|
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 ... |
176-297 |
2.85e-70 |
|
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: 231.52 E-value: 2.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 176 DRVQKKTFTKWVNKHLLKHWRaeaqrHVNDLYEDLRDGHNLISLLEVLSGDTLPRERdvirnlrlprekGRMRFHKLQNV 255
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRER------------GRMRFHRLQNV 63
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2069539781 256 QIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 297
Cdd:cd21188 64 QTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
310-415 |
2.99e-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: 231.45 E-value: 2.99e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 310 MTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLD 389
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 2069539781 390 PEDVDVPQPDEKSIITYVSSLYDAMP 415
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
173-308 |
2.22e-68 |
|
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: 226.83 E-value: 2.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 173 DERDRVQKKTFTKWVNKHLLKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRErdvirnlrlpreKGRMRFHKL 252
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE------------KGRMRFHKL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 253 QNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 308
Cdd:cd21235 64 QNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
165-306 |
9.06e-68 |
|
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: 225.25 E-value: 9.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 165 ERAVIRIADERDRVQKKTFTKWVNKHLLKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRErdvirnlrlpreK 244
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPRE------------K 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 245 GRMRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 306
Cdd:cd21236 67 GRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
311-415 |
4.19e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 216.87 E-value: 4.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDP 390
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 2069539781 391 EDVDVPQPDEKSIITYVSSLYDAMP 415
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
173-307 |
9.66e-59 |
|
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: 199.10 E-value: 9.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 173 DERDRVQKKTFTKWVNKHLLKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGdtlprerdvirnLRLPREKGRMRFHKL 252
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSG------------VKLPREKGRMRFHRL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 253 QNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 307
Cdd:cd21237 64 QNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
311-415 |
4.25e-58 |
|
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: 196.75 E-value: 4.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQdLGVTRLLDP 390
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 2069539781 391 EDVDVPQPDEKSIITYVSSLYDAMP 415
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
309-415 |
1.09e-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: 175.62 E-value: 1.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 309 DMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQdLGVTRLL 388
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 2069539781 389 DPEDVDVPQPDEKSIITYVSSLYDAMP 415
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
311-411 |
7.87e-47 |
|
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: 164.51 E-value: 7.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDP 390
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 2069539781 391 EDVDVPQPDEKSIITYVSSLY 411
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1893-2832 |
2.20e-45 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 183.42 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1893 NEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRStSEKSKQILEAEASKLRELAEEAarlRALSEEAKRQRQLAEEE 1972
Cdd:PTZ00121 1038 NDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKP-SYKDFDFDAKEDNRADEATEEA---FGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1973 ATHQRAEAERilKEKLVAINEASRLKA--EAEIALKEKEAENERLRRLAEDeayQRRLLEEQAAQHKQDIEEKiaqlKKS 2050
