cdd:TIGR02168 993 EEYEELKERYDFL---------------TAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2009-2628 |
3.09e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2009 EEAARQRKAALEEVERLKAKVEEARR----LRERAEQ-ESARQLQlaqeAAQKRLQAEEKAHAFAVQQKEqelqqtlqqe 2083
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERqlepLERQAEKaERYRELK----EELKELEAELLLLKLRELEAE---------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2084 qsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQsaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQA 2163
Cdd:COG1196 241 ---LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------------EAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2164 EQAALRQKQAADAEMEKHKQfAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2243
Cdd:COG1196 305 ARLEERRRELEERLEELEEE-LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2244 LRVQMEELgklkARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2323
Cdd:COG1196 384 LAEELLEA----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2324 KEKmQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAER---LRLRV 2400
Cdd:COG1196 460 ALL-ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveAAYEA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2401 AEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLL 2480
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2481 Q--LKSEEMQTVRQEQLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQlfqdEVAKAQALREEQQRQQQQMQQE 2555
Cdd:COG1196 619 GdtLLGRTLVAARLEAALRRAVTLAGRLREvtlEGEGGSAGGSLTGGSRRELLA----ALLEAEAELEELAERLAEEELE 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 2556 KQQLAASMEEARRRQHEAEEGVRRQQEELQRLAqqqqqqEKLLAEENQRLRERLQHLEEERRAALARSEEIAP 2628
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALE------EQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1110-1879 |
7.91e-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: 98.59 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1110 QEAEEVLRAHEEQLKEAQAVpatlpeLEATKAALKKLRAQAEAQQPvFDALRDELRgaqevgerlqqrHGERDVEVERWR 1189
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI------LNELERQLKSLERQAEKAER-YKELKAELR------------ELELALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1190 ErvtlLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVRE---QLRQEKALL 1266
Cdd:TIGR02168 236 E----LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1267 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPV-----ASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLT 1341
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1342 SQYIRFISETLRRMEEE-ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAV 1420
Cdd:TIGR02168 392 ELQIASLNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1421 EAQEQKRSIQEELQHLR------QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE----GELQALR 1490
Cdd:TIGR02168 472 EAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1491 ARAEEAEAQKRQAQEEAERLRR----------QVQDETQRKRQAEAELALRVQAEAEAAREK-QRALQALEELRLQAEEA 1559
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1560 ERRLRQAEAERARQVQVALE---------TAQRSAEAEL-----QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRA 1625
Cdd:TIGR02168 632 DNALELAKKLRPGYRIVTLDgdlvrpggvITGGSAKTNSsilerRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1626 QQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL 1705
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1706 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARA 1785
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1786 EEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE------DAVRQRAEAERVLAEKLAAISEATRL 1859
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEElreklaQLELRLEGLEVRIDNLQERLSEEYSL 951
|
810 820
....*....|....*....|.
gi 1920237952 1860 KTEAEIALKEK-EAENERLRR 1879
Cdd:TIGR02168 952 TLEEAEALENKiEDDEEEARR 972
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
190-287 |
1.90e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 86.63 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 190 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 268
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237952 269 DVPQPDEKSIITYVSSLYD 287
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1356-2092 |
2.06e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 97.20 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1356 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQh 1435
Cdd:NF041483 560 EETERAIAARQAEAAEELTRLHTEAEERLTAAE---EALADARAEAERIRREAAEETER---LRTEAAERIRTLQAQAE- 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1436 lrqsSEAEiqaKARQVEAAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1514
Cdd:NF041483 633 ----QEAE---RLRTEAAADASAARAEGENVAVRLRSEAaAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1515 QDETQRKRQAEAELAlrvQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQVqvalETAQRSAeaelqSEHA 1594
Cdd:NF041483 706 EEAARRRREAEETLG---SARAEADQERERAREQSEEL---LASARKRVEEAQAEAQRLV----EEADRRA-----TELV 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1595 SFAEKTAQLERTlkeehvAVVQLREEATRraqqqaeaeraraeaerelerwqlkanEALRLRLQAEEVAQQksLTQAEAE 1674
Cdd:NF041483 771 SAAEQTAQQVRD------SVAGLQEQAEE---------------------------EIAGLRSAAEHAAER--TRTEAQE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1675 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ--------------- 1739
Cdd:NF041483 816 EADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqd 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1740 ----RQLLEEELARLQREAAA-----ATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrel 1810
Cdd:NF041483 893 aartRADAREDANRIRSDAAAqadrlIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA------ 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1811 AEEAARLRALAEEAKRQrqlAEEDAVRQRAEAERVLAEklaAISEATRLKTEAEialkekeAENERLRRLAEDEAFQRR- 1889
Cdd:NF041483 967 TGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAE---AAAEAERLRTEAR-------EEADRTLDEARKDANKRRs 1033
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1890 ---------LLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 1960
Cdd:NF041483 1034 eaaeqadtlITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTDADELLVGAR 1113
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1961 R----IRGTAEDtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLK--------AK 2028
Cdd:NF041483 1114 RdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANseaskvriAA 1192
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2029 VEEARRLRERAEQESARQLQLAQ------EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2092
Cdd:NF041483 1193 VKKAEGLLKEAEQKKAELVREAEkikaeaEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLEALES 1262
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
71-171 |
1.29e-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: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 71 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 146
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1920237952 147 IRNDDIADGNPKLTLGLIWTIILHF 171
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
186-285 |
1.45e-18 |
|
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: 83.68 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 265
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237952 266 ED-VDVPQPDEKSIITYVSSL 285
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
804-870 |
3.41e-18 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 81.15 E-value: 3.41e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 804 QLKPRSpaHPMRGRVPLLAVCDYKQVEVTVHKGDECQMVGPAQPFYWKVLGSSCSEAAMPSVCFLVP 870
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
72-169 |
4.06e-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: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 72 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 147
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1920237952 148 RNDDI-ADGNPKLTLGLIWTIIL 169
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
186-286 |
4.09e-18 |
|
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: 82.78 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 265
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1920237952 266 EDVDV--PQPDEKSIITYVSSLY 286
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
182-287 |
4.17e-18 |
|
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: 82.69 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 182 SEDMTAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 261
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1920237952 262 LLDPEDV-DVPQPDEKSIITYVSSLYD 287
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
189-285 |
4.64e-18 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 82.36 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 189 EKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 264
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1920237952 265 PEDVDVPQPDEKSIITYVSSL 285
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1350-1938 |
5.39e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 92.29 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1350 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AQGLQRRMQEEVARREEVAVEA 1422
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1423 QEQKRSIQEELQHLRQ-----------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE-----------RQRG 1480
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1481 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELrLQAEEAE 1560
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL-IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1561 RRLRQAeAERarqvqvALETAQRSaeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAER 1640
Cdd:COG4913 474 ERWRGA-IER------VLGGFALT----LLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1641 ELERWQLKANEALRLR---LQAEEVAQ----QKSLTQAEAEKQKEEAEREARRRGKAEE-----QAVRQRELAEQELEK- 1707
Cdd:COG4913 543 KPHPFRAWLEAELGRRfdyVCVDSPEElrrhPRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAEl 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1708 QRQLAEGTAQ-QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLLASKA 1783
Cdd:COG4913 623 EEELAEAEERlEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1784 RAEEESRSTSEKsKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRlKTEA 1863
Cdd:COG4913 703 ELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID-ALRA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1864 EIALKEKEAENERLRRLAEDEAFQ-------------RRLLEEQAAQHKADIEARLAQLRKasESELERQKGLVEDTLRQ 1930
Cdd:COG4913 781 RLNRAEEELERAMRAFNREWPAETadldadleslpeyLALLDRLEEDGLPEYEERFKELLN--ENSIEFVADLLSKLRRA 858
|
....*...
gi 1920237952 1931 RRQVEEEI 1938
Cdd:COG4913 859 IREIKERI 866
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1348-1919 |
2.45e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.10 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1348 ISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAEREAQGLQRRMQEEVARREE 1417
Cdd:PRK02224 218 LDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1418 vaveaqeqkrsIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1494
Cdd:PRK02224 291 -----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1495 EAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRalQALEELRLQAEEAERRLRQAEAErarqv 1574
Cdd:PRK02224 360 ELREEAAELESELEEAREAV--EDRREEIEELEEEIEELRERFGDAPVDL--GNAEDFLEELREERDELREREAE----- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1575 qvaLETAQRSAEAELQSEHASFAE-KTAQLERTLKE-EHVAVVQLREEatrraqqqaeaeraraeaerelerwQLKANEA 1652
Cdd:PRK02224 431 ---LEATLRTARERVEEAEALLEAgKCPECGQPVEGsPHVETIEEDRE-------------------------RVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1653 LRLRLQAEEVAQQKSLTQAEAEKqkeeaerearrrgKAEEQAVR---QRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1729
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLV-------------EAEDRIERleeRREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1730 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAeMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1809
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRER 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1810 LAEEAARLRALAEEAKRQRqLAEEDAVRQRAEA--ERVlAEKLAAISEAtRLKTEAEIALKEKEAEN-ERLR-RLAEDEA 1885
Cdd:PRK02224 629 LAEKRERKRELEAEFDEAR-IEEAREDKERAEEylEQV-EEKLDELREE-RDDLQAEIGAVENELEElEELReRREALEN 705
|
570 580 590
....*....|....*....|....*....|....*.
gi 1920237952 1886 FQRRL--LEEQAAQHKADIEARLAQLRKASESELER 1919
Cdd:PRK02224 706 RVEALeaLYDEAEELESMYGDLRAELRQRNVETLER 741
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1408-2313 |
3.75e-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: 89.65 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1408 MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrlriEEEIRVVRLQLEATERQRGGAEGELQ 1487
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-----KKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1488 ALRARAEEAEAQKRQAQEEAERLRRQVQDetqrKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAE 1567
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIE----KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1568 AERARQVQVALETAQRSAEAELQSEHASFAEKtaqleRTLKEEHVAVVQLREEatrraqqqaeaeraraeaerelerwql 1647
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEEL-----EKELKELEIKREAEEE--------------------------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1648 kANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI 1727
Cdd:pfam02463 357 -EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1728 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEA----- 1802
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKvllal 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1803 -EAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1881
Cdd:pfam02463 516 iKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1882 EDEAFQRRLLeeqAAQHKADIEARLAQ---------LRKASESELERQKGLVEDTLRQRRQVEEEILALKG---SFEKAA 1949
Cdd:pfam02463 596 VLEIDPILNL---AQLDKATLEADEDDkrakvvegiLKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEvkaSLSELT 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1950 AGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKV 2029
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2030 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARE 2109
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK---VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2110 RAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaadAEMEKHKQFAEQAL 2189
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKE---EKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2190 RQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEvteaarQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRD 2269
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE------EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAI 980
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1920237952 2270 KDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLA 2313
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1355-2226 |
4.79e-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: 89.26 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1355 MEEEERLAEQQRAEERERLAEVEaaLEKQRQLAEAHAQAKAQAEREAQGLqrRMQEEVARREEVAVEAQEQKRSIQEELQ 1434
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELK--LKEQAKKALEYYQLKEKLELEEEYL--LYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1435 HLRQSSEAEIQakarqvEAAERSRLRIEEE--IRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1512
Cdd:pfam02463 255 SSKQEIEKEEE------KLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1513 QVQDETQRKRQAEAELAL--RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEAE 1588
Cdd:pfam02463 329 ELKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAakLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1589 LQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSL 1668
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1669 TQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEE 1745
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1746 ELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaeagrfRELAEEAARLRALAEEAK 1825
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV------VEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1826 RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEAR 1905
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1906 LAQLRKaseSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQ 1985
Cdd:pfam02463 723 LADRVQ---EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1986 laaeeerrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2065
Cdd:pfam02463 800 ----------------EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2066 AFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAA 2145
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2146 AEKLRKEAEQEAARRAQAEQAALRQKQAadAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA 2225
Cdd:pfam02463 944 EADEKEKEENNKEEEEERNKRLLLAKEE--LGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
.
gi 1920237952 2226 E 2226
Cdd:pfam02463 1022 F 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
977-1886 |
5.48e-17 |
|
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: 89.36 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 977 QQLLQSLEQGEQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQKAQAEVDGLGKGVARLSA 1056
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1057 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL---------KTISLVIRSTQEAEEVLRAHEEQLKEAQ 1127
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1128 AVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERvtlllerwqavlaqT 1206
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE--------------L 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1207 DVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAvplansqavreqlrqekalleDIERHGEKVEECQRFAKQY 1286
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1287 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR 1366
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1367 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGlqrRMQEEVARREEVAVEAQEQKRS-------------IQEEL 1433
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1434 QHLRQSSEA--------------EIQAKARQ-------VEAAERSRlRIEEEIRVVRLQLEATERQ---RGGA-EGELQA 1488
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvefdpKYEPAFKYvfgdtlvVEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1489 LRARAEEAEAQkrQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeAEAAREKQRALQALEELRLQAEEAERRlRQAEA 1568
Cdd:TIGR02169 667 LFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRL-------DELSQELSDASRKIGEIEKEIEQLEQE-EEKLK 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1569 ERARQVQVALETAQRSAEAElQSEHASFAEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaeRELERWQLK 1648
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENV-KSELKELEARIEELEEDLHKLEEALNDLEAR-------------------LSHSRIPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1649 ANEalrLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIR 1728
Cdd:TIGR02169 797 QAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEE 872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1729 LRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAEAGRFR 1808
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDPKGEDE 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1809 ELAEEAARLRALAEEAKR-QRQLAEEDAVRQRA--EAERVLAEKLAAISEATRLKTEAEiALKEKEAENERLRRLAEDEA 1885
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKREVFMEA 1023
|
.
gi 1920237952 1886 F 1886
Cdd:TIGR02169 1024 F 1024
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1326-1979 |
8.93e-17 |
|
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: 88.59 E-value: 8.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1326 EYVDLRTR-----YSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAERE 1400
Cdd:TIGR02169 212 RYQALLKEkreyeGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1401 AQGLQRRMQEEVARREEvAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAaersrlrIEEEIRVVRLQLEATERQRG 1480
Cdd:TIGR02169 289 QLRVKEKIGELEAEIAS-LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1481 GAEGELQALRARAEEAEAQKR--------------QAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRAL 1546
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAetrdelkdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1547 QA-LEELRLQAEEAERRLRQAEAER--ARQVQVALETAQRSAEAELQS--EHASFAEKTAQLERTLKEEHVAVVQLREEa 1621
Cdd:TIGR02169 440 EEeKEDKALEIKKQEWKLEQLAADLskYEQELYDLKEEYDRVEKELSKlqRELAEAEAQARASEERVRGGRAVEEVLKA- 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1622 trraqQQAEAERARAEAERELERWQLKANEALRLRLQA-----EEVAQQK---------------SLTQAEAEKQKEEAE 1681
Cdd:TIGR02169 519 -----SIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvedDAVAKEAiellkrrkagratflPLNKMRDERRDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1682 REARRRGKA---------EEQAVR---QRELAEQELEKQRQL--------------------------AEGTAQQRLAAE 1723
Cdd:TIGR02169 594 SEDGVIGFAvdlvefdpkYEPAFKyvfGDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1724 QELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQR 1799
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1800 LEAEAgrfrELAEEAARLRALaEEAKRQRQLAEED--------AVRQRAEAERVLAEKLAAISEATRlktEAEIALKEKE 1871
Cdd:TIGR02169 754 ENVKS----ELKELEARIEEL-EEDLHKLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLR---EIEQKLNRLT 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1872 AENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG 1951
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
730 740
....*....|....*....|....*...
gi 1920237952 1952 KAELELELGRIRGTAEDTLRSKEQAEQE 1979
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
186-285 |
1.21e-16 |
|
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: 78.36 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 265
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1920237952 266 ED-VDVPQPDEKSIITYVSSL 285
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1135-2061 |
3.91e-16 |
|
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: 86.56 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1135 ELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerlqqrhgerdveverwrervtlllerwqavlaqtdvRQRELE 1214
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------------------------------------------ELKLKE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1215 QLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALL-EDIERHGEKVEECQRFAKQYINAIKDY 1293
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSkQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1294 ELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRtryselstltsqyIRFISETLRRMEEEERLAEQQRAEERERL 1373
Cdd:pfam02463 285 EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE-------------KKKAEKELKKEKEEIEELEKELKELEIKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1374 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaeiQAKARQVEA 1453
Cdd:pfam02463 352 EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ------LEDLLKEEK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1454 AERSRLRIEEEIRVVRLQLEATERQrggaegelqaLRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1533
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEK----------EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1534 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ-LERTLKEEHV 1612
Cdd:pfam02463 496 EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQkLVRALTELPL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1613 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGK--A 1690
Cdd:pfam02463 576 GARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVslE 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1691 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK 1770
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIN 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1771 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKL 1850
Cdd:pfam02463 736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1851 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDT-LR 1929
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELeSK 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1930 QRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAArQRQLAAEEERRRREAEERVQKSLAAEE 2009
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE-EADEKEKEENNKEEEEERNKRLLLAKE 970
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2010 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAE 2061
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1441-2367 |
4.99e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.89 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1441 EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA-----QKRQAQEEAERLRRQVQ 1515
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellkEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1516 DETQRKRQAEAELALRVQAEAEAAR------EKQRALQALEELRLQAEEAE-----RRLRQAEAERARQVQVALETaqrs 1584
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSIAEKERELEDAEER---- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1585 aEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQaeaeraraeaerelerwqlkanEALRLRLQAEEVAQ 1664
Cdd:TIGR02169 324 -LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----------------------EDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1665 QKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1743
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1744 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAGRFRELAEeaarlral 1820
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHGTVAQLGS-------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1821 aeeAKRQRQLAEEDAVRQRAEAERVLAEKLAAiseatrlktEAEIALKEKEAENER---LRRLAEDEAFQRRLLEEQAAQ 1897
Cdd:TIGR02169 533 ---VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRDERRDLSILSEDGVIG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1898 HKADIEARLAQLRKASESELeRQKGLVEDTLRQRRQVEE-EILALKGS-FEKAAA--GKAElelelgRIRGTAEDTLRSK 1973
Cdd:TIGR02169 601 FAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKyRMVTLEGElFEKSGAmtGGSR------APRGGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1974 EQAEQEAARqrqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ-----ESARQLQ 2048
Cdd:TIGR02169 674 AELQRLRER-------------------------LEGLKRELSSLQSELRRIENRLDELSQELSDASRkigeiEKEIEQL 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2049 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraAEEAEAARERAEREAAQSRRQVEEAERL 2128
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE---------EDLHKLEEALNDLEARLSHSRIPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2129 KQSAEeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEE 2208
Cdd:TIGR02169 800 LSKLE--------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2209 tdhqksiLDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRlLQEEAEKMKQVA 2288
Cdd:TIGR02169 866 -------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIE 937
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 2289 EEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2367
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1153-2063 |
7.22e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 85.61 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1153 QQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1222
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1223 YRESADPLGAWLRDAKQR-QEQIQAVP--LANSQAVREQLRQEKALLE-DIERHGEKVEECQRFAKQYINAIKDYELQLV 1298
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKmQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1299 TYKAQLEPVASPAKK-PKVQSGSESIIQEyVDLRTRYSElstltsqyirfisETLRRMEEEERLAEQQRAEERERLAEVE 1377
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEE-------------KGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1378 AalekqrQLAEAHAQAkAQAEREAQGLQRRMQEEVARREevavEAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERS 1457
Cdd:pfam01576 229 A------QIAELRAQL-AKKEEELQAALARLEEETAQKN----NALKKIRELEAQISELQEDLESERAARNK----AEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1458 RLRIEEEIRVVRLQLEATErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELalrvqaeA 1536
Cdd:pfam01576 294 RRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------T 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1537 EAAREKQRALQALEELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQ 1616
Cdd:pfam01576 363 EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1617 LREEATRRAQQQAEAERARAEAERELERWQLKANEALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVR 1696
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL---------------EDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1697 QRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK------ 1770
Cdd:pfam01576 501 LQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektkn 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1771 -VRAEMEVLLAS-------------------KARAEEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQ 1829
Cdd:pfam01576 577 rLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLAEEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1830 LAEEDAVRQRAEAERVLAEKLAA---ISEATRLKTEAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADI 1902
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVgknVHELERSKRALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDL 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1903 EARlaqlrkaSESELERQKGLVedtlRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAAR 1982
Cdd:pfam01576 734 QAR-------DEQGEEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1983 QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAE 2061
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQD 882
|
..
gi 1920237952 2062 EK 2063
Cdd:pfam01576 883 EK 884
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
190-287 |
1.04e-15 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 76.07 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 190 KLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 268
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1920237952 269 DVPQPDEKSIITYVSSLYD 287
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1368-1930 |
1.18e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.97 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1368 EERERLAEVEAALEKQRQLAEAHAQAKAQAEreaqglQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRqsseaeIQAK 1447
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDARE------QIELLEPIRELAERYAAARERLAELEYLRAALR------LWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1448 ARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE-AQKRQAQEEAERLRRQvQDETQRKRQAEA 1526
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERE-LEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1527 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS-------EHASFAEK 1599
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerrksnIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1600 TAQLERTLKEEHVAV------VQLREEAtrraqqqaeaeraraeaerelERWQLKANEAL---RLRL--------QAEEV 1662
Cdd:COG4913 446 RDALAEALGLDEAELpfvgelIEVRPEE---------------------ERWRGAIERVLggfALTLlvppehyaAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1663 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAETEQG--- 1736
Cdd:COG4913 505 VNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAITRAGqvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1737 ------------------------EQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRST 1792
Cdd:COG4913 585 gngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1793 S-EKSKQRLEAEagrFRELAEEAARLRALAEEAKRQRQlAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 1871
Cdd:COG4913 665 SaEREIAELEAE---LERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1872 AENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRkaseSELERQKGLVEDTLRQ 1930
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIDALR----ARLNRAEEELERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
932-1620 |
1.19e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.72 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 932 EQRQALRSLELHYQA----FLRDSQDAGgfgPEDRLQAEREYGSCSRHYQQLLQSLEQGEQE----ESRCQRCISELKDI 1003
Cdd:TIGR02168 217 ELKAELRELELALLVlrleELREELEEL---QEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1004 RLQLEACETRTVH---RLRlPLDKEPARECAQRITEQQKAQAEVDGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELEL 1080
Cdd:TIGR02168 294 ANEISRLEQQKQIlreRLA-NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1081 TLGKL-EQVRSLSAIYLEKLKTISLvIRSTQEaeeVLRAHEEQLKEAQAVPATlpelEATKAALKKLRAQAEAQQPVFDA 1159
Cdd:TIGR02168 373 RLEELeEQLETLRSKVAQLELQIAS-LNNEIE---RLEARLERLEDRRERLQQ----EIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1160 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTLL---LERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRD 1236
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1237 AKQR---------------QEQIQAVPLANSQAVR---EQLRQEK----ALLEDIERHGEKVEECQRFAKQYINAIKDYE 1294
Cdd:TIGR02168 525 LSELisvdegyeaaieaalGGRLQAVVVENLNAAKkaiAFLKQNElgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1295 LQLVTYKAQLEPVASP---------------AKKPKVQSGSESIIQEYVDLRTRYS--------ELSTL-TSQYIRFISE 1350
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1351 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1430
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1431 EELQHLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1510
Cdd:TIGR02168 765 ELEERLEEAEEEL--------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1511 RRQVQDETQRKRQAEAELAlrvqaeaeaarekqRALQALEELRLQAEEAERRLRQAEAERArQVQVALETAqRSAEAELQ 1590
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIE--------------SLAAEIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELS 900
|
730 740 750
....*....|....*....|....*....|..
gi 1920237952 1591 SEHASFAEKTAQLERTLKE--EHVAVVQLREE 1620
Cdd:TIGR02168 901 EELRELESKRSELRRELEElrEKLAQLELRLE 932
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1325-1981 |
2.29e-15 |
|
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: 83.73 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1325 QEYVDLRTRYSELSTLTSQYIRFISETLRRMEE-EERLAE--QQRAEERERLAEVEAALEKQRQLAEAhAQAKAQAEREA 1401
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFGYKSDETLIASRQEErQETSAElnQLLRTLDDQWKEKRDELNGELSAADA-AVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1402 QGLQRRMQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAeIQAKARQVEAA-ERSRLRIEEEIRVV--------RLQL 1472
Cdd:pfam12128 327 LEDQHGAFLDA--DIETAAADQEQLPSWQSELENLEERLKA-LTGKHQDVTAKyNRRRSKIKEQNNRDiagikdklAKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1473 EATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEA-----EAAREKQ--- 1543
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENfderiERAREEQeaa 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1544 -----RALQALEELRLQAEEAERRLRQAEAeRARQVQVALETAQR-------------SAEAELQSEHASFAEKTAQLER 1605
Cdd:pfam12128 484 naeveRLQSELRQARKRRDQASEALRQASR-RLEERQSALDELELqlfpqagtllhflRKEAPDWEQSIGKVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1606 TLKEEHVAVVQLREEATRRaqqqaeaeraraeaerelerwqlkaneALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREAR 1685
Cdd:pfam12128 563 TDLDPEVWDGSVGGELNLY---------------------------GVKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1686 RRGKAEEQAvRQRELAEQELEKQrQLAEGTAQQRLA-AEQELIRLraeTEQGEQQRQLLEEELARLQREaaaATQKRREL 1764
Cdd:pfam12128 616 AREKQAAAE-EQLVQANGELEKA-SREETFARTALKnARLDLRRL---FDEKQSEKDKKNKALAERKDS---ANERLNSL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1765 EAELAKVraEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQraeaer 1844
Cdd:pfam12128 688 EAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRD------ 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1845 vLAEKlaAISEATRLKTEAEIalKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKG-L 1923
Cdd:pfam12128 760 -LASL--GVDPDVIAKLKREI--RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAI-SELQQQLArL 833
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 1924 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTlrSKEQAEQEAA 1981
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDA--NSEQAQGSIG 889
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2816-2854 |
2.59e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.36 E-value: 2.59e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 2816 LLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 2854
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
68-167 |
3.08e-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: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 68 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 142
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 1920237952 143 KLVNIRNDDIADGNPKLTLGLIWTI 167
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3475-3513 |
5.87e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 5.87e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3475 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEMNRVL 3513
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4053-4091 |
5.87e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.20 E-value: 5.87e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 4053 LLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEMNEIL 4091
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1759-2626 |
7.60e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.04 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1759 QKRRELEAELAKVrAEMEvllASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEdavRQ 1838
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFD---RKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE---KR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1839 RAEAERVLAEKLAAisEATRLKTEAEIAlkEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASESELE 1918
Cdd:TIGR02169 222 EYEGYELLKEKEAL--ERQKEAIERQLA--SLEEELEKLTEEISE-------LEKRLEEIEQLLEELNKKIKDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1919 RQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDtlrSKEQAEQEAARQRQLAAEEERRRREAE 1998
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1999 ERVQKSLAAEEEAARQR---KAALEEVERLKAKVEE----ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHA 2066
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRdelKDYREKLEKLKREINElkreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2067 FAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAA 2146
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELY----------------------DLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2147 EKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTAlrlqleetdhQKSIldEELQRLKA- 2225
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVA----------KEAI--ELLKRRKAg 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2226 EVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENR-----------ALVLRDKDSAQRLLQ---------EEAEKMK 2285
Cdd:TIGR02169 574 RATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARRLMGkyrmvtlegELFEKSG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2286 QVA----EEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2352
Cdd:TIGR02169 654 AMTggsrAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2353 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARaeEDARRFRKQAEDIGERLYRTE 2432
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2433 LATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQalqqsfLSEKDS 2512
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD------LESRLG 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2513 LLQRERC-IEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG---------VRRQQE 2582
Cdd:TIGR02169 886 DLKKERDeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvqaeLQRVEE 965
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1920237952 2583 ELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEEI 2626
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYEEVLKRldeLKEKRAKLEEERKAILERIEEY 1012
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
188-299 |
8.80e-15 |
|
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: 73.49 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 188 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 267
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 1920237952 268 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 299
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
64-170 |
1.02e-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: 73.08 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 64 ADERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIA 133
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYA 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1920237952 134 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 170
Cdd:cd21219 71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
874-1604 |
1.11e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.64 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 874 QEAQEAIARLEAQHQALVALWHQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQD 953
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 954 AggfgpEDRLQA-EREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQ 1032
Cdd:TIGR02168 370 L-----ESRLEElEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1033 RITEQQKAQAEVDGLGKGVARLSAE-AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLS---AIYLEKLKTISLVIRS 1108
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvKALLKNQSGLSGILGV 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1109 TQEAEEVlrahEEQLKeaQAVPATLPE---------LEATKAALKKLrAQAEAQQPVFDALrDELRGAQEVGERLQQRHG 1179
Cdd:TIGR02168 525 LSELISV----DEGYE--AAIEAALGGrlqavvvenLNAAKKAIAFL-KQNELGRVTFLPL-DSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1180 ERDV-----EVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYR------ESADPLGAWLRDAKQRqeqiQAVP 1248
Cdd:TIGR02168 597 IEGFlgvakDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgDLVRPGGVITGGSAKT----NSSI 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1249 LANSQAVREqLRQEKALLEDIERHGEKveecqrfakqyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYV 1328
Cdd:TIGR02168 673 LERRREIEE-LEEKIEELEEKIAELEK-------------ALAELRKELEELEEELE---------QLRKELEELSRQIS 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1329 DLRTRYSELST---LTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ 1405
Cdd:TIGR02168 730 ALRKDLARLEAeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1406 ---RRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQR 1479
Cdd:TIGR02168 810 aelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1480 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA-LRVQAEAEAAREKQRALQALEELRLQAEE 1558
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1920237952 1559 AERRLRQAEAERARQVQVALEtaqrsAEAELQSEHASFAEKTAQLE 1604
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLA-----AIEEYEELKERYDFLTAQKE 1010
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1255-1919 |
1.24e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.50 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1255 VREQLRQEKALLEDIERhgekveecqrfAKQYINAIKDYELQLVTYKAQ---LEPVaspakkpkvqsgsESIIQEYVDLR 1331
Cdd:COG4913 213 VREYMLEEPDTFEAADA-----------LVEHFDDLERAHEALEDAREQielLEPI-------------RELAERYAAAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1332 TRYSELSTLTSQY-IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEREAQGLQR 1406
Cdd:COG4913 269 ERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1407 RMQEEVARREEVAVEAQEQKRSI--------------QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1472
Cdd:COG4913 349 RLERELEERERRRARLEALLAALglplpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1473 EATERQRGGAEGELQALRARAEEAeaqkrqAQEEAERLR-----RQVQDETQRKRQAeAELALRVQA-----EAEAAREK 1542
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEA------LGLDEAELPfvgelIEVRPEEERWRGA-IERVLGGFAltllvPPEHYAAA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1543 QRALQALE-ELRLQAEEAERRLRQAEAER------ARQVQVALETAQRSAEAELQSehaSFAEKTAQLERTLKEEHVAV- 1614
Cdd:COG4913 502 LRWVNRLHlRGRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELGR---RFDYVCVDSPEELRRHPRAIt 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1615 --VQLREEATrraqqqaeaERARAEAERELERWQL-KANEALRLRLQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAE 1691
Cdd:COG4913 579 raGQVKGNGT---------RHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL----------EAE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1692 EQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQREAAAATQKRRELEAEL 1768
Cdd:COG4913 640 LDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEI 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1769 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1848
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1849 -KLAAISEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELER 1919
Cdd:COG4913 796 fNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1110-1610 |
1.31e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1110 QEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfDALRDELRGAQEVGERLQQRHGERDVEVERWR 1189
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1190 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ---AVPLANSQAVREQLRQEKALL 1266
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1267 EDIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESIIQEYVDLRTRYSELSTLtsqyir 1346
Cdd:PRK02224 387 EELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT------ 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1347 fISETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAK--AQAEREAQG 1403
Cdd:PRK02224 435 -LRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEdlVEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1404 LQRR---MQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvRLQLEATERQRG 1480
Cdd:PRK02224 514 LEERredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1481 GAEGELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDETQRKRQAEAELAlrvQAEAEAARE-KQRALQALeelrlq 1555
Cdd:PRK02224 592 ERIRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYL------ 662
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1556 aEEAERRLRQAEAERAR-QVQVALETAQRSAEAELQSEHASFAEKTAQLErTLKEE 1610
Cdd:PRK02224 663 -EQVEEKLDELREERDDlQAEIGAVENELEELEELRERREALENRVEALE-ALYDE 716
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1070-1823 |
1.55e-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: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1070 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLkeaqavPATLPELEATKAALKKLRAQ 1149
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCM------PDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1150 AEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEverwrervtllLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdp 1229
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR-----------IEELRAQEAVLEETQERINRARKAAPLAAHIK-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1230 lgAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAS 1309
Cdd:TIGR00618 301 --AVTQIEQQAQRIHTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1310 PAKKPKVQSGSESIIQEyvDLRTRYSELSTLTSQYIRFISETLRRMEEEERL--AEQQRAEERERLAEVEAALEKQRQ-- 1385
Cdd:TIGR00618 377 LTQHIHTLQQQKTTLTQ--KLQSLCKELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQce 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1386 -LAEAHAQAKAQAERE-------AQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA--EIQAKARQVEAAE 1455
Cdd:TIGR00618 455 kLEKIHLQESAQSLKEreqqlqtKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidNPGPLTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1456 RSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE 1535
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1536 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVV 1615
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1616 QLREEATRRAQQQAEAERARAEAERELERWQLkANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREArrrgkaEEQAV 1695
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE------AHFNN 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1696 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQREAAAATQKRRELEAELAK 1770
Cdd:TIGR00618 767 NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 1771 VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE 1823
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1350-1841 |
1.74e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.20 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1350 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA--QAKAQAEREAQGLQRRMQEEVARREEVAvEAQEQKR 1427
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELR-ELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1428 SIQEELQHLRQSSEaeiqakarqvEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1507
Cdd:COG4717 167 ELEAELAELQEELE----------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1508 ER--LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSA 1585
Cdd:COG4717 237 EAaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1586 EAElqsehasfaektaQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAqq 1665
Cdd:COG4717 317 EEE-------------ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1666 ksltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQqrqlLEE 1745
Cdd:COG4717 382 -----------------------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE----LEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1746 ELARLQREAAAATQKRRELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAK 1825
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
|
490
....*....|....*....
gi 1920237952 1826 RQRQLAEED---AVRQRAE 1841
Cdd:COG4717 504 EAREEYREErlpPVLERAS 522
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
188-287 |
1.96e-14 |
|
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: 72.31 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 188 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 267
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1920237952 268 VDV--PQPDEKSIITYVSSLYD 287
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
71-171 |
3.14e-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: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 71 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 142
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1920237952 143 KLVNIRNDDIADGNPKLTLGLIWTIILHF 171
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1344-2063 |
3.37e-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: 80.01 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1344 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQ 1423
Cdd:TIGR00618 140 YKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1424 EQKRSIQEELQHLR--QSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL---RARAEEAEA 1498
Cdd:TIGR00618 219 ERKQVLEKELKHLReaLQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInraRKAAPLAAH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1499 QKRQAQEEAERLRRQVQ-DETQRKRQAEAELALRVQAEAEAAREKQRALQAL--EELRLQAEEAERRLRQAEAERARQVQ 1575
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsQEIHIRDAHEVATSIREISCQQHTLT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1576 VALETAQRSAEAELQSEHASFAEKTaqlertlkeehvavvQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL 1655
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELD---------------ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELC 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1656 RLQAEEVAQQKSLTQAEAEKQKEEAerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQ 1735
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQESAQSL--------KEREQQLQTKEQIHLQETRKKAVVL----ARLLELQEEPCPLCGSCI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1736 GEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLAS----KARAEEESRSTSEKSKQR---------LEA 1802
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQraslKEQMQEIQQSFSILTQCDnrskedipnLQN 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1803 EAGRFRELAEEAARLR-ALAEEAKRQ-RQLAEEDAVRQRAEAERVLAEKLAaiSEATRLKTEAEIALKEKEAENERLRRL 1880
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEdMLACEQHALlRKLQPEQDLQDVRLHLQQCSQELA--LKLTALHALQLTLTQERVREHALSIRV 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1881 AEDEAFQRRLLEEQAAQHKADieaRLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELG 1960
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKE---QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1961 RIRGTAEDTLRSKEQAEQEAARQrqlaaeeerrRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2040
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNEE----------VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816
|
730 740
....*....|....*....|....
gi 1920237952 2041 QE-SARQLQLAQEAAQKRLQAEEK 2063
Cdd:TIGR00618 817 DIlNLQCETLVQEEEQFLSRLEEK 840
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
960-1499 |
3.62e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 960 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLrlpldkeparecAQRITEQQK 1039
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL------------EELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1040 AQAEVDGLGKGVARLSAEAEKVLAlpepspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1119
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEE---------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1120 EEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERw 1199
Cdd:COG1196 413 LERLERLEE------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1200 qavlaqtdvRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIERHGEKVEEC 1279
Cdd:COG1196 486 ---------LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-LEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1280 QRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEE 1358
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1359 ERLAEQQRAEERERLAEVEAALEKQRqLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQ 1438
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGS-LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 1439 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1499
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1162-1941 |
4.62e-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: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1162 DELRGAQEVGERLQQRHGERDvEVERWRERVTLLLERwqaVLAQTDVRQRELEQLGRqlryYREsadplgawLRDAKQRQ 1241
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELE-EVEENIERLDLIIDE---KRQQLERLRREREKAER----YQA--------LLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1242 EQiqAVPLANSQAVREQLRQEKALLEDIERHGEKVEEcqrfakqyinAIKDYELQLVTYKAQLEPVASPAKKpkvqSGSE 1321
Cdd:TIGR02169 224 EG--YELLKEKEALERQKEAIERQLASLEEELEKLTE----------EISELEKRLEEIEQLLEELNKKIKD----LGEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1322 SIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA 1401
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1402 QGLQRRMQEEVARREEVAVEAQEQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGG 1481
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKL-EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1482 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEEL---RLQA-- 1556
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVlkaSIQGvh 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1557 ----------EEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFA-----EKTAQLERTLKEEHVA-------- 1613
Cdd:TIGR02169 525 gtvaqlgsvgERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplNKMRDERRDLSILSEDgvigfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1614 --------------------VVQLREEATRRAQQQAEAERA--------------RAEAERELERWQLKAnEALRLRLQA 1659
Cdd:TIGR02169 605 lvefdpkyepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEgelfeksgamtggsRAPRGGILFSRSEPA-ELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1660 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAV---RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1736
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeieKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1737 EQQRQLLEEELARLQreAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAEEAAR 1816
Cdd:TIGR02169 764 EARIEELEEDLHKLE--EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEYLEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1817 LRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAA 1896
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1897 QHKADIEA---RLAQLRKASESELERQKGL--VEDTLRQRRQVEEEILAL 1941
Cdd:TIGR02169 921 ELKAKLEAleeELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRAL 970
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
186-283 |
5.13e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.87 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 261
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 1920237952 262 LLDPEDVDVPQPDEKSIITYVS 283
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
188-291 |
5.21e-14 |
|
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: 71.23 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 188 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 267
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1920237952 268 VDV--PQPDEKSIITYVSSLYDAMPR 291
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
191-286 |
6.09e-14 |
|
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: 70.85 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 191 LLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 269
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1920237952 270 VPQPDEKSIITYVSSLY 286
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1337-2248 |
6.71e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.06 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1337 LSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEV----EAALEKQRQLAEAHAQAkAQAEREAQGLQRRMQEEV 1412
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEStdlqEQIAELQAQIAELRAQL-AKKEEELQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1413 ARREEvaveAQEQKRSIQEELQHLRQSSEAEIQAKARqveaAERSRLRIEEEIRVVRLQLEATErqrgGAEGELQALRAR 1492
Cdd:pfam01576 257 AQKNN----ALKKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1493 AE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaeaEAAREKQRALQALEELRlQAEEAERRLRQAEAERA 1571
Cdd:pfam01576 325 REqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1572 RQVQVALETAQRSAEAELQSEHASFAEktAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1651
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1652 ALRlrlqAEEVAQQKSLTQAEAEKqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRA 1731
Cdd:pfam01576 475 ELL----QEETRQKLNLSTRLRQL---------------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1732 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAK-------VRAEMEVLLAS-------------------KARA 1785
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1786 EEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---ISEATRLKT 1861
Cdd:pfam01576 612 EEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVgknVHELERSKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1862 EAEIALKEKEAENERLR-RLAEDEAFQRRL---LEEQAAQHKADIEARlaqlrkaSESELERQKGLVedtlRQRRQVEEE 1937
Cdd:pfam01576 689 ALEQQVEEMKTQLEELEdELQATEDAKLRLevnMQALKAQFERDLQAR-------DEQGEEKRRQLV----KQVRELEAE 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1938 ILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2017
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKN 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2018 ALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSVLERLRSEAE 2095
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRKSTL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2096 AARR---AAEEAEAARERAEREAAQSRRQVEEAeRLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQ 2172
Cdd:pfam01576 918 QVEQlttELAAERSTSQKSESARQQLERQNKEL-KAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKL 996
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2173 AADAE---------MEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2243
Cdd:pfam01576 997 VRRTEkklkevllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVST 1076
|
....*
gi 1920237952 2244 LRVQM 2248
Cdd:pfam01576 1077 LKSKL 1081
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3734-3772 |
1.20e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.35 E-value: 1.20e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3734 LLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPELHDRL 3772
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1086-1589 |
1.36e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1086 EQVRSLSAI--YLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPatlpELEATKAALKKLRAQAEAQQPVFDALRDE 1163
Cdd:COG4913 249 EQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEA----ELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1164 LRGAQEV-----GERLQQRhgERDVE-VERWRERVTLLLERWQAVLAQTDVR---------------QRELEQLGRQLRY 1222
Cdd:COG4913 325 LDELEAQirgngGDRLEQL--EREIErLERELEERERRRARLEALLAALGLPlpasaeefaalraeaAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1223 YRESADPLGAWLRDAKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IE 1270
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1271 R--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQS------GSESIIQEYVD--LRTRY 1334
Cdd:COG4913 482 RvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSlagkldFKPHPFRAWLEaeLGRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1335 S--------ELST----LTSQYIRFISETLRRMEEEERL---------AEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1393
Cdd:COG4913 560 DyvcvdspeELRRhpraITRAGQVKGNGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1394 KAQAEREAQGLQRRmqEEVARREEVAVEAQEQKRSIQEELQHLRQSSeAEIQAKARQVEAAERSRLRIEEEIRVVRLQLE 1473
Cdd:COG4913 640 LDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1474 ATERQRGGAEGELQALRARAEEAE------------------AQKRQAQEEAERLRRQVQDETQRKRQAEAEL------- 1528
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEdlarlelralleerfaaaLGDAVERELRENLEERIDALRARLNRAEEELeramraf 796
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 1529 -------ALRVQAEAEAAREKQRALQALEELRL---QAEEAERRLRQAEAERArQVQVALETAQRSAEAEL 1589
Cdd:COG4913 797 nrewpaeTADLDADLESLPEYLALLDRLEEDGLpeyEERFKELLNENSIEFVA-DLLSKLRRAIREIKERI 866
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1646-2506 |
1.94e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.42 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1646 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1721
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1722 --AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1799
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1800 LEAEAGRFRELAEEAARLRALAEEAKRQRQlaeedavrQRAEAERVLAEKLAAISEatrLKTEAEIALKEKEAENERLRR 1879
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSE--------ELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1880 LAED-EAFQRRLLEEQAAQhkADIEARLAQLRKaSESELERQKGLVEDTLRQRRQVEEeilalkgsfekaaagkaELELE 1958
Cdd:TIGR02169 460 LAADlSKYEQELYDLKEEY--DRVEKELSKLQR-ELAEAEAQARASEERVRGGRAVEE-----------------VLKAS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1959 LGRIRGTAEDTLRSKEQ---AEQEAARQRqlaaeeerrrrEAEERVQKSLAAEE--EAARQRK---AALEEVERLKAKVE 2030
Cdd:TIGR02169 520 IQGVHGTVAQLGSVGERyatAIEVAAGNR-----------LNNVVVEDDAVAKEaiELLKRRKagrATFLPLNKMRDERR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2031 EARRLRERAEQESARQLqlaQEAAQKRlqaeEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2110
Cdd:TIGR02169 589 DLSILSEDGVIGFAVDL---VEFDPKY----EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2111 AEREAAQSRRQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2187
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2188 ALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQveEELFSLRVQMEELGKLKARIEAENRALvl 2267
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREI-- 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2268 rDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQK 2347
Cdd:TIGR02169 818 -EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKER 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2348 ELAQEQARRLQEDKEQMAQQlaqetqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfRKQAEDIGER 2427
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQ-----------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAE 959
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 2428 LYRTELAtqekvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSF 2506
Cdd:TIGR02169 960 LQRVEEE-------IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENF 1031
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1077-1599 |
2.07e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1077 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEvLRAHEEQLKEAQAvpaTLPELEATKAALKKLRAQAEAQQpv 1156
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE-LARLEAELERLEA---RLDALREELDELEAQIRGNGGDR-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1157 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLRD 1236
Cdd:COG4913 340 LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1237 AKQRQEQIQA-----------VPlANSQAVREQLRQEKALLED---------------------IER--HGEK----VEE 1278
Cdd:COG4913 417 LRRELRELEAeiaslerrksnIP-ARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIERvlGGFAltllVPP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1279 cQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsiiqeyvdlrtrysELSTLTSQYIRFISETLRRM- 1355
Cdd:COG4913 496 -EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRf 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1356 -----EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQAKAQAEREAQGLQRRMQEEVARREEVAvE 1421
Cdd:COG4913 560 dyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-A 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1422 AQEQKRSIQEELQHLRQSSEAEIQakarqVEAAERSRLRIEEEIRvvrlQLEAterqrggAEGELQALRARAEEAEAQKR 1501
Cdd:COG4913 639 ELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1502 QAQEEAERLRRQVQDETQRKRQAEAEL-ALRVQAEAEAAREKQRALQALEELRlqAEEAERRLRQAEAERARQVQVALET 1580
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRA 780
|
570
....*....|....*....