Cdd:PTZ00121 1114 ARKAEEAKKK--AEDARKAEEARKAEDarKAEEARKAEDAKRVEIARKAED---ARKAEEARKAEDAKKAEAA----RKA 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2051 SEselerqkslvddtVRQrrlvEEEIRilklnfeKASHGKTDLELELTRIKQSAEEIQRSKEqaEREAEELRQLaleEEN 2130
Cdd:PTZ00121 1185 EE-------------VRK----AEELR-------KAEDARKAEAARKAEEERKAEEARKAED--AKKAEAVKKA---EEA 1235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2131 HRREAEAKVKKISAAEQEAARQCKAALEEVERLKA--KAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHlAAVQ 2208
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK-AEEA 1314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2209 QKEQELLQTRQQEQSILDKLREEAERAKKAAEDAefariKAEQEAAlsrqlVEEAERMKQRAEEEAQTKAKAQEDAEKLR 2288
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA-----KAEAEAA-----ADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2289 KEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEEtdhqksilEEEQQRLKDEVTEA 2368
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE--------AKKADEAKKKAEEA 1456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2369 MKQkvqveEELFKVKVQMEELIKLKTRIEEENKMLITKDKDNMQKFLAEEAEKmkqvAEEAARLSVEAQEAARLRELAEQ 2448
Cdd:PTZ00121 1457 KKA-----EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK----AAEAKKKADEAKKAEEAKKADEA 1527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2449 DLAQQRSLAEKIlkEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKeQMQLRLAEEA--------EGFQKTLEAE 2520
Cdd:PTZ00121 1528 KKAEEAKKADEA--KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK-NMALRKAEEAkkaeeariEEVMKLYEEE 1604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2521 RQRQLEITANAERLKVQVTELSlaqaKAEEEAKR---FKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKL 2597
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELK----KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2598 RKAIADLEQEKEKLKREAELlQQKSEEMQTAQKEQLRQETQMLQQtfrsekdvllQKERFVEEEKAKLEKlfQEEVNKAQ 2677
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKKA----------EEENKIKAEEAKKEA--EEDKKKAE 1747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2678 GLKAEQErQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEEN--QKLREKLEQLQEEQK 2755
Cdd:PTZ00121 1748 EAKKDEE-EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiiEGGKEGNLVINDSKE 1826
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2756 TALAQTREIMIQTDDLPQEVVAPSQVPQMKAVPNGRDMIDGISQNGEAELAFDGIRQKVSAKKLAEagiLSRESMEK 2832
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEK---IDKDDIER 1900
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
178-298 |
2.58e-45 |
|
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: 160.24 E-value: 2.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 178 VQKKTFTKWVNKHLLKhwraEAQRHVNDLYEDLRDGHNLISLLEVLSGdtlprerdvirnLRLPREKGRMRFHKLQNVQI 257
Cdd:cd21186 2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTG------------KKLKPEKGRMRVHHLNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2069539781 258 ALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 298
Cdd:cd21186 66 ALQVLEQNNVKLVNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
165-294 |
5.26e-45 |
|
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: 159.84 E-value: 5.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 165 ERAVIR-IADERDRVQKKTFTKWVNKHLLKHwraeaQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRErdvirnlrlprE 243
Cdd:cd21246 2 ERSRIKaLADEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKP-----------T 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 244 KGRMRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 294
Cdd:cd21246 66 KGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
311-411 |
8.79e-45 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 158.71 E-value: 8.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDP 390
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2069539781 391 EDVDVPQPDEKSIITYVSSLY 411
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
172-411 |
1.02e-42 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 168.58 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 172 ADERDRVQKKTFTKWVNKHLLKhwraEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERdvirnlrlprEKGRMRFHK 251
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEYN----------ETPETRIHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 252 LQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GM 330
Cdd:COG5069 69 MENVSGRLEFIKGKGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 331 RCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVE--NLEQAFSVAEQDLGVTRLLDPEDV-DVPQPDEKSIITYV 407
Cdd:COG5069 146 DTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYV 225
|
....
gi 2069539781 408 SSLY 411
Cdd:COG5069 226 SWYI 229
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1511-2730 |
3.82e-42 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 171.93 E-value: 3.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1511 LAEVEAQLEKQRQ-LAEAHARAKAQAEKEALELQRRMEEEVS-RRQLVAVDAEQQKQTIQQelsqmkLSSDAQIQAKlKL 1588
Cdd:NF041483 96 LRDARAQTQRILQeHAEHQARLQAELHTEAVQRRQQLDQELAeRRQTVESHVNENVAWAEQ------LRARTESQAR-RL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1589 IEEvefSRRKVEEEIRMVRLQLE---ATERQRAGAEDElqalRDRAEeAERQKRLAQEEAERLRKQVKDESQKKREAEDE 1665
Cdd:NF041483 169 LDE---SRAEAEQALAAARAEAErlaEEARQRLGSEAE----SARAE-AEAILRRARKDAERLLNAASTQAQEATDHAEQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1666 LKHKVQAEQQAAREKQKALEDLQKLRLQaeEAERRMKQAELEKERQVQLAHEAAQK---SAEADLQSRRLSFAEKTAQLe 1742
Cdd:NF041483 241 LRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAAAKqlaSAESANEQRTRTAKEEIARL- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1743 lslqqehitITHLQEEAERLKKlqlEAEQSREEADKEVEKWRQKANEALRlRLQAEEVAHKKALAQEEAEKQKEDAEREA 1822
Cdd:NF041483 318 ---------VGEATKEAEALKA---EAEQALADARAEAEKLVAEAAEKAR-TVAAEDTAAQLAKAARTAEEVLTKASEDA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1823 RKRSK-AEESALRQKELAEQELEKQRKLAEGTAQQkflaeqelirLKAEVengeqqrllleeelfrlKNEVNEAVQKRKE 1901
Cdd:NF041483 385 KATTRaAAEEAERIRREAEAEADRLRGEAADQAEQ----------LKGAA-----------------KDDTKEYRAKTVE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1902 LEEELAKLRAEMELLLQSKAKTEEESRSTS--EKSKQILEAeASKLRELAEEAarlralseeakrqRQLAEEEATHQRAE 1979
Cdd:NF041483 438 LQEEARRLRGEAEQLRAEAVAEGERIRGEArrEAVQQIEEA-ARTAEELLTKA-------------KADADELRSTATAE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1980 AERILKEklvAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAA-QHKQDIEEKIAQLKKSSESELERQ 2058
Cdd:NF041483 504 SERVRTE---AIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAArELREETERAIAARQAEAAEELTRL 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2059 KslvddTVRQRRLVEEEiRILKLNFEKASHGKTDLELELTRIK-QSAEEIQRSKEQAEREAEELRQLALEEENHRR-EAE 2136
Cdd:NF041483 581 H-----TEAEERLTAAE-EALADARAEAERIRREAAEETERLRtEAAERIRTLQAQAEQEAERLRTEAAADASAARaEGE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2137 A-KVKKISAAEQEAARQCKAALEEVERLKAKAEEA--RRQKELAEKESERQiqlaQEAAQKRIVAEEKAHlAAVQQKEQE 2213
Cdd:NF041483 655 NvAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAaeRVGTEAAEALAAAQ----EEAARRRREAEETLG-SARAEADQE 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2214 LLQTRQQEQSILDKLREEAERAKKAA----EDAEFARIK----AEQEA--------ALSRQLVEEAERMKQRAEEEAQ-T 2276
Cdd:NF041483 730 RERAREQSEELLASARKRVEEAQAEAqrlvEEADRRATElvsaAEQTAqqvrdsvaGLQEQAEEEIAGLRSAAEHAAErT 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2277 KAKAQEDAEKLRKEAELEAARRAQAEQaalKQKQLADAEMAKHKKFAEQTLRQkAQVEQEltkvKLQLEETDHQKSILEE 2356
Cdd:NF041483 810 RTEAQEEADRVRSDAYAERERASEDAN---RLRREAQEETEAAKALAERTVSE-AIAEAE----RLRSDASEYAQRVRTE 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2357 EQQRLKDEVTEAMKQKVQVEEELFKVK----VQMEELIKLKTRIEEENKMLITKDKDNMQKFLAEEAEKMK-QVAEEAAR 2431
Cdd:NF041483 882 ASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQ 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2432 LSVEAQ-EAARLRELAEQDLAQQRSLAEKILKE----KMQAVQEATRLKAEA--EVLQKQKDLAQEQAKKLQEDKEQMQL 2504
Cdd:NF041483 962 LIAEATgEAERLRAEAAETVGSAQQHAERIRTEaervKAEAAAEAERLRTEAreEADRTLDEARKDANKRRSEAAEQADT 1041
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2505 RLAEEAEGFQKTLEAERQRQLEITANAErlkvqvtelslAQAKAEEEAKRfkKQAEQISQKlhqtelATQEKMTLVqtle 2584
Cdd:NF041483 1042 LITEAAAEADQLTAKAQEEALRTTTEAE-----------AQADTMVGAAR--KEAERIVAE------ATVEGNSLV---- 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2585 iQRQQSDSD----------------AEKLRKAI-ADLEQEKEKLKREAellqqkSEEMQTAQKEQLRQETQMLQQTFRSE 2647
Cdd:NF041483 1099 -EKARTDADellvgarrdatairerAEELRDRItGEIEELHERARRES------AEQMKSAGERCDALVKAAEEQLAEAE 1171
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2648 KdvllQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEearkkqAEAEENVRQKQEELQRLEK 2727
Cdd:NF041483 1172 A----KAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAE------AEAKRTVEEGKRELDVLVR 1241
|
...