gi 1920237952 1581 AQRSAEAELQSEHASFAEK 1599
Cdd:COG4913 781 RLNRAEEELERAMRAFNRE 799
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1727-2540 |
2.69e-13 |
|
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: 76.93 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1727 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEAea 1804
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLMN-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1805 grfrelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAErvlAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1884
Cdd:TIGR00618 172 ------LFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ---LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1885 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEeilalkgsfeKAAAGKAELELELGRIRG 1964
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1965 TAEdtLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2044
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2045 rQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2124
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2125 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2204
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2205 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLkarIEAENRAlvlrdKDSAQRLLQEEAEKm 2284
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL---TEKLSEA-----EDMLACEQHALLRK- 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2285 KQVAEEAARLSVAAQEAARLRQLAEEDLAQqraLAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA--RRLQEDKE 2362
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHA---LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSekEQLTYWKE 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2363 QMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEdigERLYRTELATQEKVMLV 2442
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK---ARTEAHFNNNEEVTAAL 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2443 QTLeTQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQ 2522
Cdd:TIGR00618 775 QTG-AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
810
....*....|....*...
gi 1920237952 2523 EKAKLEQlfQDEVAKAQA 2540
Cdd:TIGR00618 854 YEECSKQ--LAQLTQEQA 869
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2168-2627 |
3.39e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2247
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2248 MEELGKLKARIEAEnRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2327
Cdd:TIGR02168 311 LANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2328 QAVQEATRLKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2406
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2407 QARAEEDARRFRKQAEDIGERLYRTE-----------------------------LATQEKV------------------ 2439
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsgilgvLSELISVdegyeaaieaalggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2440 MLVQTLETQRQ--QSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE-----------------------MQTVRQEQ 2494
Cdd:TIGR02168 550 VVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsylLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2495 LLQETQALQ------------------------QSFLSEKDSLLQRERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQ 2550
Cdd:TIGR02168 630 DLDNALELAkklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 2551 QMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2627
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1367-2473 |
4.24e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.53 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1367 AEERERLaeVEAALEKQRQLAEAHAQAKAQAEReaqglqrrmQEEVARREEvavEAQEQKRSIQEELQ----HLRQSSEA 1442
Cdd:PRK04863 278 ANERRVH--LEEALELRRELYTSRRQLAAEQYR---------LVEMARELA---ELNEAESDLEQDYQaasdHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1443 EIQAKA--RQVEAAERSRLRIEEEIRVVRlqlEATERQrggaegelqalraraEEAEAQKRQAQEEAERLRRQVQDETQr 1520
Cdd:PRK04863 344 LRQQEKieRYQADLEELEERLEEQNEVVE---EADEQQ---------------EENEARAEAAEEEVDELKSQLADYQQ- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1521 krqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVALETAQRSAEAElqsEH 1593
Cdd:PRK04863 405 --------ALDVQQTR--AIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ---AA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1594 ASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALRlrlqaeevaqqksltqaea 1673
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEVS-----RSEA-----------------------WD-VARELLR------------------- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1674 ekqkeeaerearrrgkaeeQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1753
Cdd:PRK04863 504 -------------------RLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1754 AAAAtqkRRELEAELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1833
Cdd:PRK04863 563 LEAR---LESLSESVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1834 dAVRQRAEAERVLAEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAEDeaFQRRLLEEQ----AAQHKADIEARLAQ 1908
Cdd:PRK04863 632 -YMQQLLERERELTVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER--FGGVLLSEIyddvSLEDAPYFSALYGP 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1909 LRKASeseLERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG--KAElELELGRIRGTAEDTLR-SKEQAEQ---EAAR 1982
Cdd:PRK04863 709 ARHAI---VVPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSvfSVE-ELEKAVVVKIADRQWRySRFPEVPlfgRAAR 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1983 QRQLaaeeerrrreaeervqkslaaeEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLA---------QEA 2053
Cdd:PRK04863 785 EKRI----------------------EQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeaelRQL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2054 AQKRLQAEEKahafavqqkeqelqqtlqqeqsvLERLRSeaeaarraaeeaeaareraerEAAQSRRQVEEAERLKQSae 2133
Cdd:PRK04863 843 NRRRVELERA-----------------------LADHES---------------------QEQQQRSQLEQAKEGLSA-- 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2134 eqaqaqaqaqaaaekLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRlqleeTDhqk 2213
Cdd:PRK04863 877 ---------------LNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ-----SD--- 933
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2214 silDEELQRLKAEVTEAARQRGQVEEELFSLrvqmEELGKLKARIEAENRALVLRDKDSAQRLLQ---EEAEKMKQVAEE 2290
Cdd:PRK04863 934 ---PEQFEQLKQDYQQAQQTQRDAKQQAFAL----TEVVQRRAHFSYEDAAEMLAKNSDLNEKLRqrlEQAEQERTRARE 1006
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2291 AARlsvaaQEAARLRQLAE--EDLAQQRALAEKMLKEKMQAVQEAT-RLKAEAE-LLQQQKELAQEQARRLQEDKEQMAQ 2366
Cdd:PRK04863 1007 QLR-----QAQAQLAQYNQvlASLKSSYDAKRQMLQELKQELQDLGvPADSGAEeRARARRDELHARLSANRSRRNQLEK 1081
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2367 QLaqetqgfqkTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEkvmlvqtLE 2446
Cdd:PRK04863 1082 QL---------TFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAYLS-------AD 1145
|
1130 1140
....*....|....*....|....*..
gi 1920237952 2447 TQRQQSDRDAERLREAIAELEHEKDKL 2473
Cdd:PRK04863 1146 ELRSMSDKALGALRLAVADNEHLRDVL 1172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1133-1592 |
6.00e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.57 E-value: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1133 LPELEATKAALKKLRAQAEAqqpvFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTL--LLERWQAVLAQTDVRQ 1210
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1211 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQekaLLEDIERHGEKVEECQRFAKQYINAI 1290
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1291 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESII-------QEYVDLRTRYSELSTLTSQYIRFISETLRRMEE--EE 1359
Cdd:COG4717 223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1360 RLAEQQRAEERERL--AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKrsIQEELQHLR 1437
Cdd:COG4717 303 EAEELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1438 QSSEAEIQAKARQVEAAErsrlRIEEEIRVVRLQLEA--TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1515
Cdd:COG4717 381 VEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1516 DETQRKRQAEAElalrvqaeaeaarekqralQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQRSAEAELQSE 1592
Cdd:COG4717 457 ELEAELEQLEED-------------------GELAELLQELEELKAELRELAEEWAALklALELLEEAREEYREERLPP 516
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
188-283 |
6.85e-13 |
|
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: 67.80 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 188 KEKLLLWSQRMVEGCqglRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 266
Cdd:cd21229 5 KKLMLAWLQAVLPEL---KITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1920237952 267 DVDVPQPDEKSIITYVS 283
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
89-168 |
8.14e-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: 67.62 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 89 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 160
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1920237952 161 LGLIWTII 168
Cdd:cd21223 105 LALLWRII 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3068-3106 |
8.42e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.04 E-value: 8.42e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3068 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPELHEKL 3106
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
188-289 |
9.30e-13 |
|
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: 67.80 E-value: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 188 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 267
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1920237952 268 -VDVPQPDEKSIITYVSSLYDAM 289
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2170-2700 |
1.13e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2170 QKQAADAEMEKHKQFAEQALRqkaqVEQELTAlrlqleETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV-QM 2248
Cdd:PTZ00121 1121 KKKAEDARKAEEARKAEDARK----AEEARKA------EDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrKA 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2249 EELGKLKA--RIEAENRALVLRDKDSAQRllQEEAEKMKQV--AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2324
Cdd:PTZ00121 1191 EELRKAEDarKAEAARKAEEERKAEEARK--AEDAKKAEAVkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2325 EKMQAVQEATrlKAEaELLQQQKELAQEQARRLQEDKEqmAQQLAQETQGFQKTLETERQRQlEMSAEAERLRLRVAEMS 2404
Cdd:PTZ00121 1269 QAAIKAEEAR--KAD-ELKKAEEKKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAE-EAKKKADAAKKKAEEAK 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2405 RAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLEtQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlKS 2484
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK-KA 1420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2485 EEMQTvRQEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQ--DEVAKAQALREEQQRqqqqmqqekqqlAAS 2562
Cdd:PTZ00121 1421 DEAKK-KAEEKKKADEAKKKAEEAKKADEAKKK---AEEAKKAEEAKKkaEEAKKADEAKKKAEE------------AKK 1484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2563 MEEARRRQHEAeegvRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR-SEEIAPSRA-AAARALPNG 2640
Cdd:PTZ00121 1485 ADEAKKKAEEA----KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkAEEKKKADElKKAEELKKA 1560
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2641 QDAADGPAAAAEPEHAFDGLRR-----KVPAQRLQEVGVL-------SAEELQQLAQGRTTVAELAQREDVR 2700
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLyeeekkmKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
186-286 |
1.20e-12 |
|
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: 67.41 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 265
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1920237952 266 ED-VDVPQPDEKSIITYVSSLY 286
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1336-1553 |
1.31e-12 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 73.37 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1336 ELSTLTSQYIR-----FISETLRRMEEEERLAEQQRAEeRERLAEVEAAlEKQRQLAEAHAQAKAQAER----EAQGLQR 1406
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAIA-QANREAEEAELEQEREIETariaEAEAELA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1407 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqLEATERQRGGAEGEL 1486
Cdd:COG2268 248 KKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAE-------LEADVRKPAEAEKQA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 1487 QALRARAeEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR 1553
Cdd:COG2268 321 AEAEAEA-EAEAIRAKGLAEAEGKRALA--EAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1111-1607 |
1.36e-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: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1111 EAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELrgAQEVGERLQQRHGERDVEVERWRE 1190
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1191 RVTLLLERWQAVLAQ-TDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDI 1269
Cdd:COG4913 317 RLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1270 ERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFIS 1349
Cdd:COG4913 397 EEELEALEEALAEAEA---ALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1350 ETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAEREAQGLQRRM- 1408
Cdd:COG4913 465 ELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKLd 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1409 ----------QEEVARREEVA-VEAQEQ----KRSIQEELQ--------------HLRQ------SSEAEIQAKARQVEA 1453
Cdd:COG4913 542 fkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRSryvlgfDNRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1454 AERSRLRIEEEIRVVRLQLEATERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDETQRK 1521
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1522 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEAELQSEHASFAEK 1599
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRAR 781
|
....*...
gi 1920237952 1600 TAQLERTL 1607
Cdd:COG4913 782 LNRAEEEL 789
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1353-1855 |
1.67e-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: 74.60 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1353 RRMEEEERLAEQQRAEERERLAE----VEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRS 1428
Cdd:COG3096 242 RMTLEAIRVTQSDRDLFKHLITEatnyVAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSAR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1429 iQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELqalraraEEAEAQKRQAQE 1505
Cdd:COG3096 322 -ESDLEQDYQAASdhlNLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1506 EAERLRRQVQDETQrkrqaeaelALRVQAEAeaAREKQRALQALEELR-------LQAEEAERRLRQAEAERARQVQVAL 1578
Cdd:COG3096 390 EVDSLKSQLADYQQ---------ALDVQQTR--AIQYQQAVQALEKARalcglpdLTPENAEDYLAAFRAKEQQATEEVL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1579 ETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEAtrraqqqaeaeraraeaerelerWQlKANEALR---- 1654
Cdd:COG3096 459 ELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQA-----------------------WQ-TARELLRryrs 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1655 LRLQAEEVAQQKSltqaeaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETE 1734
Cdd:COG3096 507 QQALAQRLQQLRA------------------QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1735 QGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEA 1804
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLERER 640
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 1805 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISE 1855
Cdd:COG3096 641 EATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLLSEIYD 691
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1354-2478 |
1.80e-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: 74.44 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1354 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHAQAKAQAEREAqglqrrmqEEVARREEVAVEAQEQKRSI 1429
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNALQEQLQAET--------ELCAEAEEMRARLAARKQEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1430 QEELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKRQAQEEAER 1509
Cdd:pfam01576 74 EEILHEL----ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR-------QKLQLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1510 LRRQVQDETQRKRQAE---AELALRVQAEAEAA------REKQRALQALEELRLQAEEAERRlrqaEAERARQVQVALET 1580
Cdd:pfam01576 143 LEDQNSKLSKERKLLEeriSEFTSNLAEEEEKAkslsklKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1581 AQRSAEAELQsehASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKANEALRLRLQaE 1660
Cdd:pfam01576 219 DLQEQIAELQ---AQIAELRAQLAKKEEELQAALARLEEETAQKNNALK----------------KIRELEAQISELQ-E 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1661 EVAQQKSltqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGT-----AQQRLAA--EQELIRLR--- 1730
Cdd:pfam01576 279 DLESERA----------------------ARNKAEKQRRDLGEELEALKTELEDTldttaAQQELRSkrEQEVTELKkal 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1731 -AETEQGEQQRQ-----------LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQ 1798
Cdd:pfam01576 337 eEETRSHEAQLQemrqkhtqaleELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK-RKKLEGQLQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1799 RLEA---EAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERV---LAEKLAAISEATRLKTEAEIALKEKE 1871
Cdd:pfam01576 416 ELQArlsESERQRaELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLesqLQDTQELLQEETRQKLNLSTRLRQLE 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1872 AENERLRRLAEDEAFQRRLLEEQAAQHkadiEARLAQLRKASESELERQKGLVEDtlrqRRQVEEEILALKGSFEKAAAG 1951
Cdd:pfam01576 496 DERNSLQEQLEEEEEAKRNVERQLSTL----QAQLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1952 KAELELELGRIRGTAEDTLRSKEQaeqeaarQRQLAAEEERRRREAEErvqksLAAEEEAARQRKAALEEVERLKAKVEE 2031
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDLDH-------QRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAEAEAREKE 635
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2032 ARRLRERAEQESARQLQLAQEAAQKRLQAEekahafavqqkeqelqqtlqqeqsvLERLRSEAEAARRAAEEAEAARERA 2111
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELERSKRAL 690
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2112 EREAAQSRRQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKQfaeQALRQ 2191
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQ 750
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2192 KAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKD 2271
Cdd:pfam01576 751 VRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE 830
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2272 SAQRLLQEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2351
Cdd:pfam01576 831 SEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2352 EQARRLQEDKEQMAQQLAQETQGFQKtLETERQrqlEMSAEAERLRLRVAEMSRAQ---------------ARAEEDARR 2416
Cdd:pfam01576 910 DRLRKSTLQVEQLTTELAAERSTSQK-SESARQ---QLERQNKELKAKLQEMEGTVkskfkssiaaleakiAQLEEQLEQ 985
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2417 FRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQ 2478
Cdd:pfam01576 986 ESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAS 1047
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
73-174 |
1.94e-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: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 73 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 145
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILHFQIS 174
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1484-2062 |
2.78e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1484 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaEAELALRVQAEAEAAREKQRALQALEELRLQAEEA--ER 1561
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1562 RLRQAEAERARQVQVALETA---QRSAEAELQSEHASFAEKTAQLERTLKEehvavvqLREEATRRAQQQAEAERARAEA 1638
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------LEEERDDLLAEAGLDDADAEAV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1639 ERELERWQlKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEaerearrrgKAEEQAVRQRELA---EQELEKQRQLAEGT 1715
Cdd:PRK02224 313 EARREELE-DRDEELRDRLEECRVAAQAHNEEAESLREDAD---------DLEERAEELREEAaelESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1716 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR---AEMEVLLA------------ 1780
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqpve 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1781 --SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--EDAVRQRAEAERVLAEKLAAISEA 1856
Cdd:PRK02224 463 gsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1857 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE---------ARLAQLRKASESELERQKGLVE-- 1925
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAEln 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1926 ----DTLRQRRqveEEILALKGSFEKAAAGKAELELElgrirgTAEDTLRSKEQAEQEAARQRqlaaeeerrrreaeERV 2001
Cdd:PRK02224 623 derrERLAEKR---ERKRELEAEFDEARIEEAREDKE------RAEEYLEQVEEKLDELREER--------------DDL 679
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 2002 QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2062
Cdd:PRK02224 680 QAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3810-3848 |
3.24e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.24e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3810 LLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDTHDQL 3848
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3399-3437 |
4.98e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.98e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3399 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3437
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4322-4360 |
5.18e-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: 5.18e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 4322 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4360
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
188-287 |
5.98e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 65.05 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 188 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 263
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1920237952 264 DPEDVdVPQPDEKSIITYVSSLYD 287
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1689-1910 |
7.00e-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: 70.56 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1768
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1769 AKVRAE----------------MEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1831
Cdd:COG4942 100 EAQKEElaellralyrlgrqppLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1832 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeafqrRLLEEQAAQHKADIEARLAQLR 1910
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA------RLEAEAAAAAERTPAAGFAALK 252
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2186-2510 |
7.35e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 72.08 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2186 EQALRQKAQVEQELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSL--RVQMEELGKLK-------A 2256
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2257 RIEAENRALVLRDKDSAQRLLQEEaekmKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKMLKEKMQAVQEATRL 2336
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2337 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARR 2416
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2417 fRKQAEDIGERLYRTELATQEKVM--------LVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2488
Cdd:pfam17380 486 -RKRAEEQRRKILEKELEERKQAMieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
330 340
....*....|....*....|..
gi 1920237952 2489 TVRQEQLLQETQALQQSFLSEK 2510
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVESEK 586
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1887-2627 |
7.64e-12 |
|
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: 72.31 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1887 QRRLLEEQAA---QHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIR 1963
Cdd:pfam02463 153 ERRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1964 GTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQES 2043
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2044 ARQLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRR 2120
Cdd:pfam02463 313 EEKLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2121 QVEEAErlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELT 2200
Cdd:pfam02463 393 KEEELE--LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2201 ALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEE 2280
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2281 AEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqralaekmlkekmqavqeaTRLKAEAELLQQQKELAQEQARRLQED 2360
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARK------------------------LRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2361 KEQMAQQLAQETQGFQKTLETERQRQLEMSaeaERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVM 2440
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2441 LVQTLETQRQQSdrdaERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCI 2520
Cdd:pfam02463 684 KAESELAKEEIL----RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2521 EQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGvrrQQEELQRLAQQQQQQEKLLAE 2600
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELE 836
|
730 740
....*....|....*....|....*..
gi 1920237952 2601 ENQRLRERLQHLEEERRAALARSEEIA 2627
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEI 863
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1028-1613 |
9.92e-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: 71.91 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1028 RECAQRITEQQKAQAEVDGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEqvrslsaiylEKLKTISLVIR 1107
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----------------ELEELLAELE----------AQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1108 STQEAEEVLRAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQqpvFDALRDELRGAQEVGERLQQRHGERDvEVE 1186
Cdd:COG3096 575 EAVEQRSELRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEA---LADSQEVTAAMQQLLEREREATVERD-ELA 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1187 RWRERVTLLLERWQAVLAQTDVRQREL-EQLGRQL--RYYR----ESADPLGAWLRDAKQrqeqiqAVPLANSQAVREQL 1259
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPRLLALaERLGGVLlsEIYDdvtlEDAPYFSALYGPARH------AIVVPDLSAVKEQL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1260 RQEKALLED---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKPKVQSGSESIIQEYVDL 1330
Cdd:COG3096 725 AGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLEELRAERDELAEQYAKA 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1331 RTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQE 1410
Cdd:COG3096 805 SFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQLKEQLQLLNKLLP 881
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1411 EV---------ARREEVAVE---AQEQKRSIQEELQHLRQSSE--AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATE 1476
Cdd:COG3096 882 QAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALS 961
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1477 --RQR------GGAEGEL-------QALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE 1541
Cdd:COG3096 962 evVQRrphfsyEDAVGLLgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQE 1041
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 1542 -KQRALQALEELRLQAEEaERRLRQAEAERARQVQVALETAQRSAEAELQSEHASF--AEKTAQLERTLKEEHVA 1613
Cdd:COG3096 1042 lEELGVQADAEAEERARI-RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLrkAERDYKQEREQVVQAKA 1115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3977-4015 |
1.18e-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: 1.18e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3977 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4015
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1385-1755 |
1.28e-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: 71.31 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1385 QLAEAHAQAKAQAEREAQGLQRRMQEEVARREevaveaqeqKRSIQEELQHLRQSSEAEiqaKARQVEA-------AERS 1457
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQE---------KEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1458 RLRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQ-AEA 1536
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1537 EAAREKQRALQALEELRLQAEEA-ERRLRQAEAERARQVQ-VALETAQRSAEAE-LQSEHASFAEKTAQLERTLKEEHVA 1613
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMErVRLEEQERQQQVErLRQQEEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1614 VVQLREeatrraqqqaeaeraraeaereLERWQLKANEalrlRLQAEEVAQQKSLTQAEAEKQKEEAEREARRrgKAEEQ 1693
Cdd:pfam17380 490 EEQRRK----------------------ILEKELEERK----QAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEE 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 1694 AVRQrelaeQELEKQRQLAEgtaqQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1755
Cdd:pfam17380 542 RRKQ-----QEMEERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3144-3182 |
1.31e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.31e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3144 LLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKETSAAL 3182
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
186-286 |
1.58e-11 |
|
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: 63.90 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 265
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1920237952 266 ED-VDVPQPDEKSIITYVSSLY 286
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1097-1982 |
1.67e-11 |
|
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: 71.16 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1097 EKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpvfdalrdelrgaqevgerlqq 1176
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----------------------------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1177 rhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplgawlrDAKQRQEQIQAVPLANSQAVR 1256
Cdd:pfam02463 231 ---YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEE--------KEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1257 EQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsesiIQEYVDLRTRYSE 1336
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL-----EKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1337 LSTLTSQYIRFISETLRRMEEEERLA-----EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEE 1411
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKseeekEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1412 VARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR-IEEEIRVVRLQLEATERQRGGAEGELQALR 1490
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESkARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1491 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ-AEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1569
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVrALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1570 RARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERELERWQLKA 1649
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE----GLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1650 NEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1729
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1730 RAETEQGEQQRQLLEEELARLQREAAAATQKrrELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1809
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEE--ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1810 LAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 1889
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1890 LLEEQAAQHKADIEARLAQLRKASESELERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDT 1969
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEE---RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|...
gi 1920237952 1970 LRSKEQAEQEAAR 1982
Cdd:pfam02463 1006 KLIRAIIEETCQR 1018
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2212-2619 |
1.69e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2212 QKSILDEELQRLKAEVTEAARQRG---QVEEELFSLRVQMEELGKLKARIEAENRAL--------VLRDKDSAQRLLQEE 2280
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLekllqllpLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2281 AEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQED 2360
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2361 KEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEED---------------ARRFRKQAEDIG 2425
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2426 ERLYRTELATQEkvmlvQTLETQRQQSDRDAERLREAI--AELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL- 2502
Cdd:COG4717 302 KEAEELQALPAL-----EELEEEELEELLAALGLPPDLspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALl 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2503 QQSFLSEKDSLLQRERCIEQEKAKLEQLfqdEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2582
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237952 2583 ELQRLAQQQQQQEK-----LLAEENQRLRERLQHLEEERRAA 2619
Cdd:COG4717 454 ELAELEAELEQLEEdgelaELLQELEELKAELRELAEEWAAL 495
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1324-1822 |
1.86e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.14 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1324 IQEYVDLRTRYSELSTLTSQYirFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAqg 1403
Cdd:COG3096 248 IRVTQSDRDLFKHLITEATNY--VAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARES-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1404 lqrrmqeevarreevAVEAQEQKRSiqeelQHLrqsseAEIQAKARQVEAAERSRLRIEEeirvVRLQLEATERQRGGAE 1483
Cdd:COG3096 324 ---------------DLEQDYQAAS-----DHL-----NLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1484 GELqalraraEEAEAQKRQAQEEAERLRRQVQDETQrkrqaeaelALRVQaeAEAAREKQRALQALEELR-------LQA 1556
Cdd:COG3096 375 EQL-------AEAEARLEAAEEEVDSLKSQLADYQQ---------ALDVQ--QTRAIQYQQAVQALEKARalcglpdLTP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1557 EEAERRLRQAEAERARQVQVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVavvqlREEATRRAQQQAEAERARA 1636
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---AARRQFEKAYELVCKIAGEVE-----RSQAWQTARELLRRYRSQQ 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1637 EAERELERWQLKANEA-LRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGT 1715
Cdd:COG3096 509 ALAQRLQQLRAQLAELeQRLRQQQNAERLLEEF-------------------CQRIGQQLDAAEELEELLAELEAQLEEL 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1716 AQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRRELEAE----LAKVRAEMEVLLaSKARAEEESRS 1791
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARIKEL-AARAPAWLAAQDALERLREQSGEaladSQEVTAAMQQLL-EREREATVERD 647
|
490 500 510
....*....|....*....|....*....|....*
gi 1920237952 1792 TSEKSKQRLEAEAgrfRELA----EEAARLRALAE 1822
Cdd:COG3096 648 ELAARKQALESQI---ERLSqpggAEDPRLLALAE 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1418-1621 |
1.88e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1418 VAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE 1497
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1498 AQKRQAQEEAERLRRQVQDET----QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRL-----RQAEA 1568
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLaelaaLRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 1569 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1621
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
629-807 |
2.05e-11 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 66.70 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 629 LHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQ 708
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 709 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTATRLEDLLQDAQDEKEQLSEY 788
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 1920237952 789 RGHLSGLAKRAKAIVQLKP 807
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1699-2619 |
2.24e-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: 70.59 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1699 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAeME 1776
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1777 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDavrqraeaervLAEKLAAISEA 1856
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLEEE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1857 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRrlleEQAAQHKADIEARLAQLRKASESELERQKGLVEdtLRQRRqvEE 1936
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGEELEALKTELEDTLDTTAAQQE--LRSKR--EQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1937 EILALKGSFEKAAAGKAELELELGRIRGTAEDTLrsKEQAEQeAARQRQLAAEEERRRREAEERVQKSL----AAEEEAA 2012
Cdd:pfam01576 328 EVTELKKALEEETRSHEAQLQEMRQKHTQALEEL--TEQLEQ-AKRNKANLEKAKQALESENAELQAELrtlqQAKQDSE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2013 RQRKAALEEVERLKAKVEEARRLRERAEQESARqLQLAQEAAQKRLQAEEKahafavqqKEQELQQTLQQEQSVLERLRS 2092
Cdd:pfam01576 405 HKRKKLEGQLQELQARLSESERQRAELAEKLSK-LQSELESVSSLLNEAEG--------KNIKLSKDVSSLESQLQDTQE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2093 EAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQ 2172
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2173 AADAEMEKHKQFAEQALRQKAQVEQELTALRLQLeetDHQKSILDEELQRLKAEVTEAArqrgqvEEELFSLRVQMEelg 2252
Cdd:pfam01576 556 ALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVSNLEKKQKKFDQMLA------EEKAISARYAEE--- 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2253 klKARIEAENRalvlrDKDSAQRLLQEEAEKMKQVAEEAARlsvaaqeAARLRQLAEEDLAQQRALAEKMLKE----KMQ 2328
Cdd:pfam01576 624 --RDRAEAEAR-----EKETRALSLARALEEALEAKEELER-------TNKQLRAEMEDLVSSKDDVGKNVHElersKRA 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2329 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLEtERQRQL-----EMSAEAERLRLRVAEM 2403
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE-EKRRQLvkqvrELEAELEDERKQRAQA 768
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2404 SRAQARAEEDARRFRKQAEDIGERlyRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLK 2483
Cdd:pfam01576 769 VAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQ 846
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2484 SEEMQTVRQE-QLLQETQALQQ---SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQL 2559
Cdd:pfam01576 847 EDLAASERARrQAQQERDELADeiaSGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTEL 926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2560 AAS---------------------------MEEARRRQHEA-----EEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRE 2607
Cdd:pfam01576 927 AAErstsqksesarqqlerqnkelkaklqeMEGTVKSKFKSsiaalEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKE 1006
|
970
....*....|..
gi 1920237952 2608 RLQHLEEERRAA 2619
Cdd:pfam01576 1007 VLLQVEDERRHA 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1730-2046 |
2.30e-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: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1730 RAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElAKVRAEMEVLLASKARAEEESRSTSEKSkqrlEAEAGRFRE 1809
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERERELERIRQEERKR----ELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1810 LAEEAARLRALaEEAKRQRQLAEEdAVRQRAEAERV--LAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA-- 1885
Cdd:pfam17380 370 IAMEISRMREL-ERLQMERQQKNE-RVRQELEAARKvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAre 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1886 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKglvedtlRQRRQVEEEilaLKGSFEKAAAGKAELELELGRIRGT 1965
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK-------RDRKRAEEQ---RRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1966 AEDTLRSKEQAEQEAARQRQlaaeeerrrREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2045
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE---------AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
.
gi 1920237952 2046 Q 2046
Cdd:pfam17380 589 A 589
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1526-2062 |
2.76e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 70.66 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1526 AELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE-RARQVQVALETAQRSAEAELQSEHAS--------F 1596
Cdd:COG3899 712 ARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppaS 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1597 AEKTAQLERTLKEEHVAVVQLREEATRRAQQ--QAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQkslTQAEAE 1674
Cdd:COG3899 792 ARAYANLGLLLLGDYEEAYEFGELALALAERlgDRRLEARALFNLGFILHWLGPLREALELLREALEAGLE---TGDAAL 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1675 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA 1754
Cdd:COG3899 869 ALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAA 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1755 AAATQKRRELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1834
Cdd:COG3899 949 AAAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAAL 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1835 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1914
Cdd:COG3899 1016 AAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1915 SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRR 1994
Cdd:COG3899 1096 ALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAAL 1175
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 1995 REAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2062
Cdd:COG3899 1176 AALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1437-2062 |
3.12e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 70.25 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1437 RQSSEAEIQAKARQVEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1510
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1511 RRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAeLQ 1590
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1591 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAerelerwqlkANEALRLRLQAEEVAQQKSLTQ 1670
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAED----------DLQALESELREQLEAGKLEFNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1671 AEAEKQKEEAEREARRRG-KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1749
Cdd:pfam12128 438 EEYRLKSRLGELKLRLNQaTATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1750 LQREAAAATQ----KRRELEAELAKVRAEMEVLLASKARAEEESRS------TSEKSKQRLEAEAGRFRELAEEAARLRA 1819
Cdd:pfam12128 518 RQSALDELELqlfpQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTdldpevWDGSVGGELNLYGVKLDLKRIDVPEWAA 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1820 LAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHK 1899
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1900 A-------DIEARLAQLRKASESELERQKG---------------LVEDTLRQRRQVEEEILALKGSFE----------- 1946
Cdd:pfam12128 678 DsanerlnSLEAQLKQLDKKHQAWLEEQKEqkreartekqaywqvVEGALDAQLALLKAAIAARRSGAKaelkaletwyk 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1947 --------------KAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 2012
Cdd:pfam12128 758 rdlaslgvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADT 837
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 2013 RQRKAALEevERLKAKVEEARRLRE-----RAEQESARQLQLAQEAAQKRLQAEE 2062
Cdd:pfam12128 838 KLRRAKLE--MERKASEKQQVRLSEnlrglRCEMSKLATLKEDANSEQAQGSIGE 890
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1407-2505 |
3.31e-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: 70.20 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1407 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEA--AERSRLRIEEEIRvVRLQLEATErqrggAEG 1484
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqAETELCAEAEEMR-ARLAARKQE-----LEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1485 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDetqrkrqAEAELalrvqAEAEAAREKqralqaleeLRLQAEEAERRLR 1564
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQD-------LEEQL-----DEEEAARQK---------LQLEKVTTEAKIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1565 QAEAErarqvqVALETAQRSaeaELQSEHASFAEKTAQLERTLKEEHVAVVQL-----REEATRRAQQQAEAERARAEAE 1639
Cdd:pfam01576 135 KLEED------ILLLEDQNS---KLSKERKLLEERISEFTSNLAEEEEKAKSLsklknKHEAMISDLEERLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1640 RELERWQLKAnEALRLRlqaEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1719
Cdd:pfam01576 206 LEKAKRKLEG-ESTDLQ---EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE--LQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1720 LAAEqelirlRAETEQGEQQRQLLEEELARLQRE---AAAATQKRRELEAelakvRAEMEVLLASKArAEEESRSTSEKS 1796
Cdd:pfam01576 280 LESE------RAARNKAEKQRRDLGEELEALKTEledTLDTTAAQQELRS-----KREQEVTELKKA-LEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1797 KQRLEAEAGRFRELAEE---AARLRALAEEAK--------------RQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1859
Cdd:pfam01576 348 QEMRQKHTQALEELTEQleqAKRNKANLEKAKqalesenaelqaelRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1860 KTEAEIALKEKEAENERLRRLAEDeafqrrlLEEQAAQHKADIEARLAQLRKASE--SELERQKGLVEDTLrqrRQVEEE 1937
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNE-------AEGKNIKLSKDVSSLESQLQDTQEllQEETRQKLNLSTRL---RQLEDE 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1938 ILALKGSFEKAAAGKAELELELGRIRGTAEDTlrsKEQAEQEAARQRQLaaeeerrrreaeERVQKSLAAEEEAARQRka 2017
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM---KKKLEEDAGTLEAL------------EEGKKRLQRELEALTQQ-- 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2018 aLEEVERLKAKVEEAR-RLRERAE-----QESARQLQLAQEAAQKR---LQAEEKA-HAFAVQQKEQELQQTLQQEQSVL 2087
Cdd:pfam01576 561 -LEEKAAAYDKLEKTKnRLQQELDdllvdLDHQRQLVSNLEKKQKKfdqMLAEEKAiSARYAEERDRAEAEAREKETRAL 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2088 ERLRSeaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAA 2167
Cdd:pfam01576 640 SLARA----------------------LEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEM 697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQaadaEMEKHKQFAEQA-LR-------QKAQVEQELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQvee 2239
Cdd:pfam01576 698 KTQLE----ELEDELQATEDAkLRlevnmqaLKAQFERDLQARDEQGEE---KRRQLVKQVRELEAELEDERKQRAQ--- 767
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2240 eLFSLRVQME-ELGKLKARIEAENRAlvlrdKDSAQRLLQEEAEKMKQVAeeaarlsvaaqeaarlRQLAEEDLAQQRAL 2318
Cdd:pfam01576 768 -AVAAKKKLElDLKELEAQIDAANKG-----REEAVKQLKKLQAQMKDLQ----------------RELEEARASRDEIL 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2319 AEKMLKEKmqavqeatRLKA-EAELLQQQKELA-QEQARR-LQEDKEQMAQQLAQETQGfqKTLETERQRQLEmsaeaER 2395
Cdd:pfam01576 826 AQSKESEK--------KLKNlEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDEKRRLE-----AR 890
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2396 LRLRVAEMSRAQARAEEDARRFRKQAEDIgERLyRTELATQEKvmLVQTLETQRQQSDRDAERLREAIAELEHE-KDKLK 2474
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQV-EQL-TTELAAERS--TSQKSESARQQLERQNKELKAKLQEMEGTvKSKFK 966
|
1130 1140 1150
....*....|....*....|....*....|.
gi 1920237952 2475 QEAQLLQLKSEEMqtvrQEQLLQETQALQQS 2505
Cdd:pfam01576 967 SSIAALEAKIAQL----EEQLEQESRERQAA 993
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2740-2778 |
3.48e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.42 E-value: 3.48e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 2740 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPELHHKL 2778
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2174-2530 |
4.06e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.68 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2174 ADAEMEKHKQFAEQA--LRQKA-QVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE 2250
Cdd:PRK02224 344 AESLREDADDLEERAeeLREEAaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2251 LGKLKARIEAENRALVLRDKDsAQRLLQE-EAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKM 2327
Cdd:PRK02224 424 LREREAELEATLRTARERVEE-AEALLEAgKCPECGQPVEGSPHVETIEEDRERVEELEAEleDLEEEVEEVEERLERAE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2328 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSraQ 2407
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRER-AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN--S 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2408 ARAEEDARrfRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERL---REAIAELEHEKDklkqEAQLLQLKS 2484
Cdd:PRK02224 580 KLAELKER--IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLaekRERKRELEAEFD----EARIEEARE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1920237952 2485 EEMQTVR-QEQLLQETQALQQsflsEKDSLLQRERCIEQEKAKLEQL 2530
Cdd:PRK02224 654 DKERAEEyLEQVEEKLDELRE----ERDDLQAEIGAVENELEELEEL 696
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1370-1895 |
5.88e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 69.50 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1370 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1449
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1450 QVEAAERSRLRIEEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDETQRKRQAEA 1526
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1527 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1606
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1607 LKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARR 1686
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1687 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA 1766
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1767 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1846
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1920237952 1847 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQA 1895
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2169-2371 |
6.03e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.87 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2169 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2248
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2249 EELGK---LKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2325
Cdd:COG4942 114 YRLGRqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237952 2326 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2371
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1008-1563 |
7.92e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1008 EACETRTVHRLRLPLDKEPARECAQRITEQQKAqaevDGLGKGV--ARLSAEAEKVLAlPEPSPAAPTLRSELELTLGKL 1085
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAeeAKKKADAAKKKA-EEAKKAAEAAKAEAEAAADEA 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1086 EQVRSLS-AIYLEKLKTISLVIRSTQEAEEVLRAhEEQLKEAQAVPATLPELEATKAALKK---LRAQAEAQQPVfdalr 1161
Cdd:PTZ00121 1360 EAAEEKAeAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKadeAKKKAEEKKKA----- 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1162 DELRGAQEvgERLQQRHGERDVEVERWRERVTLLLERwqavlaqtdvrQRELEQLGRQLRYYREsADPLGAWLRDAKQRQ 1241
Cdd:PTZ00121 1434 DEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEE-----------AKKADEAKKKAEEAKK-ADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1242 EQIQAVPLANSQAVREQLRQEKALLEDIERHGE--KVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSG 1319
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADE----AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1320 SESIIQEYVDLR----TRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERlaeveaalEKQRQLAEAHAQAKA 1395
Cdd:PTZ00121 1576 KNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK--------KKVEQLKKKEAEEKK 1647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1396 QAEReaqgLQRRMQEEVARREEVAVEAQEQKRSIQEelqhLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVRLQLEAT 1475
Cdd:PTZ00121 1648 KAEE----LKKAEEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDE--------KKAAEALKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1476 ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElalrvQAEAEAAREKQRALQALEELRLQ 1555
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK-----KEEEKKAEEIRKEKEAVIEEELD 1786
|
....*...
gi 1920237952 1556 AEEAERRL 1563
Cdd:PTZ00121 1787 EEDEKRRM 1794
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
66-165 |
8.54e-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: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 66 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 137
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1920237952 138 RHRQVKLVNIRNDDIADGNPKLTLGLIW 165
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
188-288 |
1.12e-10 |
|
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: 61.60 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 188 KEKLLLWSQRMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 267
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1920237952 268 VdVPQPDEKSIITYVSSLYDA 288
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1343-2060 |
1.38e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.22 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1343 QYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEA 1422
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1423 QEQKRSIQEELQHLRQ---SSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1492
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1493 --AEEAEAQKRQAQEEAERLRRQVQDET-QRKRQAEAELAlRVQAEAEAAREKQRALQAleelrlQAEEAERRLRQAEAE 1569
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRIeQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1570 RARQVQvALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAeaerelerwQLKA 1649
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ---------KLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1650 NEALRLRLQAEEVAQQKSLtqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1720
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1721 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTQKRRELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1796
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1797 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAV----RQ----------------------RAEAERVLAEK 1849
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQqienmtqlvgqhgrtagamqveKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1850 LAAISEATRLKTEAEIALKEKEAE---------------NERLRRLAEDEAFQRRLLEEQAAQHK------ADIEARLAQ 1908
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARvsdlelekvklvnagSERLRAVKDIKQERDQLLNEVKTSRNelnslsEDYEVLKRN 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1909 LRKASE------SELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAG-KAELELELGRIrgtaeDTLRSK----EQAE 1977
Cdd:pfam15921 683 FRNKSEemetttNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGmQKQITAKRGQI-----DALQSKiqflEEAM 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1978 QEAARQRQLAAEEERRRREAEERV---QKSLAAEEEAARQRKAALEE--------VERLKAKVEEARRLRERAEQESARq 2046
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEkvanmevaLDKASLQFAECQDIIQRQEQESVR- 836
|
810
....*....|....