gi 2069539781 2728 QRQ 2730
Cdd:NF041483 1242 RRE 1244
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
174-298 |
1.73e-41 |
|
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: 149.45 E-value: 1.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 174 ERDRVQKKTFTKWVNKHLLKHwraEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERDviRNLRlprekgrmRFHKLQ 253
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKG--RRLK--------RVHFLS 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2069539781 254 NVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 298
Cdd:cd21241 68 NINTALKFLESKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
298-413 |
7.68e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 147.89 E-value: 7.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 298 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSV 377
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2069539781 378 AEQDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 413
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1518-2292 |
1.44e-40 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 167.24 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1518 LEKQRQLAEAHARAKAQAEKEALELQRR--MEEEVSRRQLVAVDAEQQKQTIQQELSQMKLS--SDAQIQAKLKLIEEVE 1593
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIDgnHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNraDEATEEAFGKAEEAKK 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1594 FSRRKVEEEIRMVRLQLEATERQRA----GAEDELQALRDRAEEAERQKRLAQ--EEAERLRKQVKDESQKKREAEDELK 1667
Cdd:PTZ00121 1106 TETGKAEEARKAEEAKKKAEDARKAeearKAEDARKAEEARKAEDAKRVEIARkaEDARKAEEARKAEDAKKAEAARKAE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 HKVQAEQQAAREKQKALEDLQKLR--LQAEEAERRMKQAELEKERQVQLAHEAAQ--KSAEADLQSRRLSFAEKTAQLEL 1743
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEeeRKAEEARKAEDAKKAEAVKKAEEAKKDAEeaKKAEEERNNEEIRKFEEARMAHF 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1744 SLQQEHITITHlQEEAERLKKLQ--LEAEQSRE-EADKEVEKWRQKANEALRlrlqAEEvAHKKAlaqEEAEKQKEDAER 1820
Cdd:PTZ00121 1266 ARRQAAIKAEE-ARKADELKKAEekKKADEAKKaEEKKKADEAKKKAEEAKK----ADE-AKKKA---EEAKKKADAAKK 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1821 EARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQ--ELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQK 1898
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkaDAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1899 RKELEEelAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEA-EASKLRELAEEAARLRALSEEAKRQRQlaEEEATHQR 1977
Cdd:PTZ00121 1417 KKKADE--AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkKAEEAKKKAEEAKKADEAKKKAEEAKK--ADEAKKKA 1492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1978 AEAerilKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDeayQRRLLEEQAAQHKQDIEE--KIAQLKKSSE-SE 2054
Cdd:PTZ00121 1493 EEA----KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADElkKAEELKKAEEkKK 1565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2055 LERQKSLVDDTVRQRRLVEEEIRILKLNFEKAshgktdLELELTRIKQSAEEIqRSKEQAEREAEELRQlaleEENHRRE 2134
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEV------MKLYEEEKKMKAEEA-KKAEEAKIKAEELKK----AEEEKKK 1634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2135 AEaKVKKISAAEQEAARQCKAALEE----VERLKAKAEEARRQKELAEKESE----RQIQLAQEAAQKRIVAEEKAHLAA 2206
Cdd:PTZ00121 1635 VE-QLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEELKKKEAE 1713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2207 VQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEfariKAEQEAALSRQLVEEAERMKQ--RAEEEAQTKAKAQEDA 2284
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK----KDEEEKKKIAHLKKEEEKKAEeiRKEKEAVIEEELDEED 1789
|
....*...
gi 2069539781 2285 EKLRKEAE 2292
Cdd:PTZ00121 1790 EKRRMEVD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1621-2475 |
1.50e-40 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 167.24 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1621 EDELQALRD-RAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKlrlqAEEAER 1699
Cdd:PTZ00121 1078 DFDFDAKEDnRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARK----AEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1700 RMKQAELEKERQVQLAHEAAQ-KSAEAdlqSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADK 1778
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDaKKAEA---ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1779 EVEKWRQKANEALR---LRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQ 1855
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKaeeERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1856 QKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSK 1935
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1936 QILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAeriLKEKLVAINEASRLKAEAEIALKEKEAENERL 2015
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE---AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2016 RRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEeirilklnFEKASHGKTDLEL 2095
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE--------AKKAEEAKKADEA 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2096 ELTRIKQSAEEIQRSKEQaeREAEELRQLaleeENHRREAEAKVKKISAAEQ----EAARQCKAALEEVERLKAKAEEAR 2171
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEEL--KKAEEKKKA----EEAKKAEEDKNMALRKAEEakkaEEARIEEVMKLYEEEKKMKAEEAK 1613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2172 RqkelAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELlqtRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQ 2251
Cdd:PTZ00121 1614 K----AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL---KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2252 EAALSRQLVEEAERmKQRAEEEAQTKAKAQEDAEKLRKEAEleaarRAQAEQAALKQKQLADAEMAKHKKFAEQtlrQKA 2331
Cdd:PTZ00121 1687 EKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKKAEE-----ENKIKAEEAKKEAEEDKKKAEEAKKDEE---EKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2332 QVEQELTKVKLQLEETDHQKSILEEEQQRLKDEvteamKQKVQVEEELFKVKVQMEELIKLKtrieEENKMLITKDKDNM 2411
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE-----KRRMEVDKKIKDIFDNFANIIEGG----KEGNLVINDSKEME 1828
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2412 QKFLAEEAEKMKQVAEEAArlSVEAQEAARLRELAEQDLAQQRSLAEKILKEK-MQAVQEATRLK 2475
Cdd:PTZ00121 1829 DSAIKEVADSKNMQLEEAD--AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDdEEEIEEADEIE 1891
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
310-415 |
5.97e-40 |
|
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: 145.15 E-value: 5.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 310 MTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLD 389
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 2069539781 390 PEDVDVPQPDEKSIITYVSSLYDAMP 415
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
165-294 |
9.85e-40 |
|
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: 144.75 E-value: 9.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 165 ERAVIR-IADERDRVQKKTFTKWVNKHLLKHwraeaQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRErdvirnlrlprE 243
Cdd:cd21193 2 EKGRIRaLQEERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP-----------N 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 244 KGRMRFHKLQNVQIALDYLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 294
Cdd:cd21193 66 RGRLRVQKIENVNKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
174-298 |
1.01e-39 |
|
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: 144.64 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 174 ERDRVQKKTFTKWVNKHLLKHWRAEAqrhVNDLYEDLRDGHNLISLLEVLSGDtlprerdvirnlRLPREKGRM--RFHK 251
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQ------------KLPIESGRVlqRAHK 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2069539781 252 LQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 298
Cdd:cd21190 66 LSNIRNALDFLTKRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1627-2259 |
1.40e-39 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 162.80 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1627 LRDRAEEAERQKRLAQEEAER-------LRKQVKdesQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAER 1699
Cdd:COG1196 170 YKERKEEAERKLEATEENLERledilgeLERQLE---PLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1700 RMKQAELEKERQvqlahEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHIT----------ITHLQEEAERLKKLQLEA 1769
Cdd:COG1196 247 ELEELEAELEEL-----EAELAELEAELEELRLELEELELELEEAQAEEYELlaelarleqdIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1770 EQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKL 1849
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1850 AEGTAQQKFLAEQELIRLKAEVEngeqqrllleeelfRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRS 1929
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELE--------------ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1930 TSEKSKQILEAEASKLRELAEEAARLRALsEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKE 2009
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLL-LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2010 AENERLRRLAEDEAYQRRLLEEQAAQHKQDIEekIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHG 2089
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP--LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2090 KTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEE 2169
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2170 ARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILD--KLREEAERAKK---------- 2237
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDleELERELERLEReiealgpvnl 784
|
650 660
....*....|....*....|..