gi 1920237952 2047 LQLAQEAAQKRLQA 2060
Cdd:pfam15921 837 LKLQHTLDVKELQG 850
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1356-1856 |
1.39e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 68.35 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1356 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-----EAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1430
Cdd:COG3899 741 EEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRhgnppASARAYANLGLLLLGDYEEAYEFGELALALA 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1431 EELQHLRQSSEAEIqAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1510
Cdd:COG3899 821 ERLGDRRLEARALF-NLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1511 RRQVQDETQRKRQAEAELALRVQAEAEAAREkqRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1590
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAA--LALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1591 SEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQ 1670
Cdd:COG3899 978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1671 AEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1750
Cdd:COG3899 1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1751 QREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1830
Cdd:COG3899 1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217
|
490 500
....*....|....*....|....*.
gi 1920237952 1831 AEEDAVRQRAEAERVLAEKLAAISEA 1856
Cdd:COG3899 1218 EAAALLLLLLLAALALAAALLALRLL 1243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2266-2622 |
1.56e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2266 VLRDKDSAQRLLQEEA---EKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRAL---AEKMlkEKMQAVQEATRlKA 2338
Cdd:TIGR02168 149 IIEAKPEERRAIFEEAagiSKYKERRKETERKLERTRENlDRLEDILNELERQLKSLerqAEKA--ERYKELKAELR-EL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2339 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQET---QGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2415
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTaelQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2416 RFRKQAEDIGERLYRtelatqekvmlvqtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL 2495
Cdd:TIGR02168 306 ILRERLANLERQLEE--------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2496 LQEtQALQQSFLSEKDSLLQRERCIEQEKAKLEQLfqdeVAKAQALreeqQRQQQQMQQEKQQLAASMEEARRRQHEAE- 2574
Cdd:TIGR02168 372 SRL-EELEEQLETLRSKVAQLELQIASLNNEIERL----EARLERL----EDRRERLQQEIEELLKKLEEAELKELQAEl 442
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237952 2575 EGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2622
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1692-2066 |
1.90e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1692 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1769
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1770 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAV------------- 1836
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1837 --RQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1914
Cdd:COG4717 265 ggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1915 SELERQKGLVE-DTLRQRRQVEEEILALKGSFEKAAAGKAElelelgRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERR 1993
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 1994 RREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2066
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1423-1612 |
2.10e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.98 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1423 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL--EATERQRGGAEGELQALRARAEEAEAQK 1500
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQkkQAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1501 RQAQEEAERLRRQV-QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1579
Cdd:PRK09510 147 AKAEAEAKRAAAAAkKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|...
gi 1920237952 1580 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHV 1612
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2266-2621 |
2.70e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2266 VLRDKDSAQRLLQEEAEKMKQ-----VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQAVQEA-TRLK 2337
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERykelkAELRELELALLVLRLEELREELEELQEELKEAEEELeeLTAELQELEEKlEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2338 AEAELLQQQKELAQE---QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2414
Cdd:TIGR02168 274 LEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2415 RRFRKQAEdigerlyrtelatqEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKSE-EMQTVRQE 2493
Cdd:TIGR02168 354 ESLEAELE--------------ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARlERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2494 QLLQETQALQQSFLSEKDSLLQRErcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHeA 2573
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAE--LEELEEELEEL-QEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-S 493
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237952 2574 EEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLqHLEEERRAALA 2621
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-SVDEGYEAAIE 540
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
72-168 |
3.74e-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: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 72 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 137
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1920237952 138 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 168
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1692-2438 |
3.77e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1692 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1771
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1772 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1851
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1852 AISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRlleeqaaqhKADIEARLAQLRKAseseLERQKGLVEDTLR-- 1929
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELE--AEIASLERR---------KSNIPARLLALRDA----LAEALGLDEAELPfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1930 -QRRQVEEEILALKGSFEKAaagkaelelelgrIRGTAEDTLRSKEQAEQ--EAARQRQLAAEeerrrreaeerVQKSLA 2006
Cdd:COG4913 464 gELIEVRPEEERWRGAIERV-------------LGGFALTLLVPPEHYAAalRWVNRLHLRGR-----------LVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2007 AEEEAARQRKAALEE--VERLKAKVEEARrlrERAEQESARQLQLAQEAAQKRLQAEEKA--------HAFAVQQKEQEL 2076
Cdd:COG4913 520 RTGLPDPERPRLDPDslAGKLDFKPHPFR---AWLEAELGRRFDYVCVDSPEELRRHPRAitragqvkGNGTRHEKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2077 QQTLQqeqSVLerlrseaeaarraaeeaeaareraereAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEaeqe 2156
Cdd:COG4913 597 RIRSR---YVL---------------------------GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDA---- 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2157 aarraqaeqaaLRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQ 2236
Cdd:COG4913 643 -----------LQERREALQRLAEY-SWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2237 VEEELFSLRvqmEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2316
Cdd:COG4913 711 LKGEIGRLE---KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2317 ALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLeterqrQLEMSAEAER 2395
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVADL------LSKLRRAIRE 861
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 2396 LRLRVAEMSRA----------------QARAEEDARRFRKQAEDIGERLYRTELATQEK 2438
Cdd:COG4913 862 IKERIDPLNDSlkripfgpgrylrleaRPRPDPEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1028-1616 |
4.86e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1028 RECAQRITEQQKAQaevdglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELEltlgkleqvrslsaiylEKLKTISLVI 1106
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELE-----------------ARLESLSESV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1107 RSTQEAEEVLRAHEEQLK-EAQAVPATLPELEATKAALKKLRAQAEaqqpvfdalrDELRGAQEVGERLQQrHGERDVEV 1185
Cdd:PRK04863 575 SEARERRMALRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSG----------EEFEDSQDVTEYMQQ-LLEREREL 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1186 ERWRERVTlllERWQAVLAQTD-VRQRELEQLGRQLRYyresADPLGAWL----------RDAKQRQ----EQIQAVPLA 1250
Cdd:PRK04863 644 TVERDELA---ARKQALDEEIErLSQPGGSEDPRLNAL----AERFGGVLlseiyddvslEDAPYFSalygPARHAIVVP 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1251 NSQAVREQLRQEKALLEDI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK----VQSG 1319
Cdd:PRK04863 717 DLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRAE 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1320 SESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1399
Cdd:PRK04863 795 REELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAD--PEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKE 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1400 EAQGLQR-----------RMQEEVARREEVAVEAQEQKRSIQ---------EELQHLRQSSEAEIQAKARQVEAAE---- 1455
Cdd:PRK04863 873 GLSALNRllprlnlladeTLADRVEEIREQLDEAEEAKRFVQqhgnalaqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqr 952
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1456 --RSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDETQRKRQAEAELALR 1531
Cdd:PRK04863 953 daKQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASLKSS 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1532 VQAEAEAAREKQRALQAL---------EELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQsehaSFAEKTAQ 1602
Cdd:PRK04863 1029 YDAKRQMLQELKQELQDLgvpadsgaeERARARRDELHARLSANRSRRN-----QLEKQLTFCEAEMD----NLTKKLRK 1099
|
650
....*....|....
gi 1920237952 1603 LERTLKEEHVAVVQ 1616
Cdd:PRK04863 1100 LERDYHEMREQVVN 1113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1546-2041 |
5.50e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1546 LQALEELRLQAEEAE---RRLRQAEAERARQVQVALE-TAQRSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEA 1621
Cdd:PRK02224 161 LGKLEEYRERASDARlgvERVLSDQRGSLDQLKAQIEeKEEKDLHERLNGLESELAELDEEIER-YEEQREQARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1622 TRRAQQQAEAERARAEAERELERWQLKANEALRLRLQ-AEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1700
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREElAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1701 AEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1780
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1781 SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE----------------DAVRQRAEAER 1844
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphvETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1845 VLAEKLAAIsEATRLKTEAEIALKEKEAENE-RLRRLAEdeafQRRLLEEQAAQHKADIEA---RLAQLRKAS---ESEL 1917
Cdd:PRK02224 479 ELEAELEDL-EEEVEEVEERLERAEDLVEAEdRIERLEE----RREDLEELIAERRETIEEkreRAEELRERAaelEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1918 ERQKglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELElELGRIRgtaeDTLRSKEQAEQEAARQRQLAAEEERRRREA 1997
Cdd:PRK02224 554 EEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIR----TLLAAIADAEDEIERLREKREALAELNDER 625
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1920237952 1998 EERVQkslaaeeeAARQRKAALEEvERLKAKVEEARRLRERAEQ 2041
Cdd:PRK02224 626 RERLA--------EKRERKRELEA-EFDEARIEEAREDKERAEE 660
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1781-2052 |
5.64e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 65.74 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1781 SKARAEEESRSTSEKSKQRLEAEAGRF-RELAEEAARlralAEEAKRQRQLAEEDAVrqrAEAERVLAEKLAAISEATRL 1859
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREAR----HKKAAEARAAKDKDAV---AAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1860 KTEAEIALKEKEAEnERLRRLAEDEAFQRRLLEEQAAQHKADIEARL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 1937
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1938 ILALKGSFEKAAAGKAELELELgrirgTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2017
Cdd:PRK05035 586 IARAKAKKAAQQAASAEPEEQV-----AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237952 2018 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2052
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1703-2064 |
6.77e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1703 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR--EAAAATQKRRELEAELAKVRAEMEvlla 1780
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1781 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLK 1860
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1861 TEAEIALKEKEAENERLRRL---------------AEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVE 1925
Cdd:COG4717 229 LEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1926 DTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERrrreaeerVQKSL 2005
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--------LAEAG 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2006 AAEEEAARQRKAALEEVERLKAKVEEA-RRLRERAEQESARQLQLAQEAAQKRLQAEEKA 2064
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEELEELEEE 440
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1110-1561 |
7.08e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1110 QEAEEVLRAHEEQLK--EAQAVPATLPELEATKAALKKLRAQAEAQQPVFDAlrDELRGAQEVGERLQQRHGErdvEVER 1187
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA--DELKKAEELKKAEEKKKAE---EAKK 1571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1188 WRERVTLLLERWQavlaqtDVRQRELEQLGRQLRYYRESADPLGAWLRdaKQRQEQIQAvplansqavrEQLRQEKALLE 1267
Cdd:PTZ00121 1572 AEEDKNMALRKAE------EAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKA----------EELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1268 DIERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAKKPkvqsgSESIIQEYVDLRtRYSELSTLTSQYIRF 1347
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEE----LKKAEEENKIKAAEEAKKAEEDKKK-----AEEAKKAEEDEK-KAAEALKKEAEEAKK 1703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1348 ISETLRRMEEEERLAEQQRAEERERLAEVEaalekqrqlaeahaQAKAQAEREaqglqRRMQEEVARREEVAVEAQEQKR 1427
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAE--------------EAKKEAEED-----KKKAEEAKKDEEEKKKIAHLKK 1764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1428 SIQEELQHLRQSSEAEIQAKARqvEAAERSRLRIEEEIRVVRLQLEATerQRGGAEGELQALRARAEEAEAQKRQAqEEA 1507
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELD--EEDEKRRMEVDKKIKDIFDNFANI--IEGGKEGNLVINDSKEMEDSAIKEVA-DSK 1839
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1508 ERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRaLQALEELRLQAEEAER 1561
Cdd:PTZ00121 1840 NMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDL-KEDDEEEIEEADEIEK 1892
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1114-1933 |
8.19e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.75 E-value: 8.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1114 EVLRAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpvfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERvt 1193
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1194 llLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReQLRQEKALLE----DI 1269
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1270 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQY-- 1344
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLqq 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1345 IRFISETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREE 1417
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1418 VAVEAQEQkRSIQEELQHLRQSSEAE----------IQAKARQVEAAERSRLRIEEEIRVVRLQLEATErQRGGAEGE-L 1486
Cdd:PRK04863 598 LAARAPAW-LAAQDALARLREQSGEEfedsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGSEDPrL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1487 QALRAR-----------------AEEAEA---QKRQA--QEEAERLRRQVQDET-------------QRKRQA-----EA 1526
Cdd:PRK04863 676 NALAERfggvllseiyddvsledAPYFSAlygPARHAivVPDLSDAAEQLAGLEdcpedlyliegdpDSFDDSvfsveEL 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1527 ELALRVQ-AEAE--------------AAREKQralqaLEELRLQAEEAERRLRQAEAERaRQVQVALETAQR-------- 1583
Cdd:PRK04863 756 EKAVVVKiADRQwrysrfpevplfgrAAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAFSRfigshlav 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1584 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVA 1663
Cdd:PRK04863 830 AFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEA 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1664 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--------------LAEGTAQQRLAAEQEL-IR 1728
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahFSYEDAAEMLAKNSDLnEK 989
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1729 LRAETEQGEQQRQLLEEEL--------------ARLQREAAAATQKRRELEAELAK--VRAEMEVLLASKARAEE----- 1787
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGAEERARARRDElharl 1069
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1788 ----ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAVRQRAEAERVLAEKLAAIS--EAT 1857
Cdd:PRK04863 1070 sanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRLHRRELAYLSadELR 1148
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1858 RLKTEAEIALKEKEAENERLR---RLAEDEAFQ----------RRLLEEQAAQhkaDIeARLAQLRKASEsELERQKGLV 1924
Cdd:PRK04863 1149 SMSDKALGALRLAVADNEHLRdvlRLSEDPKRPerkvqfyiavYQHLRERIRQ---DI-IRTDDPVEAIE-QMEIELSRL 1223
|
....*....
gi 1920237952 1925 EDTLRQRRQ 1933
Cdd:PRK04863 1224 TEELTSREQ 1232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2279-2700 |
9.10e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2279 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK-AEAELLQQQKELAQ--EQAR 2355
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARkaEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2356 RLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRlRVAEMSRAQ-ARAEEDARRF---RKQAEDIGERLYRT 2431
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEdAKKAEAVKKAeeaKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2432 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQllqlKSEEMQTVrqEQLLQETQALQQSFLSEKD 2511
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK----KAEEKKKA--DEAKKKAEEAKKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2512 SLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME-----------EARRRQHEAE---EGV 2577
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkadaakkkaEEKKKADEAKkkaEED 1403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2578 RRQQEELQRLAQQQQQQEKLL--AEENQRLRERLQHLEEERRAalarseEIAPSRAAAARALPNGQDAADGPAAAAEPEH 2655
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKKA------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1920237952 2656 AFDGLRRKVPAQRLQEVGVLSAEELQQLAQGRTTVAELAQREDVR 2700
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1218-1888 |
9.77e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1218 RQLRYYRESADPLGAWLRDAKQRQEQIQAvpLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDY---- 1293
Cdd:PRK03918 111 SSVREWVERLIPYHVFLNAIYIRQGEIDA--ILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikrt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1294 ---ELQLVTYKAQLEPVASPAKK-----PKVQSGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQ 1365
Cdd:PRK03918 189 eniEELIKEKEKELEEVLREINEisselPELREELEKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEER 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1366 RAEERERLAEVE---AALEKQRQLAEAHAQAK-----------------AQAEREAQGLQRRMQEEVARREEVAvEAQEQ 1425
Cdd:PRK03918 268 IEELKKEIEELEekvKELKELKEKAEEYIKLSefyeeyldelreiekrlSRLEEEINGIEERIKELEEKEERLE-ELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1426 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1505
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1506 EAERLRRQVQDETQRKRQAEAELALRVQAEAEAarEKQRALQALEELRLQAEEAERRLRQAEAERARQ--VQVALETAQ- 1582
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEq 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1583 -RSAEAELQSEHASFAEKTAQLERTLKEEhvaVVQLREEATRRAQqqaeaeraraeaerelerwQLKANEALRLRLQAEE 1661
Cdd:PRK03918 505 lKELEEKLKKYNLEELEKKAEEYEKLKEK---LIKLKGEIKSLKK-------------------ELEKLEELKKKLAELE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1662 VAQQKsltqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLaEGTAQQRLAAEQELIRLRaeteQGEQQRQ 1741
Cdd:PRK03918 563 KKLDE----------------------LEEELAELLKELEELGFESVEEL-EERLKELEPFYNEYLELK----DAEKELE 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1742 LLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLasKARAEEESRSTSEKskqrleaeagrFRELAEEAARLRALA 1821
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREE-----------YLELSRELAGLRAEL 682
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1822 EEAKRQRQLAEEDAvrqraeaeRVLAEKLAAISEATRLKTEAEIALKEKEAENERLRR---LAEDEAFQR 1888
Cdd:PRK03918 683 EELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERVEELREKVKKykaLLKERALSK 744
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
64-171 |
1.13e-09 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 59.14 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 64 ADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDYLRH 139
Cdd:cd21222 10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMED 89
|
90 100 110
....*....|....*....|....*....|..
gi 1920237952 140 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 171
Cdd:cd21222 90 AGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1523-1890 |
1.32e-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: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1523 QAEAELALRVQAEAEAAREKQRALQALEELrlqAEEAERRLRQAEAERARQvqvaletaqrsaeAELQSEHASFAEktaq 1602
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEK---AREVERRRKLEEAEKARQ-------------AEMDRQAAIYAE---- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1603 lertlkEEHVAVVQLREeatrraqqqaeaeraraeaereLERWQLKANEALRLRLQAEEVAQQksLTQAEAEKQKEEAER 1682
Cdd:pfam17380 339 ------QERMAMERERE----------------------LERIRQEERKRELERIRQEEIAME--ISRMRELERLQMERQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1683 EARRRGKAEEQAVRQRELAEQE-----LEKQRQLAEGTAQQRLAAEQELIRLraETEQGEQQRQLLEEELARLQReaaaa 1757
Cdd:pfam17380 389 QKNERVRQELEAARKVKILEEErqrkiQQQKVEMEQIRAEQEEARQREVRRL--EEERAREMERVRLEEQERQQQ----- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1758 TQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAvR 1837
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER-R 535
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1838 QRAEAER---VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRL 1890
Cdd:pfam17380 536 REAEEERrkqQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
961-1610 |
1.48e-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: 64.70 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 961 DRLQAEREYgscSRHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRITEQQKA 1040
Cdd:TIGR02169 201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1041 QAEVDGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKL--------KTISLVIRS 1108
Cdd:TIGR02169 257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELedaeerlaKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1109 TQEAEEVLRAHEEQLKEAQAVPAtlpELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGE-------- 1180
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkreldrl 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1181 ------RDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQ--------- 1245
Cdd:TIGR02169 412 qeelqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEkelsklqre 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1246 -----AVPLANSQAVREQLRQEKALLEDI--------------ERHGEKVE-------------------ECQRFAKQY- 1286
Cdd:TIGR02169 492 laeaeAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgERYATAIEvaagnrlnnvvveddavakEAIELLKRRk 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1287 --------INAIK---------------DYELQLVTYKAQLEPVASPAKKPKV-----QSGSESIIQ-----------EY 1327
Cdd:TIGR02169 572 agratflpLNKMRderrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGDTLvvediEAARRLMGKyrmvtlegelfEK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1328 VDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRR 1407
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1408 MQEEVARREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAAERSRLRIE-----EEIRVVRLQLEATERQRGGA 1482
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSEL-KELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1483 EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK---RQAEAELALRVQAEAEAAREKQRALQALEE----LRLQ 1555
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiEKEIENLNGKKEELEEELEELEAALRDLESrlgdLKKE 890
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 1556 AEEAERRLRQAEaERARQVQVALETAqRSAEAELQSEHASFAEKTAQLERTLKEE 1610
Cdd:TIGR02169 891 RDELEAQLRELE-RKIEELEAQIEKK-RKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1255-1845 |
2.11e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1255 VREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDlrtRY 1334
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE---EY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1335 SELSTLTSQYIrfisETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLaeahaqakaqaeREAQGLQRRMQEEVAR 1414
Cdd:PRK03918 296 IKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELE---EKEERL------------EELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1415 REEvAVEAQEQKRSIQEELQHLRQS-SEAEIQAKARQVEAAERSRLRIEEEIRVV---RLQLEATERQRGGAEGELQALR 1490
Cdd:PRK03918 357 LEE-RHELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1491 ARA---------EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvqaEAEAAREKQRALQALEELRLQAEEAER 1561
Cdd:PRK03918 436 GKCpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEKVLKKESELIKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1562 RLRQAEAERarqvqvaLETAQRSAEaELQSEHASFAEKTAQLERTLKEEHvavvQLREEATRRAQQQAEAERARAEAERE 1641
Cdd:PRK03918 511 KLKKYNLEE-------LEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1642 LERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLA 1721
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1722 AEQELIRLRAETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlaSKARAEEESrstSEKSKQRLE 1801
Cdd:PRK03918 657 SEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER--EKAKKELEK---LEKALERVE 724
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1802 AEAGRFRELAEEAARlRALAEEAKRQRQLAEE------DAVRQRAEAERV 1845
Cdd:PRK03918 725 ELREKVKKYKALLKE-RALSKVGEIASEIFEEltegkySGVRVKAEENKV 773
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1708-1914 |
2.25e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1708 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEE 1787
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1788 ESRSTSEKSKQRLEA--------------EAGRFRELAEEAARLRALAEEAKRQ-----RQLAEEDAVRQRAEAERvlAE 1848
Cdd:COG4942 98 ELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQaeelrADLAELAALRAELEAER--AE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1849 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASE 1914
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1362-1560 |
2.33e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.90 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1362 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARReevavEAQEQKrsiQEELQHLRQSS 1440
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQ-----AALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1441 EAEIQAKARQVEAAERSRlRIEEEIRvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDETQR 1520
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237952 1521 KRQAEAELAL-RVQAEAEAAREKQRALQALEELRLQAEEAE 1560
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1107-1303 |
2.68e-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: 60.54 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1107 RSTQEAEEVLRAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPVFDALrdelrgaQEVGERLQQRHGERDVEVe 1186
Cdd:cd00176 7 RDADELEAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1187 rwRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLRDAKQRQEQIQavPLANSQAVREQLRQEKALL 1266
Cdd:cd00176 78 --QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELE 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237952 1267 EDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1303
Cdd:cd00176 153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
186-288 |
2.81e-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: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 186 TAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 264
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1920237952 265 PEDVDVPQPDEKSIITYVSSLYDA 288
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2168-2626 |
2.96e-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: 63.83 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILdeelqRLKAEVTEAARQRGQVEEELFSLRVQ 2247
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2248 MEELGKLKARIEA--ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---RLRQLAEE---DLAQQRALA 2319
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2320 EKMLKEKMQAVQEATRLKAEAELLQQ------QKELAQEQARRLQEDKEQMAQQLAQETQGFQK-------------TLE 2380
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqslkereqqlqTKE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2381 TERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLR 2460
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2461 EAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQRERCIE---------QEKAKLEQLF 2531
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI--TVRLQDLTEKLSEAEDMLACEQHALLrklqpeqdlQDVRLHLQQC 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2532 QDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEAR---------------------------------RRQHEAEEGVR 2578
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmqsekeqltywkemlaqcqtllRELETHIEEYD 717
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1920237952 2579 RQQEELQRLAQQQQQQeklLAEENQRLRERLQHLEEERRAALARSEEI 2626
Cdd:TIGR00618 718 REFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTVLKARTEA 762
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2265-2616 |
3.00e-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: 63.60 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2265 LVLRDKDSAQRLLQEEAEKM-----KQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaE 2339
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMeqerlRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------Q 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2340 AELLQQQKELAQEQARRL----QEDKEQMAQQLAQETQGFQKTLETERQR-QLEMSAEAERLRLRVAEMSRAQARAEEDA 2414
Cdd:pfam17380 333 AAIYAEQERMAMERERELerirQEERKRELERIRQEEIAMEISRMRELERlQMERQQKNERVRQELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2415 RRFRKQAEDIGERLYRTELATQEKVmlvQTLETQRQqsdRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQ 2494
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREV---RRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2495 LLQETQalqqsflsekdsllqRERCIEQEKAKLEQLFQDEVAKAQALREEqqrqqqqmqqekqqlaasMEEarRRQHEAE 2574
Cdd:pfam17380 487 KRAEEQ---------------RRKILEKELEERKQAMIEEERKRKLLEKE------------------MEE--RQKAIYE 531
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1920237952 2575 EGVRRQQEELQRlaqqqqqqEKLLAEENQRLRERLQHLEEER 2616
Cdd:pfam17380 532 EERRREAEEERR--------KQQEMEERRRIQEQMRKATEER 565
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1731-2320 |
3.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1731 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAG--- 1805
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRele 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1806 --------RFRELAEEAARLRALAEEAKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRlktEAEIALKEKEAENERL 1877
Cdd:PRK03918 266 erieelkkEIEELEEKVKELKELKEKAEEYIKLSEF--YEEYLDELREIEKRLSRLEEEIN---GIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1878 RRLAEDEAFQRRLLEEQAAQHKA--DIEARLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEILAL---KGSFEKA 1948
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKItarIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1949 AAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLaaeeerrrrEAEERVQKSLAAEEEAARQRKAALEEVERLKAK 2028
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYT---------AELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2029 VEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAeeaeaa 2107
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE------ 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2108 reraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQ 2187
Cdd:PRK03918 563 ------------KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2188 ALRQKAQVEQELTALRLQLEETdhQKSILDEELQRLKAEVTEaarqrgqVEEELFSLRVQMEELGKLKARIEAEnralvL 2267
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKT-----L 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 2268 RDkdsaqrlLQEEAEKMKQVAEEAARLSVAAQEAARLRQ--LAEEDLAQQRALAE 2320
Cdd:PRK03918 697 EK-------LKEELEEREKAKKELEKLEKALERVEELREkvKKYKALLKERALSK 744
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1210-1588 |
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 1920237952 1210 QRELEQLGRQLRYYRESADplgawlrDAKQRQEQIQA-VPLANSQAvREQLRQekaLLEDIERHGEKVEECQRFAKQYIN 1288
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLD-------QLKEQLQLLNKlLPQANLLA-DETLAD---RLEELREELDAAQEAQAFIQQHGK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1289 AIkdyelqlvtykAQLEPVASPAKKPKVQSgsESIIQEYVDLRTRYSELStltsQYIRFISETLRRM------EEEERLA 1362
Cdd:COG3096 918 AL-----------AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRLK----QQIFALSEVVQRRphfsyeDAVGLLG 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1363 EQQRAEE--RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEevarreevaveAQEQKRSIQEELQHLrqss 1440
Cdd:COG3096 981 ENSDLNEklRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL---- 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1441 eaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQ 1513
Cdd:COG3096 1046 --GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRL 1123
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 1514 VQDETQRKRQAEAELalrvqaeaeaarekqrALQALEELRLQAEEAERRLRQAEAERArQVQVALETAQRSAEAE 1588
Cdd:COG3096 1124 ARDNDVERRLHRREL----------------AYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEDPRRPE 1181
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1124-1545 |
4.01e-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: 63.22 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1124 KEAQAVPATLPELEA-----------------TKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERdVEVE 1186
Cdd:pfam17380 221 KEVQGMPHTLAPYEKmerrkesfnlaedvttmTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEK-MEQE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1187 RWR---ERVTLLLERWQAVLAQTDVRQRELEqlgRQLRYYRESAdplgawlRDAKQRQEQIQAVPLANSQAVREQLRQEK 1263
Cdd:pfam17380 300 RLRqekEEKAREVERRRKLEEAEKARQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEERKRELERIRQEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1264 ALLEDierhgEKVEECQRFakqyinaikdyelqlvtykaQLEPvaspakkpkvQSGSESIIQEYVDLRtrysELSTLTSQ 1343
Cdd:pfam17380 370 IAMEI-----SRMRELERL--------------------QMER----------QQKNERVRQELEAAR----KVKILEEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1344 YIRFISETLRRMEEEERLAEQQRAEERERLAEveaalEKQRQLAEAHAQakaQAEREAQGLQRRMQEEVARREEVAVEAQ 1423
Cdd:pfam17380 411 RQRKIQQQKVEMEQIRAEQEEARQREVRRLEE-----ERAREMERVRLE---EQERQQQVERLRQQEEERKRKKLELEKE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1424 EQKRSIQEELQhlRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleatERQRGGAEGElqalRARAEEAEAQKRQA 1503
Cdd:pfam17380 483 KRDRKRAEEQR--RKILEKELEERKQAMIEEERKRKLLEKEME---------ERQKAIYEEE----RRREAEEERRKQQE 547
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1920237952 1504 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRA 1545
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
181-283 |
4.38e-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: 57.10 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 181 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 259
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 1920237952 260 TRLLDPEDVDVPQPDEKSIITYVS 283
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1387-1610 |
4.45e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1387 AEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEE 1463
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1464 EIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1543
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1544 RALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQSEHASFAEKTAQLERTLKEE 1610
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1504-1985 |
4.56e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1504 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQR 1583
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1584 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREeatrraqqqaeaeraraeaerelerwqlKANEALRLRLQAEEVA 1663
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEE----------------------------LEAELAELQEELEELL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1664 QQKSLTQAeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1743
Cdd:COG4717 184 EQLSLATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1744 EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEE 1823
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1824 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKAD 1901
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1902 IEARLAQLRKASESELERQKGLVEDTLRQR-RQVEEEILALKGSFEKAAAGKAELELELGRIRGtaEDTLRSKEQAEQEA 1980
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEEL 481
|
....*
gi 1920237952 1981 ARQRQ 1985
Cdd:COG4717 482 KAELR 486
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4398-4436 |
4.80e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.64 E-value: 4.80e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 4398 FLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTAQKL 4436
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1700-1931 |
4.86e-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: 61.40 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1700 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAelakvraemevll 1779
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1780 askARAEEESRSTSEKSKQRLEAEAGRfrelAEEAARLRALAEEAKRQrqlAEEDAVRQRAEAervlAEKLAaisEATRL 1859
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1860 KTEAEiALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIE----ARLAQLRKASESELERQKGLVEDTLRQR 1931
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
71-170 |
5.44e-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: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 71 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 145
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILH 170
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4320-4357 |
6.89e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 6.89e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1920237952 4320 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4357
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1831-2364 |
7.82e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1831 AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 1910
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1911 KASESELERQKGLVEDT--LRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAA 1988
Cdd:PRK03918 266 ERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1989 EEERrrreaeerVQKSLAAEEEAArqrkaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfA 2068
Cdd:PRK03918 346 KLKE--------LEKRLEELEERH-------ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-K 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2069 VQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEReaaqsRRQVEEAERLKQSAEEQAQAQAQAQAAAEK 2148
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELL-----EEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2149 LRKEAEQEAARraqaeqaaLRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA--- 2225
Cdd:PRK03918 485 LEKVLKKESEL--------IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkk 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2226 EVTEAARQRGQVEEELFSLRVQMEELG---------KLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLS 2295
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGfesveeleeRLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAfEELA 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2296 VAAQEAARLR-QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2364
Cdd:PRK03918 637 ETEKRLEELRkELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2175-2625 |
7.86e-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: 62.29 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2175 DAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKaevtEAARQRGQVEEELFSLRVQMEELGKL 2254
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2255 KARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEA-ARLSVAAQEAARLRQLA------EEDLAQQRALAEKMLKEKM 2327
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIhTELQSKMRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2328 QAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLaqetQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQ 2407
Cdd:TIGR00618 356 HIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKL----QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2408 ARAEEDARRFRKQAEDIGER----------LYRTELATQEKVMLVQTLETQRQQSDR-----DAERLREAIAELEHEKDK 2472
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTaqceklekihLQESAQSLKEREQQLQTKEQIHLQETRkkavvLARLLELQEEPCPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2473 LKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQM 2552
Cdd:TIGR00618 511 IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 2553 QQEKQQLAASMEEARRR------QHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2625
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEdmlaceQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1378-1602 |
7.96e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.36 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1378 AALEKQRQLAEAHAQAKAQAEREAQGLQRrmQEEVarREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAK---ARQVEAA 1454
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKqaaLKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1455 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDETQRKRQAEAELALRVQ 1533
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1534 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1602
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1352-1572 |
8.46e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1352 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1431
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1432 ---ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1508
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1509 RLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1572
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1358-1572 |
1.15e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 60.24 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1358 EERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSiQEELQHLR 1437
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQK-QAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1438 QSSEAEIQAKA-RQVEAAERSRLRIEEEirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE----AERLRR 1512
Cdd:TIGR02794 128 QAAEAKAKAEAeAERKAKEEAAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKA 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1513 QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERAR 1572
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1106-2043 |
1.22e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1106 IRSTQEAEEVLRAHEEQLKEAQAvpatlpeleatkaALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQ--RHGERdv 1183
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQY-------------RLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK-- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1184 eVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVReqlrqek 1263
Cdd:COG3096 349 -IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1264 ALledierhgEKVEECQRFAKQYINAIKDYelqLVTYKAQLEpvaspakkpkvqsgseSIIQEYVDLRTRYSELSTLTSQ 1343
Cdd:COG3096 421 AL--------EKARALCGLPDLTPENAEDY---LAAFRAKEQ----------------QATEEVLELEQKLSVADAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1344 YIRFIsETLRRMEEE-ERLAEQQRAEERER-------LAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARR 1415
Cdd:COG3096 474 FEKAY-ELVCKIAGEvERSQAWQTARELLRryrsqqaLAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1416 EEVAVEAQEQKRSIQEELQHLRQSSEAEIQakarqveaaersrlrieeeirvvrlqleaTERQRGGAEGELQALRARAEE 1495
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSE-----------------------------LRQQLEQLRARIKELAARAPA 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1496 AeaqkRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAeeaeRRLRQAE-AERARQV 1574
Cdd:COG3096 604 W----LAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQI----ERLSQPGgAEDPRLL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1575 Q----------------VALETAQR-------SAEAELQSEHASFAEKTAQLERTLkeEHVAVVQLREEATRRAQQQAEA 1631
Cdd:COG3096 676 AlaerlggvllseiyddVTLEDAPYfsalygpARHAIVVPDLSAVKEQLAGLEDCP--EDLYLIEGDPDSFDDSVFDAEE 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1632 ERARAEAERELERWQL-------------KANEALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQR 1698
Cdd:COG3096 754 LEDAVVVKLSDRQWRYsrfpevplfgraaREKRLEELRAERDELAEQYA------------------------KASFDVQ 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1699 ELaeQELEKQ-RQLAEGTAQQRLAAEQElirlrAETEQGEQQRQLLEEELARL----QREAAAATQKRRELEAeLAKVRA 1773
Cdd:COG3096 810 KL--QRLHQAfSQFVGGHLAVAFAPDPE-----AELAALRQRRSELERELAQHraqeQQLRQQLDQLKEQLQL-LNKLLP 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1774 EMEVL----LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAKRQRQL---AEEDAVRQRAEAER 1844
Cdd:COG3096 882 QANLLadetLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpEQFEQLQADYLqakEQQRRLKQQIFALS 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1845 VLAEKLAAISEAtrlktEAEIALKEKEAENERLR---RLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 1921
Cdd:COG3096 962 EVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1922 GLvedtlrQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG--TAEDTLRSKEQAEQEAARQRqlaaeeerrrreaEE 1999
Cdd:COG3096 1037 EL------EQELEELGVQADAEAEERARIRRDELHEELSQNRSrrSQLEKQLTRCEAEMDSLQKR-------------LR 1097
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 1920237952 2000 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRL--RERAEQES 2043
Cdd:COG3096 1098 KAERDYKQEREQVVQAKAGWCAVLRLARDNDVERRLhrRELAYLSA 1143
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
181-288 |
1.32e-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: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 181 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 259
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1920237952 260 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 288
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2168-2624 |
1.45e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRGQVEEELF 2242
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2243 SLRVQMEELG-----KLKARIEAENRALVLRDKDSAQrlLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2316
Cdd:COG4913 327 ELEAQIRGNGgdrleQLEREIERLERELEERERRRAR--LEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2317 ALAEKMLKEKMQAVQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM------------------------ 2364
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervl 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2365 ---AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyRTELATQEKVML 2441
Cdd:COG4913 485 ggfALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWL-EAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2442 VQTLE-------------------TQRQQSDRDAERL--------REAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQ-- 2492
Cdd:COG4913 564 VDSPEelrrhpraitragqvkgngTRHEKDDRRRIRSryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDal 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2493 EQLLQETQALQQSFLSEKDsLLQRERCIEQEKAKLEQL--FQDEVAKAQALREEqqrqqqqmqqekqqLAASMEEARRRQ 2570
Cdd:COG4913 644 QERREALQRLAEYSWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEE--------------LEAELEELEEEL 708
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 2571 HEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSE 2624
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1389-1848 |
1.47e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.57 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1389 AHAQAKAQAEREAQGLQRRMQEEVARreeVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVV 1468
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLA---LAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1469 RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQA 1548
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1549 LEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1628
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1629 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1708
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1709 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1788
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1789 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1848
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1501-2021 |
1.88e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1501 RQAQEEAERLRRQVQD----ETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARqvqv 1576
Cdd:COG4913 238 ERAHEALEDAREQIELlepiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER---- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1577 aLETAQRSAEAELQSEHASFAEKTAQLERTLKEEhvavvqlreeatrraqqqaeaeraraeaereLERWQLKANEALRLR 1656
Cdd:COG4913 314 -LEARLDALREELDELEAQIRGNGGDRLEQLERE-------------------------------IERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1657 LQAEEVAQQKSLTQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1736
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1737 EQQRQLLEEELARLQREAAAATQ-KRRELE--AELAKVRAE-------MEVLLASKAR---------------------- 1784
Cdd:COG4913 432 ERRKSNIPARLLALRDALAEALGlDEAELPfvGELIEVRPEeerwrgaIERVLGGFALtllvppehyaaalrwvnrlhlr 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1785 ------------AEEESRSTSEKS-KQRLEAEAGRFR-----ELAEEAARLRALAEEA-----------------KRQRQ 1829
Cdd:COG4913 512 grlvyervrtglPDPERPRLDPDSlAGKLDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgnGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1830 LAEEDAVRQR----AEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEE-----QAAQHKA 1900
Cdd:COG4913 592 KDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvaSAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1901 DIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRirgtAEDTLRSKEQAEQEA 1980
Cdd:COG4913 672 ELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE----LQDRLEAAEDLARLE 746
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1920237952 1981 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2021
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1373-1785 |
2.01e-08 |
|
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: 61.03 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1373 LAEVEAALEKQRQLAEAHAQAkaqaeREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE----------- 1441
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1442 --------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1513
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1514 VQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEH 1593
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1594 ASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEA 1673
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1674 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1753
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 1920237952 1754 AAAATQKRRELEAELAKVRAEMEVLLASKARA 1785
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
73-167 |
2.82e-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: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 73 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 144
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1920237952 145 VNIRNDDIADGNPKLTLGLIWTI 167
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
533-722 |
3.71e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 57.07 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 533 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQLSPATRGAY---RDCLGRLD 609
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 610 LQYAKLLSSSKARLRSLE---SLHGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEI 686
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1920237952 687 QSTGDRLLREDHP-ARPTAESFQAALQTQWSWMLQLC 722
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1111-1466 |
4.68e-08 |
|
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: 59.69 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1111 EAEEVLRAHEEQLKEAQAVPATL-PELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWR 1189
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1190 ERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLrDAKQRQEQIQAVPLANSQAVREQLRQEKALLED- 1268
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERr 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1269 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSELstltsqyirfi 1348
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELE---------ALLNERASLEEALALLRSELEEL----------- 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1349 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ------------------LAEAHAQAKAQAEREAQGLQRRMQE 1410
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerlseeysltleEAEALENKIEDDEEEARRRLKRLEN 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1411 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAErsrlRIEEEIR 1466
Cdd:TIGR02168 980 KIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE----EIDREAR 1031
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1701-1888 |
4.76e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1701 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA--AATQKRRELEAELAKVRAEMEVL 1778
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAKAAAAAKAKAEAEAKRA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1779 LASKARAEEESrstseksKQRLEAEAgrfRELAEEAARLRALAEEAKrqrQLAEEDAVRQRAEAERVlAEKLAAISEATR 1858
Cdd:PRK09510 157 AAAAKKAAAEA-------KKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAE 222
|
170 180 190
....*....|....*....|....*....|
gi 1920237952 1859 LKTEAEIALKEKEAENERLRRLAEDEAFQR 1888
Cdd:PRK09510 223 AKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2186-2626 |
5.39e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.47 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2186 EQALRQKAQVEQELTALRLQL-EETDHQKSILDEELQRLKAEVTEAARQRGQV---EEELFSLRVQMEELGKLKARIEAE 2261
Cdd:pfam12128 404 EARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2262 NRAlvlrdkdsaQRLLQEEAEKMKQVAEEAARlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAE 2341
Cdd:pfam12128 484 NAE---------VERLQSELRQARKRRDQASE---------ALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAP 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2342 LLQQQ--KELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA-------QARAEE 2412
Cdd:pfam12128 546 DWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsarekQAAAEE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2413 DARRFRKQAE--DIGERLYRTELaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTV 2490
Cdd:pfam12128 626 QLVQANGELEkaSREETFARTAL-KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2491 RQEQLLQETQALQQSFL---SEKDSLLQR-----ERCIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQMQQEKQQLAAS 2562
Cdd:pfam12128 705 QKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRSGAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREIRTLERK 783
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 2563 MEEARRRQHEAEEGVRRQQE----ELQRLAQQQQQQEKLLAEENQRL-------RERLQHLEEERRAALARSEEI 2626
Cdd:pfam12128 784 IERIAVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQLarliadtKLRRAKLEMERKASEKQQVRL 858
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1423-1963 |
5.59e-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: 59.27 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1423 QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1500
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1501 RQAQEEAERLRRQVQDETQRKRQAEAELALrVQAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEAERAr 1572
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1573 QVQVALETAQRS-AEAELQSEHASFA--EKTAQLERTLKEEHVAVVQLREEATRRAQQQAeaeraraeaerelerwQLKA 1649
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1650 NEALRLRLQAEEVAQQKSltqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQEL 1726
Cdd:pfam05701 255 ASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1727 IRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagr 1806
Cdd:pfam05701 319 LRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1807 frelAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEA--ENERLRRLAEDE 1884
Cdd:pfam05701 390 ----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1885 AFQR----------------RLLEEQAaqhKADIEARLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKGSFEKA 1948
Cdd:pfam05701 466 DSPRgvtlsleeyyelskraHEAEELA---NKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKA 541
|
570
....*....|....*
gi 1920237952 1949 AAGKAELELELGRIR 1963
Cdd:pfam05701 542 KEGKLAAEQELRKWR 556
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1507-1966 |
6.24e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 59.26 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1507 AERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAleelRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1586
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1587 AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQK 1666
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1667 SLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1746
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1747 LARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1826
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1827 QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARL 1906
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1907 AQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTA 1966
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2177-2625 |
6.41e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2177 EMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEE------ELFSLRVQMEE 2250
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiklseFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2251 LGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2328
Cdd:PRK03918 312 IEKRLSRLEEEINGIeeRIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2329 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQ-----RQLEMSAEAERLRLRVAEM 2403
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2404 SRAQ---ARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKL-KQEAQL 2479
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2480 LQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRER-----CIEQEKAKLEQL--FQDEVAKAQALREEQQRQQQQM 2552
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELepFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 2553 QQEKQQLAASMEEARRRQHEAEEgVRRQQEELQRlaqqqqqqeKLLAEENQRLRERLQHLEEERRAALARSEE 2625
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEE-LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
190-285 |
7.21e-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: 54.23 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 190 KLLL-WSQrMVEGCQGLRCDNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNL-----------------------EN 245
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 246 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 285
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1664-1859 |
7.43e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.28 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1664 QQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1743
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1744 EEELARLQREAAAATQKRRELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1823
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237952 1824 AKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRL 1859
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2218-2486 |
7.97e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2218 EELQRLKAEVTEAARQRGQVE------EELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkQVAEEA 2291
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2292 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQE 2371
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2372 TQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedigerlyrtelatqekvmlVQTLETQRQQ 2451
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE---------------------IASLERRKSN 437
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237952 2452 SDRDAERLREAIAE-LEHEKDKLKQEAQLLQLKSEE 2486
Cdd:COG4913 438 IPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1491-1942 |
9.93e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1491 ARAEEAEAQKRQAQEEAERLRRQVQD-ETQRKRQAEAELAL----RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQ 1565
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELeelrEELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1566 AEAERARQVQV-----ALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEaer 1640
Cdd:COG4717 151 LEERLEELRELeeeleELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE--- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1641 elerwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAvrqrELAEQELEKQRQLAEGTAQQRL 1720
Cdd:COG4717 228 -----ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA----GVLFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1721 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRstsEKSKQRL 1800
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---EQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1801 EAEAGrfrelAEEAARLRALAEEAKRQRQLAEEdavrqRAEAERVLAEKLAAISEATRLKTEAEiaLKEKEAENERLRRL 1880
Cdd:COG4717 376 LAEAG-----VEDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 1881 AEDEafqrrllEEQAAQHKADIEARLAQLrkASESELERQKGLVEDTLRQRRQVEEEILALK 1942
Cdd:COG4717 444 LEEE-------LEELREELAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1411-1576 |
1.02e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 58.61 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1411 EVARR----EEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegel 1486
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1487 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEtqrkrqaeaelalrvQAEAEAAREKQRALQALEElRLQAEEAERRLRQ 1565
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 1920237952 1566 AEAERARQVQV 1576
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1442-1594 |
1.05e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.96 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1442 AEIQAKARQVEA-AERsrlriEEEIRVVRLQLEATERQrggAEGELQALRARAEEAEAQKRQAQEEAERlrrqvqdETQR 1520
Cdd:COG2268 195 AEIIRDARIAEAeAER-----ETEIAIAQANREAEEAE---LEQEREIETARIAEAEAELAKKKAEERR-------EAET 259
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 1521 KRqAEAELALRVQaEAEAAREKQRALQALE---ELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHA 1594
Cdd:COG2268 260 AR-AEAEAAYEIA-EANAEREVQRQLEIAErerEIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRA 334
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4051-4087 |
1.14e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.56 E-value: 1.14e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1920237952 4051 IRLLEAQIATGGIIDPEESHRLPVDVAYQRGLFDEEM 4087
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1077-1525 |
1.43e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1077 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKA-------ALKKLRAQ 1149
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAelaelpeRLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1150 AEAQQPVFDALRDELRGAQEVGERLQQrhgERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADP 1229
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1230 LGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVeecqrfakQYINAIKDYELQLVTYKAQLEPVAS 1309
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV--------LFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1310 PAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRfiseTLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA 1389
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELL----ELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1390 HAQAKAQAEREAQGLQRRmQEEVARREEVAVEAQEQKRSIQEELQHLRQSS-EAEIQAKARQVEAAERSRLRIEEEIRVV 1468
Cdd:COG4717 380 GVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 1469 RLQLEATERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDETQRKRQAE 1525
Cdd:COG4717 459 EAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1350-1610 |
1.48e-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: 56.85 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1350 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSI 1429
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1430 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1509
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1510 LR-RQVQDETQRK-RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1587
Cdd:pfam13868 206 LRaKLYQEEQERKeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR 285
|
250 260
....*....|....*....|...
gi 1920237952 1588 ELQSEHASFAEKTAQLERTLKEE 1610
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAA 308
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1058-1620 |
1.58e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1058 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEaqaVPATLPELE 1137
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1138 ATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLqqrhgerdvevERWRERvtllLERWQAVLAQTDVRQRELEQLG 1217
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL-----------SRLEEE----INGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1218 RQLRYYRESADPLGAWLR---DAKQRQEQIqavplansqavrEQLRQEKALL--EDIERHGEKVEECQRFAKQYINAIKD 1292
Cdd:PRK03918 345 KKLKELEKRLEELEERHElyeEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1293 YELQLVTYKAQLEPVASPAKKPKVQS---GSESIIQEYVDLRTRYSElstltsqYIRFISETLRRMEEEERlaeqqraEE 1369
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1370 RERLAEVEAALEKQRQLAEAHAQAKaqaereaqglQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1449
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAE----------QLKELEE--KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1450 QVEAAERsrlrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1529
Cdd:PRK03918 547 ELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1530 lRVQAEAEAAREK-QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERtLK 1608
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK-LK 700
|
570
....*....|..
gi 1920237952 1609 EEHVAVVQLREE 1620
Cdd:PRK03918 701 EELEEREKAKKE 712
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1358-1985 |
2.12e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.50 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1358 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAQGLQRRMQEEVARREEV 1418
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1419 AVEAQEQKRSIQEELQHLRQ-SSEAEIQAKARQVEAAERSRL----RIEEEIRVVRLQLEATERQRGGAEGELQALRARa 1493
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGWRAQFsqqtSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1494 EEAEAQKRQAQEEAER-----LRRQVQDETQRKRQAEAelalrvqAEAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1568
Cdd:PRK10246 410 EVAAALAQHAEQRPLRqrlvaLHGQIVPQQKRLAQLQV-------AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1569 ERARQVQVALETAQRsaeAELQS----------EHASFAEKTAqLERTlkeehvaVVQLREEATRRAQQQAeaeraraea 1638
Cdd:PRK10246 483 ICEQEARIKDLEAQR---AQLQAgqpcplcgstSHPAVEAYQA-LEPG-------VNQSRLDALEKEVKKL--------- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1639 erelerwqlkANEALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQ 1718
Cdd:PRK10246 543 ----------GEEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1719 RLAAEQELIRLRAETEQGEQQRQLLEEELArLQREAAAATQKRRELEAELAKVRAEMEVLLASKA------RAEEESRST 1792
Cdd:PRK10246 591 TLQPQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLAT 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1793 SEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAVrqRAEAERVLAEKLAAISEATrLKTEAEIALKEKEA 1872
Cdd:PRK10246 670 RQQEAQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQD 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1873 ENERLR---------------RLAEDEAFQRRLLEEQAAQhkadieaRLAQLRKASESELERQKGLVEdtlrQRRQVEEE 1937
Cdd:PRK10246 741 VLEAQRlqkaqaqfdtalqasVFDDQQAFLAALLDEETLT-------QLEQLKQNLENQRQQAQTLVT----QTAQALAQ 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 1938 ILALKGSFEKAAAGKAELELELGRIRGT-AEDTLRSKE---QAEQEA-ARQRQ 1985
Cdd:PRK10246 810 HQQHRPDGLDLTVTVEQIQQELAQLAQQlRENTTRQGEirqQLKQDAdNRQQQ 862
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
66-173 |
2.34e-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: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 66 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 138
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237952 139 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 173
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1722-1922 |
2.51e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1722 AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1801
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1802 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEA 1863
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1864 EIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKG 1922
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1701-1953 |
2.83e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1701 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLA 1780
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1781 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEK 1849
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1850 LAAISEATRLKteAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLR 1929
Cdd:COG3883 174 EAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|....
gi 1920237952 1930 QRRQVEEEILALKGSFEKAAAGKA 1953
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAGAG 275
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1343-1604 |
2.85e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.88 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1343 QYIRFISETLRRMEEEERLAEQ--QRAEER-ERLAEVEAA-LEKQRQLAEAHAQAKAQA---------EREAQGLQRRMQ 1409
Cdd:PRK05035 429 QYYRQAKAEIRAIEQEKKKAEEakARFEARqARLEREKAArEARHKKAAEARAAKDKDAvaaalarvkAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1410 EEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEeirvvrlQLEATERQRGGAEGELQA 1488
Cdd:PRK05035 509 KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAiARAKAKKAA-------QQAANAEAEEEVDPKKAA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1489 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAelalrvqaeAEAAREKQRALQALEELRLQAEEAERRLRQAEA 1568
Cdd:PRK05035 582 VAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAA---------AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270
....*....|....*....|....*....|....*.
gi 1920237952 1569 ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLE 1604
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1454-1574 |
2.92e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.82 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1454 AERSRLRIEEEIRVVRLQLEATERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLR---------RQVQDETQRKR-Q 1523
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQQELDEARAALdA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 1524 AEAELAlRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1574
Cdd:COG1566 160 AQAQLE-AAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1708-1908 |
3.42e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.42 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1708 QRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRqllEEELARLQREAAAATQKRRELEAELAKVraemevllaskaraEE 1787
Cdd:COG2268 191 RRKIAEIIRDARIAEAE--AERETEIAIAQANR---EAEEAELEQEREIETARIAEAEAELAKK--------------KA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1788 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEA-----ERVLAEKLAAISEAtrlKTE 1862
Cdd:COG2268 252 EERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELeadvrKPAEAEKQAAEAEA---EAE 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237952 1863 AEIALKEKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 1908
Cdd:COG2268 329 AEAIRAKGLAEAEGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAK 375
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1737-1921 |
4.49e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1737 EQQRQLLEEELAR-LQREAAAATQKRRELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1815
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1816 RLRALAEeakrqrQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRrllEEQA 1895
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK--AEAEAKKK---AAAE 214
|
170 180
....*....|....*....|....*.
gi 1920237952 1896 AQHKADIEARLAQLRKASESELERQK 1921
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAKAAAEK 240
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2286-2739 |
4.57e-07 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 56.52 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2286 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMA 2365
Cdd:COG4995 9 LLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2366 QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2445
Cdd:COG4995 89 LLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2446 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2525
Cdd:COG4995 169 ALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2526 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRL 2605
Cdd:COG4995 249 ALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2606 RERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLRRKVPAQRLQEVGVLSAEELQQLAQ 2685
Cdd:COG4995 329 ALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQL 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 2686 GRTTVAELAQREDVRHYLQGRSSIAGLL-LKPADEKLTIYAALRRQLLSPGTALI 2739
Cdd:COG4995 409 LRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1689-1906 |
5.04e-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: 55.24 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRreleAEL 1768
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA----KEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1769 AKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDA---VRQRAEAERV 1845
Cdd:TIGR02794 148 AAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEA-----KAKAEAEAKAKAEEAKAKAEAAKAKAaaeAAAKAEAEAA 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 1846 LAEKLAAISEATRLKTEAEIAL-KEKEAENERLRRLAEDEAFQRRLleeqAAQHKADIEARL 1906
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAAAGSEVDKY----AAIIQQAIQQNL 276
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1761-2467 |
5.17e-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: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1761 RRELEAELAKVRAEMEVLLASKARAEEESRStsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRA 1840
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQ--IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1841 EAERvlaeklaaiSEATRLKTEAEIALKEKEAENERLRRLaedeafqrrllEEQAAQHKADIEARLAQLRKASESELERQ 1920
Cdd:COG4913 298 EELR---------AELARLEAELERLEARLDALREELDEL-----------EAQIRGNGGDRLEQLEREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1921 KGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaaeeerrrreaeer 2000
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR--------------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2001 vqkSLAAEEEAARQRKAAL-EEVERLKAKVEEARRLRE------------RAEQES-------------------ARQLQ 2048
Cdd:COG4913 423 ---ELEAEIASLERRKSNIpARLLALRDALAEALGLDEaelpfvgelievRPEEERwrgaiervlggfaltllvpPEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2049 LAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAAREraereaaqSRRQVEEAERL 2128
Cdd:COG4913 500 AALRWVN-RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRF--------DYVCVDSPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2129 KQSAEEQAQAQaqaqaaaekLRKeaeqeaarraqaEQAALRQKQAADAEMEKHkQFAEQALRQKAQVEQELTALRLQLEE 2208
Cdd:COG4913 571 RRHPRAITRAG---------QVK------------GNGTRHEKDDRRRIRSRY-VLGFDNRAKLAALEAELAELEEELAE 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2209 TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQmEELGKLKARIEAenralvLRDKDSAQRLLQEEAEKMKQVA 2288
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAELEAELER------LDASSDDLAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2289 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQ 2367
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlGDAVERELRENLEERIDALRAR 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2368 LAQETQGFQKTleterqrqleMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERL------YRTELATQEKVML 2441
Cdd:COG4913 782 LNRAEEELERA----------MRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYeerfkeLLNENSIEFVADL 851
|
730 740
....*....|....*....|....*.
gi 1920237952 2442 VQTLETQRQQSDRDAERLREAIAELE 2467
Cdd:COG4913 852 LSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2174-2374 |
5.64e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2174 ADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEE--- 2250
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2251 --------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2322
Cdd:COG3883 94 alyrsggsVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2323 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQG 2374
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2181-2484 |
5.96e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2181 HKQFAEQALRQKAQVEQ---ELTALRLQLEETDHQKSILDEELQRLKAEVTEAarqrgqvEEELFSLRVQME-------- 2249
Cdd:PRK04863 336 HLNLVQTALRQQEKIERyqaDLEELEERLEEQNEVVEEADEQQEENEARAEAA-------EEEVDELKSQLAdyqqaldv 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2250 ---------------------------ELGKLKARIEAenraLVLRDKDSAQRLLQEE-----AEKMKQVAEEAARL--- 2294
Cdd:PRK04863 409 qqtraiqyqqavqalerakqlcglpdlTADNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrk 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2295 ---SVAAQEAARLRQLAEEDLAQQRALAEKM---------LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2362
Cdd:PRK04863 485 iagEVSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2363 QMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAE-MSRAQA--RAEEDARRFRKQAEDigerlyrtELATQEKV 2439
Cdd:PRK04863 565 ARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARAPAwlAAQDALARLREQSGE--------EFEDSQDV 629
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2440 M--LVQTLETQRQQSdRDAERLREAIAELEHEKDKLKQ-----EAQLLQLKS 2484
Cdd:PRK04863 630 TeyMQQLLERERELT-VERDELAARKQALDEEIERLSQpggseDPRLNALAE 680
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1488-1886 |
6.44e-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: 56.11 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1488 ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAeaelalrvqaeAEAAREKQRALQAL---------EELRLQAEE 1558
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQ-----------LDQLKEQLQLLNKLlpqanlladETLADRLEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1559 AERRLRQAEAERA--RQVQVALETAQRSAEAeLQSEHASFAEktaqlertLKEEHVAVVQLREEATRRAQQQAEAERARA 1636
Cdd:COG3096 898 LREELDAAQEAQAfiQQHGKALAQLEPLVAV-LQSDPEQFEQ--------LQADYLQAKEQQRRLKQQIFALSEVVQRRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1637 EAERELERWQLKANEALRLRLQAeevaqqksltqaeaekqkeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTA 1716
Cdd:COG3096 969 HFSYEDAVGLLGENSDLNEKLRA-------------------------------------RLEQAEEARREAREQLRQAQ 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1717 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREA-----AAATQKRRELEAELAKVRAEmevllaskaraeeesRS 1791
Cdd:COG3096 1012 AQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdaeaeERARIRRDELHEELSQNRSR---------------RS 1076
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1792 TSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAK----RQRQLAEEDAVRQRAEAERVL---AEKLAAISEatrlk 1860
Cdd:COG3096 1077 QLEKQLTRCEAEmdslQKRLRKAERDYKQEREQVVQAKagwcAVLRLARDNDVERRLHRRELAylsADELRSMSD----- 1151
|
410 420
....*....|....*....|....*....
gi 1920237952 1861 tEAEIALKEKEAENERLR---RLAEDEAF 1886
Cdd:COG3096 1152 -KALGALRLAVADNEHLRdalRLSEDPRR 1179
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1113-1775 |
6.91e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.95 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1113 EEVLRAHEEQLKE-----AQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVER 1187
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1188 WRERVT-------LLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAK-QRQEQIQAvPLANSQAVReQL 1259
Cdd:pfam01576 417 LQARLSeserqraELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQeLLQEETRQ-KLNLSTRLR-QL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1260 RQEKALLEdiERHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAK-----KPKVQSGSESIIQEYVDLRTRY 1334
Cdd:pfam01576 495 EDERNSLQ--EQLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLEEKAAAY 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1335 SELS-------------TLTSQYIRFISETLRR-------MEEEERLAEQQRAEERERlAEVEAALEKQRQLAEAHA--- 1391
Cdd:pfam01576 569 DKLEktknrlqqelddlLVDLDHQRQLVSNLEKkqkkfdqMLAEEKAISARYAEERDR-AEAEAREKETRALSLARAlee 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1392 --QAKAQAEREAQGLQRRMQEEVARREEV------------AVEAQEQKRSIQEE-------------------LQHLRQ 1438
Cdd:pfam01576 648 alEAKEELERTNKQLRAEMEDLVSSKDDVgknvhelerskrALEQQVEEMKTQLEeledelqatedaklrlevnMQALKA 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1439 SSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEAEAQKRQAQEEAERLR 1511
Cdd:pfam01576 728 QFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKLQ 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1512 RQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERAR-QVQVALETAQRSA 1585
Cdd:pfam01576 805 AQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGASGKSA 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1586 eaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAE-----AERARAEAERELERWQL-KANEALRLRLQA 1659
Cdd:pfam01576 880 ---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelAAERSTSQKSESARQQLeRQNKELKAKLQE 956
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1660 EEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQA-----VRQRELAEQEL----EKQRQLAEGTAQQRLAAEQELIRLR 1730
Cdd:pfam01576 957 MEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVllqvEDERRHADQYKDQAEKGNSRMKQLK 1036
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1920237952 1731 AETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEM 1775
Cdd:pfam01576 1037 RQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1493-1610 |
7.06e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.26 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1493 AEEAEAQKRQAQEEAErLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRAlQALEELRLQAEEAERRLRQA--EAER 1570
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARA-EAEAAYEIAEANAEREVQRQleIAER 288
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1920237952 1571 ARQVQVALETAQRsAEAELQSEHASFAEktAQLERTLKEE 1610
Cdd:COG2268 289 EREIELQEKEAER-EEAELEADVRKPAE--AEKQAAEAEA 325
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2169-2610 |
7.15e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.95 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2169 RQKQAADAEMEKHKQFAEQALRqkaqvEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRV 2246
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLD-----EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2247 QMEE-------LGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMK----------QVAEEAARLS-VAAQEAARLRQLA 2308
Cdd:pfam01576 167 NLAEeeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAeLRAQLAKKEEELQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2309 E-----EDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL--AQETQGFQKTLET 2381
Cdd:pfam01576 247 AalarlEEETAQKNNALKKIRELEAQISE---LQEDLESERAARNKAEKQRRDLGEELEALKTELedTLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2382 ERQRQLEMSAEAERLRLRVAEMSRAQARaeedaRRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLRE 2461
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMR-----QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2462 AIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQL-------------------------------------LQETQALQQ 2504
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAeklsklqselesvssllneaegkniklskdvsslesqLQDTQELLQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2505 SFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQekqqLAASMEEARRRQHEAEEGVRRQQEEL 2584
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD----MKKKLEEDAGTLEALEEGKKRLQREL 554
|
490 500 510
....*....|....*....|....*....|
gi 1920237952 2585 ----QRLAQQQQQQEKLlaeenQRLRERLQ 2610
Cdd:pfam01576 555 ealtQQLEEKAAAYDKL-----EKTKNRLQ 579
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2814-2850 |
8.60e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 8.60e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1920237952 2814 IRLLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEM 2850
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2267-2704 |
9.13e-07 |
|
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: 55.36 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2267 LRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2346
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2347 KELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRqLEMSAEAERLRLRVAEMSRAQARAEEdarrFRKQAEDI 2424
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAV-LEETQERINRARKAAPLAAHIKAVTQ----IEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2425 GERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKS---EEMQTVRQEQLLQETQA 2501
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCqqhTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2502 LQQSFLSEKDSLLQRErciEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ 2581
Cdd:TIGR00618 393 QKLQSLCKELDILQRE---QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2582 EELQRLAQQQQQQEKlLAEENQRLRERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFDGLR 2661
Cdd:TIGR00618 470 EREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 2662 RKVPA-----QRLQEVGVLSAEELQQLAQGRTTVAELAQR-----EDVRHYLQ 2704
Cdd:TIGR00618 549 HQLTSerkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNlqnitVRLQDLTE 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2272-2488 |
1.00e-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: 54.38 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2272 SAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrqlAEEDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQ 2351
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2352 EQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2431
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 2432 ELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQ 2488
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1885-2374 |
1.02e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1885 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQkglvEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRg 1964
Cdd:COG4717 41 AFIRAMLLERLEKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1965 tAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2044
Cdd:COG4717 116 -EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2045 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVL-ERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVE 2123
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2124 EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQA------LRQKAQVEQ 2197
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldrIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2198 ELTALRLQLEETDHQKSIlDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL-GKLKARIEAENRALVLRDKDSAQRL 2276
Cdd:COG4717 355 EAEELEEELQLEELEQEI-AALLAEAGVEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2277 LQEEAEKMKQVAEEAARLSVAAQEA-ARLRQLAEEDLAQQRALAEKMLKEKMQ-AVQEATRLKAEAELLQQQKELAQEqa 2354
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELeAELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALELLEEAREEYRE-- 511
|
490 500
....*....|....*....|
gi 1920237952 2355 RRLQEDKEQMAQQLAQETQG 2374
Cdd:COG4717 512 ERLPPVLERASEYFSRLTDG 531
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1490-1620 |
1.06e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 54.96 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1490 RARAEEAEAQ------KRQAQEEAerlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAER-- 1561
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1562 -RLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ----LERTLKEEHVAVVQLREE 1620
Cdd:pfam15709 411 rLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQrqkeLEMQLAEEQKRLMEMAEE 474
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4154-4182 |
1.13e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.71 E-value: 1.13e-06
10 20
....*....|....*....|....*....
gi 1920237952 4154 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4182
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1353-1621 |
1.20e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.15 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1353 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVeaQEQKRSIQEE 1432
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM--DEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1433 LQHLRQSSEAEIQAKARQVEAAERSRLRI---------EEEIRVVRLQLEATERQRggAEGELQALRARAEEAEAQKRQA 1503
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeerEEDERILEYLKEKAEREE--EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1504 QEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQR 1583
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270
....*....|....*....|....*....|....*...
gi 1920237952 1584 SAEAELQSEhasfAEKTAQLERTLKEEHVAVVQLREEA 1621
Cdd:pfam13868 272 EDEEIEQEE----AEKRRMKRLEHRRELEKQIEEREEQ 305
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1689-2062 |
1.46e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1768
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1769 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAVRQRAEAERVL 1846
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1847 AEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRLLEEQAAQhkadiearlaqlrkASESELERQKGLVED 1926
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKSQ--------------NGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1927 TLRQRRQVEEEilalkgsfEKAAAGKAELELELGRIRGTAEDtlrsKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 2006
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRRRRQE----KESEEFEKLRQKQQEAELELEELKKKREERRKLL 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 2007 AEEEaaRQRKAalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2062
Cdd:pfam02029 294 EEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2339-2625 |
1.69e-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: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2339 EAELLQQQKELAQEQA----RRLQEDKEQMAQQ-LAQETQgfQKTLETERQRQLEMS-----AEAERLRLRVAEMSRAQA 2408
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQErLRQEKE--EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2409 RAEEDARRFRKQAEDI-GERLYRTELATQ-EKVMLVQTLETQRQQSDrdaERLREAIAELEHEKDKLKQEAQLLQLKSEE 2486
Cdd:pfam17380 345 ERERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2487 MQTVRQEQLLQETQALQQsflsekdslLQRERCIEQEKAKLEQLfqdevakaqalreeqqRqqqqMQQEKQQLAASMEEA 2566
Cdd:pfam17380 422 MEQIRAEQEEARQREVRR---------LEEERAREMERVRLEEQ----------------E----RQQQVERLRQQEEER 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2567 RRRQHEAEEGVRRQQ--EELQRLAQQQQQQEKLLAE-ENQRLRERLQHLEEERRAALARSEE 2625
Cdd:pfam17380 473 KRKKLELEKEKRDRKraEEQRRKILEKELEERKQAMiEEERKRKLLEKEMEERQKAIYEEER 534
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1357-1541 |
1.86e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.66 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1357 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvaveaqEQKRSIQEELQhl 1436
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA------EAKKKAEAEAA-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1437 rQSSEAEIQAKARQVEAAersrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1516
Cdd:PRK09510 177 -KKAAAEAKKKAEAEAAA----------------KAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 1920237952 1517 ETQRKRQAEAELALRVQAEAEAARE 1541
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1411-2038 |
1.87e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1411 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ----------LEATERQRG 1480
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEvkeleelkeeIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1481 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEaEAAREKQRALQALEELRLQAEEAE 1560
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1561 RRLRQAEAERARQVQValetaqRSAEAELQSEHASFaEKTAQLERTLKEEHVAVVQLREEatrraqqqaeaeraraeaer 1640
Cdd:PRK03918 328 ERIKELEEKEERLEEL------KKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKR-------------------- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1641 elerwqLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREarrrgkaeEQAVRQRELAEQELEKqrqlAEGTAQ--Q 1718
Cdd:PRK03918 381 ------LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL--------KKEIKELKKAIEELKK----AKGKCPvcG 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1719 RLAAEQELIRLRAEteqgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVraEMEVLLASKARAE----EESRSTSE 1794
Cdd:PRK03918 443 RELTEEHRKELLEE----------YTAELKRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLkelaEQLKELEE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1795 KSK----QRLEAEAGRFRELAEEAARLRalaeeaKRQRQLAEEdaVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEK 1870
Cdd:PRK03918 511 KLKkynlEELEKKAEEYEKLKEKLIKLK------GEIKSLKKE--LEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1871 --EAENERLRRLAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKAsESELERQKGLVEDTLRQRRQVEEEILALKGSF--- 1945
Cdd:PRK03918 583 gfESVEELEERLKELEPFYNEYLELKDAEK--ELEREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYsee 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1946 --EKAAAGKAELELELGRIRGTAEDTLRSKEQAEqeaarqrqlaaeeerrrreaeervqKSLAAEEEAARQRKAALEEVE 2023
Cdd:PRK03918 660 eyEELREEYLELSRELAGLRAELEELEKRREEIK-------------------------KTLEKLKEELEEREKAKKELE 714
|
650
....*....|....*
gi 1920237952 2024 RLKAKVEEARRLRER 2038
Cdd:PRK03918 715 KLEKALERVEELREK 729
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3473-3509 |
2.06e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.06e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1920237952 3473 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEM 3509
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2178-2402 |
2.17e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2178 MEKHKQFAEQALR----QKAQVEQELTALRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2251
Cdd:COG3206 166 LELRREEARKALEfleeQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2252 GKLKARIEAENRALVlrDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqAVQ 2331
Cdd:COG3206 246 RAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS---LEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 2332 EATRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLET--ERQRQLEMSAEAERLRLRVAE 2402
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESllQRLEEARLAEALTVGNVRVID 392
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2266-2619 |
2.23e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2266 VLRDKDSAQRLLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2339
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2340 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAQETQGFQKTLETER-------QRQLEMSAEAERLRLRVAEMSRAQAR 2409
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDadaeaveARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2410 AEEDARRFRKQAEDIGERlyrtelaTQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQT 2489
Cdd:PRK02224 340 HNEEAESLREDADDLEER-------AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2490 VRQEqllqetqalqqsFLSEKDSLLQRERCIEqekAKLEQLfQDEVAKAQALREE--------------QQRQQQQMQQE 2555
Cdd:PRK02224 413 FLEE------------LREERDELREREAELE---ATLRTA-RERVEEAEALLEAgkcpecgqpvegspHVETIEEDRER 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2556 KQQLAASMEEARRRQHEAEEGVRRQQE------ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2619
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1353-1614 |
2.27e-06 |
|
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: 53.50 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1353 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR--REEVAVEAQEQKRSIQ 1430
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1431 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleaterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1510
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1511 RRQVQDETQRKRQAEAELALRVQAEAEAAREK----QRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1586
Cdd:pfam15558 168 KVQENNLSELLNHQARKVLVDCQAKAEELLRRlsleQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 1920237952 1587 AELQSEHASFAEKTAQLERTLKEEHVAV 1614
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1688-1908 |
2.44e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.80 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1688 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqreaaaATQKRREL 1764
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1765 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeagrfrelaEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1844
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 1845 VLAEKLAAISEATRLKTEAEIALkeKEAENERLRRLAE-DEAFQRRLLEEQAAQHKADIEARLAQ 1908
Cdd:pfam15709 447 AEAEKQRQKELEMQLAEEQKRLM--EMAEEERLEYQRQkQEAEEKARLEAEERRQKEEEAARLAL 509
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
71-179 |
2.51e-06 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 50.06 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 71 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 137
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1920237952 138 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 179
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1486-1760 |
2.60e-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: 53.23 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1486 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQA--------LEELRLQAE 1557
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQelaaleaeLAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1558 EAERRLRQAEAERARQVQVALETAQRSAEAELQSehasfAEKTAQLERTLKEEHVAVVQLREEATRRAQqqaeaerarae 1637
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRA----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1638 aerelerwQLKANEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEgtaq 1717
Cdd:COG4942 158 --------DLAELAALRAELEAERAELEALL----------------------AELEEERAALEALKAERQKLLAR---- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1920237952 1718 qrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQK 1760
Cdd:COG4942 204 ----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2273-2600 |
2.83e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.00 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2273 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2352
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2353 QARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERlrlRVAEMSRAQARAEEDARRFRKQAEDIGERLYrte 2432
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREI--- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2433 latqeKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqllqlksEEMQTVRQEQLLQETQALQQSFLSEKDS 2512
Cdd:pfam13868 187 -----ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKERE--------EAEKKARQRQELQQAREEQIELKERRLA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2513 LLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQ 2592
Cdd:pfam13868 254 EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEE 333
|
....*...
gi 1920237952 2593 QQEKLLAE 2600
Cdd:pfam13868 334 ERQKKLKE 341
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2178-2481 |
3.19e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2178 MEKHKQFAEQALRQKAQVEQELTAlrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKAR 2257
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2258 IEAENRALvlrdKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAarlRQLAEE--DLAQQRALaekmLKEKMQavqeatr 2335
Cdd:TIGR04523 466 LETQLKVL----SRSINKIKQNLEQKQKELKSKEKELKKLNEEK---KELEEKvkDLTKKISS----LKEKIE------- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2336 lKAEAELLQQQKELAQeqarrLQEDKEQMAQQLAQETqgfqktLETERQRQLEmsaEAERLRLRVAEMSRAQARAEEDAR 2415
Cdd:TIGR04523 528 -KLESEKKEKESKISD-----LEDELNKDDFELKKEN------LEKEIDEKNK---EIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 2416 RFRKQAEDIGERLyrtelatQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQ 2481
Cdd:TIGR04523 593 QKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1420-2255 |
3.31e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.90 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1420 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAersrLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1499
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKA----CEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1500 KRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKqraLQALEELR-LQAEEAERRLRQAEAERARQVQVAL 1578
Cdd:TIGR00606 261 LSKIMKLDNEIKALKSRKKQMEKD-NSELELKMEKVFQGTDEQ---LNDLYHNHqRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1579 ETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRL--R 1656
Cdd:TIGR00606 337 LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLcaD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1657 LQAEEVAQQKSLTQAEAEKQKEEAEREArrrgKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG 1736
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIEL----KKEILEKKQEEL--KFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1737 EQQR--QLLEEELARLQREAAAATQKRRELEAELAKV------RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFR 1808
Cdd:TIGR00606 491 EKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFP 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1809 ELAEEAARLRALAEEAKRQRQ-LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEI----ALKEKEAENERLRRLAED 1883
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDEESDLERLKEEIEK 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1884 EAFQRRLLEEQAAQHKADIEAR---------LAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKaaagkaE 1954
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK------R 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1955 LELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRR--EAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 2032
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDV 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2033 RRLRERAEQESaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERA 2111
Cdd:TIGR00606 805 ERKIAQQAAKL-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2112 EREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKL----------RKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2181
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDqqekeelissKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 2182 KQfaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVtEAARQRGQVEEELFSLRVQMEELGKLK 2255
Cdd:TIGR00606 964 IQ--DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI-DTQKIQERWLQDNLTLRKRENELKEVE 1034
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2275-2523 |
3.33e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.90 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2275 RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2350
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2351 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAE-AERLRLRVAEMSRAQARA----EEDARRFRKQAEDIG 2425
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2426 ERLYRTELATQEKVMLVQTLETQRQQ------SDRDAERLREAIAELEhEKDKLKQ----EAQLL--QLKSEEMQTvRQE 2493
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQldteMAQLRvqRLRYEDLLN-KQP 360
|
250 260 270
....*....|....*....|....*....|
gi 1920237952 2494 QLLQETQALQQSFLSEKDSLLQRERCIEQE 2523
Cdd:PRK10929 361 QLRQIRQADGQPLTAEQNRILDAQLRTQRE 390
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1383-1511 |
3.35e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 52.74 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1383 QRQLAEAHAQ-AKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSRLRI 1461
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1462 EEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1511
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2217-2422 |
3.46e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2217 DEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSV 2296
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2297 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2368
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 2369 AQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2422
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1899-2617 |
3.48e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1899 KADIEARLAQlRKASESELERQKGLVEDTLRQRrQVEEEILALKGSFEKAAAG-----KAELELELGRIRGTAEDTLRSK 1973
Cdd:pfam12128 199 KSMIVAILED-DGVVPPKSRLNRQQVEHWIRDI-QAIAGIMKIRPEFTKLQQEfntleSAELRLSHLHFGYKSDETLIAS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1974 EQAEQEA--ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQ 2051
Cdd:pfam12128 277 RQEERQEtsAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2052 EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQS 2131
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2132 AEEQAQaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDh 2211
Cdd:pfam12128 437 EEEYRL----------KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2212 qksildEELQRLKAEVTEAARQRGQVEEELFS--------LRVQM----EELGKLKARieaenrALVLR-------DKDS 2272
Cdd:pfam12128 506 ------EALRQASRRLEERQSALDELELQLFPqagtllhfLRKEApdweQSIGKVISP------ELLHRtdldpevWDGS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2273 AQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2352
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2353 QARRLQEDKEQMAQQLAQETQGFQKTLETERQrqlEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQA--EDIGERLYR 2430
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLN---SLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqVVEGALDAQ 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2431 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqLLQETQALQQSFLSEK 2510
Cdd:pfam12128 731 LALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE-VLRYFDWYQETWLQRR 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2511 DSLLQRERCIEQEKAKLEQlfqdevakaqalreEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQ 2590
Cdd:pfam12128 810 PRLATQLSNIERAISELQQ--------------QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATL 875
|
730 740
....*....|....*....|....*..
gi 1920237952 2591 QQQQEKllAEENQRLRERLQHLEEERR 2617
Cdd:pfam12128 876 KEDANS--EQAQGSIGERLAQLEDLKL 900
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2190-2621 |
3.50e-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: 53.60 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2190 RQKAQVEQELTALRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALV 2266
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2267 LRDKDSAQRLLQEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2345
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2346 QKELAQEQA--RRLQEDKEQMAQQLAQETQGFQKTL----ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRK 2419
Cdd:pfam07111 347 VTSQSQEQAilQRALQDKAAEVEVERMSAKGLQMELsraqEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2420 QAEDIGERLYRTELATQE----------KVMLVQTLETQRQQSDRDAERLREAIAELEH---EKDKLKQEAQL-LQLKSE 2485
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKvhtikglmarKVALAQLRQESCPPPPPAPPVDADLSLELEQlreERNRLDAELQLsAHLIQQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2486 EMQTVRQE-------------QLLQETQALQQSFLS---EKDSLLQRERCIEQEKAKLEQ-LFQDEVAKAQALREEQQRQ 2548
Cdd:pfam07111 507 EVGRAREQgeaerqqlsevaqQLEQELQRAQESLASvgqQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEKVAEV 586
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 2549 QQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2621
Cdd:pfam07111 587 ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhratQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLA 663
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1356-1521 |
3.68e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.54 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1356 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQH 1435
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1436 LRQSSEAEIQAKARQVEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRARAEEAEAQK------RQAQ 1504
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 1920237952 1505 EEAERLRRQVQDETQRK 1521
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
71-178 |
3.84e-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: 49.66 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 71 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 137
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237952 138 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 178
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1788-2629 |
4.01e-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: 53.58 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1788 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIAL 1867
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1868 KEKEAENERlrrlAEDEAFQRRLLEEQAAQHkaDIEARLAQLRKASESELERQKGLVEDTLRQR--------RQVEEEIL 1939
Cdd:pfam15921 161 KEDMLEDSN----TQIEQLRKMMLSHEGVLQ--EIRSILVDFEEASGKKIYEHDSMSTMHFRSLgsaiskilRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1940 ALKGSF----EKAAAGKAELELELGRIRGTAEDTLrskEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR 2015
Cdd:pfam15921 235 YLKGRIfpveDQLEALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2016 KAA----LEEVE----RLKAKVEEARRLRERAEQESARQLQLAQ----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2083
Cdd:pfam15921 312 NSMymrqLSDLEstvsQLRSELREAKRMYEDKIEELEKQLVLANseltEARTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2084 QSVLERlrseaeaarraaeeaeaareraereaAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2163
Cdd:pfam15921 392 ELSLEK--------------------------EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2164 EQAALRQKQAADAEMEKHKQFAEQALRQKA---QVEQELTALRLQLEETDHQKSILDEELQR----LKAEVTEAARQRGQ 2236
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDLTASLQEkeraIEATNAEITKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2237 VE---EELFSLRVQMEELGKLKAriEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQ-EAArlrQLAEEDL 2312
Cdd:pfam15921 526 VDlklQELQHLKNEGDHLRNVQT--ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKA---QLEKEIN 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2313 AQQRALAE-KMLKEKMQAvqEATRLKAEAELLQQQK-ELAQEQARRLQEDKEqmaqqLAQETQGFQKTLETERQRQLEMS 2390
Cdd:pfam15921 601 DRRLELQEfKILKDKKDA--KIRELEARVSDLELEKvKLVNAGSERLRAVKD-----IKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2391 AEAERLRlrvaemsraqaraeedaRRFRKQAEDIGERLYRTELATQE-KVMLVQTLETQRQQSDRDAERLREA------I 2463
Cdd:pfam15921 674 EDYEVLK-----------------RNFRNKSEEMETTTNKLKMQLKSaQSELEQTRNTLKSMEGSDGHAMKVAmgmqkqI 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2464 AELEHEKDKLKQEAQLLQlksEEMQTVRQEQ-LLQEtqalqqsflsEKDSLLQRERCIEQEKAKLEQlfQDEVAKAQALR 2542
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLE---EAMTNANKEKhFLKE----------EKNKLSQELSTVATEKNKMAG--ELEVLRSQERR 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2543 eeqqrqqqqMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA----EENQRLRERLQhleeeRRA 2618
Cdd:pfam15921 802 ---------LKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQgpgyTSNSSMKPRLL-----QPA 867
|
890
....*....|.
gi 1920237952 2619 ALARSEEIAPS 2629
Cdd:pfam15921 868 SFTRTHSNVPS 878
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1254-1986 |
4.10e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.19 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1254 AVREQLRQEKALLEDierhGEKVEECQRFAKQyinaikdyELQLVTYKAQLepvaspakkpKVQSGsesiIQEYVDLRTR 1333
Cdd:pfam05483 96 SIEAELKQKENKLQE----NRKIIEAQRKAIQ--------ELQFENEKVSL----------KLEEE----IQENKDLIKE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1334 yselSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAQGLQRRMQEEva 1413
Cdd:pfam05483 150 ----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK---MILAFEELRVQAENARLEMHFKLKED-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1414 rreevaveaqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1493
Cdd:pfam05483 221 ----------------HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1494 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELR----LQAEEAERRLRQAEaE 1569
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsFVVTEFEATTCSLE-E 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1570 RARQVQVALEtaqrSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATrraqqqaeaerarAEAERELERWQLKA 1649
Cdd:pfam05483 364 LLRTEQQRLE----KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKK-------------ILAEDEKLLDEKKQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1650 NEALRLRLQAEEvaQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQR-QLAEGTAQ--------QRL 1720
Cdd:pfam05483 427 FEKIAEELKGKE--QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHcdklllenKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1721 AAEQE--LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA---ELAKVRAEMEVLL---ASKARAEEESRST 1792
Cdd:pfam05483 505 TQEASdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESvreEFIQKGDEVKCKLdksEENARSIEYEVLK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1793 SEKSKQRLEAEAGRFRELAEEAAR-LRALAEEAKRQRQlaEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKE 1871
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKnIEELHQENKALKK--KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1872 AENERL--RRLAEdEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRrqvEEEILALKGSFEKAA 1949
Cdd:pfam05483 663 IEDKKIseEKLLE-EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQS 738
|
730 740 750
....*....|....*....|....*....|....*..
gi 1920237952 1950 AGKAELELELGRIRGtaeDTLRSKEQAEQEAARQRQL 1986
Cdd:pfam05483 739 SAKAALEIELSNIKA---ELLSLKKQLEIEKEEKEKL 772
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1337-1592 |
4.31e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1337 LSTLTSQYIRFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAEREAQGLQRRMQEEVAR 1414
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1415 ReevaVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRARAE 1494
Cdd:COG3206 228 L----AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR--AQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1495 EAEAQKRQaqeEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAeaeRARQV 1574
Cdd:COG3206 302 ALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL---LQRLE 375
|
250
....*....|....*...