gi 2069539781 2238 AAEDaEFARIKAEQEaALSRQL 2259
Cdd:COG1196 785 LAIE-EYEELEERYD-FLSEQR 804
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
307-411 |
1.81e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 140.91 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 307 SEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTR 386
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 2069539781 387 LLDPEDVDVPQPDEKSIITYVSSLY 411
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
171-294 |
3.25e-38 |
|
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: 141.32 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 171 IADERDRVQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRErdvirnlrlprEKGRMRFH 250
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKP-----------TRGRMRIH 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2069539781 251 KLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 294
Cdd:cd21318 95 SLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
307-411 |
5.71e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.81 E-value: 5.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 307 SEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTR 386
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 2069539781 387 LLDPEDVDVPQPDEKSIITYVSSLY 411
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1511-2128 |
6.47e-38 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 157.41 E-value: 6.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1511 LAEVEAQLEK-QRQlaeaharaKAQAEKeALELQRRMEEevsRRQLVAVDAEQQKQtiqqelsqmklssdAQIQAKLKLI 1589
Cdd:COG1196 195 LGELERQLEPlERQ--------AEKAER-YRELKEELKE---LEAELLLLKLRELE--------------AELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1590 EEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALrdRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHK 1669
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEA--QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1670 VQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEH 1749
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1750 ITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAE 1829
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1830 ESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELF---RLKNEVNEAVQKRKELEEEL 1906
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaALQNIVVEDDEVAAAAIEYL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1907 AKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKE 1986
Cdd:COG1196 567 KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1987 KLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTV 2066
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2067 RQRRLVEEEIRILKLNFEKASHGKTDLELELTriKQSAEEIQRSKEQAEREAEEL---RQLALEE 2128
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPE--PPDLEELERELERLEREIEALgpvNLLAIEE 789
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1512-2292 |
9.05e-38 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 158.00 E-value: 9.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1512 AEVEAQLEKQRQLAEAHARAKAQAEKEA--LELQRRMEE----EVSRRQLVAVDAEQQKQTIQ-QELSQMKLSSDAQIQA 1584
Cdd:PTZ00121 1124 AEDARKAEEARKAEDARKAEEARKAEDAkrVEIARKAEDarkaEEARKAEDAKKAEAARKAEEvRKAEELRKAEDARKAE 1203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1585 KLKLIEEVefsrRKVEEEIRmvrlqleATERQRAGAEDELQALRDRAEEAERQKRLAQEEAER----------LRKQVKD 1654
Cdd:PTZ00121 1204 AARKAEEE----RKAEEARK-------AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRkfeearmahfARRQAAI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1655 ESQKKREAEDELK--HKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERqvqlAHEAAQKSAEADLQSRRL 1732
Cdd:PTZ00121 1273 KAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK----ADAAKKKAEEAKKAAEAA 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1733 SFAEKTAQLELSLQQEHITITHLQEEAERLK--KLQLEAEQSR--EEADKEVEKWRQKANEalrlrLQAEEVAHKKAlaq 1808
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadAAKKKAEEKKkaDEAKKKAEEDKKKADE-----LKKAAAAKKKA--- 1420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1809 EEAEKQKEDAEREARKRSKAEESalRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEvengeqqrllleeelfrl 1888
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE------------------ 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1889 knevneavQKRKELEeelAKLRAEmelllQSKAKTEEESRSTSEKSKqileAEASKLRELAEEAARLRAlSEEAKRQRQL 1968
Cdd:PTZ00121 1481 --------EAKKADE---AKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAKKADEA 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1969 AEEEathQRAEAERILKEKLVAINEASRlkaEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLK 2048
Cdd:PTZ00121 1540 KKAE---EKKKADELKKAEELKKAEEKK---KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2049 KSSEselERQKSlvdDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQlalEE 2128
Cdd:PTZ00121 1614 KAEE---AKIKA---EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK---AE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2129 ENHRREAEA------------KVKKISAAEQEAARQCKAALEE----VERLKAKAEEARRQKELAEKESERQIQLAQEAA 2192
Cdd:PTZ00121 1685 EDEKKAAEAlkkeaeeakkaeELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2193 QKRIVAEE--KAHLAAVQQ--KEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQ 2268
Cdd:PTZ00121 1765 EEEKKAEEirKEKEAVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLE 1844
|
810 820
....*....|....*....|....*
gi 2069539781 2269 RAEEEAQTK-AKAQEDAEKLRKEAE 2292
Cdd:PTZ00121 1845 EADAFEKHKfNKNNENGEDGNKEAD 1869
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
165-294 |
1.43e-36 |
|
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: 136.34 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 165 ERAVIR-IADERDRVQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRErdvirnlrlprE 243
Cdd:cd21317 17 ERSRIKaLADEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKP-----------T 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 244 KGRMRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 294
Cdd:cd21317 81 KGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
310-411 |
1.49e-36 |
|
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: 135.37 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 310 MTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLD 389
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 2069539781 390 PEDVDVPQPDEKSIITYVSSLY 411
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1677-2621 |