gi 1920237952 1575 QVALETAQRSAEAELQSE 1592
Cdd:COG3206 376 EARLAEALTVGNVRVIDP 393
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1373-1467 |
4.36e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.42 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1373 LAEVEAALEKQRQLAEAHAQAKAQAEREAqglqRRMQEEVARREEVAVEAQEQKRSIQEELQHLR-QSSEAEIQAKARQV 1451
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 1920237952 1452 EAAERSRLRI---EEEIRV 1467
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2170-2355 |
4.41e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.11 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2170 QKQAADAEMEKHKQFAEQALRQKAQvEQELTALRLQLEETDHQKSILDEELQRLKAEVTeaarqrgQVEEELFSLRVQME 2249
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSIK-------QVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2250 ELGK---LKARI-----EAENRALVLrdkdsaQRLLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALA 2319
Cdd:pfam05667 381 ELEKqykVKKKTldllpDAEENIAKL------QALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLE 454
|
170 180 190
....*....|....*....|....*....|....*....
gi 1920237952 2320 E-KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2355
Cdd:pfam05667 455 EiKELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3732-3767 |
4.51e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 4.51e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1920237952 3732 RQLLEAQAATGFLLDPVKGERLAVDEAVRKGLVGPE 3767
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1442-1621 |
4.58e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.16 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1442 AEIQAKARQVEAAERSRLRIEEEirvvrlQLEATERQRGGAEGELQALRARAEEAEAqKRQAQEEAERLRRQVQDETQRK 1521
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQ------QAEEAEKQRAAEQARQKELEQRAAAEKA-AKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1522 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1601
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
170 180
....*....|....*....|
gi 1920237952 1602 QLERTLKEEHVAVVQLREEA 1621
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEA 225
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1694-2436 |
4.60e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1694 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQrEAAAATQKrrelea 1766
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEK------ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1767 eLAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAVRQRAEAERvl 1846
Cdd:COG3096 349 -IERYQEDLEEL---TERLEEQEEVVEEAAEQLAEAEA-RLEAAEEEVDSLKS--QLADYQQAL---DVQQTRAIQYQ-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1847 aEKLAAISEATRLKTEAEIALKEKEAENERLRRlAEDEAFQRRLleeQAAQHKADIEARLAQLRKAseseLERQKGLVED 1926
Cdd:COG3096 417 -QAVQALEKARALCGLPDLTPENAEDYLAAFRA-KEQQATEEVL---ELEQKLSVADAARRQFEKA----YELVCKIAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1927 TLRQRR-QVEEEILALKGSFEKAAAGKAELELELGrirgtaedtlrskeQAEQEAARQRQLAAEEERRRREAEERVQKSL 2005
Cdd:COG3096 488 VERSQAwQTARELLRRYRSQQALAQRLQQLRAQLA--------------ELEQRLRQQQNAERLLEEFCQRIGQQLDAAE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2006 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEA-----AQKRLQ--AEEKAHAFAVQQkeqelqQ 2078
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaAQDALErlREQSGEALADSQ------E 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2079 TLQQEQSVLERLRseaeaarraaeeaeaareraerEAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeklrkeaeqeaa 2158
Cdd:COG3096 628 VTAAMQQLLERER----------------------EATVERDELAARKQ------------------------------- 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2159 rraQAEQAALRQKQAADAEMEKHKQFAEQ----------------------AL--------------------------- 2189
Cdd:COG3096 655 ---ALESQIERLSQPGGAEDPRLLALAERlggvllseiyddvtledapyfsALygparhaivvpdlsavkeqlagledcp 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2190 ---------------------------------RQ-------------KAQVEQELTALRLQLEETD---HQKSILDEEL 2220
Cdd:COG3096 732 edlyliegdpdsfddsvfdaeeledavvvklsdRQwrysrfpevplfgRAAREKRLEELRAERDELAeqyAKASFDVQKL 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2221 QRL--------------------KAEVTEAARQRGQVEEELFSLRVQM----EELGKLKARIEAENRAL----VLRDKDS 2272
Cdd:COG3096 812 QRLhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLADETL 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2273 AQRL--LQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlKEKMQAVQEATRLKAEA---------- 2340
Cdd:COG3096 892 ADRLeeLREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQ----ADYLQAKEQQRRLKQQIfalsevvqrr 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2341 -------------------ELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQkTLETERQRQLEMSAEAERlrlRVA 2401
Cdd:COG3096 968 phfsyedavgllgensdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ---ELE 1043
|
890 900 910
....*....|....*....|....*....|....*...
gi 1920237952 2402 EMS-RAQARAEEDA--RRFRKQAEDIGERLYRTELATQ 2436
Cdd:COG3096 1044 ELGvQADAEAEERAriRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2170-2354 |
4.84e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2170 QKQAADAEMEKHKQFAEQA--LRQKAQVEQEltalRLQLEETDHQKSildeelQRLKAEVTEAARQRGQVEEELFSLRVQ 2247
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLEKERLAA------QEQKKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2248 MEELGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEK-----MKQVAEEAARLSVAAQEAARLRQLAEE---DLAQQRAL 2318
Cdd:PRK09510 141 AAAAAKAKAEAEAKRaAAAAKKAAAEAKKKAEAEAAKkaaaeAKKKAEAEAAAKAAAEAKKKAEAEAKKkaaAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237952 2319 AEKmlKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2354
Cdd:PRK09510 221 AEA--KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1350-1583 |
5.25e-06 |
|
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: 52.35 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1350 ETLRRMEEEERLAEQQRAEERERLA--EVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEvavEAQEQKR 1427
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGreERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQ---RKQCQEQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1428 SIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA------EAQKR 1501
Cdd:pfam15558 128 RLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELlrrlslEQSLQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1502 QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ----RALQALEELRL-QAEEAERRLRQAEAERARQVQV 1576
Cdd:pfam15558 208 RSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERqehkEALAELADRKIqQARQVAHKTVQDKAQRARELNL 287
|
....*..
gi 1920237952 1577 ALETAQR 1583
Cdd:pfam15558 288 EREKNHH 294
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2218-2626 |
5.32e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2218 EELQRLKAEVteAARQRGQVEEELFSLRVQMEELGKLKARIEaENRALVLRDKDSAQRLLQEEAEKMKQ---VAEEAARL 2294
Cdd:PRK02224 187 GSLDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIERYE-EQREQARETRDEADEVLEEHEERREEletLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2295 SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaqetQG 2374
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA----QA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2375 FQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2454
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI--------------EELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2455 DAERLREAIAELEHEKDKLKQEAQLLQ--LKSEEMQTVRQEQLLQE------TQALQQSflSEKDSLLQRERCIEQEKAK 2526
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEatLRTARERVEEAEALLEAgkcpecGQPVEGS--PHVETIEEDRERVEELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2527 LEQL------FQDEVAKAQALREEQQR--QQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLL 2598
Cdd:PRK02224 484 LEDLeeeveeVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430
....*....|....*....|....*....|....
gi 1920237952 2599 AEENQRLRERLQHLEE------ERRAALARSEEI 2626
Cdd:PRK02224 564 EEEAEEAREEVAELNSklaelkERIESLERIRTL 597
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3937-3974 |
5.70e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 5.70e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1920237952 3937 QRFLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTA 3974
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
181-288 |
6.00e-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: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 181 QSEDMTAKEKLLLWSQRMVEGcqgLRCDNFTTSWRDGRLFNAIIHRHKPTLI-DMNKVYRQTNLENLDQAFSVAERDLGV 259
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1920237952 260 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 288
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1391-1613 |
6.23e-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: 51.77 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1391 AQAKAQAEREAQGLQ---RRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKArqveaAERSRLRIEEEIRV 1467
Cdd:TIGR02794 46 GAVAQQANRIQQQKKpaaKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1468 vrlQLEATERQRggaegelqALRARAEEAEAqKRQAQEEAerlRRQVQDETQRKRQAEAelalrvQAEAEAAREKQRAL- 1546
Cdd:TIGR02794 121 ---AEEAKAKQA--------AEAKAKAEAEA-ERKAKEEA---AKQAEEEAKAKAAAEA------KKKAEEAKKKAEAEa 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1547 --QALEELRLQAEEAERRLRQAE----------AERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA 1613
Cdd:TIGR02794 180 kaKAEAEAKAKAEEAKAKAEAAKakaaaeaaakAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1688-1970 |
8.04e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1688 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1767
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1768 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ----LAEEDAVRQRAEAE 1843
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1844 RVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL 1923
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1920237952 1924 VEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 1970
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1536-2067 |
8.39e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1536 AEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQV--ALETAQRSAEAELQS------EHASFAEKTAQLERTL 1607
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKlekevkELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1608 KEEHVAVVQLRE---EATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREA 1684
Cdd:PRK03918 248 ESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1685 RRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR--LQREA 1754
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKeeIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1755 AAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQ-RQLAE 1832
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKElRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1833 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERlRRLAEDEAFQRRLLEEqaAQHKADIEARLAQLRKA 1912
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK-EKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1913 SEsELERQKGLVEDTLRQR-----RQVEEEILALKGSFEK---AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQR 1984
Cdd:PRK03918 565 LD-ELEEELAELLKELEELgfesvEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1985 QLAAEEERRrreaeervqKSLAAEEEAARQRKAALE---EVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQ 2059
Cdd:PRK03918 644 ELRKELEEL---------EKKYSEEEYEELREEYLElsrELAGLRAELEELEKRREEIKKtlEKLKEELEEREKAKKELE 714
|
....*...
gi 1920237952 2060 AEEKAHAF 2067
Cdd:PRK03918 715 KLEKALER 722
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2168-2614 |
8.42e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHKQFAEQALRQ-----KAQVEQELTA---LRLQLEETDHQKSI-LDEELQRLKAEVTEAARQRGQVE 2238
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQvymdlNNNIEKMILAfeeLRVQAENARLEMHFkLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2239 EELFSLRVQM-EELGKLKARI----EAENRALVLRDKDSAQ-RLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2312
Cdd:pfam05483 240 KQVSLLLIQItEKENKMKDLTflleESRDKANQLEEKTKLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2313 AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ--------KELAQEQARRLQEDKEQMaQQLAQETQgfQKTLETERQ 2384
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeattcslEELLRTEQQRLEKNEDQL-KIITMELQ--KKSSELEEM 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2385 RQLEMSAEAERLRLRVAeMSRAQARAEEdarrfRKQAEDIGERLYRTElatQEKVMLVQTLETQRQQSDRDAERLREAIA 2464
Cdd:pfam05483 397 TKFKNNKEVELEELKKI-LAEDEKLLDE-----KKQFEKIAEELKGKE---QELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2465 ELEHEKDKLKQEAQLLQLKSEEMqTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQdevaKAQALREE 2544
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIEL-TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK----QIENLEEK 542
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2545 QQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEE 2614
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2196-2625 |
8.44e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2196 EQELTALRLQLEETDHQKSILDEElQRLKAEvtEAARQRGQVEeelfslRVQMEelGKLKariEAENRALVLRDKDSaqR 2275
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLE-EQLDEE--EAARQKLQLE------KVTTE--AKIK---KLEEDILLLEDQNS--K 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2276 LLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE-KMQAVQEATRLKAEAELLQqqkelAQEQA 2354
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEeKGRQELEKAKRKLEGESTD-----LQEQI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2355 RRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQA--RAEEDAR-RFRKQAEDIGERL--Y 2429
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEdlESERAARnKAEKQRRDLGEELeaL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2430 RTELA-TQEKVMLVQTLETQRQQsdrDAERLREAIaelehEKDKLKQEAQLLQLKSEEMQTVR--QEQLLQ--------- 2497
Cdd:pfam01576 305 KTELEdTLDTTAAQQELRSKREQ---EVTELKKAL-----EEETRSHEAQLQEMRQKHTQALEelTEQLEQakrnkanle 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2498 -ETQALQQSFL---SEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQalreEQQRQQQQMQQEKQQLAASMEEARRRQHEA 2573
Cdd:pfam01576 377 kAKQALESENAelqAELRTLQQAKQDSEHKRKKLEGQLQELQARLS----ESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 2574 EEGVRRQQEELQRLAQQQQQQEKLLAEENQR---LRERLQHLEEERRAALARSEE 2625
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQklnLSTRLRQLEDERNSLQEQLEE 507
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1315-1529 |
8.65e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1315 KVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA-- 1389
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1390 --HAQAKAQAEREAQGLQRRMQeevARREEVaveaqEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrv 1467
Cdd:COG4942 125 llSPEDFLDAVRRLQYLKYLAP---ARREQA-----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 1468 vrlqleaTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1529
Cdd:COG4942 195 -------AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2327-2472 |
9.10e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 52.33 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2327 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQ-QLAQetQGFQKTLETERQRQLEMSAEAERLR 2397
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARgRLER--QKMHDKAKAEEQRTKLLELQAESAA 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 2398 LRVAEMSRAQARAEEDARRFRKQAEdigerLYRTEL-ATQEKVMLVQTLETQRQQSDRDAERlREAIAELEHEKDK 2472
Cdd:PTZ00491 711 VESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1238-1557 |
9.16e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.36 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1238 KQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQ 1317
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1318 SGSESIIQEYVDLRTRYSELSTLTSQ---YIRFISETLRRMEeeerlaeQQRAEERERLAEVEAALEKQRQLAEAHAQAK 1394
Cdd:PRK10929 102 MSTDALEQEILQVSSQLLEKSRQAQQeqdRAREISDSLSQLP-------QQQTEARRQLNEIERRLQTLGTPNTPLAQAQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1395 AQAereaqglqrrMQEEVARReevaveaqeqkRSIQEELQhLRQSSEAEIQAKAR-QVEAAERSRLRIEEEIRVVRLQLE 1473
Cdd:PRK10929 175 LTA----------LQAESAAL-----------KALVDELE-LAQLSANNRQELARlRSELAKKRSQQLDAYLQALRNQLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1474 aTERQRggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ-------AEAEAAREKQRAL 1546
Cdd:PRK10929 233 -SQRQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQrmdliasQQRQAASQTLQVR 299
|
330
....*....|.
gi 1920237952 1547 QALEELRLQAE 1557
Cdd:PRK10929 300 QALNTLREQSQ 310
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3939-3977 |
9.99e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 9.99e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3939 FLEGTSSIAGVLVDATKERLSVYQAMKKGIIRPGTAFEL 3977
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1365-2069 |
1.08e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1365 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-EAQGlqrrmqeevarrEEVAVEAQEQKRSIQEELQHLRQsseae 1443
Cdd:PRK10246 168 ERAELLEELTGTEIYGQISAMVFEQHKSARTELEKlQAQA------------SGVALLTPEQVQSLTASLQVLTD----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1444 iqakarqveaaersrlriEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvQDETQRKRQ 1523
Cdd:PRK10246 231 ------------------EEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKA-------QPQLAALSL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1524 AEAELALRVQAEaeaarEKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQrsaeaELQSEHASFAEKTAql 1603
Cdd:PRK10246 286 AQPARQLRPHWE-----RIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLA-- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1604 ertlkeEHVAVVQLREE-----ATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLtqaeaekqke 1678
Cdd:PRK10246 354 ------EHDRFRQWNNElagwrAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQ---------- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1679 eaerearrrgKAEEQAVRQR--ELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqREAAA 1756
Cdd:PRK10246 418 ----------HAEQRPLRQRlvALHGQIVPQQKRLAQ-LQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADV-KTICE 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1757 ATQKRRELEAELAKVRAEMEVLL--ASKARAEEESRS-TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1833
Cdd:PRK10246 486 QEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQAlEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDES 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1834 DAvRQRAEAERVLAEKLAAISEA--TRLKTEAEIA--LKEKEAENERLRRLAEDEAFQRRLLE--EQAAQHKADIEARLA 1907
Cdd:PRK10246 566 EA-QSLRQEEQALTQQWQAVCASlnITLQPQDDIQpwLDAQEEHERQLRLLSQRHELQGQIAAhnQQIIQYQQQIEQRQQ 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1908 QLR----------------------KASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 1965
Cdd:PRK10246 645 QLLtalagyaltlpqedeeaswlatRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHE 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1966 AEDTLRSK-----EQAEQEAARQRQLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEevERLKAKVEEARRLRER 2038
Cdd:PRK10246 725 QCLSLHSQlqtlqQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAAllDEETLTQLEQLK--QNLENQRQQAQTLVTQ 802
|
730 740 750
....*....|....*....|....*....|.
gi 1920237952 2039 AEQESARQLQLAQEAAQKRLQAEEKAHAFAV 2069
Cdd:PRK10246 803 TAQALAQHQQHRPDGLDLTVTVEQIQQELAQ 833
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1751-2072 |
1.15e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1751 QREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRlEAEAGRFRELAEEAARLralaeEAKRQRQL 1830
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKE----EKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM-----AMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1831 AEEDAVRQRAEAERVLAEKLAAisEATRLKtEAEIALKEKEAENERLRRLAEdEAFQRRLLEEQAAQHKADIEARLAQLR 1910
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1911 KASESELERQ-KGLVEDTLRQRRQVEEEilalkgsfekaaagKAELELELGRIRGTAEDTLRSKEQAEQEaaRQRQLAAE 1989
Cdd:pfam17380 427 AEQEEARQREvRRLEEERAREMERVRLE--------------EQERQQQVERLRQQEEERKRKKLELEKE--KRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1990 EERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARrlRERAEQESARQLQLAQE---AAQKRLQAEEKAHA 2066
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERrriQEQMRKATEERSRL 568
|
....*.
gi 1920237952 2067 FAVQQK 2072
Cdd:pfam17380 569 EAMERE 574
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2285-2501 |
1.17e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.00 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2285 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2364
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2365 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKvmlvQT 2444
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 2445 LETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA 2501
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2186-2625 |
1.39e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2186 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAenral 2265
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2266 vLRDKDSAQRLLQEEAEKMKQVAEEaarlsvaaqeaaRLRQLAEedlaqQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2345
Cdd:PRK03918 236 -LKEEIEELEKELESLEGSKRKLEE------------KIRELEE-----RIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2346 QKELAQEQARRLQEDKEQMA--QQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMsRAQARAEEDARRFRKQAED 2423
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSrlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2424 IGERLyrTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKqeAQLLQLKS---------EEMQTVRQEQ 2494
Cdd:PRK03918 377 LKKRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK--KAIEELKKakgkcpvcgRELTEEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2495 LLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEvAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAE 2574
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 2575 EGVRRQQEELQRLAqQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEE 2625
Cdd:PRK03918 532 EKLIKLKGEIKSLK-KELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1830-2530 |
1.42e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1830 LAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKAdiEARLAQL 1909
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLES--SREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1910 RKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQlaae 1989
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1990 eerrrrEAEERVQKSLAAEEEAAR---QRKAALE-EVERLKAKVE---EARRLRERAEQESARQLQLAQEAAQKRLQAEE 2062
Cdd:TIGR00606 319 ------RELVDCQRELEKLNKERRllnQEKTELLvEQGRLQLQADrhqEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2063 K-AHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQ 2141
Cdd:TIGR00606 393 KnFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2142 AQAAAEKLRKEAE---------------QEAARRAQAEQAALRQKQAADAEME----------------KHKQFAEQALR 2190
Cdd:TIGR00606 473 ILELDQELRKAERelskaeknsltetlkKEVKSLQNEKADLDRKLRKLDQEMEqlnhhtttrtqmemltKDKMDKDEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2191 Q-KAQVEQELTAL------RLQLEETDHQKS----ILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGklkariE 2259
Cdd:TIGR00606 553 KiKSRHSDELTSLlgyfpnKKQLEDWLHSKSkeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE------D 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2260 AENRALVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQeaaRLRQLAEED-----LAQQRALAEKMLKEKMQAVQEA 2333
Cdd:TIGR00606 627 KLFDVCGSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQ---FITQLTDENqsccpVCQRVFQTEAELQEFISDLQSK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2334 TRLkAEAELLQQQKELAQEQARRlqEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSR--AQARAE 2411
Cdd:TIGR00606 704 LRL-APDKLKSTESELKKKEKRR--DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllGTIMPE 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2412 EDARRFRKQAEDIGERLYRtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVR 2491
Cdd:TIGR00606 781 EESAKVCLTDVTIMERFQM-ELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
730 740 750
....*....|....*....|....*....|....*....
gi 1920237952 2492 QeQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2530
Cdd:TIGR00606 860 Q-HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
68-167 |
1.42e-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: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 68 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 143
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1920237952 144 LVNIRNDDIADGNPKLTLGLIWTI 167
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2448-2637 |
1.46e-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: 50.92 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2448 QRQQSDRDAERLREAIAELEHEKDKLKQEAQLL--QLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKA 2525
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALlkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2526 KLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASME------EARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2599
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237952 2600 EENQRLRERLQHLEEERRAALARSEEIAPSRAAAARAL 2637
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2336-2622 |
1.47e-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: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2336 LKAEAELLQQQKELAQEQARRlqedkEQMAQQLAQETQGfQKTLETERQrqlemsAEAERLRLRVAEMsraqaRAEEDAR 2415
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRL-----VEMARELEELSAR-ESDLEQDYQ------AASDHLNLVQTAL-----RQQEKIE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2416 RFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEA----QLLQLKsEEMQTVR 2491
Cdd:COG3096 351 RYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqQAVQAL-EKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2492 Q---------EQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQ------DEVAKAQA-------LREEQQRQQ 2549
Cdd:COG3096 430 GlpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiaGEVERSQAwqtarelLRRYRSQQA 509
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 2550 QQMQQEKqqLAASMEEARRRQHEAEEgVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALAR 2622
Cdd:COG3096 510 LAQRLQQ--LRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1331-1472 |
1.52e-05 |
|
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: 49.98 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1331 RTRYSELSTLTSQYIRFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaqakAQAEREAQglqR 1406
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKR----------YQDQLEAQ---R 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1407 RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQL 1472
Cdd:pfam12037 123 RRNEELLRKQEESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQ 188
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1351-1567 |
1.72e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.02 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1351 TLRRMEEEERLAEQQRAEERERLAEVEAALEkqrqlaEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQ 1430
Cdd:pfam02029 134 EIREKEYQENKWSTEVRQAEEEGEEEEDKSE------EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1431 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRV-VRLQLEATERQRGGAEG-ELQALRARAEEAEAQKRQAQEEAE 1508
Cdd:pfam02029 208 KSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLeAEQKLEELRRRRQEKESeEFEKLRQKQQEAELELEELKKKRE 287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1509 RLRRQVQDETQRKRQAEAELALRVQaeaeaaREKQRALQALEelRLQAEEAERRLRQAE 1567
Cdd:pfam02029 288 ERRKLLEEEEQRRKQEEAERKLREE------EEKRRMKEEIE--RRRAEAAEKRQKLPE 338
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1487-1751 |
1.76e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1487 QALRARAEEAEAQKRQAQEEAERLRRQVqDETQRKRQA--EAELALRVQAEAEAAREKQRALQA-LEELRLQAEEAERRL 1563
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1564 RQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerele 1643
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI---------------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1644 rwqlkanEALRLRLQAEEVAQQKSLtqaeaekqkeeaerearrrgKAEEQAVRQRelaEQELEKQRQLAEGTAQQRLAAE 1723
Cdd:COG3206 301 -------AALRAQLQQEAQRILASL--------------------EAELEALQAR---EASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*...
gi 1920237952 1724 QELIRLRAETeqgEQQRQLLEEELARLQ 1751
Cdd:COG3206 351 AELRRLEREV---EVARELYESLLQRLE 375
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1721-1816 |
1.81e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.49 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1721 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1800
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 1920237952 1801 EAEAGRFrELAEEAAR 1816
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1363-1517 |
1.97e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1363 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaqglQRRMQEEVARREEVAVEAQEQKRSIqeelqhlrqSSEA 1442
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE----IKRLELEIEEVEARIKKYEEQLGNV---------RNNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 1443 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1517
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2168-2615 |
2.09e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTalrlQLEETDHQKSILDEELQRLKAEVTEAARQRGQVE-----EELF 2242
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2243 SLRVQMEELgklKARIEAENRALVLRDkDSAQRLL---QEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALA 2319
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLemlQSKGLPKKSGEEDWERTRRIAEAEMQLGHL--EVLLDQKEKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2320 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqedkEQMAQQLAQETQgfqkTLETErqrqLEMSAEAERLRLR 2399
Cdd:pfam10174 208 NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL----ERNIRDLEDEVQ----MLKTN----GLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2400 VAEMSRAQARaeedarrFRK-QAEDIGERLYRTE---LATQEKVmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQ 2475
Cdd:pfam10174 276 QMEVYKSHSK-------FMKnKIDQLKQELSKKEselLALQTKL---ETLTNQNSDCKQHIEVLKESLTAKEQRAAILQT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2476 EAQLLQLKSEEMQTV-----RQEQLLQETQALQQSFLSE-KDSLLQRERCIEQEKAKLEQL---FQDEVAKAQALREEQQ 2546
Cdd:pfam10174 346 EVDALRLRLEEKESFlnkktKQLQDLTEEKSTLAGEIRDlKDMLDVKERKINVLQKKIENLqeqLRDKDKQLAGLKERVK 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 2547 RQQQQMQQEKQQLAaSMEEARRrqhEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEE 2615
Cdd:pfam10174 426 SLQTDSSNTDTALT-TLEEALS---EKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPE 490
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1401-2037 |
2.10e-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: 50.88 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1401 AQGLQR---RMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATER 1477
Cdd:pfam05483 73 SEGLSRlysKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1478 QRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElaLRVQAEaeaarekqralQALEELRLQAE 1557
Cdd:pfam05483 153 TRHLCN-LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE--LRVQAE-----------NARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1558 EAERRLRQAEAERARQV-----QVALETAQrSAEAElqsehasfaEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAE 1632
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEIndkekQVSLLLIQ-ITEKE---------NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1633 RARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQla 1712
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR-- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1713 egTAQQRLaaeqelirlraetEQGEQQRQLLEEELARLQREAAAATQ----KRRELEaELAKVRAEMEVLLASKARAEEE 1788
Cdd:pfam05483 367 --TEQQRL-------------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1789 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLkteaeialk 1868
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL--------- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1869 ekeaENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEI 1938
Cdd:pfam05483 500 ----ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENA 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1939 LALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKsLAAEEEAARQR--- 2015
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKfee 654
|
650 660 670
....*....|....*....|....*....|....*...
gi 1920237952 2016 ----------------KAALEEVERLKAKVEEARRLRE 2037
Cdd:pfam05483 655 iidnyqkeiedkkiseEKLLEEVEKAKAIADEAVKLQK 692
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1362-1790 |
2.21e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1362 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1441
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1442 AEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1521
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1522 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1601
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1602 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1681
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1682 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1761
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 1920237952 1762 RELEAELAKVRAEMEVLLASKARAEEESR 1790
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
71-178 |
2.30e-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: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 71 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 137
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1920237952 138 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 178
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2168-2373 |
2.31e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADA-----EMEKHKQFAEQALRQKaqveqeltalrlQLEETDH---------QKSILDEELQRLKAEVTEAARQ 2233
Cdd:NF012221 1561 LADKERAEAdrqrlEQEKQQQLAAISGSQS------------QLESTDQnaletngqaQRDAILEESRAVTKELTTLAQG 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2234 RGQVEEElfslRVQMEELGKlKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQ--------VAEEAARLSVAAQEAAR 2303
Cdd:NF012221 1629 LDALDSQ----ATYAGESGD-QWRNPFAGGLLdrVQEQLDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSEAGVAQGEQ 1703
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2304 LRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQ 2373
Cdd:NF012221 1704 NQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1548-1986 |
2.38e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 50.79 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1548 ALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQ---------LR 1618
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALrlaaalapfWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1619 EEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQR 1698
Cdd:COG3903 557 LRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1699 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVL 1778
Cdd:COG3903 637 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1779 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATR 1858
Cdd:COG3903 717 AAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1859 LKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEI 1938
Cdd:COG3903 797 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAA 876
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1920237952 1939 LALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQL 1986
Cdd:COG3903 877 AAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
66-174 |
2.48e-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: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 66 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 136
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237952 137 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 174
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1387-1602 |
2.49e-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: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1387 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQAKARQVEAAERsrlRIEEEIR 1466
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1467 VVRLQLEATERQrGGAEGELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDETQRKRQAEA 1526
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1527 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQ 1602
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3808-3844 |
2.51e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.51e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237952 3808 LRLLDAQLATGGIVDPRLGFHLPLDVAYQRGYLDKDT 3844
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1646-2064 |
2.60e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1646 QLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1725
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1726 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1805
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1806 RFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA 1885
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1886 FQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGT 1965
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1966 AEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2045
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 1920237952 2046 QLQLAQEAAQKRLQAEEKA 2064
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1280-1611 |
2.79e-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: 50.40 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1280 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESIIQEYVDLRTRY-SELSTLTSQyirfiSETLRRMEEE 1358
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1359 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ----RRMQEEVArreEVAVEAQEQKRSIQEELQ 1434
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPtntyKTLELEIA---ESDVEVKKAELELVKEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1435 HLRQSSEAEIQAKAR-QVEAAERSRLrieEEIRVVRLQLEATERQRGGAE-GELQALRARAEEAEAQKRQA--------- 1503
Cdd:NF033838 198 KEPRDEEKIKQAKAKvESKKAEATRL---EKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDKPKRRAkrgvlgepa 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1504 -----QEEAERLRRQVQDET-------QRKRQAEAE-LALRVQAEAEAAREKQR---ALQALEELRLQAEEAERRLRQAE 1567
Cdd:NF033838 275 tpdkkENDAKSSDSSVGEETlpspslkPEKKVAEAEkKVEEAKKKAKDQKEEDRrnyPTNTYKTLELEIAESDVKVKEAE 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1920237952 1568 A----ERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEH 1611
Cdd:NF033838 355 LelvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1854-2607 |
2.90e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.59 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1854 SEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQ 1933
Cdd:NF041483 22 AEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRPAYDGADIGYQAEQLLRNAQIQADQLRADAERELRDARA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1934 VEEEIlaLKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQ----------AEQEAARQRQLAAEEERRRREAEERVQK 2003
Cdd:NF041483 102 QTQRI--LQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQtveshvnenvAWAEQLRARTESQARRLLDESRAEAEQA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2004 SLAAEEEAARqrkAALEEVERLKAKVEEARRLRE----RAEQESARQLQLAQEAAQKRLQAEEKAHAF-------AVQQK 2072
Cdd:NF041483 180 LAAARAEAER---LAEEARQRLGSEAESARAEAEailrRARKDAERLLNAASTQAQEATDHAEQLRSStaaesdqARRQA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2073 EQELQQTLQQEQSVLERLR-----SEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAE 2147
Cdd:NF041483 257 AELSRAAEQRMQEAEEALRearaeAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2148 KLRKEAEQEAARRAQAEQAALRQKQAAdAEMEKHKQFAEQALRQKAQVEQELTalRLQLEETDHQKSILDEELQRLKAEV 2227
Cdd:NF041483 337 ADARAEAEKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVLTKASEDAKATT--RAAAEEAERIRREAEAEADRLRGEA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2228 TEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAAR-----LSVAAQEA 2301
Cdd:NF041483 414 ADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARtaeelLTKAKADA 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2302 ARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAQQLAQETQGFQKTLE 2380
Cdd:NF041483 494 DELRSTATAESERVRTEAiERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQ 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2381 TERQRQLE-MSAEAERlRLRVAEMSRAQARAEedARRFRKQAEDIGERLyRTELAtqekvmlvQTLETQRQQSDRDAERL 2459
Cdd:NF041483 571 AEAAEELTrLHTEAEE-RLTAAEEALADARAE--AERIRREAAEETERL-RTEAA--------ERIRTLQAQAEQEAERL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2460 R-EAIAELEHEkdKLKQEAQLLQLKSEEMQtvRQEQLLQETQALQQSFLSEKDSLLQRercIEQEKAKleqlfqdevaka 2538
Cdd:NF041483 639 RtEAAADASAA--RAEGENVAVRLRSEAAA--EAERLKSEAQESADRVRAEAAAAAER---VGTEAAE------------ 699
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2539 qalreeqqrqqqqmqqekqQLAASMEEARRRQHEAEEGVRRQQEEL-QRLAQQQQQQEKLLAEENQRLRE 2607
Cdd:NF041483 700 -------------------ALAAAQEEAARRRREAEETLGSARAEAdQERERAREQSEELLASARKRVEE 750
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
961-1531 |
2.95e-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: 50.50 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 961 DRLQAEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLRlpldkepaRECAQRITEQQK 1039
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLR--------RELDDRNMEVQR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1040 AQAEVDGL-----GKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEE 1114
Cdd:pfam15921 431 LEALLKAMksecqGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1115 VlraheeqlkeaqavpatlpeLEATKAALKKLRAQAEAQQPVFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRER 1191
Cdd:pfam15921 511 A--------------------IEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1192 VTLLLE-------RWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLR--DAKQRQEQIQAVPLANSQAvrEQLRQE 1262
Cdd:pfam15921 571 IENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRelEARVSDLELEKVKLVNAGS--ERLRAV 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1263 KALLEDIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesiiqeyvdLRTRYSELSTLTS 1342
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1343 qyirfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAHAQAKAqaereaqglqrrMQEEVARREEVAVEA 1422
Cdd:pfam15921 714 --------TLKSMEGSDGHA-------------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNA 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1423 QEQKRSIQEELQHLRQsseaeiqakarqveaaersrlrieeeirvvRLQLEATERQRggAEGELQALRA---RAEEAEAQ 1499
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQ------------------------------ELSTVATEKNK--MAGELEVLRSqerRLKEKVAN 808
|
570 580 590
....*....|....*....|....*....|..
gi 1920237952 1500 KRQAQEEAERLRRQVQDETQRKRQAEAELALR 1531
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2168-2470 |
3.13e-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: 49.68 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHkqfAEQALRQKAQVEQELTALRLQLEETDHQksildeeLQRLKAEVTEAARQRGQVEEELFSLRVQ 2247
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2248 MEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2326
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2327 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAQETQGFQKTLEterqrqlEMSAEAERLRLRVAEMSRA 2406
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRLA-------GLEADLERRTQQFQEMQRA 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 2407 QARAEEDARRFRKQAEDIGERLYRTE---LATQEKV-MLVQTLETQRQQSDRDAERLREaiaELEHEK 2470
Cdd:pfam19220 320 RAELEERAEMLTKALAAKDAALERAEeriASLSDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2184-2415 |
3.24e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 49.69 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2184 FAEQALRQKAQ---VEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQrgqveeelfsLRVQMEELGKLKARIEA 2260
Cdd:PRK11637 38 FSAHASDNRDQlksIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRK----------LRETQNTLNQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2261 ENRalvlrdkdSAQRLLQEEAEKMKqvaeeaarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQA----VQEAtRL 2336
Cdd:PRK11637 108 LNA--------SIAKLEQQQAAQER---------LLAAQLDAAFRQGEHTGLQLILSGEESQRGERILAyfgyLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2337 KAEAELLQQQKELAQEqaRRLQEDKEQMAQQLAQETQGFQKTLETER-----------------QRQL-EMSAEAERLRL 2398
Cdd:PRK11637 170 ETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEQARnerkktltglesslqkdQQQLsELRANESRLRD 247
|
250
....*....|....*...
gi 1920237952 2399 RVAEMSR-AQARAEEDAR 2415
Cdd:PRK11637 248 SIARAEReAKARAEREAR 265
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1421-1558 |
3.32e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1421 EAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGA---------EGELQA 1488
Cdd:COG1579 21 RLEHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1489 LRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEE 1558
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2247-2627 |
3.37e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 49.99 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2247 QMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2326
Cdd:COG5281 1 AAALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2327 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2406
Cdd:COG5281 81 AAALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2407 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2486
Cdd:COG5281 161 AAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2487 MQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEA 2566
Cdd:COG5281 241 SAAAQALAALAAAAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2567 R-RRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIA 2627
Cdd:COG5281 321 AqALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWA 382
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
873-1523 |
3.54e-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: 50.35 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 873 NQEAQEAIARlEAQHQALVALWhQLHTEMKSLLAWQSLGRDMQlirsWSLATFRTLKPEE------------QRQALRsL 940
Cdd:TIGR00618 223 VLEKELKHLR-EALQQTQQSHA-YLTQKREAQEEQLKKQQLLK----QLRARIEELRAQEavleetqerinrARKAAP-L 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 941 ELHYQAFLRDSQDAGGFGPEDRLQaEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRL 1020
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1021 PLDKEPARECAQRIT----EQQKAQAEVDGLGKGVARLSAEAEKVLALPEPSPAAptlRSELELTLGKLEQVRSLSAIYL 1096
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTtltqKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA---KKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1097 EKLKtisLVIRSTQEAEEVLRAHEEQLKEAQAVpaTLPELEATKAALKKLRAQAEAQQPVFDALR---------DELRGA 1167
Cdd:TIGR00618 452 QCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPL 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1168 QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakqRQEQIQAV 1247
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL---------QNITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1248 PLansqaVREQLRQEKALLEDIERHGEKVEECQRFAK--QYINAIKDYELQLVTYKAQLEpvASPAKKPKVQSGSESIIQ 1325
Cdd:TIGR00618 598 DL-----TEKLSEAEDMLACEQHALLRKLQPEQDLQDvrLHLQQCSQELALKLTALHALQ--LTLTQERVREHALSIRVL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1326 EYVDLRTRYSELSTLTSQY--IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQG 1403
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKeqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1404 LQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1483
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE 830
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1920237952 1484 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQ 1523
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1689-1911 |
3.73e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEEQAVRQRELAEQELEK-QRQLAEgtaqqrlaAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRE-LEA 1766
Cdd:COG1842 16 ALLDKAEDPEKMLDQAIRDmEEDLVE--------ARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREdLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1767 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1846
Cdd:COG1842 88 EALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 1847 AEklaaiseatrlkteAEIALKEKEAENERLRRLAEDEAFQRRLLEeqaAQHKADIEARLAQLRK 1911
Cdd:COG1842 168 ER--------------MEEKIEEMEARAEAAAELAAGDSLDDELAE---LEADSEVEDELAALKA 215
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1414-1767 |
3.89e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1414 RREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1493
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1494 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1573
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1574 VQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEAL 1653
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1654 RLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1733
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 1920237952 1734 EQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1767
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1398-1592 |
3.92e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 50.02 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1398 EREAQGLQRRMQEEVarreEVAVEAQEQKRSIQEELQhlrqsseaEIQAKARqveaAERSRL--RIE-EEIRVVRLQLEA 1474
Cdd:PTZ00491 643 ERTRDSLQKSVQLAI----EITTKSQEAAARHQAELL--------EQEARGR----LERQKMhdKAKaEEQRTKLLELQA 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1475 TerqrgGAEGELQAlRARAE-EAEAQKRQAQEEAErlrrqVQDETQRKRqaeaelALRVQAEAEAAREKQRALQALEELR 1553
Cdd:PTZ00491 707 E-----SAAVESSG-QSRAEaLAEAEARLIEAEAE-----VEQAELRAK------ALRIEAEAELEKLRKRQELELEYEQ 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237952 1554 LQAE---EAERRLRQAEAERARQVQVAL--ETAQRSAEA--ELQSE 1592
Cdd:PTZ00491 770 AQNEleiAKAKELADIEATKFERIVEALgrETLIAIARAgpELQAK 815
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1110-1609 |
3.95e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1110 QEAEEVLRAHEEQlkeaQAVPATLPELEATKAALKK-LRAQAEAQQpvfdaLRDELRGAQEVG-------ERLQQRHGER 1181
Cdd:PRK04863 496 DVARELLRRLREQ----RHLAEQLQQLRMRLSELEQrLRQQQRAER-----LLAEFCKRLGKNlddedelEQLQEELEAR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1182 ----DVEVERWRERVTLLlerwQAVLAQTDVRQRELEQLGRQLRYYRESADPL----GAWLRDAKQRQEQIQ--AVPLAN 1251
Cdd:PRK04863 567 leslSESVSEARERRMAL----RQQLEQLQARIQRLAARAPAWLAAQDALARLreqsGEEFEDSQDVTEYMQqlLERERE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1252 SQAVREQLRQEK-ALLEDIER----HGEKVEECQRFAKQ-------------------YINA-------------IKDYE 1294
Cdd:PRK04863 643 LTVERDELAARKqALDEEIERlsqpGGSEDPRLNALAERfggvllseiyddvsledapYFSAlygparhaivvpdLSDAA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1295 LQLVT--------YKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSelstltsqyiRFISETL-RRMEEEERLAEQQ 1365
Cdd:PRK04863 723 EQLAGledcpedlYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYS----------RFPEVPLfGRAAREKRIEQLR 792
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1366 RaeERERLAEveaalekqrqlaeahaqAKAQAEREAQGLQRRMQE---------EVARREEVAVEAQEQKRSIQEELQHL 1436
Cdd:PRK04863 793 A--EREELAE-----------------RYATLSFDVQKLQRLHQAfsrfigshlAVAFEADPEAELRQLNRRRVELERAL 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1437 RQSSEAEIQAKARQVEAAERSRL--------------RIEEEIRVVRLQLEATE------RQRGGA----EGELQALRAR 1492
Cdd:PRK04863 854 ADHESQEQQQRSQLEQAKEGLSAlnrllprlnlladeTLADRVEEIREQLDEAEeakrfvQQHGNAlaqlEPIVSVLQSD 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1493 AEEAEAQKR---QAQEEAERLRRQVQDET---QRKRQAEAELALRVQAEAEAAREKQRalQALEELRLQAEEAERRLRQA 1566
Cdd:PRK04863 934 PEQFEQLKQdyqQAQQTQRDAKQQAFALTevvQRRAHFSYEDAAEMLAKNSDLNEKLR--QRLEQAEQERTRAREQLRQA 1011
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1920237952 1567 EAERARQVQValetaqrsaEAELQSEHASFAEKTAQLERTLKE 1609
Cdd:PRK04863 1012 QAQLAQYNQV---------LASLKSSYDAKRQMLQELKQELQD 1045
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
964-1402 |
4.11e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 964 QAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRITE 1036
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1037 QQKAQAEVDGLGKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVL 1116
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1117 R------AHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRE 1190
Cdd:COG4717 233 EneleaaALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1191 RVTLLLERWQAVLAQTDVRQREleqlgrQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEkALLEDIE 1270
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE-AGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1271 RHGEKVEECQRFaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELstltSQYIRFISE 1350
Cdd:COG4717 386 ELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL----REELAELEA 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1351 TLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQ 1402
Cdd:COG4717 461 ELEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1348-1572 |
4.30e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1348 ISETLRRMEEEERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQglqRRMQEEVARREEVavEAQEQKR 1427
Cdd:pfam02029 100 VAERKENNEEEENSSWEKEEKRDSRLGRYKEE-ETEIREKEYQENKWSTEVRQAE---EEGEEEEDKSEEA--EEVPTEN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1428 SIQEELQHLRQSSEAEIQAKARQVEaaERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKrQAQEEA 1507
Cdd:pfam02029 174 FAKEEVKDEKIKKEKKVKYESKVFL--DQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFL-EAEQKL 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1508 ERLRRQVQD------ETQRKRQAEAELALrvqAEAEAAREKQRAL--------QALEELRLQAEEAERRLRQAEAERAR 1572
Cdd:pfam02029 251 EELRRRRQEkeseefEKLRQKQQEAELEL---EELKKKREERRKLleeeeqrrKQEEAERKLREEEEKRRMKEEIERRR 326
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3361-3399 |
4.53e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.09 E-value: 4.53e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3361 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3399
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1096-1564 |
4.69e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.74 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1096 LEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraQAEAQQpVFDALRDELRGAQEVGERLQ 1175
Cdd:pfam05557 51 QELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1176 QRHGERDVEVERWRERVTLLLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLRDAKQRQEQIqavpl 1249
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1250 ANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK------------PKVQ 1317
Cdd:pfam05557 200 PELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaqdtglnlRSPE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1318 SGSESIIQEYVDLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL---------- 1386
Cdd:pfam05557 280 DLSRRIEQLQQREIVLKEENSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgy 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1387 ------------AEAHAQAKAQAEREAQGLQRRMQ---EEVARREEVAVEA----QEQKRSIQEELQHLRQ--------S 1439
Cdd:pfam05557 359 railesydkeltMSNYSPQLLERIEEAEDMTQKMQahnEEMEAQLSVAEEElggyKQQAQTLERELQALRQqesladpsY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1440 SEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DE 1517
Cdd:pfam05557 439 SKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlKR 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1920237952 1518 TQRKRQAEAELALRVQAEAEAAREKQralqaLEELRLQAEEAERRLR 1564
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3361-3396 |
4.75e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.75e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1920237952 3361 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3396
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1362-1759 |
4.93e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1362 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEElqhlrqsse 1441
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1442 aeiqaKARQVEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1521
Cdd:COG3064 75 -----AAKKLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1522 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTA 1601
Cdd:COG3064 144 AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1602 QLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAE 1681
Cdd:COG3064 224 RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAAL 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 1682 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQ 1759
Cdd:COG3064 304 AAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLA 381
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1838-2228 |
4.94e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1838 QRAEAERVLAEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRLLEEQAAqhkadIEARLAQLRKASESEL 1917
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAA-----IYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1918 ERQKglVEDTLRQRRQVEEEilalkgsfekaaagkaELELELGRIRGTaeDTLRSKEQAEQEAARQRqlaaeeerrrrea 1997
Cdd:pfam17380 351 ERIR--QEERKRELERIRQE----------------EIAMEISRMREL--ERLQMERQQKNERVRQE------------- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1998 EERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKeqel 2076
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK---- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2077 qqtlqqeqsvleRLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQE 2156
Cdd:pfam17380 474 ------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2157 aarraqaeqaalRQKQaadAEMEKHKQFAEQALRqkaqVEQELTALRLQLEETDHQKSILDEELQRLKAEVT 2228
Cdd:pfam17380 542 ------------RRKQ---QEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4147-4175 |
5.40e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.40e-05
10 20
....*....|....*....|....*....