1.52e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 154.14 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1677 AREKQKALEDLQKLRLQAEEAeRRMKQAELEKERQVQLAHEAAQKSAEADlQSRRLSFAEKTAQLELSLQQEHITITHLQ 1756
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEA-KKTETGKAEEARKAEEAKKKAEDARKAE-EARKAEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1757 EEAERLKKLQLEAEQSREEADKEVEKWRQkaneALRLRlQAEEVAHKKALAQEEAEKQKEDAeREARKRSKAEEsaLRQK 1836
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRK----AEELR-KAEDARKAEAARKAEEERKAEEA-RKAEDAKKAEA--VKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1837 ELAEQELEKQRKlaegtAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKEleeelaklraemell 1916
Cdd:PTZ00121 1233 EEAKKDAEEAKK-----AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA--------------- 1292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1917 lqskakteEESRSTSEKSKqileaeASKLRELAEEAARlralSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASR 1996
Cdd:PTZ00121 1293 --------DEAKKAEEKKK------ADEAKKKAEEAKK----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1997 LKAEAEIALKEKEAEnerlrRLAEDEAYQRrlleEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRlvEEEI 2076
Cdd:PTZ00121 1355 AADEAEAAEEKAEAA-----EKKKEEAKKK----ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK--ADEA 1423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2077 RILKLNFEKASHGKTDLELeltriKQSAEEIQRSKEQAeREAEELRQLAlEEENHRREAEAKVKKISAAEqEAARQCKAA 2156
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEE-----AKKADEAKKKAEEA-KKAEEAKKKA-EEAKKADEAKKKAEEAKKAD-EAKKKAEEA 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2157 LEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRivAEEKAHLAAVQQKEQELlqtRQQEQSILDKLREEAERAK 2236
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK--KADEAKKAEEKKKADEL---KKAEELKKAEEKKKAEEAK 1570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2237 KAAEDAEFARIKAEQEAALSRQLVEEAERMkqrAEEEAQTKAKAQEDAEKLRKEAEleaarraqaeqaALKQKQLADAEM 2316
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKL---YEEEKKMKAEEAKKAEEAKIKAE------------ELKKAEEEKKKV 1635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2317 AKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQksilEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRI 2396
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2397 EEENK---MLITKDKDNMQKF--LAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEA 2471
Cdd:PTZ00121 1712 AEEKKkaeELKKAEEENKIKAeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2472 TRLKAEaevlQKQKDLaQEQAKKLQEDKEQMQLRLAEEAEGFQ---KTLEAERQRQLEITANAERLKVQVTELSLAQAKA 2548
Cdd:PTZ00121 1792 RRMEVD----KKIKDI-FDNFANIIEGGKEGNLVINDSKEMEDsaiKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNK 1866
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2549 EEEAKRFKKQAEQISQKLHQTELATQekmtlVQTLEIQRQQSDSDAEKLRKAIADLEQEKEK-LKREAELLQQK 2621
Cdd:PTZ00121 1867 EADFNKEKDLKEDDEEEIEEADEIEK-----IDKDDIEREIPNNNMAGKNNDIIDDKLDKDEyIKRDAEETREE 1935
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
295-411 |
5.20e-36 |
|
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: 134.80 E-value: 5.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 295 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQA 374
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2069539781 375 FSVAEQDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 411
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
174-298 |
5.40e-36 |
|
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: 133.80 E-value: 5.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 174 ERDRVQKKTFTKWVNKHLLKHWRAEAqrhVNDLYEDLRDGHNLISLLEVLSGDtlprerdvirnlRLPREKGRMRFHKLQ 253
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQ------------QLPREKGHNVFQCRS 65
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2069539781 254 NVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 298
Cdd:cd21242 66 NIETALSFLKNKSIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
314-415 |
6.37e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 133.32 E-value: 6.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 314 EKLLL-WSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED 392
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2069539781 393 VDVPQPDEKSIITYVSSLYDAMP 415
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1627-2398 |
2.57e-35 |
|
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: 149.44 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1627 LRDRAEEAERQKRLAQEEAERLRKQVkdesqkkREAEDELKH-KVQAEQ-QAAREKQKALEDLQK----LRLQAEEAERR 1700
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDIL-------NELERQLKSlERQAEKaERYKELKAELRELELallvLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1701 MKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLElSLQQEHITITHLQEEAERLKKLQLE----AEQSREEA 1776
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE-ELQKELYALANEISRLEQQKQILRErlanLERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1777 DKEVEKWRQKANEAlrlrlqAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQ 1856
Cdd:TIGR02168 322 EAQLEELESKLDEL------AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1857 KfLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAvqKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQ 1936
Cdd:TIGR02168 396 A-SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1937 ILEAEASKLRELAEEAARLRALS--EEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKE------- 2007
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLErlQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGrlqavvv 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2008 --KEAENERLRRLAEDEAYQRRLLEEQAAQHkQDIEEKIAQLKKSSESELERQKSLV----------------------- 2062
Cdd:TIGR02168 553 enLNAAKKAIAFLKQNELGRVTFLPLDSIKG-TEIQGNDREILKNIEGFLGVAKDLVkfdpklrkalsyllggvlvvddl 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2063 DDTVRQRRLVEEEIRILKLNFEKASHG----KTDLELELTRIKQSAE--EIQRSKEQAEREAEELRQLALEEENHRREAE 2136
Cdd:TIGR02168 632 DNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2137 AKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQ 2216
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2217 TRQQEQ-----SILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEA 2291
Cdd:TIGR02168 792 EQLKEElkalrEALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2292 EleaarraQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLK---DEVTEA 2368
Cdd:TIGR02168 872 E-------SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLQER 944
|
810 820 830
....*....|....*....|....*....|....*....