gi 1920237952 4147 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4175
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1528-1797 |
5.41e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1528 LALRVQAEAEAAREKQRALQALEElRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTL 1607
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1608 KEEHVAVVQLREeatrraqqqaeaeRARAEAERELERWQLKANEALRLRLQAEEVAQqksltqaeaekqKEEAEREARRR 1687
Cdd:COG4942 90 KEIAELRAELEA-------------QKEELAELLRALYRLGRQPPLALLLSPEDFLD------------AVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1688 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAE 1767
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260 270
....*....|....*....|....*....|
gi 1920237952 1768 LAKVRAEMEVLLASKARAEEESRSTSEKSK 1797
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1658-1834 |
5.59e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1658 QAEEVAQQKsltQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1733
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1734 EQGEQQRQLLEEELArlQREAAAATQKRRELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1808
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 1920237952 1809 ELAEEAARLRALAEEAKRQRQLAEED 1834
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
70-171 |
5.73e-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: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 70 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 145
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1920237952 146 NIRNDDIADGNPKLTLGLIWTIILHF 171
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1698-2410 |
5.80e-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: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1698 RELAEQELEKQRQLAEGTAQQRLAAE---QELIRLRAETEQGEQQRQLLEEELARLQ-REAAAATQK-RRELEAELA--- 1769
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKiLRELDTEISylk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1770 ----KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAER 1844
Cdd:pfam15921 238 grifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1845 VLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQL-----RKASESELER 1919
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEK 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1920 QK-----------GLVEDTLRQR---RQVEEEIL-ALKGSFEKAAAGkaELELELGRIRGtaedtlrSKEQAEQEAARQR 1984
Cdd:pfam15921 398 EQnkrlwdrdtgnSITIDHLRRElddRNMEVQRLeALLKAMKSECQG--QMERQMAAIQG-------KNESLEKVSSLTA 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1985 QLAAEEERRRREAEERVQKSLAAE--EEAARQRKAALEEVER-LKAKVEEARRLRERAEQesarQLQLAQEaaqkrLQAE 2061
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLEssERTVSDLTASLQEKERaIEATNAEITKLRSRVDL----KLQELQH-----LKNE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2062 EKaHAFAVQQKEQELQQTLQQEQSVLERLRseaeaarraaeeaeaareraereaaqsrRQVEEAERLkqsaeeqaqaqaq 2141
Cdd:pfam15921 540 GD-HLRNVQTECEALKLQMAEKDKVIEILR----------------------------QQIENMTQL------------- 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2142 aqaaaeklrkeaeqeaarraqaeqaalrqkqaadaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQ 2221
Cdd:pfam15921 578 ------------------------------------VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2222 RLKAEVTEAARQRGQV----EEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLLQEEAEKMKQVAEE-AARL 2294
Cdd:pfam15921 622 ELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKlKMQL 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2295 SVAAQEAARLR---QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAqe 2371
Cdd:pfam15921 702 KSAQSELEQTRntlKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS-- 779
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1920237952 2372 tqgfqkTLETERQR---QLE-MSAEAERLRLRVAEMSRAQARA 2410
Cdd:pfam15921 780 ------TVATEKNKmagELEvLRSQERRLKEKVANMEVALDKA 816
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2168-2618 |
5.98e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHKQFA--EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSL 2244
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTklQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTlDDQWKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2245 R----VQMEELGKLKARIEA-ENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAA---------RLRQLAEE 2310
Cdd:pfam12128 307 NgelsAADAAVAKDRSELEAlEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKhqdvtakynRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2311 DLA------QQRALAEKMLKEKMQAVQEATRLKAEAEL---LQQQKELAQEQARRLQEDKEQMAQQLAQETQGfQKTLET 2381
Cdd:pfam12128 387 QNNrdiagiKDKLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2382 ERQRQLEMSAEAERLRLRVAEMSRAQaraeEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQ-RQQSDRDAERLR 2460
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQ----SELRQARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2461 EAIAELEHEKDKLKQEAQL----LQLKSEEMQTVRQEQLLQETQALQQSflsEKDSLLQRERCIEQEKAKLEQLFQDEVA 2536
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLhrtdLDPEVWDGSVGGELNLYGVKLDLKRI---DVPEWAASEEELRERLDKAEEALQSARE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2537 KAQALreeqqrqqqqmQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLA----QQQQQQEKLLAEENQRLRERLQHL 2612
Cdd:pfam12128 619 KQAAA-----------EEQLVQANGELEKASREETFARTALKNARLDLRRLFdekqSEKDKKNKALAERKDSANERLNSL 687
|
....*.
gi 1920237952 2613 EEERRA 2618
Cdd:pfam12128 688 EAQLKQ 693
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1348-1553 |
6.03e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1348 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-REEVAVEAQEQK 1426
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1427 RSIQEELQHLRQsseaeiqakarQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKR----- 1501
Cdd:COG1842 94 AELEAQAEALEA-----------QLAQLEEQVEKLKEALRQLESKLEELKAKK-------DTLKARAKAAKAQEKvneal 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1502 ------QAQEEAERLRRQVqDETQRKRQAEAELALR--VQAEAEAAREKQRALQALEELR 1553
Cdd:COG1842 156 sgidsdDATSALERMEEKI-EEMEARAEAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
208-285 |
6.10e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 44.60 E-value: 6.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 208 DNFTTSWRDGRLFNAIIHRHKPTLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 285
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1712-2208 |
6.32e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.47 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1712 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV----------RAEMEVLLAS 1781
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1782 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKT 1861
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1862 EAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILAL 1941
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1942 KGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2021
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2022 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAA 2101
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2102 EEAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2181
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 1920237952 2182 KQFAEQALRQKAQVEQELTALRLQLEE 2208
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1439-1652 |
6.99e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1439 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1516
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1517 -ETQRKRQAEAELAL------------RVQAEAEAAREKQRALQALEELRLQAEEAerrlrQAEAERARQVQVALETAQR 1583
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1584 SAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEA 1652
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1835-2046 |
7.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1835 AVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIeARLAQLRKASE 1914
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-AELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1915 SELERQKGLVEDTL----RQRRQVEEEILALKGSFEKAAAGKA-------ELELELGRIRGTAEDTLRSKEQAEQEAARQ 1983
Cdd:COG4942 97 AELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQylkylapARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 1984 RQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ 2046
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3142-3178 |
7.03e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 7.03e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1920237952 3142 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGYLDKET 3178
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1319-1621 |
7.24e-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: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1319 GSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQ--------RQLAEAH 1390
Cdd:pfam19220 63 AYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEA-LERQlaaeteqnRALEEEN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1391 AQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRsiqeeLQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRL 1470
Cdd:pfam19220 142 KALREEAQAAEKALQRAEGELATARERLALLEQENRR-----LQALSEEQAAELAELTRRLAELETQLDATRARLRALEG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1471 QL--EATERQRGGAEGELQALRARAEEAEaqkrqaqeeaerLRRQVQDETQRKRQAE---AELALRVQAEAEAAREKQRa 1545
Cdd:pfam19220 217 QLaaEQAERERAEAQLEEAVEAHRAERAS------------LRMKLEALTARAAATEqllAEARNQLRDRDEAIRAAER- 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 1546 lqALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSE--HASFAEKTAQLERTlkEEHVAVVQLREEA 1621
Cdd:pfam19220 284 --RLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEmlTKALAAKDAALERA--EERIASLSDRIAE 357
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2280-2415 |
7.35e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.72 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2280 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2359
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 2360 DKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDAR 2415
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE 328
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2010-2354 |
7.80e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2010 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2081
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2082 qeqsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERlKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArra 2161
Cdd:pfam17380 362 -----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKVEMEQIRAEQEEA--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2162 qaeqaalRQKQAADAEMEKhkqfaeqalrqkaqvEQELTALRLQLEETDHQKSILDEElqrlkaevtEAARQRGQVEeel 2241
Cdd:pfam17380 433 -------RQREVRRLEEER---------------AREMERVRLEEQERQQQVERLRQQ---------EEERKRKKLE--- 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2242 fslrvqMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEK 2321
Cdd:pfam17380 479 ------LEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
330 340 350
....*....|....*....|....*....|....*..
gi 1920237952 2322 MLKEKMQ-AVQEATRLKA---EAELLQQQKELAQEQA 2354
Cdd:pfam17380 553 RIQEQMRkATEERSRLEAmerEREMMRQIVESEKARA 589
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1415-1575 |
7.83e-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: 48.98 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1415 REEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE 1494
Cdd:pfam07111 490 RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELT 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1495 EAEAQKRQAQEEA-----ERLRRQVQDETQ-----RKRQAEAELALRvQAEAEAAREKQRAlqalEELRLQAEEAerrlR 1564
Cdd:pfam07111 570 QQQEIYGQALQEKvaeveTRLREQLSDTKRrlneaRREQAKAVVSLR-QIQHRATQEKERN----QELRRLQDEA----R 640
|
170
....*....|..
gi 1920237952 1565 QAEAER-ARQVQ 1575
Cdd:pfam07111 641 KEEGQRlARRVQ 652
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1483-1617 |
8.18e-05 |
|
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: 48.22 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1483 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDetqRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERR 1562
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1563 LRQAEAERARQ-VQVALETAQRSAEAELQSE-HA---SFAEKTAQLERTLKEEHVAVVQL 1617
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlHQlteTLIQKQTMLEALSTEKNSLVLQL 200
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2187-2414 |
8.61e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2187 QALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKL--KARIEAENRA 2264
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2265 LVLRDKDSAQRLLQE--EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2342
Cdd:COG3883 93 RALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2343 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDA 2414
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1833-2311 |
8.82e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1833 EDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLleEQAAQHKADIEARLAQLRKA 1912
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1913 seselerqkglvedtLRQRRQVEEEILALKgsfEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEER 1992
Cdd:COG4717 155 ---------------LEELRELEEELEELE---AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1993 RRREAEervqKSLAAEEEAARQRKAALEEVERLKakveearRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQK 2072
Cdd:COG4717 217 EAQEEL----EELEEELEQLENELEAAALEERLK-------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2073 EQELQQTLQQEQSVLERLRseaeaarraaeeaEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKE 2152
Cdd:COG4717 286 LALLFLLLAREKASLGKEA-------------EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2153 AEQEAARRAQAEQAALRQKQAADaeMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQ-KSILDEELQRLKAEVTEAA 2231
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2232 RQR-GQVEEELFSLRVQMEELGKLKARIEAENRAlvLRDKDSAQRLLQEEAE---KMKQVAEEAARLSVAAQEAARLRQL 2307
Cdd:COG4717 431 EEElEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEElkaELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1920237952 2308 AEED 2311
Cdd:COG4717 509 YREE 512
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1885-2410 |
1.06e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 48.72 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1885 AFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEkAAAGKAELELELGRIRG 1964
Cdd:COG3321 867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA-LLALVALAAAAAALLAL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1965 TAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2044
Cdd:COG3321 946 AAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALA 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2045 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEE 2124
Cdd:COG3321 1026 ALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAA 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2125 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRL 2204
Cdd:COG3321 1106 LLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAAL 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2205 QLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEElgklkARIEAENRALVLRDKDSAQRLLQEEAEKM 2284
Cdd:COG3321 1186 AAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAA-----ALALLALAAAAAAVAALAAAAAALLAALA 1260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2285 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2364
Cdd:COG3321 1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1920237952 2365 AQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARA 2410
Cdd:COG3321 1341 LALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1522-1806 |
1.11e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1522 RQAEAELALRVQAEAEAAREKQR--ALQAleelRLQAEEAER--RLRQAEAERARQVQVALETAQRSAEAELQSEHASFA 1597
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARfeARQA----RLEREKAAReaRHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1598 EKTAQlertlKEEHVAVVQLREEATRRAQQQAEAERARAEAERelerwQLKANEALRLRLQAEEVAQQKSLTqaeAEKQK 1677
Cdd:PRK05035 508 IKAGA-----RPDNSAVIAAREARKAQARARQAEKQAAAAADP-----KKAAVAAAIARAKAKKAAQQAANA---EAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1678 EEAEREARRRGKAEEQAvrqRELAEQELEKQRQLAEGTAQQRLAAEQELIrLRAETEQGEQQRQLLEEElarlqreaaAA 1757
Cdd:PRK05035 575 VDPKKAAVAAAIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAI-ARAKAKKAEQQANAEPEE---------PV 641
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1920237952 1758 TQKRRELEAELAKVRAEmevlLASKARAEEESRSTSEKSKQRLEAEAGR 1806
Cdd:PRK05035 642 DPRKAAVAAAIARAKAR----KAAQQQANAEPEEAEDPKKAAVAAAIAR 686
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1692-2402 |
1.15e-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: 48.56 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1692 EQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR-----LQREAAAATQKRRELEA 1766
Cdd:pfam05483 98 EAELKQKENKLQENRKIIE-AQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1767 ELAKVR---AEMEVLLASKARAEEESRSTSEKSkqRLEAEAgrfrELAEEAARLRALAEEAKRQRQlaeedavrqraEAE 1843
Cdd:pfam05483 177 EREETRqvyMDLNNNIEKMILAFEELRVQAENA--RLEMHF----KLKEDHEKIQHLEEEYKKEIN-----------DKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1844 RVLAEKLAAISEATRLKTEAEIALKEKEaenERLRRLAEDEAFQRRLLEeQAAQHKADIEARLAQLRKASESELERQKGL 1923
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESR---DKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1924 VED---TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEerrrreaeer 2000
Cdd:pfam05483 316 EEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME---------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2001 VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQAEEK-AHAFAVQqkeqeLQ 2077
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeIHDLEIQ-----LT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2078 QTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqea 2157
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM----------------------------- 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2158 arraqaeQAALRQKQAadaEMEKHKQFAEQALRQKAQVEQELTALRLQLE--------ETDHQKSILD---EELQRLKAE 2226
Cdd:pfam05483 512 -------TLELKKHQE---DIINCKKQEERMLKQIENLEEKEMNLRDELEsvreefiqKGDEVKCKLDkseENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2227 VTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEeaarLSVAAQEAARLRQ 2306
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE----LASAKQKFEEIID 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2307 LAEEDLAQQRALAEKMLKEKMQA---VQEATRLKAEAELLQQQK--------ELAQEQARRLQEDKEQ---MAQQLAQET 2372
Cdd:pfam05483 658 NYQKEIEDKKISEEKLLEEVEKAkaiADEAVKLQKEIDKRCQHKiaemvalmEKHKHQYDKIIEERDSelgLYKNKEQEQ 737
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1920237952 2373 QGFQKTLETER----------QRQLEMS-AEAERLRLRVAE 2402
Cdd:pfam05483 738 SSAKAALEIELsnikaellslKKQLEIEkEEKEKLKMEAKE 778
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
71-168 |
1.21e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 71 QKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 137
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1920237952 138 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 168
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1494-1573 |
1.23e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.41 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1494 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAE------AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1566
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvaleglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 1920237952 1567 EAERARQ 1573
Cdd:PRK11448 218 RKEITDQ 224
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1496-1621 |
1.29e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1496 AEAQKRQAQEEAERLRRQVQDETQRKRQAEaELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLR----QAEAERA 1571
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAlkqkQAEEAAA 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1572 RQVQVA----------LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1621
Cdd:PRK09510 140 KAAAAAkakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA 199
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1168-1573 |
1.31e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1168 QEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAV 1247
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1248 planSQAVREQLRQEKALLED---IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSE--- 1321
Cdd:TIGR00606 774 ----LGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIElnr 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1322 SIIQEYVD-LRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQR---------AEERERLAEVEAALEKQRQLAEAHA 1391
Cdd:TIGR00606 850 KLIQDQQEqIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTevqslireiKDAKEQDSPLETFLEKDQQEKEELI 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1392 QAKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1471
Cdd:TIGR00606 930 SSKETSNKKAQDKVNDIKEKV---KNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD 1006
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1472 LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALrvqaeaeAAREKQRALQALEE 1551
Cdd:TIGR00606 1007 IDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKRNHVLALGRQKG 1079
|
410 420
....*....|....*....|..
gi 1920237952 1552 LRLQAEEAERRLRQAEAERARQ 1573
Cdd:TIGR00606 1080 YEKEIKHFKKELREPQFRDAEE 1101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2009-2622 |
1.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2009 EEAARQRKAALEEVERLKAKVEEARRlreraeqeSARQLQLAQEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqSVLE 2088
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERYAAARERL--------------------AELE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2089 RLRSEAEAARRAAEEAEAARERAEREAAQSRRQvEEAERLKQsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2168
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAELEELRAELARLE-AELERLEA-----------------RLDALREELDELEAQIRGNGG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2169 RQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETdhqKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQM 2248
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2249 EELGKLKARIEAENRALVLRDKDSAQRLLQeeaekMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2323
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSNIPARLLA-----LRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2324 ------KEKMQAVQEAT-RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETE--RQRQLEMSAEAE 2394
Cdd:COG4913 489 ltllvpPEHYAAALRWVnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgRRFDYVCVDSPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2395 RLRLRVAEMSRA-QARAeeDARRFRKQAEDIGERLYRTELATQEKvmlVQTLETQRQQSDRDAERLREAIAELEHEKDKL 2473
Cdd:COG4913 569 ELRRHPRAITRAgQVKG--NGTRHEKDDRRRIRSRYVLGFDNRAK---LAALEAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2474 KQEAQLLQ-LKSEEMQTVRQEQLLQETQALQQsflsekdsllQRERcIEQEKAKLEQLfQDEVAKAQALREEQQRQQQQM 2552
Cdd:COG4913 644 QERREALQrLAEYSWDEIDVASAEREIAELEA----------ELER-LDASSDDLAAL-EEQLEELEAELEELEEELDEL 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 2553 QQEKQQLAASMEEARRRQHEAEEGVRRqQEELQRLAQQQQQQEKLLAEENQRLRERL-QHLEEERRAALAR 2622
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEA-AEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRAR 781
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2191-2434 |
1.39e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.53 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2191 QKAQVEQELTALRLQleetdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2270
Cdd:TIGR02794 44 DPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2271 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAELLQ 2344
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2345 QQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQaedI 2424
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA---I 272
|
250
....*....|
gi 1920237952 2425 GERLYRTELA 2434
Cdd:TIGR02794 273 QQNLYDDPSF 282
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1358-1587 |
1.39e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 47.67 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1358 EERLAEQQRAEERERLAEVEAAlEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELqhlr 1437
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGA-EISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1438 qsSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1517
Cdd:PRK07735 86 --TEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1518 TQRKRQAEAELALrvqaeaEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEA 1587
Cdd:PRK07735 164 KAKAKAAAAAKAK------AAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGN 227
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3105-3141 |
1.45e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.45e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237952 3105 KLLSAEKAVTGYKDPYSGQSVSLFQALKKGLIPREQG 3141
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2278-2376 |
1.48e-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: 47.19 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2278 QEEAEKMKQVAEEAARLSVAAQEAARL----RQLAEEDLAQQRALAE--KMLKEKMQavQEATRLKAEAELLQQQKElaQ 2351
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLeeqqRELEQKLEDQERSYEEhlRQLKEKME--EERENLLKEQERALESKL--K 266
|
90 100
....*....|....*....|....*
gi 1920237952 2352 EQARRLQEDKEQMAQQLAQETQGFQ 2376
Cdd:cd16269 267 EQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2185-2574 |
1.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2185 AEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT--EAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2262
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2263 RALVlRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKekmQAVQEATRLKAEAEL 2342
Cdd:COG4717 156 EELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE---EAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2343 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLET----------------------ERQRQLEMSAEAERLRLRV 2400
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlgllallfllLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2401 AEMSRAQARAEEDARRFRKQAEDIGER---LYRTELATQEKVMLVQTLETQRQQSDRDAER---LREAIAELEHEKDKLK 2474
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEElleLLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2475 QEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQ 2554
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|
gi 1920237952 2555 EKQQLAASMEEARRRQHEAE 2574
Cdd:COG4717 472 AELLQELEELKAELRELAEE 491
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2184-2350 |
1.53e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.54 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2184 FAEQALrqkAQVEQELTALRLQLEETDHQKSILDEElqrlkAEVTEAARQRGQVEEELFSLRVQMEELgklkarieaenR 2263
Cdd:COG3524 181 FAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAAL-----------R 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2264 AlVLRDKDSAQRLLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEAE 2341
Cdd:COG3524 242 S-YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEAA 317
|
....*....
gi 1920237952 2342 llQQQKELA 2350
Cdd:COG3524 318 --RQQRYLA 324
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1431-1805 |
1.53e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1431 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEAT----ERQRGGAEGELQALRARAEEAEAQKRQAQEE 1506
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1507 AERL---RRQVQDETQRKRQAEAELALRVQAEAEAAREKQralQALEELRLQAEEAERRLRQAEAERaRQVQVALETAQ- 1582
Cdd:pfam07888 110 SEELseeKDALLAQRAAHEARIRELEEDIKTLTQRVLERE---TELERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1583 --RSAEAELQSEHASFAEKTAQLERtLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLqaE 1660
Cdd:pfam07888 186 elRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV-EGLGEEL--S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1661 EVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1740
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 1741 QLLEEELArlqREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1805
Cdd:pfam07888 342 EKLEVELG---REKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1692-1887 |
1.58e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1692 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1768
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1769 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1833
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 1834 DAVRQRAEAERVLAEKLAAIS-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1887
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1321-1532 |
1.64e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1321 ESIIQEYVDLRTRYSelSTLTSQYIRFISETLRRMEEEERLAEQQRAEERERL------AEVEAALEKQRQLAEAHAQAK 1394
Cdd:COG3206 155 NALAEAYLEQNLELR--REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlsEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1395 AQAeREAQGLQRRMQEEVARREEVAVEA-------------QEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRI 1461
Cdd:COG3206 233 AEL-AEAEARLAALRAQLGSGPDALPELlqspviqqlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1462 EEEIRVVRLQLEATERQRGGAEGELQALRARAE---EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRV 1532
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV 385
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3977-4011 |
1.65e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.65e-04
10 20 30
....*....|....*....|....*....|....*
gi 1920237952 3977 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4011
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1723-1873 |
1.73e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1723 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLE 1801
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1802 AE----AGRFRELAEEAARLRALAEEAKRQRQLAEEdavrQRAEAERVLAEKLAAISEATRlKTEAEIALKEKEAE 1873
Cdd:COG1579 96 KEieslKRRISDLEDEILELMERIEELEEELAELEA----ELAELEAELEEKKAELDEELA-ELEAELEELEAERE 166
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2185-2619 |
1.78e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2185 AEQALRQKAQVEQELTALRLQL-------EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLK-A 2256
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApA 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2257 RIEAENRALVLRD------KDSA------QRLLQEE----------AEKMKQVAEEAARLSVAA-QEAARLRQLAE---- 2309
Cdd:COG3096 604 WLAAQDALERLREqsgealADSQevtaamQQLLEREreatverdelAARKQALESQIERLSQPGgAEDPRLLALAErlgg 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2310 -------EDLAQQRA-LAEKMLKEKMQA--VQEATRLKAEAE----------LLQQQKELAQEQARRLQEDKEQMAQQLA 2369
Cdd:COG3096 684 vllseiyDDVTLEDApYFSALYGPARHAivVPDLSAVKEQLAgledcpedlyLIEGDPDSFDDSVFDAEELEDAVVVKLS 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2370 QETQGFQKTLE------TERQRQLE-MSAEAERLRLRVAEMS---RAQARAEEDARRFrkqaedIGERLYRTELATQEKV 2439
Cdd:COG3096 764 DRQWRYSRFPEvplfgrAAREKRLEeLRAERDELAEQYAKASfdvQKLQRLHQAFSQF------VGGHLAVAFAPDPEAE 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2440 MlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQsflsEKDSLLQRERC 2519
Cdd:COG3096 838 L--AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELRE----ELDAAQEAQAF 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2520 IEQEKAKLEQLfqdeVAKAQALReeqqrqqqQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLA 2599
Cdd:COG3096 912 IQQHGKALAQL----EPLVAVLQ--------SDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLL 979
|
490 500
....*....|....*....|....
gi 1920237952 2600 EENQ----RLRERLQHLEEERRAA 2619
Cdd:COG3096 980 GENSdlneKLRARLEQAEEARREA 1003
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1805-2051 |
1.95e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1805 GRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1884
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1885 AFQRRLLEEQAAQHKADIE------ARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELE 1958
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIReleediKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1959 LGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2037
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 1920237952 2038 RAEQESAR-QLQLAQ 2051
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2189-2629 |
2.03e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2189 LRQKAQVEQ-ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIeaenralvl 2267
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2268 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2347
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2348 ELAQEQARRLQEDKEQMAQQLAQET--QGFQKTLETERQRQLEMSAEAERLRlrvAEMSRAQARAEEDARRFRKQAEDIG 2425
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2426 ERL--YRTELAT--QEKVMLVQTLETQRQQSD----------------------------RDAERLREAIAELEHEKDKL 2473
Cdd:PRK01156 416 VKLqdISSKVSSlnQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeksnhiinhynEKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2474 KQEAQLLQ-----LKSEEM-QTVRQEQLLQETQALQQSFLSE----KDSLLQRERCIEQEKA-KLEQLFQDEVAKAQALR 2542
Cdd:PRK01156 496 DEKIVDLKkrkeyLESEEInKSINEYNKIESARADLEDIKIKinelKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2543 EEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEG-----------VRRQQEELQRLaqqqqQQEKLLAEENQRLRERLQH 2611
Cdd:PRK01156 576 VISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpddksyidksIREIENEANNL-----NNKYNEIQENKILIEKLRG 650
|
490
....*....|....*...
gi 1920237952 2612 LEEERRAALARSEEIAPS 2629
Cdd:PRK01156 651 KIDNYKKQIAEIDSIIPD 668
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4286-4319 |
2.26e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237952 4286 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4319
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2183-2629 |
2.31e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2183 QFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2262
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2263 RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2342
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2343 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2422
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2423 DIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQAL 2502
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2503 QQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQE 2582
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1920237952 2583 ELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2629
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALA 522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1321-1665 |
2.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1321 ESIIQEYVDLRTRYSELST---LTSQYIRFISETLRRMEEEERLAE-QQRAEE-RERLAEVEAALEKQRQLAEAHAQAKA 1395
Cdd:COG4717 98 EELEEELEELEAELEELREeleKLEKLLQLLPLYQELEALEAELAElPERLEElEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1396 QAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQ---- 1471
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE----ELEELEEELEQLENELEAAALEERLKEARllll 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1472 --------------LEATERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQ 1533
Cdd:COG4717 254 iaaallallglggsLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1534 AEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV----------------------QVALETAQRSAEAELQS 1591
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeelraaleqaeeYQELKEELEELEEQLEE 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1592 -----EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKAnEALRLRLQAEEVAQQ 1665
Cdd:COG4717 414 llgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ-ELEELKAELRELAEE 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2388-2622 |
2.44e-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: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2388 EMSAEAERLRLRVAEMSRAQARAEeDARRFRKQAEDIgERLYRTELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAE 2465
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALE-DAREQIELLEPI-RELAERYAAARERLAELEYLRAALRlwFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2466 LEHEKDKLKQEAQLLQLKSEEMQtvrqEQLLQETQALQQSFLSEKDSLlqrERCIEQEKAKLEQLFQdevaKAQALREEQ 2545
Cdd:COG4913 300 LRAELARLEAELERLEARLDALR----EELDELEAQIRGNGGDRLEQL---EREIERLERELEERER----RRARLEALL 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 2546 QRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQqqqekllaeenQRLRERLQHLEEERRAALAR 2622
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL-----------RDLRRELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2390-2638 |
2.69e-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: 46.68 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2390 SAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHE 2469
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2470 KDKLKQEAQLLQLKSEEMQTVRQEQLLqetqaLQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2549
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2550 QqmqqEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALARSEEIAPS 2629
Cdd:COG4942 174 A----ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*....
gi 1920237952 2630 RAAAARALP 2638
Cdd:COG4942 250 ALKGKLPWP 258
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1484-1706 |
2.70e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1484 GELQALRARAEEAEAQ-KRQAQEEAERLRRQVQDETQRKRQAEAElalRVQAEAEAAREKQRALQALEELRlQAEEAERR 1562
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQrKKKEQQQAEELQQKQAAEQERLKQLEKE---RLAAQEQKKQAEEAAKQAALKQK-QAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1563 LRQAEAERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAtrraqqqaeaeraraeaerel 1642
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA--------------------- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1643 erwQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1706
Cdd:PRK09510 200 ---KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
960-1621 |
2.82e-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: 47.27 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 960 EDRLQAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRITEQQK 1039
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1040 AQAEVDGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAH 1119
Cdd:pfam02463 373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1120 EEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQE-------VGERLQQRHGERDVEVERWRERV 1192
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRIISAHGRLG 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1193 TLLLERWQAVLAQTDVRQRELEQLG-----RQLRYYRESADPLGAWLRDAKQRQEQIQAVPLA---NSQAVREQLRQEKA 1264
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATAdeveeRQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleIDPILNLAQLDKAT 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1265 LLEDIERHGEKV----EECQRFAKQYINAiKDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTL 1340
Cdd:pfam02463 613 LEADEDDKRAKVvegiLKDTELTKLKESA-KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1341 TSQYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVA 1419
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSrLKKEEKEEEKSELSL 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1420 VEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrLQLEATERQRGGAEGELQALRARAEEAEAQ 1499
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE---EEQLLIEQEEKIKEEELEELALELKEEQKL 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1500 KRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1579
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1920237952 1580 TAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEA 1621
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1689-1882 |
2.94e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1768
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1769 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAE 1848
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 1920237952 1849 KLAAISEATRLKTEAEIALKEKEAENERLRRLAE 1882
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1689-1901 |
3.03e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEElarlqreaaaatqkRRE 1763
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE--------------SRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1764 LEAELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRAL 1820
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1821 AEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRlLEEQAAQHKA 1900
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ-ADAKGAKQDE 1776
|
.
gi 1920237952 1901 D 1901
Cdd:NF012221 1777 S 1777
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1383-1562 |
3.04e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1383 QRQLAEAHAQAK---AQAEREAQglqrrmqeevARREEVAVEAqeqkrsiQEELQHLRQSSEAEIQAKARQVEAAERsRL 1459
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAE----------AIKKEALLEA-------KEEIHKLRNEFEKELRERRNELQKLEK-RL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1460 RIEEEIrvVRLQLEATERQRGGAEGELQALRARAEEAEAQkrqaQEEAERLRRQVQDETQR-----KRQAEAELALRVqa 1534
Cdd:PRK12704 92 LQKEEN--LDRKLELLEKREEELEKKEKELEQKQQELEKK----EEELEELIEEQLQELERisgltAEEAKEILLEKV-- 163
|
170 180
....*....|....*....|....*....
gi 1920237952 1535 EAEAAREKQRALQALEElrlQA-EEAERR 1562
Cdd:PRK12704 164 EEEARHEAAVLIKEIEE---EAkEEADKK 189
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2168-2342 |
3.35e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEE---LFSL 2244
Cdd:PRK09510 80 QRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEakrAAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2245 RVQMEELGKLKARIEAENRALVLRDK----DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAE 2320
Cdd:PRK09510 160 AKKAAAEAKKKAEAEAAKKAAAEAKKkaeaEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAE 239
|
170 180
....*....|....*....|..
gi 1920237952 2321 KmlKEKMQAVQEATRLKAEAEL 2342
Cdd:PRK09510 240 K--AAAAKAAEKAAAAKAAAEV 259
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1780-1977 |
3.41e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1780 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAVRQRAEAERVLAEKLAAISEATRL 1859
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1860 KTEAEIALKEKEAENerlrrlAEDEAfQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEIL 1939
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1920237952 1940 ALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAE 1977
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3028-3065 |
3.81e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.81e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1920237952 3028 RRALRGSGVIAGVWLEEAGQKLSIYEALRKDLLQPEAA 3065
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1692-1939 |
3.86e-04 |
|
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: 46.21 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1692 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQR-------EAAAATQKRREL 1764
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1765 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEE--DAVRQRAE 1841
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEarNQLRDRDE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1842 AERVLAEKLaaiSEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQK 1921
Cdd:pfam19220 277 AIRAAERRL---KEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSD 353
|
250
....*....|....*...
gi 1920237952 1922 GLveDTLRQRRQVEEEIL 1939
Cdd:pfam19220 354 RI--AELTKRFEVERAAL 369
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1696-2412 |
3.88e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1696 RQRELAEQEleKQRQLAEGTAQQRLAAEQ-ELIRLRAeTEQGEQQRQLLEeelaRLQREAAAATQKRR---ELEAELAKV 1771
Cdd:PRK10246 251 RLDELQQEA--SRRQQALQQALAAEEKAQpQLAALSL-AQPARQLRPHWE----RIQEQSAALAHTRQqieEVNTRLQST 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1772 RAEMEVLLASKARAEEESRSTSEKSKQRLeAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAVRQRAEAERvlaEKLA 1851
Cdd:PRK10246 324 MALRARIRHHAAKQSAELQAQQQSLNTWL-AEHDRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQLTHAE---QKLN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1852 AISEATRLKTEAEIAlkekeaenERLRRLAEDEAFQRRLLEEQaAQHkADIEARLAQLrKASESELERQKGLVEDTLRQR 1931
Cdd:PRK10246 398 ALPAITLTLTADEVA--------AALAQHAEQRPLRQRLVALH-GQI-VPQQKRLAQL-QVAIQNVTQEQTQRNAALNEM 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1932 RQVEEEilalkgsfekaaagKAElelELGRIRGTAEDTLRSKEQAEQEAarQRQLAAEEERRRREAEERVQKSLAAEEEA 2011
Cdd:PRK10246 467 RQRYKE--------------KTQ---QLADVKTICEQEARIKDLEAQRA--QLQAGQPCPLCGSTSHPAVEAYQALEPGV 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2012 ARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERL 2090
Cdd:PRK10246 528 NQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNITLQPQDDIQPWL 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2091 rseaeaarraaeeaeaareraereaaqsrrqvEEAERLKQsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaEQAALRQ 2170
Cdd:PRK10246 603 --------------------------------DAQEEHER---------------------------------QLRLLSQ 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2171 KQAADAEMEKH----KQFAEQALRQKAQVEQELTALRLQLEETDHQKSIL---DEELQRLKAEVTEAARQRGQVE--EEL 2241
Cdd:PRK10246 618 RHELQGQIAAHnqqiIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRIQqlTPL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2242 FSLRVQMEELGKLKARIEAEN------RALVLRDKDSA--QRLLQEEAEKMKQVAEEAARL--SVAAQEAARLRQLAEED 2311
Cdd:PRK10246 698 LETLPQSDDLPHSEETVALDNwrqvheQCLSLHSQLQTlqQQDVLEAQRLQKAQAQFDTALqaSVFDDQQAFLAALLDEE 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2312 LAQQralAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQK--TLETERQRQLEM 2389
Cdd:PRK10246 778 TLTQ---LEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLREntTRQGEIRQQLKQ 854
|
730 740
....*....|....*....|....
gi 1920237952 2390 SAEA-ERLRLRVAEMSRAQARAEE 2412
Cdd:PRK10246 855 DADNrQQQQALMQQIAQATQQVED 878
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2175-2371 |
3.88e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2175 DAEMEKHKQFAEQALR---QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQR------GQVEEELFSLR 2245
Cdd:PRK11281 55 EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2246 VQMEELGklKARIEAENRALVLRDK--------DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAeedLAQQRA 2317
Cdd:PRK11281 135 DQLQNAQ--NDLAEYNSQLVSLQTQperaqaalYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAL---LNAQND 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2318 LAEKMLK--EKMQAVQEATR--LKAEAELLQQQKELAQE--QARRLQEDKEQMAQQLAQE 2371
Cdd:PRK11281 210 LQRKSLEgnTQLQDLLQKQRdyLTARIQRLEHQLQLLQEaiNSKRLTLSEKTVQEAQSQD 269
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1689-1860 |
3.90e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.93 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLeeelarlqreaaaatqkrrELEAE 1767
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLL-------------------ELQAE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1768 LAKVRAemevllASKARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVL 1846
Cdd:PTZ00491 708 SAAVES------SGQSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAK 778
|
170
....*....|....
gi 1920237952 1847 AEKLAAIsEATRLK 1860
Cdd:PTZ00491 779 AKELADI-EATKFE 791
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1688-1869 |
4.08e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1688 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQREAAAATQKRRELEA 1766
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1767 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDavrqrAEAERV 1845
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 1920237952 1846 LAEKLAAISEATRLKTEAEIALKE 1869
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1381-1512 |
4.19e-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: 43.88 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1381 EKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHL--RQSSEAEIQAKARQVEAAERSR 1458
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1459 LRIEEEIRVVRLQLEATERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1512
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1421-1556 |
4.31e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.81 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1421 EAQEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAERSRLRIEEEI-RVVRLQleateRQRGGAEGELQALRARAEEAE 1497
Cdd:COG1566 87 QAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDEARAALDAAQ 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1498 AQKRQAQEEAERLRRQVQDETQrKRQAEAELAlrvQAEAEAAREKQRalqaLEELRLQA 1556
Cdd:COG1566 162 AQLEAAQAQLAQAQAGLREEEE-LAAAQAQVA---QAEAALAQAELN----LARTTIRA 212
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1329-1609 |
4.32e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1329 DLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQrAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRM 1408
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEEL-SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1409 QEEVARREEVAVEAQEQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGE 1485
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1486 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAARE-KQRALQALEELRLQAE- 1557
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEa 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 1558 EAERRLRQAEAERARQVQVALETAQR-SAEAELQSEHASFAEKTAQLERTLKE 1609
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3436-3472 |
4.33e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.33e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1920237952 3436 KLLSAEKAVTGYRDPYSGSTISLFQAMKKGLVLREHG 3472
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2268-2438 |
4.44e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2268 RDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR-LKAEAELLQQQ 2346
Cdd:TIGR02794 65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAkAKAEAEAERKA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2347 KELAQEQARrlqEDKEQMAQQLAQetqgfQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGE 2426
Cdd:TIGR02794 145 KEEAAKQAE---EEAKAKAAAEAK-----KKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAE 216
|
170
....*....|..
gi 1920237952 2427 RLYRTELATQEK 2438
Cdd:TIGR02794 217 AAAAAAAEAERK 228
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1443-1610 |
4.45e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1443 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQvQDETQRKR 1522
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1523 QAEAelalrVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVQ--VALETAQRSAEAELQSEHASFAEK 1599
Cdd:COG1579 90 EYEA-----LQKEIESLKRRISDLeDEILELMERIEELEEELAELEAELAELEAelEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|.
gi 1920237952 1600 TAQLERTLKEE 1610
Cdd:COG1579 165 REELAAKIPPE 175
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1689-1918 |
4.71e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEEL--------ARLQR 1752
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARpdnsaviaAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1753 EAAAATQKRRELEAE-----LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelaeeAARLRALAeeAKRQ 1827
Cdd:PRK05035 527 KAQARARQAEKQAAAaadpkKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKA--KKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1828 RQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAedeafqrrlleeqAAQHKAdiEARLA 1907
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVA-------------AAIARA--KARKA 660
|
250
....*....|.
gi 1920237952 1908 QLRKASESELE 1918
Cdd:PRK05035 661 AQQQANAEPEE 671
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1613-2068 |
4.95e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.55 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1613 AVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEE 1692
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1693 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVR 1772
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1773 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA 1852
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1853 ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRR 1932
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1933 QVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 2012
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 2013 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2068
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2455-2585 |
4.98e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2455 DAERLREAIAELEHEKDKLKQEAQLLqlkseemqtvrqEQLLQETQALQQSFLSEKDSLLQRErciEQEKAKLEQLFQDE 2534
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2535 V--AKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGV-------RRQQEELQ 2585
Cdd:PRK00409 579 IkeAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKekkkkkqKEKQEELK 638
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1439-1573 |
5.05e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1439 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDET 1518
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 1519 QRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQ 1573
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1430-1788 |
5.16e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1430 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1509
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1510 LRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAEL 1589
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1590 QSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLT 1669
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1670 QAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1749
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340 350
....*....|....*....|....*....|....*....
gi 1920237952 1750 LQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1788
Cdd:COG4372 332 LAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1356-1621 |
5.27e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.57 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1356 EEEERLAEQQRAEERER----------LAEVEAALEKQR---QLAEAHAQAKAQAEREAQGLQRR----MQEEVARREEV 1418
Cdd:PRK10811 507 EEAMALPSEEEFAERKRpeqpalatfaMPDVPPAPTPAEpaaPVVAAAPKAAAATPPAQPGLLSRffgaLKALFSGGEET 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1419 AVEAQEQKRSIQEElqhlRQSSEaeiQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA 1498
Cdd:PRK10811 587 KPQEQPAPKAEAKP----ERQQD---RRKPRQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQA 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1499 QKRQAQEEAERLRRQVQDETQRKRQAEAELAlrvQAEAEAarekqralQALEELRLQAEEAERRLRQAEAERAR------ 1572
Cdd:PRK10811 660 EVTEKARTQDEQQQAPRRERQRRRNDEKRQA---QQEAKA--------LNVEEQSVQETEQEERVQQVQPRRKQrqlnqk 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 1573 ---QVQVALETAQRSAEAELQSEHASfAEKTAQLERTLKEEHVAVVQLREEA 1621
Cdd:PRK10811 729 vriEQSVAEEAVAPVVEETVAAEPVV-QEVPAPRTELVKVPLPVVAQTAPEQ 779
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3397-3432 |
5.65e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.65e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1920237952 3397 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3432
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2295-2573 |
5.84e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.37 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2295 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAqETQG 2374
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLA-AISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2375 FQKTLETERQRQLEMSAEAERlrlrvaemsraqARAEEDARRFRKQAEDIGERLyrtelatqekvmlvQTLETQRQQSDR 2454
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR------------DAILEESRAVTKELTTLAQGL--------------DALDSQATYAGE 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2455 DAERLREAIAE--LEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSllqrerciEQEKAKLEQLFQ 2532
Cdd:NF012221 1642 SGDQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQDID 1713
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237952 2533 DEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRR-QHEA 2573
Cdd:NF012221 1714 DAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1700-1985 |
6.10e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.84 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1700 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLL 1779
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1780 ASKARAEEESRSTSEKSKQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedavrqraeAERVLAeKLAAISEAtRL 1859
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1860 KTEAEialkekeaenerLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVedtlrqrrqveeeil 1939
Cdd:PRK11637 170 ETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT--------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1940 ALKGSFEKAAAGKAELELELGRIRGT-AEDTLRSKEQAEQEA-------ARQRQ 1985
Cdd:PRK11637 223 GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3068-3101 |
6.23e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.23e-04
10 20 30
....*....|....*....|....*....|....
gi 1920237952 3068 LLEAQAGTGHIIDPTTSARLTVDEAVRAGLVGPE 3101
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1679-1842 |
6.24e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1679 EAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREaaaat 1758
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAETARAE---AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE----- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1759 QKRRELEAELaKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEedAVRQ 1838
Cdd:COG2268 301 REEAELEADV-RKPAE-----AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEA 372
|
....
gi 1920237952 1839 RAEA 1842
Cdd:COG2268 373 AAKP 376
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2013-2502 |
7.00e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2013 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRS 2092
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2093 EAeaarraaeeaeaareraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAArraqaeqaalRQKQ 2172
Cdd:COG4717 144 LP-------------------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLE----------QLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2173 AADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKA-EVTEAARQRGQVEEELFSLRVQMEEL 2251
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2252 GKLKARI------EAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2325
Cdd:COG4717 269 LSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2326 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKtleTERQRQLEMSAEAERLRLRVAEMSR 2405
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQEL---KEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2406 AQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAER--LREAIAELEHEKDKLKQEAQLLQLK 2483
Cdd:COG4717 426 DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELeeLKAELRELAEEWAALKLALELLEEA 505
|
490
....*....|....*....
gi 1920237952 2484 SEEMQTVRQEQLLQETQAL 2502
Cdd:COG4717 506 REEYREERLPPVLERASEY 524
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1688-1810 |
7.16e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1688 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQR-----EAAAATQKR 1761
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1762 RELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1810
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1345-1609 |
7.38e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1345 IRFISETLRRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREAQGLQrrmqeevarreevavEAQ 1423
Cdd:pfam00038 20 VRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLR---------------LAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1424 EQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQA 1503
Cdd:pfam00038 85 EDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKI---------------------ESLK---EELAFLKKNH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1504 QEEAERLRRQVQDETQ-------RKRQAEAELA-LRVQAEAEAAREKQRA----LQALEELRLQAEEAERRLRQAEAERA 1571
Cdd:pfam00038 141 EEEVRELQAQVSDTQVnvemdaaRKLDLTSALAeIRAQYEEIAAKNREEAeewyQSKLEELQQAAARNGDALRSAKEEIT 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1572 ---RQVQ-------------VALETAQRSAEAELQSEHASFAEKTAQLERTLKE 1609
Cdd:pfam00038 221 elrRTIQsleielqslkkqkASLERQLAETEERYELQLADYQELISELEAELQE 274
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2172-2495 |
7.61e-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: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2172 QAADAEMEKHKQFAEQALRQKAQVEQELtalRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEEL 2251
Cdd:pfam13868 16 LAAKCNKERDAQIAEKKRIKAEEKEEER---RLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2252 GKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2331
Cdd:pfam13868 93 YEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE-FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2332 EATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLAQETQGF---QKTLETERQRQLEMSAEAERLRLRVAEMSRA 2406
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRaqQEKAQDEKAERDELRAKLYQEEQERkerQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2407 QARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQtLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEE 2486
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR-LEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRER 330
|
....*....
gi 1920237952 2487 MQTVRQEQL 2495
Cdd:pfam13868 331 IEEERQKKL 339
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2191-2530 |
8.02e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2191 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVT-------EAARQRGQVEEELFSLRVQMEELGKLKARIEAENR 2263
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnnkynDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2264 AL-----VLRDKDSAQRLLQEEAEKMK----QVAEEAARLSVAAQEAARLRQLAEE---DLAQQRALAEKMLKEKMQAVQ 2331
Cdd:TIGR04523 198 KLelllsNLKKKIQKNKSLESQISELKkqnnQLKDNIEKKQQEINEKTTEISNTQTqlnQLKDEQNKIKKQLSEKQKELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2332 EATR-----------LKAEAELLQQQKE---------LAQEQARRLQEDKEQMAQ------QLAQETQGFQKTLETERQR 2385
Cdd:TIGR04523 278 QNNKkikelekqlnqLKSEISDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQnnkiisQLNEQISQLKKELTNSESE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2386 QLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAE 2465
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 2466 LEHEKDKLKQEAQLLQLKSEEMQTVRqEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQL 2530
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTR-ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1103-1758 |
8.53e-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: 45.87 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1103 SLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPE-LEATKAALKKLRAQAEAQqpvfdalRDELR-GAQEVGERLQQRHGE 1180
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNnIEKMILAFEELRVQAENA-------RLEMHfKLKEDHEKIQHLEEE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1181 RDVEVERWRERVTLLLerwqavlAQTDVRQRELEQLGRQLRYYRESADPLgawlrdakQRQEQIQAVPLANSQAVREQLR 1260
Cdd:pfam05483 231 YKKEINDKEKQVSLLL-------IQITEKENKMKDLTFLLEESRDKANQL--------EEKTKLQDENLKELIEKKDHLT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1261 QEkalLEDIERHGEKVEECQRFAKQYINAIKDYELQLVTYK-AQLEPVASPAK---------KPKVQSGSESIIQEYVDL 1330
Cdd:pfam05483 296 KE---LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeAQMEELNKAKAahsfvvtefEATTCSLEELLRTEQQRL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1331 RTRYSELSTLTSQYIRFISEtLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAEREAQGLQRRMQE 1410
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSE-LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF-EKIAEELKGKEQELIFLLQAREK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1411 EVARREEVAVEAQEQKRSIQEELQHLRQSSEAEiqaKARQVEAAERSRLRIEEEIRVVR------LQLEATERQRGGAEG 1484
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE---KLKNIELTAHCDKLLLENKELTQeasdmtLELKKHQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1485 ELQALRARAEEAEAQKRQAQEEAERLRR---QVQDETQRKRQAEAELALRVQAEAEAAREKQRALQ-ALEELRLQAEEAE 1560
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREefiQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEnKCNNLKKQIENKN 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1561 RRLRQAEAE-RARQVQVALETAQRSA--------EAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRaqqqaea 1631
Cdd:pfam05483 608 KNIEELHQEnKALKKKGSAENKQLNAyeikvnklELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKA------- 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1632 eraraeaerelerwQLKANEALRLRLQAEEVAQQKsltqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL 1711
Cdd:pfam05483 681 --------------KAIADEAVKLQKEIDKRCQHK-----------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1920237952 1712 AEGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAT 1758
Cdd:pfam05483 736 EQSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2210-2371 |
8.60e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2210 DHQKSILDEELQRLKAEVTEAARQRGQVEEELfsLRVQMEELGKLKARieaenralvlRDKDSAQRLLQEEAEKMKQVAE 2289
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQ--ERLKQLEKERLAAQ----------EQKKQAEEAAKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2290 EAARLSVAAQEAARLRQLAEEDLAQQrALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELAQEQArrlQEDKEQMAQ 2366
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKKKAEAEAAKKAaaeAKKKAEAEAAAKAAAEAKKKA---EAEAKKKAA 212
|
....*
gi 1920237952 2367 QLAQE 2371
Cdd:PRK09510 213 AEAKK 217
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1689-2070 |
8.65e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAEL 1768
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1769 AKVRAEMEVLLASKARAEEESRSTSEKSK--QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVL 1846
Cdd:COG3064 100 AAKEAEAAAAAEKAAAAAEKEKAEEAKRKaeEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1847 AEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVED 1926
Cdd:COG3064 180 AALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1927 TLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLA 2006
Cdd:COG3064 260 LGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEA 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 2007 AEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQ 2070
Cdd:COG3064 340 ALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGL 403
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2031-2482 |
8.90e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 45.73 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2031 EARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARER 2110
Cdd:COG4995 3 ALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2111 AEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALR 2190
Cdd:COG4995 83 AALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2191 QKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDK 2270
Cdd:COG4995 163 AALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2271 DSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA 2350
Cdd:COG4995 243 LAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2351 QEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYR 2430
Cdd:COG4995 323 LLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2431 TELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2482
Cdd:COG4995 403 LAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQL 454
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1353-1541 |
8.90e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.67 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1353 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEE 1432
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARA-AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1433 LQHLRQSSEAEIQAKARQVEAAERSRLRieeeiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1512
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231
|
170 180
....*....|....*....|....*....
gi 1920237952 1513 QVQDETQRKRQAEAELALRVQAEAEAARE 1541
Cdd:PRK12678 232 RRDRRDARGDDNREDRGDRDGDDGEGRGG 260
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1692-1973 |
9.37e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1692 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1771
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1772 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLA 1851
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1852 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQR 1931
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1920237952 1932 RQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSK 1973
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2171-2459 |
9.48e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2171 KQAADAEMEKHKQFaEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAaRQRGQVEEELfslRVQMEE 2250
Cdd:COG3096 402 QQALDVQQTRAIQY-QQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-EQKLSVADAA---RRQFEK 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2251 LGKLKARIEAEnralVLRDK--DSAQRLLQEEAEKMKQvaeeAARLSVAAQEAARLRQLAEEdlaQQRA--LAEKMLKEK 2326
Cdd:COG3096 477 AYELVCKIAGE----VERSQawQTARELLRRYRSQQAL----AQRLQQLRAQLAELEQRLRQ---QQNAerLLEEFCQRI 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2327 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaQETQGFQKTLETERQRQLEMSAEAERLRlrvaEMSRA 2406
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL-EQLRARIKELAARAPAWLAAQDALERLR----EQSGE 620
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 2407 QARAEEDARRFRKQAedigerLYRTELATQEKvmlvQTLETQRQQSDRDAERL 2459
Cdd:COG3096 621 ALADSQEVTAAMQQL------LEREREATVER----DELAARKQALESQIERL 663
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1354-1470 |
9.55e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1354 RMEEEERLAEQQRAEERERLAEVEA---ALEKQ-RQLAEAHAQAKAQAEREAQGLQRRMQEEVAR-----REEVAVEAQE 1424
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKlkeELEEKkEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiikelRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237952 1425 QKRS-IQEELQHLRQSSEAEIQAKARQVEAAErsRLRIEEEIRVVRL 1470
Cdd:PRK00409 604 VKAHeLIEARKRLNKANEKKEKKKKKQKEKQE--ELKVGDEVKYLSL 648
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1362-1523 |
1.00e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1362 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSE 1441
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1442 AEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDETQRK 1521
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 1920237952 1522 RQ 1523
Cdd:PRK12678 216 EE 217
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4396-4433 |
1.10e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1920237952 4396 QRFLEVQYLTGGLIEPDTPGRVALDEALQRGTVDARTA 4433
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2168-2625 |
1.11e-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: 45.12 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHKQFAEQALRQKAQV----EQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFS 2243
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2244 LRVQMEELGKLKARIEAENRALVLRDKDSaqrllqEEAEKMKqvaEEAARLSVAAQEAARLRqlaeEDLAQQRALAEKML 2323
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDS------EIVKNSK---SELARIPELEKELERLR----EHNKHLNENIENKL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2324 KEKMQAVQEATRLkaeaellqQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKT-------------LETERQRQLEMS 2390
Cdd:pfam05557 225 LLKEEVEDLKRKL--------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTglnlrspedlsrrIEQLQQREIVLK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2391 AEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE-----------LATQEKVMLVQTLE------TQRQQSD 2453
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKalvrrlqrrvlLLTKERDGYRAILEsydkelTMSNYSP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2454 RDAERLREA----------IAELEHEKDKLKQEA----QLLQLKSEEMQTVRQeqllQETQALQQSFLSEKDSLLQRERC 2519
Cdd:pfam05557 377 QLLERIEEAedmtqkmqahNEEMEAQLSVAEEELggykQQAQTLERELQALRQ----QESLADPSYSKEEVDSLRRKLET 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2520 IEQEKAKLEQlfQDEVAKAQALREEQQRQQQQMQQEKQQLaasmeearrRQHEAEEGVRRQQEELQRLAqqqqqqeklla 2599
Cdd:pfam05557 453 LELERQRLRE--QKNELEMELERRCLQGDYDPKKTKVLHL---------SMNPAAEAYQQRKNQLEKLQ----------- 510
|
490 500
....*....|....*....|....*.
gi 1920237952 2600 EENQRLRERLQHLEEERRAALARSEE 2625
Cdd:pfam05557 511 AEIERLKRLLKKLEDDLEQVLRLPET 536
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2382-2627 |
1.12e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2382 ERQRQLEMSAEA-ERLRLRVAEMSRAQARAEEDARRFRKQAEdigerlYRTELATQEKVMLVQTLETQRQQsdrdAERLR 2460
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERQLKSLERQAEKAERYKE------LKAELRELELALLVLRLEELREE----LEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2461 EAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEqlLQETQALQQSFLSEKDSLLQR-ERCIEQEKAKLEQLFQDEVAKAQ 2539
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSE--LEEEIEELQKELYALANEISRlEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2540 ALREeqqrqqqqmqqekqqLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAA 2619
Cdd:TIGR02168 324 QLEE---------------LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
....*...
gi 1920237952 2620 LARSEEIA 2627
Cdd:TIGR02168 389 AQLELQIA 396
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1345-1588 |
1.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1345 IRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQE 1424
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1425 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALR-------AraeEAE 1497
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKaeleaakA---ELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1498 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVA 1577
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
250
....*....|.
gi 1920237952 1578 LETAQRSAEAE 1588
Cdd:COG3883 255 AGAAAGSAGAA 265
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
630-722 |
1.18e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.16 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 630 HGFVAAATKELMWLSDREEEEVGFDWSDRNTNMAAKKEGYSALMHELELKEKKIKEIQSTGDRLLREDHPARPTAESFQA 709
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1920237952 710 ALQTQWSWMLQLC 722
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1421-1774 |
1.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1421 EAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK 1500
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1501 RQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERA---RQVQVA 1577
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEslqEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1578 LETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRL 1657
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1658 QAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1737
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350
....*....|....*....|....*....|....*..
gi 1920237952 1738 QQRQLLEEELARLQREAAAATQKRRELEAELAKVRAE 1774
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1363-1490 |
1.22e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.11 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1363 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAqAEREaqglqRRMQEEVARREEVavEAQEQKRSIQEELQHLRQSSEA 1442
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEA-AEQE-----RKLLEEQQRELEQ--KLEDQERSYEEHLRQLKEKMEE 248
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1920237952 1443 EIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1490
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1493-1877 |
1.23e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1493 AEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAR---EKQRALQALEELRLQAEEAERRLRQAEAE 1569
Cdd:PRK10929 104 TDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQLTALQAESA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1570 RARQVQVALETAQRSAE-----AELQSEhaSFAEKTAQLERTLkeehvavvqlreeatrraqqqaeaeraraeaereler 1644
Cdd:PRK10929 184 ALKALVDELELAQLSANnrqelARLRSE--LAKKRSQQLDAYL------------------------------------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1645 wqlkanEALRLRLQAEevaqqksltqaeaekqkeeaerearrrgkaeeqavRQRElAEQELEKQRQLAEGTAQQRLAAEQ 1724
Cdd:PRK10929 225 ------QALRNQLNSQ-----------------------------------RQRE-AERALESTELLAEQSGDLPKSIVA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1725 ELIRLRAETEQGEQQRQLLeEELARLQREAAAATQKRREleaELAKVRAEMEVLLASKARAE----EESRSTSEKSKQRL 1800
Cdd:PRK10929 263 QFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQVRQ---ALNTLREQSQWLGVSNALGEalraQVARLPEMPKPQQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1801 EAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAA---------------ISEATRLK--- 1860
Cdd:PRK10929 339 DTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTqrellnsllsggdtlILELTKLKvan 413
|
410
....*....|....*...
gi 1920237952 1861 TEAEIALKE-KEAENERL 1877
Cdd:PRK10929 414 SQLEDALKEvNEATHRYL 431
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1486-1585 |
1.28e-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: 42.47 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1486 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEtQRKRQAEAElALRVQAEAEAAREKQRALQALEelrlqaEEAERR 1562
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 1920237952 1563 LRQAEAERARQVQVALETAQRSA 1585
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1370-1621 |
1.30e-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: 44.52 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1370 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKAR 1449
Cdd:pfam13868 12 NSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1450 QVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1529
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1530 LRVQAEAEAAREKQRAlqaleELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELqsehasfAEKTAQLERTLKE 1609
Cdd:pfam13868 172 EAEREEIEEEKEREIA-----RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE-------AEKKARQRQELQQ 239
|
250
....*....|..
gi 1920237952 1610 EHVAVVQLREEA 1621
Cdd:pfam13868 240 AREEQIELKERR 251
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1688-2070 |
1.30e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 45.00 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1688 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQREAAAATQK 1760
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1761 RRELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRqlaEEDA 1835
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPR---DEEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1836 VRQrAEAErVLAEKlaaiSEATRLKteaEIALKEKEAENERLRRLaedEAFQRRLLEEQAAQHKADIEARLAqlRKASES 1915
Cdd:NF033838 206 IKQ-AKAK-VESKK----AEATRLE---KIKTDREKAEEEAKRRA---DAKLKEAVEKNVATSEQDKPKRRA--KRGVLG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1916 ELERQKGLVEDTLRQRRQVEEEIL---ALKGSFEKAAAGKAELELElGRIRGTAEDTLR-----SKEQAEQEAARqrqla 1987
Cdd:NF033838 272 EPATPDKKENDAKSSDSSVGEETLpspSLKPEKKVAEAEKKVEEAK-KKAKDQKEEDRRnyptnTYKTLELEIAE----- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1988 aeEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA---KVEEARRLRERAEQESARQLQLAQEAAQKrlQAEEKA 2064
Cdd:NF033838 346 --SDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAeatRLEKIKTDRKKAEEEAKRKAAEEDKVKEK--PAEQPQ 421
|
....*.
gi 1920237952 2065 HAFAVQ 2070
Cdd:NF033838 422 PAPAPQ 427
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1434-1722 |
1.34e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1434 QHLRQSsEAEIQAKARQVEAAERSRLRIEEeirvvrlqleateRQrggaegelqalrARAEeaeaqkRQAQEEAERLRRQ 1513
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA-------------RQ------------ARLE------REKAAREARHKKA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1514 VQDETQRKRQAEAELALRVQAEAEAAREK----------QRALQALEELR-LQAEEAERRLRQAEAERARQVQVALETAQ 1582
Cdd:PRK05035 477 AEARAAKDKDAVAAALARVKAKKAAATQPivikagarpdNSAVIAAREARkAQARARQAEKQAAAAADPKKAAVAAAIAR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1583 RSAEAELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERElerwqlkANEALRLRLQAEEV 1662
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------AVAAAIARAKAKKA 629
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1663 AQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1722
Cdd:PRK05035 630 EQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2777-2813 |
1.42e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 1.42e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237952 2777 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVREHG 2813
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1790-1938 |
1.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1790 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 1868
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 1869 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 1938
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1358-1603 |
1.49e-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: 44.50 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1358 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQ----------EEVARREEVAVEAQEQKR 1427
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAelkeelrqsrEKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1428 SIQEE---LQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1504
Cdd:pfam07888 112 ELSEEkdaLLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1505 EEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVAleTAQRS 1584
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA--AQRDR 269
|
250
....*....|....*....
gi 1920237952 1585 AEAELQSEHASFAEKTAQL 1603
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQL 288
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
65-168 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 65 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 122
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1920237952 123 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 168
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2221-2415 |
1.62e-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: 44.56 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2221 QRLKAEVTEAARQRGQVEEElfslrvqmeelgklkarieaenralvlrdkdsaQRLLQEEAEKMKQVAEEAARLSVAAQE 2300
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQ---------------------------------RRLQQEQLERAEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2301 AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQQQKELAQEQARRLQEDKE---QMAQQLAQETQG 2374
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQrqkELEMQLAEEQKR 467
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1920237952 2375 FQKTLETERQRQLEMSAEAERLRLRVAEMSRaqARAEEDAR 2415
Cdd:pfam15709 468 LMEMAEEERLEYQRQKQEAEEKARLEAEERR--QKEEEAAR 506
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2331-2409 |
1.89e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 43.93 E-value: 1.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 2331 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAQETqgfqKTLETERQRQLEMSAEAERLRLRVAEMSRAQAR 2409
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQA----KALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1471-1934 |
1.93e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1471 QLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE 1550
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1551 ELRLQAEEAERRLRQAEAERARQVQValETAQRSAE--AELQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQ 1628
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKA--EEAKRKAEeeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1629 AEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1708
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1709 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEE 1788
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1789 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALK 1868
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1869 EKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQV 1934
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
875-1832 |
2.02e-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: 44.40 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 875 EAQEAIARLEAQHQALVAlwhQLHTEMKSLLAWQSLGRDMQLIRSWSLATFRTLKpEEQRQALRSLELHYQAFLRDSQDA 954
Cdd:pfam01576 219 DLQEQIAELQAQIAELRA---QLAKKEEELQAALARLEEETAQKNNALKKIRELE-AQISELQEDLESERAARNKAEKQR 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 955 GGFGPE-DRLQAEREYGSCSRHYQQLLQSleQGEQEESRCQRCISElkdirlqleacETRtVHRLRLPLDKEPARECAQR 1033
Cdd:pfam01576 295 RDLGEElEALKTELEDTLDTTAAQQELRS--KREQEVTELKKALEE-----------ETR-SHEAQLQEMRQKHTQALEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1034 ITEQQKaQAEVDGLGKGVARLSAEAEkVLALPEPSPAAPTLRSELELTLGKLE-QVRSLSAIYLEKLKtislvirstQEA 1112
Cdd:pfam01576 361 LTEQLE-QAKRNKANLEKAKQALESE-NAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESER---------QRA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1113 EEVLRAHEEQLkEAQAVPATLPELEATKAALKKLRAQAEAQ-QPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1191
Cdd:pfam01576 430 ELAEKLSKLQS-ELESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1192 VtlllerwqavlaqtdVRQRELEqlgRQLRyyresadPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIEr 1271
Cdd:pfam01576 509 E---------------EAKRNVE---RQLS-------TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE- 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1272 hgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK----VQSGSESIIQEYVDLRTRYS----ELSTLTSQ 1343
Cdd:pfam01576 563 --EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKkfdqMLAEEKAISARYAEERDRAEaearEKETRALS 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1344 YIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreaqglqrRMQEEVARREEVAVEAQ 1423
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE--------EMKTQLEELEDELQATE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1424 EQKRSIQEELQHLRQSSEAEIQAKArqvEAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEA 1496
Cdd:pfam01576 713 DAKLRLEVNMQALKAQFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAA 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1497 EAQKRQAQEEAERLRRQVQDetqrkRQAEAELALRVQAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEAERA 1571
Cdd:pfam01576 790 NKGREEAVKQLKKLQAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERD 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1572 R-QVQVALETAQRSAeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQqaeaeraraeaerelerwqlkaN 1650
Cdd:pfam01576 865 ElADEIASGASGKSA---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQ----------------------V 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1651 EALRLRLQAEEVAQQKSltqaeaekqkeeaerearrrgkaeEQAVRQRELAEQELEKQRQLAEGTAQQRLAAeqELIRLR 1730
Cdd:pfam01576 920 EQLTTELAAERSTSQKS------------------------ESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALE 973
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1731 AETEQgeqqrqlLEEELARLQREAAAATQKRRELEAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRLEAEAGRFREL 1810
Cdd:pfam01576 974 AKIAQ-------LEEQLEQESRERQAANKLVRRTEKKLKEVLLQVE----DERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
970 980
....*....|....*....|..
gi 1920237952 1811 AEEAArlRALAEEAKRQRQLAE 1832
Cdd:pfam01576 1043 EEEAS--RANAARRKLQRELDD 1062
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1430-1620 |
2.03e-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: 42.73 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1430 QEELQHLRQSSEAEIQakarqveaaersrlRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1509
Cdd:pfam15665 13 EAEIQALKEAHEEEIQ--------------QILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1510 LRRQVQDetqRKRQAEAELALRVQAEA----EAAREKQRALQALEELRLQAE-EAERRLRQAEAERARQVQVALETaqrs 1584
Cdd:pfam15665 79 YKRRVEE---RELKAEAEHRQRVVELSreveEAKRAFEEKLESFEQLQAQFEqEKRKALEELRAKHRQEIQELLTT---- 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1920237952 1585 aeaeLQSEHASFAEKTAQLERTLKEEHVAVVQLREE 1620
Cdd:pfam15665 152 ----QRAQSASSLAEQEKLEELHKAELESLRKEVED 183
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1356-1620 |
2.06e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1356 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA-----------QGL-----------QRRMQEEVA 1413
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELkpsgqggldeeEAFldrtakreerrQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1414 RREEVAVEAQEQKRSIQEELQHlRQSSEAEIQAKARQVEaAERSRLRIEEEIRVVRL---QLEATERQRGGAEGELQALR 1490
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKEN-NEEEENSSWEKEEKRD-SRLGRYKEEETEIREKEyqeNKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1491 ARAEEAEAQKRQAQEEAERLRRQVQDE---------------TQRKRQA--EAELALRVQAEAEAAREKQRALQALE-EL 1552
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKvkyeskvfldqkrghPEVKSQNgeEEVTKLKVTTKRRQGGLSQSQEREEEaEV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1553 RLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHASFAE--KTAQLERTLKEEHVAVVQLREE 1620
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREErrKLLEEEEQRRKQEEAERKLREE 312
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2443-2626 |
2.12e-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: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2443 QTLETQRQQSDR----DAERLREAIAELEHEKDKLKqeaqllqlKSEEMQTVRQEQLLQETQ--ALQQSFLSEKDSLLQR 2516
Cdd:pfam17380 281 QKAVSERQQQEKfekmEQERLRQEKEEKAREVERRR--------KLEEAEKARQAEMDRQAAiyAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2517 ERcIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQEK 2596
Cdd:pfam17380 353 IR-QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190
....*....|....*....|....*....|.
gi 1920237952 2597 LLAEENQRL-RERLQHLEEERRAALARSEEI 2626
Cdd:pfam17380 432 ARQREVRRLeEERAREMERVRLEEQERQQQV 462
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1362-1615 |
2.17e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1362 AEQQRAEERERlaeVEAALEkqrqlaEAHAQAKAQAEREAQGL---------------------QRRMQEEVARREEVAV 1420
Cdd:PHA03247 1586 AKQQRAEATDR---VTAALR------EALAAHERRAQSEAESLanlktllrvaaipataaktldQARSVAEIVDQIELLL 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1421 EAQEQKRSIQEE----LQHLRQSSEAEIQAKARQVEAAERSRLRieeeirvVRLQLEATERQRggaegeLQALRARAEEA 1496
Cdd:PHA03247 1657 EQTEKAAELDVAavdwLEHARRVFEAHPLTAARGGGPDPLARLH-------ARLDALGETRRR------TEALRRSLEAA 1723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1497 EAQKRQAQEEAERLRRQvqdetqrkrqaeaelALRVQAEAEAAREKQRALQALEE--LRLQAEEAERRLrqaeAERARQV 1574
Cdd:PHA03247 1724 EAEWDEVWGRFGRVRGG---------------AWKSPEALRAAREQLRALQTATNtvLGLRADAHYERL----PAKYQGA 1784
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237952 1575 qVALETAQRSAEAElqsEHASFAEKTAQLERTLKEEHVAVV 1615
Cdd:PHA03247 1785 -LGAKSAERAGAVE---ELGAAVARHDGLLARLREEVVARV 1821
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1725-2072 |
2.25e-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: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1725 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAElaKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA 1804
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE--RQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1805 GRFRELAEEAARLRAlAEEAKRQRQLAEEDAVrqRAEAERVLaeklaaiseatrlkteaeialkEKEAENERLRRLAEDE 1884
Cdd:pfam07888 108 ASSEELSEEKDALLA-QRAAHEARIRELEEDI--KTLTQRVL----------------------ERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1885 AFQRRLLEEQAAQHKADIEARLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRG 1964
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLS-KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1965 TAE-------------------DTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALE----- 2020
Cdd:pfam07888 242 LQErlnaserkveglgeelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrie 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 2021 ----EVERLKAKVEEARRLRERAEQESARQ--LQLAQEAAQKRLQAEEKAhAFAVQQK 2072
Cdd:pfam07888 322 klsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQK 378
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1486-1610 |
2.26e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1486 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEaarekqralQALEELRLQAEEAERRLRQ 1565
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ---------QAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1920237952 1566 AEAERARQVqvaletaqrsAEAELQSEHASFAEKTAQLERTLKEE 1610
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2047-2482 |
2.28e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 44.19 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2047 LQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEAE 2126
Cdd:COG4995 1 LLALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2127 RLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQL 2206
Cdd:COG4995 81 ALAALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2207 EETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALVLRDKDSAQRLLQEEAEKMKQ 2286
Cdd:COG4995 161 AAAALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2287 VAEEAARLSvAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2366
Cdd:COG4995 241 LALAAAAAA-LAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2367 QLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEM-SRAQARAEEDARRFRKQAEDIGERLYRTELATQEKVMLVQTL 2445
Cdd:COG4995 320 LAALLLLLAALALLALLLLLAAAALLAAALAAALALAaALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAA 399
|
410 420 430
....*....|....*....|....*....|....*..
gi 1920237952 2446 ETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQL 2482
Cdd:COG4995 400 LLALAAAQLLRLLLAALALLLALAAYAAARLALLALI 436
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1380-1586 |
2.37e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1380 LEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEvaRREEVAVEAQEQKRSIQEELQHLrQSSEAEIQAKARQVEAaersrl 1459
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREEL-QREEERLVQKEEQLDA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1460 RIEEeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdETQRKRQAEAELALRVQAEAEaa 1539
Cdd:PRK12705 96 RAEK--------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1920237952 1540 REKQRALQALEelrlqaEEAerrlrQAEAERARQVQVAlETAQRSAE 1586
Cdd:PRK12705 157 EEKAQRVKKIE------EEA-----DLEAERKAQNILA-QAMQRIAS 191
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1374-1581 |
2.38e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1374 AEVEAALEKQRQLAEAHAQAKAQAEREAQGLQ--RRMQEEVARREEVAVEAQEQKRSIQE-----------ELQHLRQSS 1440
Cdd:PHA03247 1150 STVDAAVRAHGVLADAVAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARlgalgaaaadlAVAVRRENP 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1441 EAE------IQAKARQVEAAERSRLRIEEEIRVVrLQLEATERQRGGAEGELQAL-------RARAEEAEAQkrqAQEEA 1507
Cdd:PHA03247 1230 QAEgdraalLEAAARAVTAAREGLAACEGEFGGL-LHAEGSAGDPSPSGRALQELgkvvgatRRRADELEAA---AADLA 1305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1508 ERLRRQVQDETQRKRQAEAELAL-RVQAEAEAAREKQRALQALE-ELRLQAEEAERRLRQAEAERARQVQVALETA 1581
Cdd:PHA03247 1306 EKMAARRARASRERWAADVEAALdRVENRAEFDAVELRRLQALAaTHGYNPRDFRKRAEQALAANAKTATLALEAA 1381
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1471-1586 |
2.38e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1471 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQAL 1549
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1920237952 1550 EELR---------LQAEEAERRLRQAE-AERARQVQVALetAQRSAE 1586
Cdd:PRK09039 147 AALRrqlaaleaaLDASEKRDRESQAKiADLGRRLNVAL--AQRVQE 191
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
66-174 |
2.48e-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: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 66 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 136
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1920237952 137 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 174
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1350-1622 |
2.63e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.94 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1350 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAQGLQRRMQEevARREEVAVEAQEQKRSI 1429
Cdd:pfam03528 96 DEVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQ-WNQYRESAEREIADLRRRLSE--GQEEENLEDEMKKAQED 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1430 QEELQHLRQSSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALraraeeaEAQKRQAQEEAE 1508
Cdd:pfam03528 173 AEKLRSVVMPMEKEIAAlKAKLTEAEDKIKELEASKMKELNHYLEAEKSCRTDLEMYVAVL-------NTQKSVLQEDAE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1509 RLRRQVQDETQRkrqaeaeLALRVQAEAEAAREKQRAL-QALEELRLQAEEAERRLRQAEAERARQVqvalETAQRSAEA 1587
Cdd:pfam03528 246 KLRKELHEVCHL-------LEQERQQHNQLKHTWQKANdQFLESQRLLMRDMQRMESVLTSEQLRQV----EEIKKKDQE 314
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237952 1588 ELQSEHASFAEKTAQLERTLKEEHVAVVQLREEAT 1622
Cdd:pfam03528 315 EHKRARTHKEKETLKSDREHTVSIHAVFSPAGVET 349
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1692-1836 |
2.65e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1692 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKV 1771
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 1772 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAV 1836
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAI 356
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2168-2332 |
2.68e-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: 42.60 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2168 LRQKQAADAEMEKHKQFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQ 2247
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2248 mEELGKLKARIEAENRALVLRDkDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2327
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 1920237952 2328 QAVQE 2332
Cdd:COG1579 167 ELAAK 171
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
533-627 |
2.76e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 533 LRYLQDLLAWVEENQRRLDSAEWGVDLPSVEAQLGSHRGLHQSVEEFRTKIERARTDEGQL---SPATRGAYRDCLGRLD 609
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1920237952 610 LQYAKLLSSSKARLRSLE 627
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1404-2069 |
2.78e-03 |
|
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: 43.97 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1404 LQRRMQeevARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRL---RIEEEIRVVR-LQLEATERQR 1479
Cdd:pfam07111 21 LERRLD---TQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQelrRLEEEVRLLReTSLQQKMRLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1480 GGA-EGELQALRARAEEAEAQK-RQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKqralqALEELRLQAE 1557
Cdd:pfam07111 98 AQAmELDALAVAEKAGQAEAEGlRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEE-----ALSSLTSKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1558 EAERRLRQAEAERARQVQvALETAQRsaEAELQSEHASFAEKTAQLERTLKEEHVAVV--QLREEATRRAQQQAEAERAR 1635
Cdd:pfam07111 173 GLEKSLNSLETKRAGEAK-QLAEAQK--EAELLRKQLSKTQEELEAQVTLVESLRKYVgeQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1636 AEAERELERWQLKAN-EALRLRLQaeevaqqkSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG 1714
Cdd:pfam07111 250 TMQHLQEDRADLQATvELLQVRVQ--------SLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1715 TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQReaaAATQKRRELEAELAKVRA-EMEVLLASKARAEEESRSTS 1793
Cdd:pfam07111 322 LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQR---ALQDKAAEVEVERMSAKGlQMELSRAQEARRRQQQQTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1794 EKSKQRLEAEAGRFRELAEEAARLRaLAEEAKRQRQLAEE--DAVRQRAEAERVLAEKLAAIS---EATRLKTEAEIALK 1868
Cdd:pfam07111 399 AEEQLKFVVNAMSSTQIWLETTMTR-VEQAVARIPSLSNRlsYAVRKVHTIKGLMARKVALAQlrqESCPPPPPAPPVDA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1869 EKEAENERLRRlaedeafQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKA 1948
Cdd:pfam07111 478 DLSLELEQLRE-------ERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1949 AAGKAELELELGRIRGTAEDTLRSKEQAEQEA-----ARQRQLAAEEERRRREAEERVQK---SLAAEEEAARQRKAALE 2020
Cdd:pfam07111 551 RQGQQESTEEAASLRQELTQQQEIYGQALQEKvaeveTRLREQLSDTKRRLNEARREQAKavvSLRQIQHRATQEKERNQ 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2021 EVERLK--AKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEKAHAFAV 2069
Cdd:pfam07111 631 ELRRLQdeARKEEGQRLARRVQElERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1359-1620 |
2.80e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1359 ERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAkaqaereaqgLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRq 1438
Cdd:pfam10174 453 ERLKEQREREDRERLEELE-SLKKENKDLKEKVSA----------LQPELTEKESSLIDLKEHASSLASSGLKKDSKLK- 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1439 SSEAEIQA-------------KARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQK----- 1500
Cdd:pfam10174 521 SLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKndkdk 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1501 ----------RQAQEEAERLR--RQVQDETQRKRQAEAELALRVQ-AEAEAAREKQRA--LQALEELRLQAEEAERRLRQ 1565
Cdd:pfam10174 601 kiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDATKARLSS 680
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 1566 AE--------------AERARQVQVALETAQRSAEAELQSEHASFA--EKTAQLERTLKEEhvaVVQLREE 1620
Cdd:pfam10174 681 TQqslaekdghltnlrAERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE---VMALKRE 748
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2287-2530 |
2.92e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.56 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2287 VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--KEKMQAVQEATRLKAEAELLQQQKELAQEQAR--------- 2355
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYlaKEEDLKRQNAVLQEAQVELDALQNQLALARAEmenikavat 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2356 ----RLQEDKEQMAQQLAQETQGFQKTL-ETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRfrkqaedigerlyR 2430
Cdd:pfam03528 86 vsenTKQEAIDEVKSQWQEEVASLQAIMkETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRR-------------R 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2431 TELATQEkvmlvQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQA--------- 2501
Cdd:pfam03528 153 LSEGQEE-----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLEAekscrtdle 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1920237952 2502 -------LQQSFLSEKDSLLQRE-----RCIEQEKAKLEQL 2530
Cdd:pfam03528 228 myvavlnTQKSVLQEDAEKLRKElhevcHLLEQERQQHNQL 268
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
77-167 |
2.96e-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: 40.36 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 77 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 149
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 1920237952 150 DDIADGNPKLTLGLIWTI 167
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1434-1923 |
3.01e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1434 QHLRQSSEAEIQAKARqVEAAERSRLRIEEEIRVVRLQLEATERQRGGA--EGELQALRARAEEAEAQKRQAQEEAERLR 1511
Cdd:COG3064 2 QEALEEKAAEAAAQER-LEQAEAEKRAAAEAEQKAKEEAEEERLAELEAkrQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1512 RQVQDETQRKRQAEAELAlRVQAEAEAAREKQRALQALEELRLQAEEaerrlRQAEAERARQVQVALETAQRSAEAELQS 1591
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKA-KAAKEAEAAAAAEKAAAAAEKEKAEEAK-----RKAEEEAKRKAEEERKAAEAEAAAKAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1592 EHASFAEKTAQLERTLKEEhVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1671
Cdd:COG3064 155 EAARAAAAAAAAAAAAAAR-AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1672 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1751
Cdd:COG3064 234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1752 REAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1831
Cdd:COG3064 314 EEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1832 EEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRK 1911
Cdd:COG3064 394 AAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDG 473
|
490
....*....|..
gi 1920237952 1912 ASESELERQKGL 1923
Cdd:COG3064 474 GAVLADLLLLGG 485
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2293-2411 |
3.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2293 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELaQEQARRLQEDKEQMAQQLA 2369
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 2370 ------QETQGFQKTLETERQRQLEMSAEAERLR-------LRVAEMSRAQARAE 2411
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKEI 158
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1437-1590 |
3.61e-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: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1437 RQSSEAEIQAKARQVEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1514
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1515 QDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQ 1590
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3771-3802 |
3.62e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.62e-03
10 20 30
....*....|....*....|....*....|..
gi 1920237952 3771 RLLSAERAVTGYRDPYTEQTISLFQAMKKDLI 3802
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2740-2773 |
3.66e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.66e-03
10 20 30
....*....|....*....|....*....|....
gi 1920237952 2740 LLEAQAASGFLLDPVRNRRLAVNEAVKEGIVGPE 2773
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2273-2406 |
3.66e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.47 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2273 AQRLLQE-----EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELL 2343
Cdd:PTZ00491 672 AELLEQEargrlERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRI 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 2344 QQQKELAQEQARRLQEdkeqmaqqLAQETQgfQKTLETERQRQLeMSAEAERL--------RLRVAEMSRA 2406
Cdd:PTZ00491 749 EAEAELEKLRKRQELE--------LEYEQA--QNELEIAKAKEL-ADIEATKFerivealgRETLIAIARA 808
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1077-1293 |
3.74e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1077 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQEAEEVLRAHEEQLKEAQAVPATLPELEATKAALkklraqaEAQQPV 1156
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1157 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDvrqrELEQLGRQLRYYResadpLGAWLRD 1236
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE----AAEDLARLELRAL-----LEERFAA 757
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1237 AKQRqeqiqavplANSQAVREQLRQE-KALLEDIERHGEKVEEC-QRFAKQYINAIKDY 1293
Cdd:COG4913 758 ALGD---------AVERELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1196-1469 |
3.77e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1196 LERWQAVLAQTDVRQRELEQLGRQLryyrESADplgawlRDAKQRQEQIQAVPLANSQAVREQLrqEKALLEDIERhgeK 1275
Cdd:PRK11281 65 LEQTLALLDKIDRQKEETEQLKQQL----AQAP------AKLRQAQAELEALKDDNDEETRETL--STLSLRQLES---R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1276 VEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESIIQEYVDLRTRYSelSTLTSQyiRFISETLR-R 1354
Cdd:PRK11281 130 LAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPSQRvL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1355 MEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAEREAQGLQRRM-QEEVARREEVAVEAQEQKRS-- 1428
Cdd:PRK11281 197 LQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQEAInSKRLTLSEKTVQEAQSQDEAar 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1429 ------IQEELQHLRQSSEAEIQAKAR-------------QVEAAERSRLRIEEEIRVVR 1469
Cdd:PRK11281 274 iqanplVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQISVLK 333
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1485-1619 |
3.79e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1485 ELQALRARAEEAEAQKRQAQEEAERLRRQVQdetqrkrqaE-AELALRVQAEAEAAREKQRaLQALEELRLQAEEAERRL 1563
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLE---------ElEAAALQPGEEEELEEERRR-LSNAEKLREALQEALEAL 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1564 RQAEAerarQVQVALETAQRSAEaELQSEHASFAEKTAQLERtlkeehvAVVQLRE 1619
Cdd:COG0497 236 SGGEG----GALDLLGQALRALE-RLAEYDPSLAELAERLES-------ALIELEE 279
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1706-1979 |
3.79e-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: 42.92 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1706 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASK 1782
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1783 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAVRQRAEA 1842
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1843 ErvLAEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRLLE--EQAAQHKADIEARLAQLRKASES 1915
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1916 ELERQKGLVEDTLRQRrqVEEeilalkgsFEKAaagKAELELELGRIRgtaedtlrsKEQAEQE 1979
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTL---------QEIAELE 278
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2328-2625 |
3.85e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2328 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRvaemsrAQ 2407
Cdd:pfam02029 6 EAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK------RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2408 ARAEEDARRFRKQAEDIGErlyrtELATQEKVMLVQTLETQRQQSDRDAERLREAIAELE------------------HE 2469
Cdd:pfam02029 80 QEALERQKEFDPTIADEKE-----SVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEirekeyqenkwstevrqaEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2470 KDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQ 2549
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2550 QQMQQEKQQLAA--SMEEARRRQHEAEEgvrrqqEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRA-------AL 2620
Cdd:pfam02029 235 EREEEAEVFLEAeqKLEELRRRRQEKES------EEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRrkqeeaeRK 308
|
....*
gi 1920237952 2621 ARSEE 2625
Cdd:pfam02029 309 LREEE 313
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1822-2071 |
3.97e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1822 EEAKRQRQLAEEDAVRQRAEAERVLAEKLAA-ISEATRLKTEAEIALKEKEAENerlrrlaedeafqrrlLEEQAAQHKA 1900
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGAeISKLEEENREKEKALPKNDDMT----------------IEEAKRRAAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1901 DIEARLAQLRKASESELERQkglvedtlrqrrqVEEEILALKGSFEKAAAGKAElELELGRIRGTAEDTLRSKEQAEQEA 1980
Cdd:PRK07735 66 AAKAKAAALAKQKREGTEEV-------------TEEEKAKAKAKAAAAAKAKAA-ALAKQKREGTEEVTEEEKAAAKAKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1981 ARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2060
Cdd:PRK07735 132 AAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAA 211
|
250
....*....|.
gi 1920237952 2061 EEKAHAFAVQQ 2071
Cdd:PRK07735 212 KAKAAALAKQK 222
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2285-2626 |
3.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2285 KQVAEEAARLSVAA--QEAARLRQLAEEDLAQQRALAEKmlkekmqavqEATRLKAEAELLQQQKELAQEQARR--LQED 2360
Cdd:PRK04863 260 KHLITESTNYVAADymRHANERRVHLEEALELRRELYTS----------RRQLAAEQYRLVEMARELAELNEAEsdLEQD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2361 KEQMA--QQLAQETQGFQKTLE------TERQRQLEMSAEAERLRLRVAEMSRAQA-RAEEDARRFRKQAEDIGERL--- 2428
Cdd:PRK04863 330 YQAASdhLNLVQTALRQQEKIEryqadlEELEERLEEQNEVVEEADEQQEENEARAeAAEEEVDELKSQLADYQQALdvq 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2429 YRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEaqLLQLksEEMQTVRQEQLLQETQALQ--QSF 2506
Cdd:PRK04863 410 QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE--LLSL--EQKLSVAQAAHSQFEQAYQlvRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2507 LSEKDsllqRERCIEQEKAKLEQL--FQDEVAKAQALReeqqrqqqqmqqekqqlaASMEEARRRQHEAEEGVRRQQEEL 2584
Cdd:PRK04863 486 AGEVS----RSEAWDVARELLRRLreQRHLAEQLQQLR------------------MRLSELEQRLRQQQRAERLLAEFC 543
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1920237952 2585 QRLAQQQQQQEkLLAEENQRLRERLQHLEEERRAALARSEEI 2626
Cdd:PRK04863 544 KRLGKNLDDED-ELEQLQEELEARLESLSESVSEARERRMAL 584
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1460-1590 |
4.10e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1460 RIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAA 1539
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1540 REKQRAL-----QALEELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEAELQ 1590
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKKD-----TLKARAKAAKAQEK 150
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
64-172 |
4.17e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 40.36 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 64 ADERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRH 139
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
|
90 100 110
....*....|....*....|....*....|...
gi 1920237952 140 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 172
Cdd:cd21337 94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1386-1573 |
4.22e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.92 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1386 LAEAHAQAKAQAEREAQGLQRRMQEEVARreevaveAQEQKRSIQEELQHLRQsseaeiqakarqveaaERSRLRIEEEI 1465
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVER-------AEERLRDAREALLAFRN----------------RNGILDPEATA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1466 RVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL-RVQAEaeaarekqr 1544
Cdd:COG3524 217 EALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLaSLLAE--------- 287
|
170 180 190
....*....|....*....|....*....|.
gi 1920237952 1545 alqaLEELRLQAEEAERRLRQAEA--ERARQ 1573
Cdd:COG3524 288 ----YERLELEREFAEKAYTSALAalEQARI 314
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2188-2621 |
4.27e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2188 ALRQKAQVEQ-ELTALRLQLEEtdhQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEaeNRALV 2266
Cdd:pfam10174 335 AKEQRAAILQtEVDALRLRLEE---KESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE--NLQEQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2267 LRDKDsaqRLLQEEAEKMKQVAEEAARLSVA---AQEAARLRQLAEEDLAQQRALAEKMLKEKMQAV-QEATRLKAEAEL 2342
Cdd:pfam10174 410 LRDKD---KQLAGLKERVKSLQTDSSNTDTAlttLEEALSEKERIIERLKEQREREDRERLEELESLkKENKDLKEKVSA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2343 LQQQKelaQEQARRLQEDKEQmAQQLAQ---ETQGFQKTLETERQRQLEmsaEAERLrlrVAEMSRAQaRAEEDARrfrk 2419
Cdd:pfam10174 487 LQPEL---TEKESSLIDLKEH-ASSLASsglKKDSKLKSLEIAVEQKKE---ECSKL---ENQLKKAH-NAEEAVR---- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2420 QAEDIGERLYRTELATQEKVMlvqtlETQRQQSDrdAERLREAIAELEHEK-DKLKQEAQLLQLKSEEMQTvrQEQLLQE 2498
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKE-----ESGKAQAE--VERLLGILREVENEKnDKDKKIAELESLTLRQMKE--QNKKVAN 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2499 TQALQQsflsekdsllqrercieQEKAKLEQLFQDevakaqALREEQQRQQQQMQQEKQQLAASMEEARRrqhEAEEGVR 2578
Cdd:pfam10174 623 IKHGQQ-----------------EMKKKGAQLLEE------ARRREDNLADNSQQLQLEELMGALEKTRQ---ELDATKA 676
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1920237952 2579 RQQEELQRLAQQQQQQEKLLAEENQRLRERLQHLEEERRAALA 2621
Cdd:pfam10174 677 RLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAIS 719
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2117-2303 |
4.34e-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: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2117 QSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKeaeqeaarraqaeqAALRQKQAADAEMEKHKQFAEQALRQKAQVE 2196
Cdd:pfam15709 360 QRRLQQEQLERAEK-MREELELEQQRRFEEIRLRK--------------QRLEEERQRQEEEERKQRLQLQAAQERARQQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2197 QEltALRLQLEETDHQKsildeelQRLKAEVTEAARQRGQVEEElfslrvQMEELGKLKARIEAENRALVLRDKDSAQRL 2276
Cdd:pfam15709 425 QE--EFRRKLQELQRKK-------QQEEAERAEAEKQRQKELEM------QLAEEQKRLMEMAEEERLEYQRQKQEAEEK 489
|
170 180 190
....*....|....*....|....*....|..
gi 1920237952 2277 LQEEAEKMKQVAEEAARLSVA-----AQEAAR 2303
Cdd:pfam15709 490 ARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1452-1569 |
4.36e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1452 EAAerSRLRIE-----EEIRVVRLQLEATERqrggaegELQALRaraeeaEAQKRQAQEEAERLRRQVQDETQRKRQAEA 1526
Cdd:COG0542 397 EAA--ARVRMEidskpEELDELERRLEQLEI-------EKEALK------KEQDEASFERLAELRDELAELEEELEALKA 461
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237952 1527 elalRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAE 1569
Cdd:COG0542 462 ----RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1387-1575 |
4.46e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1387 AEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEir 1466
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1467 vvRLQLEATERQRGGAEGELQALRARAEEAEA--QKRQAQEEAERLRRQVQDETQRKRQaEAELALRVQAEAEAAREKQR 1544
Cdd:PRK12678 145 --AGEGGEQPATEARADAAERTEEEERDERRRrgDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRREERGRR 221
|
170 180 190
....*....|....*....|....*....|.
gi 1920237952 1545 ALQALEELRLQAEEAERRLRQAEAERARQVQ 1575
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1498-1970 |
4.54e-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: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1498 AQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQR--ALQALEELRLQAEEAERRLRQAEAERARQvQ 1575
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELeaKRQAEEEAREAKAEAEQRAAELAAEAAKK-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1576 VALETAQRSAEAELQSEHASFAEKTAQLERTLKEEHVA----VVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1651
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAekekAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1652 ALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRA 1731
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1732 ETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1811
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1812 EEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLL 1891
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1920237952 1892 EEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTL 1970
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2282-2376 |
4.63e-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: 42.27 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2282 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2355
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 1920237952 2356 RLQEDKEQMAQQLAQETQGFQ 2376
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1895-2071 |
4.75e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1895 AAQHKADIEARLAQLRKasesELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKE 1974
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1975 QAEQEAARQRQLAAEEERRRREAEER--------------VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRErAE 2040
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE-AE 172
|
170 180 190
....*....|....*....|....*....|.
gi 1920237952 2041 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2071
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR 203
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1732-1954 |
4.76e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1732 ETEQGEQQRQLLEEELARLQ-----------REAAAATQKRRELEAELAKVRAEMEV-----LLASKARAEEESRSTSEK 1795
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHgaeiskleeenREKEKALPKNDDMTIEEAKRRAAAAAkakaaALAKQKREGTEEVTEEEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1796 SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--AVRQRAEAERVLAEKLAAISEATRLKTEAEIAL---KEK 1870
Cdd:PRK07735 91 AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAkaAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKakaKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1871 EAENERLRRLAEDEAFQRRLLEEQAAQH-KADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEE-ILALKGSFEKA 1948
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTEEeKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKaIAAAKAKAAAA 250
|
....*.
gi 1920237952 1949 AAGKAE 1954
Cdd:PRK07735 251 ARAKTK 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2329-2583 |
4.80e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2329 AVQEATRLKAEAELLQQQKEL--AQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRA 2406
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELseLQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2407 QARAEEDARRFRKQ------------AEDIGE---RLYRTELATQEKVMLVQTLETQRQQSDRDAERLREAIAELEHEKD 2471
Cdd:COG3883 85 REELGERARALYRSggsvsyldvllgSESFSDfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2472 KLKQEAQLLQLKSEEmqtvrQEQLLQETQALQQSFLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQ 2551
Cdd:COG3883 165 ELEAAKAELEAQQAE-----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270
....*....|....*....|....*....|..
gi 1920237952 2552 MQQEKQQLAASMEEARRRQHEAEEGVRRQQEE 2583
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1690-1790 |
4.85e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1690 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELA 1769
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 1920237952 1770 KvRAEMEVLLaskarAEEESR 1790
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2249-2377 |
4.85e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2249 EELGKLKARIEAENRALVLRDKDSAQrlLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2328
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 2329 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAQETQGFQK 2377
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1809-1937 |
5.02e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1809 ELAEEAARLRALAE-EAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1887
Cdd:COG2268 196 EIIRDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANA 275
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 1888 RRLLEEQAAQHKADIEARLAQLRKA-SESELERQKGLVEDTLRQRRQVEEE 1937
Cdd:COG2268 276 EREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1329-1590 |
5.25e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.72 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1329 DLRTRYSELSTLTSQyIRFISETLRRMEEEERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQaKAQAEREAQGLQRRM 1408
Cdd:COG1538 77 EVAQAYFDLLAAQEQ-LALAEENLALAEELLELARARYEAGLASRLDVLQA---EAQLAQARAQ-LAQAEAQLAQARNAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1409 QEEVARREEVAVEAQEQKRSIQEELQHLRQSSEA------EIQAKARQVEAAERsRLRIEEEIRVVRLQLEATERQRGGA 1482
Cdd:COG1538 152 ALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEalerrpDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1483 EGELQ-------------------ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1543
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1544 RALQALEEL-------RLQAEEAERRLRQAEAERarqvqVALETAQRSAEAELQ 1590
Cdd:COG1538 311 EALELARARyraglasLLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1480-1620 |
5.25e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1480 GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQrkrqaEAELALRVQAEAEAAREKQralqaleelRLQAEEa 1559
Cdd:PRK12705 19 GVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK-----ELLLRERNQQRQEARRERE---------ELQREE- 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 1560 ERRLRQAEAERARQVQVALETAQRS-AEAELQSEHASFAEKTAQLERTLKEehvaVVQLREE 1620
Cdd:PRK12705 84 ERLVQKEEQLDARAEKLDNLENQLEeREKALSARELELEELEKQLDNELYR----VAGLTPE 141
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1131-1541 |
5.40e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.75 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1131 ATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGaqevgerLQQRHGERDVEVERWRERvtllLERWQAVLAQTDVRQ 1210
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAG-------LTRRLSAAEGELEELVAR----LAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1211 RELEQLGRQLRYYRESADplgawlRDAKQRQEQIQAVPLANsQAVREQLRQEKALLEDIERHGEKVEECQRFAKQyinai 1290
Cdd:pfam19220 107 EELRIELRDKTAQAEALE------RQLAAETEQNRALEEEN-KALREEAQAAEKALQRAEGELATARERLALLEQ----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1291 kdyelqlvtykaqlepvaspaKKPKVQSGSESIIQEYVDLRTRYSELSTL---TSQYIRFISETLRRMEEEERLAEQQRA 1367
Cdd:pfam19220 175 ---------------------ENRRLQALSEEQAAELAELTRRLAELETQldaTRARLRALEGQLAAEQAERERAEAQLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1368 EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLrqssEAEIQAK 1447
Cdd:pfam19220 234 EAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL----EADLERR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1448 ARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaeAE 1527
Cdd:pfam19220 310 TQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEELQRER---AE 386
|
410
....*....|....
gi 1920237952 1528 LALrVQAEAEAARE 1541
Cdd:pfam19220 387 RAL-AQGALEIARE 399
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1354-1541 |
5.43e-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: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1354 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQglqrrmQEEVARREEVAVEAQEQKRSIQEEL 1433
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ------QEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1434 QHLRQSSEAEIQAKARQVeaaersrlrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1513
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 1920237952 1514 VQDETQR-KRQAEAElalrVQAEAEAARE 1541
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1356-1543 |
5.51e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 43.06 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1356 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER--------EAQGLQRRMQ-----EEVARREEVAVEA 1422
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegEIEAKEADHKgeteaEEVEHEGETEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1423 QEQKRSIQ--EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1497
Cdd:TIGR00927 726 TEDEGEIEtgEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1920237952 1498 AQKRQAQEEAERlRRQVQDETQRKRQAEAELALRVQAEAEAAREKQ 1543
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1482-1591 |
5.53e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1482 AEGELQALRARAE-EAEAQKR----QAQEEAERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALE-ELRLQ 1555
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREeELEKK 115
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237952 1556 AEEAERRLRQAEAERARqvqvaLETAQRSAEAELQS 1591
Cdd:PRK12704 116 EKELEQKQQELEKKEEE-----LEELIEEQLQELER 146
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1803-1912 |
5.64e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1803 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAVRQRAEAERVLAEKLAAISEATRLKTEAEIA-LKEKEAE 1873
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1920237952 1874 NErlrrlAEDEAFQRRLLEEQAAQHKAD-IEARL---AQLRKA 1912
Cdd:PRK11448 210 TS-----QERKQKRKEITDQAAKRLELSeEETRIlidQQLRKA 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2186-2627 |
6.09e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2186 EQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQ-RGQVEEELFSLRVQMEELGKLKARIEAENRA 2264
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2265 LVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE------DLAQQRALAEKMLKEKMQAVQEATRLKA 2338
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaelkeELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2339 EAELLQQQKELAQEQARRLQEDKEQMAQQLAQetqgFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFR 2418
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2419 KQAEDIGERLYRTELATQEKVMLVQTLETQRQQSdRDAERLREAIAELEHEKDK--LKQEAQLLQLKSE----------- 2485
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARAS-EERVRGGRAVEEVLKASIQgvHGTVAQLGSVGERyataievaagn 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2486 ---------EMQTVRQEQLLQETQALQQSFL-------SEKD-SLLQRERCI----------EQEKAKLEQLFQDEV--- 2535
Cdd:TIGR02169 548 rlnnvvvedDAVAKEAIELLKRRKAGRATFLplnkmrdERRDlSILSEDGVIgfavdlvefdPKYEPAFKYVFGDTLvve 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2536 ----------------------------------------------AKAQALREEQQRQQQQMQQEKQQLA---ASMEEA 2566
Cdd:TIGR02169 628 dieaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepAELQRLRERLEGLKRELSSLQSELRrieNRLDEL 707
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1920237952 2567 RRRQHEAEEGVRRQQEELQRLAQQQQQQEKLLAEenqrLRERLQHLEEERRAALARSEEIA 2627
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE----LEEDLSSLEQEIENVKSELKELE 764
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1353-1760 |
6.12e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1353 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQE 1431
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1432 ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1511
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1512 RQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQS 1591
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1592 EHASFAEKTAQLERTLKEEHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANEALRLRLQAEEVAQQKSLTQA 1671
Cdd:COG3064 264 LAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1672 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1751
Cdd:COG3064 344 LAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
....*....
gi 1920237952 1752 REAAAATQK 1760
Cdd:COG3064 424 LALAGAAGA 432
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1348-1456 |
6.16e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 41.90 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1348 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEahaqakaqAEREAQGLQRRMQEEVARReevavEA 1422
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIE--------AEKDAEVAKIQMQQKIMEK-----EA 223
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237952 1423 QEQKRSIQEELQHLRQSS--EAEIQAKARQVEAAER 1456
Cdd:cd03406 224 EKKISEIEDEMHLAREKAraDAEYYRALREAEANKL 259
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1740-2052 |
6.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1740 RQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1819
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1820 LAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRLLEEQAAQHK 1899
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1900 ADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 1979
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1920237952 1980 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2052
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
73-285 |
6.29e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 42.62 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 73 KTFTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---SLPREKGR-------MRFHKLQNVQIALDYLRHRQV 142
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 143 KLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMV------EGCQGLRCDN 209
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGlkgdkeEGIRSFGDPA 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 210 FTTSWRDGRLFNAIIHrhkPTLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPdEKSIITYV 282
Cdd:COG5069 532 GSVSGVFYLDVLKGIH---SELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP-RLDVLTFI 606
|
...
gi 1920237952 283 SSL 285
Cdd:COG5069 607 ESL 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1946-2428 |
6.30e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1946 EKAAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERvQKSLAAEEEAARQRKAALEEVERL 2025
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2026 KAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRseaeaARRAAEEAE 2105
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-----LQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2106 AARERAEREAAQSRRQVEEAERLKQsAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFA 2185
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2186 EQAL---------RQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAArqrgqveEELFSLRVQMEELGKLKA 2256
Cdd:COG4717 282 VLGLlallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2257 RIE-AENRALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmqAVQEATR 2335
Cdd:COG4717 355 EAEeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2336 LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQ-ETQGFQKTLETERQRQLEMSAEAER--LRLRVAE--MSRAQARA 2410
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEewAALKLALelLEEAREEY 509
|
490
....*....|....*....
gi 1920237952 2411 EEDAR-RFRKQAEDIGERL 2428
Cdd:COG4717 510 REERLpPVLERASEYFSRL 528
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2185-2438 |
6.41e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2185 AEQALRQKAQVEQELTALRLQLEETDHQK----------SILDEELQRLKAEVTEAARQRGQVEEELF-SLRVQMEELGK 2253
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLIRGATEGLCVHSLSkELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2254 LKARIEAEnRALVLRDKDSAQRLLQEEAEKM---KQVAEEAARLSVAAQEAARLRQLAEED------------------- 2311
Cdd:PLN02939 238 LKDDIQFL-KAELIEVAETEERVFKLEKERSlldASLRELESKFIVAQEDVSKLSPLQYDCwwekvenlqdlldratnqv 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2312 ------LAQQRALAEK--MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTL---- 2379
Cdd:PLN02939 317 ekaalvLDQNQDLRDKvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLsklk 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1920237952 2380 ETERQRQLEMSAEA------ERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRTELATQEK 2438
Cdd:PLN02939 397 EESKKRSLEHPADDmpsefwSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGK 461
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1131-1574 |
6.64e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1131 ATLPELEATKAALKKLRAQAEAQQPVFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVTLLLERWQAVLAQTDVRQ 1210
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1211 RELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRFAKQYINAI 1290
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1291 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESIIQEYVDLRTRYSELSTLTSQYIRFISETLRRMEEEERLAEQQRAEER 1370
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1371 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQ 1450
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1451 VEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAL 1530
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1920237952 1531 RVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQV 1574
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3696-3734 |
6.75e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.92 E-value: 6.75e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1920237952 3696 YLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVARQL 3734
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1442-1595 |
6.75e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.58 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1442 AEIQAKARQVEAAERSRLRIEEEIrvvrlqlEATERQRGGAEGElqALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1521
Cdd:PRK12678 29 PELRALAKQLGIKGTSGMRKGELI-------AAIKEARGGGAAA--AAATPAAPAAAARRAARAAAAARQAEQPAAEAAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1920237952 1522 RQAEAELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEAELQSEHAS 1595
Cdd:PRK12678 100 AKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERR 173
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1025-1622 |
6.80e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1025 EPARECAQRITEQQKAQAEVDGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIYlEKLKTISL 1104
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHTR-QQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1105 VIRSTQEAEEVLRAHeeQLKEAQAVPATLPELeatkaalkklrAQAEAQQPVFDALRDELRG-----AQEVGERLQQRhg 1179
Cdd:PRK10246 319 RLQSTMALRARIRHH--AAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1180 erdveveRWRERVTLLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLRDAKQRQEQIQAvplANSQA 1254
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1255 VREQLRQEKALLEDIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1307
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1308 ASPAKKPKVQSGSESIIQEYVDLRtrySELSTLTSQYIRFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1387
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1388 EAHAQ-AKAQAEREAQGLQRRMQEEVarrEEVAVEAQEQKRSIQEELQHLRQSSEAEIQAKARQV--EAAERSRL--RIE 1462
Cdd:PRK10246 596 DDIQPwLDAQEEHERQLRLLSQRHEL---QGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLpqEDEEASWLatRQQ 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1463 EEIRVVRLQLEATERQRGGAE--------GELQALRARAEEAEAQK-RQAQEEAERLRRQVQ-------DETQRKRQAEA 1526
Cdd:PRK10246 673 EAQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1527 ELALRVQAEAEAAREKQRALQALEELRLQAEEAERRLrqaeaERARQVQVALETAQRSAEAELQSEHASFAEKTAQLERT 1606
Cdd:PRK10246 753 QFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQI 827
|
650
....*....|....*.
gi 1920237952 1607 LKEEHVAVVQLREEAT 1622
Cdd:PRK10246 828 QQELAQLAQQLRENTT 843
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1717-2128 |
6.99e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1717 QQRLAAEQELIRLRAETEQGEQQRQLL---EEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRSTS 1793
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLdelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1794 EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLAAISEATRLKTEAEIALKEKEAE 1873
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1874 NERLRRLAEDEAFQRRLLEEQAAQHKADIEARLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKA 1953
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1954 ELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2033
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2034 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLERLRSEAEAARRAAEEAEAARERAER 2113
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410
....*....|....*
gi 1920237952 2114 EAAQSRRQVEEAERL 2128
Cdd:COG5278 483 ALAEAEAAAALAAAA 497
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1343-1537 |
7.06e-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: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1343 QYIRFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqakAQAEREAQgLQRRMQEEVARREEVAVEA 1422
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD---------EKAERDEL-RAKLYQEEQERKERQKERE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1423 QEQKRsiQEELQHLRQSSEAEIQAKARQvEAAERSRLRIEEEiRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1502
Cdd:pfam13868 226 EAEKK--ARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 1920237952 1503 AQEEAERLRRQVQDETQRKRQAEAELALRVQAEAE 1537
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2120-2501 |
7.11e-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: 42.57 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2120 RQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKQFAeQALRQKAQVEQEL 2199
Cdd:pfam07888 73 RQRRELES--------------------RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKD-ALLAQRAAHEARI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2200 TALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRAL--VLRDKDSAQRLL 2277
Cdd:pfam07888 132 RELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2278 QEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKELAQ---- 2351
Cdd:pfam07888 212 QDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQAAQltlq 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2352 --EQARRLQEDKEQMaqqlAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEmsraqaraeedARRFRKQAEdigerly 2429
Cdd:pfam07888 288 laDASLALREGRARW----AQERETLQQSAEADKDRIEKLSAELQRLEERLQE-----------ERMEREKLE------- 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2430 rTELATQEKVMLVQTLETQRQQSDrdaerLREAIAELEHEKDKLKQEAQllqlksEEMQTVRQEQLLQETQA 2501
Cdd:pfam07888 346 -VELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAEKQ------ELLEYIRQLEQRLETVA 405
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2216-2311 |
7.38e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2216 LDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAENRALvlrdkdsAQRLLQEEAEKMKQVAEEAARLS 2295
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL-------EAQLEQLQEKAAETSQERKQKRK 219
|
90
....*....|....*.
gi 1920237952 2296 VAAQEAARLRQLAEED 2311
Cdd:PRK11448 220 EITDQAAKRLELSEEE 235
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2246-2541 |
7.41e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.59 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2246 VQMEE---LGKLKARIEAEN-RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLA-EEDLAQQRALAE 2320
Cdd:pfam15964 341 VQMTEeanFEKTKALIQCEQlKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2321 KMLKEKMQAVQEATrlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAQETQgfqKTLETERQRQLEMS-AEAERLRL 2398
Cdd:pfam15964 421 KVTREKNSLVSQLE--EAQKQLASQEMDVTKVCGEmRYQLNQTKMKKDEAEKEH---REYRTKTGRQLEIKdQEIEKLGL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2399 RVAEMSRAQARAEEDARRFRKQAEDIGERLYRTE----LATQEKVMLVQTL----ETQRQQSDRDAERLREAIAELE--H 2468
Cdd:pfam15964 496 ELSESKQRLEQAQQDAARAREECLKLTELLGESEhqlhLTRLEKESIQQSFsneaKAQALQAQQREQELTQKMQQMEaqH 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2469 EKD----------------KLKQEAQLLQLKSEEM-QTVRQE--QLLQETQALQQSFLSEK-------DSLLQRERCIEQ 2522
Cdd:pfam15964 576 DKTvneqyslltsqntfiaKLKEECCTLAKKLEEItQKSRSEveQLSQEKEYLQDRLEKLQkrneeleEQCVQHGRMHER 655
|
330
....*....|....*....
gi 1920237952 2523 EKAKLEQLFQDEVAKAQAL 2541
Cdd:pfam15964 656 MKQRLRQLDKHCQATAQQL 674
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2196-2626 |
7.46e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2196 EQELTALRLQLEETDHQKSILDEELQRLKAEVTeAARQRGQV-EEELFSLRVQMEElgklKARIEAEnRALVLRDKDSAQ 2274
Cdd:pfam10174 302 ESELLALQTKLETLTNQNSDCKQHIEVLKESLT-AKEQRAAIlQTEVDALRLRLEE----KESFLNK-KTKQLQDLTEEK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2275 RLLQEEAEKMKQVAEEAARLSVAAQEaaRLRQLAEEDLAQQRALAEkmLKEKMQAVQEATRLKAEAelLQQQKELAQEQA 2354
Cdd:pfam10174 376 STLAGEIRDLKDMLDVKERKINVLQK--KIENLQEQLRDKDKQLAG--LKERVKSLQTDSSNTDTA--LTTLEEALSEKE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2355 R---RLQEDKEQMAQQLAQEtqgfqktLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAEDIGERLYRT 2431
Cdd:pfam10174 450 RiieRLKEQREREDRERLEE-------LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2432 ELATQEKVMLVQTLETQRQ--QSDRDAERLREAIAelehekDKLKQEAQLLQLKSEEMQTVRqeqllqetqalqqsflSE 2509
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLKkaHNAEEAVRTNPEIN------DRIRLLEQEVARYKEESGKAQ----------------AE 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2510 KDSLLQRERCIEQEK-------AKLEQLFQDEVaKAQALREEQQRQQQQMQQEKQqlAASMEEARRRQHEAEEGVRRQQ- 2581
Cdd:pfam10174 581 VERLLGILREVENEKndkdkkiAELESLTLRQM-KEQNKKVANIKHGQQEMKKKG--AQLLEEARRREDNLADNSQQLQl 657
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1920237952 2582 ----EELQRLAQQQQQQEKLLAEENQRLRERLQHLEE---ERRAALarsEEI 2626
Cdd:pfam10174 658 eelmGALEKTRQELDATKARLSSTQQSLAEKDGHLTNlraERRKQL---EEI 706
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2198-2541 |
7.48e-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: 42.70 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2198 ELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELG----KLKARIEA-ENralvlrDKDS 2272
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkynDLKKQKEElEN------ELNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2273 AQRLLQEEAEKMKQVAEEAAR----LSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ 2346
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKlellLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2347 -KELAQEQarrlQEDKEQMAQQLAQETQGFQKTLETERQRQlEMSAEAERLRlrvaemsraqaraeedarrfRKQAEDIG 2425
Cdd:TIGR04523 255 lNQLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN--------------------NQKEQDWN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2426 ERLyRTELATQEKVmlVQTLETQRQQSDRDAERLREAIAELEHEKDKLKQEAQLLQlkseemqtvrqEQLLQETQALQQs 2505
Cdd:TIGR04523 310 KEL-KSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ-----------RELEEKQNEIEK- 374
|
330 340 350
....*....|....*....|....*....|....*.
gi 1920237952 2506 FLSEKDSLLQRERCIEQEKAKLEQLFQDEVAKAQAL 2541
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1689-1829 |
7.56e-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: 41.51 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1689 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEA-- 1766
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1920237952 1767 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1829
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1189-1460 |
7.70e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1189 RERVTLLLERWQAVLAQTDVR---QRELEQLGRQLRYYRESADPLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKAL 1265
Cdd:COG4942 2 RKLLLLALLLALAAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1266 LEDIERHGEKVEECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESIIQEYvdlrtRYSELSTLTSQYI 1345
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1346 RFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRqlaeahaQAKAQAEREAQGLQRRMQEEVARREEVAVEAQEQ 1425
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1920237952 1426 KRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLR 1460
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1763-1884 |
7.74e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 42.61 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1763 ELEAELAKVRAEM--EVLLASKARAEEesrstseKSKQRLEAEAGRFR---ELAEEAARLRALAEEAKRQRQLAEEDAVR 1837
Cdd:pfam04147 155 EEEPERKKSKKEVmeEVIAKSKLHKYE-------RQKAKEEDEELREEldkELKDLRSLLSGSKRPKPEQAKKPEEKPDR 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 1838 QRAEAE-----RVLA-EKLAAISEatRLKTEAEIALKEKE----AENERLRRLAEDE 1884
Cdd:pfam04147 228 KKPDDDydklvRELAfDKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRMRGEE 282
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1697-1790 |
7.85e-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: 39.52 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1697 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEME 1776
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 1920237952 1777 VLLASKARAEEESR 1790
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1350-1463 |
8.23e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.02 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1350 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAEREAQGL-QRRMQEEVARREEVAVEAQEQKR 1427
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1920237952 1428 SIQEELQHLRQSSEAeiqAKARQVEAAERSRLRIEE 1463
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAERQRQEREK 123
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1229-1429 |
8.66e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1229 PLGAWLRDAKQRQEQIQAVPLANSQAVREQLRQEKALLEDIERHGEKVEECQRfakqyinAIKDYELQLVTYKAQL-EPV 1307
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASR-------KLRETQNTLNQLNKQIdELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1308 ASPAKKPKVQSGSESIIQEYVDLRTRYSE-------LSTLTSQ-------YIRFISE----------------TLRRMEE 1357
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAAFRQGEhtglqliLSGEESQrgerilaYFGYLNQarqetiaelkqtreelAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1358 EERLAEQQ----------------RAEERERLAEVEAALEK-QRQLAE--------------AHAQAKAQAEREAQGLQR 1406
Cdd:PRK11637 190 EEKQSQQKtllyeqqaqqqkleqaRNERKKTLTGLESSLQKdQQQLSElranesrlrdsiarAEREAKARAEREAREAAR 269
|
250 260
....*....|....*....|....
gi 1920237952 1407 -RMQEEVARREEVAVEAQEQKRSI 1429
Cdd:PRK11637 270 vRDKQKQAKRKGSTYKPTESERSL 293
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3695-3731 |
8.70e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 8.70e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1920237952 3695 RYLYGTGCVAGIYRPGSRQTLTIYQALKKGQLSAEVA 3731
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1717-1979 |
8.98e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1717 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKARAEEESRstseKS 1796
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK----EL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1797 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAVRQR--------------AEAERVLAEKLAaiseatRLKTE 1862
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGG--SIDKLRKEierlewrqqtevlsPEEEKELVEKIK------ELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1863 AEIALKEKEAENERLRRLAEDEAFQrrlleEQAAQHKADIEARLAQLRKASES------ELERQKGLVEDTLRQRRQVEE 1936
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELR-----KEAEEIHKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1920237952 1937 EILALKGSFEKAAAGKAELELELGRIRGTAEDTLRSKEQAEQE 1979
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2182-2373 |
9.21e-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: 42.12 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2182 KQFAEQALRQKAQVEQELTALRlqleETDHQKSILDEELQRLkaevtEAARQRGQVEEELFSLRVQMEELGKLKARIEAE 2261
Cdd:pfam10174 568 ARYKEESGKAQAEVERLLGILR----EVENEKNDKDKKIAEL-----ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2262 NRALVLRD---KDSAQRLLQE---EAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2334
Cdd:pfam10174 639 EEARRREDnlaDNSQQLQLEElmgALEKTRQELDATkARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAI 718
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1920237952 2335 RLK----AEAELLQQQKELAQEQARRLQEDKEQMAQQLAQETQ 2373
Cdd:pfam10174 719 SEKdaniALLELSSSKKKKTQEEVMALKREKDRLVHQLKQQTQ 761
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1353-1448 |
9.33e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.60 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1353 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAHAQAK---AQAEREAQGLqrrmqeevaRREEVAV---EAQEQ 1425
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKL---------AAEALAEaqaEAQAS 102
|
90 100
....*....|....*....|...
gi 1920237952 1426 KRSIQEELQHLRQSSEAEIQAKA 1448
Cdd:PRK07353 103 KEKARREIEQQKQAALAQLEQQV 125
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1494-1557 |
9.37e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.16 E-value: 9.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1920237952 1494 EEAEAQKRQAQEEAERLRrqvQDETQRKRQAE--AELALRVQAEAEAAREKQRALQALEELRLQAE 1557
Cdd:PLN02316 253 EKRRELEKLAKEEAERER---QAEEQRRREEEkaAMEADRAQAKAEVEKRREKLQNLLKKASRSAD 315
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1948-2449 |
9.52e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.54 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1948 AAAGKAELELELGRIRGTAEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA 2027
Cdd:COG3899 736 PPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGEL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2028 KVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ-----KEQELQQTLQQEQSVLERLRSEAEAARRAAE 2102
Cdd:COG3899 816 ALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAgletgDAALALLALAAAAAAAAAAAALAAAAAAAAR 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2103 EAEAARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHK 2182
Cdd:COG3899 896 LLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAA 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2183 QFAEQALRQKAQVEQELTALRLQLEETDHQKSILDEELQRLKAEVTEAARQRGQVEEELFSLRVQMEELGKLKARIEAEN 2262
Cdd:COG3899 976 AAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAA 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2263 RALVLRDKDSAQRLLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2342
Cdd:COG3899 1056 AAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAAL 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2343 LQQQKELAQEQARRLQEDKEQMAQQLAQETQGFQKTLETERQRQLEMSAEAERLRLRVAEMSRAQARAEEDARRFRKQAE 2422
Cdd:COG3899 1136 LLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALL 1215
|
490 500
....*....|....*....|....*..
gi 1920237952 2423 DIGERLYRTELATQEKVMLVQTLETQR 2449
Cdd:COG3899 1216 ALEAAALLLLLLLAALALAAALLALRL 1242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1508-2490 |
9.69e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1508 ERLRRQVQDETQRKRQAEAELALRVQAEAEA--------AREKQRALQALEELRLQAEEAERRLRQAEAERARQVQVALE 1579
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKAceirdqitSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1580 ---TAQRSAEAELQSEHASFAEKTAQL----ERTLKE-EHVAVVQLREEATRRAQQQAEAERARAEAERELERWQLKANE 1651
Cdd:TIGR00606 269 neiKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDlYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1652 ALRLRLQAEEVAQQKSLTQAEAEKQKEEAEREARRRGKAEEQAVRQrelaEQELEKQRQLAEG-TAQQRLAAEQELIRLR 1730
Cdd:TIGR00606 349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN----FHTLVIERQEDEAkTAAQLCADLQSKERLK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1731 aeteqgEQQRQLLEEELARLQREAAAATQKRRELEAELAKVRAEMEVLLASKAR--AEEESRSTSEKSKQRLEAEAGRFR 1808
Cdd:TIGR00606 425 ------QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRilELDQELRKAERELSKAEKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1809 ELAEEAARLRALAEEAKRQRQLAEEDAVRQRAEAERVLAEKLaaiseaTRLKTEA-EIALKEKEAENERLRRLAEDEAFQ 1887
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEML------TKDKMDKdEQIRKIKSRHSDELTSLLGYFPNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1888 RRLLE--EQAAQHKADIEARLAQLRKasesELERQKGLVEDTLRQRRQVEEEILALKGSFEKAAAGKAElELELGRIRGT 1965
Cdd:TIGR00606 573 KQLEDwlHSKSKEINQTRDRLAKLNK----ELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-ESDLERLKEE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1966 AEDTLRSKEQAEQEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2045
Cdd:TIGR00606 648 IEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2046 QLQLAqEAAQKRLQAEEKAhafavqqkeqelqqtlqqeqsvLERLRSEAEAARRAAEEAEAARERAEREAAQSRRQVEEA 2125
Cdd:TIGR00606 728 MLGLA-PGRQSIIDLKEKE----------------------IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2126 ERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQaADAEMEKHKQFAEQALRQKAQVEQEltalrlq 2205
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEK-QEKQHELDTVVSKIELNRKLIQDQQ------- 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2206 lEETDHQKSILDeELQRLKAEVTEAARQRGQVEEELFSLRVQMEELgklkARIEAENRALVLRDKDSAQRLLQEEAEKMK 2285
Cdd:TIGR00606 857 -EQIQHLKSKTN-ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL----IREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2286 QVAEEAARLSVAAQE-AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2364
Cdd:TIGR00606 931 SKETSNKKAQDKVNDiKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ 1010
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2365 AQQLAQETQGFQKTLETERQRQLEMSAE---AERLRLRVAEMSRAQARAEEDARRFRKQaedigERLYRTELATQEKVML 2441
Cdd:TIGR00606 1011 KIQERWLQDNLTLRKRENELKEVEEELKqhlKEMGQMQVLQMKQEHQKLEENIDLIKRN-----HVLALGRQKGYEKEIK 1085
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 2442 VQTLETQRQQSDRDAERLREAIAELEHEKDKLKQ--------EAQLLQLKSEEMQTV 2490
Cdd:TIGR00606 1086 HFKKELREPQFRDAEEKYREMMIVMRTTELVNKDldiyyktlDQAIMKFHSMKMEEI 1142
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2435-2685 |
9.69e-03 |
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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: 42.27 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2435 TQEKVMLVQTLETQRQQSDRDAERLREaIAELEHEKDKLKQEAQLLQLKSEEMQTVRQEQLLQETQALQQSFLSEKDSLL 2514
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIID-LEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2515 QRERCIEQEKAKLEQLFQDEVAKAQALREEQQRQQQQMQQEKQQLAASMEEARRRQHEAEEGVRRQQEELQRLAQQQQQQ 2594
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 2595 EKLLAEENQRLRERLQHLEEERRAALARSEEIAPSRAAAARALPNGQDAADGPAAAAEPEHAFD-GLRRKVPAQRLQEVG 2673
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSsAAKLKEEELELKSEE 403
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250
....*....|..
gi 1920237952 2674 VLSAEELQQLAQ 2685
Cdd:pfam02463 404 EKEAQLLLELAR 415
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| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1347-1563 |
9.73e-03 |
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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: 40.82 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1347 FISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAqglqRRMQEEVARREEVAVEAQEQK 1426
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKAR------QALAQTIARQK-QLERRL----EQQTEQAKKLEEKAQAALTKG 80
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1920237952 1427 RsiqeelQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1506
Cdd:pfam04012 81 N------EELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTSL 154
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170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1920237952 1507 AERLRRQVQDETQRKRQAEAELALRVQAEAEAAREKQRALQaLEELRLQAEEAERRL 1563
Cdd:pfam04012 155 GSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
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