gi 2069539781 2369 MKQKVQVEEELFKVKVQM---------EELIKLKTRIEE 2398
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKieddeeearRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1508-2042 |
3.04e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.55 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALEL---QRRMEEEVSRRQLVAVDAEQQKQTIQQELS---QMKLSSDAQ 1581
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELrleLEELELELEEAQAEEYELLAELARLEQDIArleERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1582 IQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKRE 1661
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1662 AEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQL 1741
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1742 ELSLQQEhitithLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLR----LQAEEVAHKKALAQEEAEKQKED 1817
Cdd:COG1196 478 ALAELLE------ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavavLIGVEAAYEAALEAALAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1818 AEREARKRSKAEESALRQKE--LAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNE- 1894
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAr 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1895 ---AVQKRKELEEELAKLRAEMELLLQSKAKTEEESRstseKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEE 1971
Cdd:COG1196 632 leaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR----ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 1972 EATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEE 2042
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1936-2756 |
9.39e-35 |
|
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: 147.51 E-value: 9.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1936 QILEAEASKLRELAEEAA---RLRALSEEAkrQRQLAEEEATHQRAEAerILKEKLVAINeasRLKAEAEIALKEKEAEN 2012
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKET--ERKLERTRENLDRLED--ILNELERQLK---SLERQAEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2013 ErlRRLAEDEAYQRRLLEEQAAQHK-QDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKT 2091
Cdd:TIGR02168 221 E--LRELELALLVLRLEELREELEElQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2092 DLELELTRIKQSAEEIQRSKEQAEREAEELrqlaleeENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEAR 2171
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEEL-------ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2172 RQKELAEKESErqiQLAQEAAQ-KRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAE 2250
Cdd:TIGR02168 372 SRLEELEEQLE---TLRSKVAQlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2251 QEaalsrQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRkeAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQK 2330
Cdd:TIGR02168 449 LE-----ELQEELERLEEALEELREELEEAEQALDAAE--RELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGI 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2331 AQVEQELTKVKLQLE---ETDhqksiLEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKD 2407
Cdd:TIGR02168 522 LGVLSELISVDEGYEaaiEAA-----LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2408 KDNMQKFLAEEAEKMKQVA----------------EEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEA 2471
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERR 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2472 TRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQlRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEE 2551
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2552 AKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQtAQKE 2631
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE-RRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2632 QLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLfQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEA 2711
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 2069539781 2712 EENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKT 2756
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA 958
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1043-1120 |
1.11e-34 |
|
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: 128.87 E-value: 1.11e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 1043 LSWQYLQRHIQQIQSWSLLIFRTMPPEEYRQTLRSLETHYQEFLRSSQDSQNFLPDDRLQVEREYSACTQKYELLLRS 1120
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1936-2625 |
1.18e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 146.62 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1936 QILEAEASKLRELAEEAA---RLRALSEEAKRQRqlaeeEATHQR-AEAERILKEKlvaINEASRLKAEAEIALKEKEAE 2011
Cdd:COG1196 148 RIIEAKPEERRAIIEEAAgisKYKERKEEAERKL-----EATEENlERLEDILGEL---ERQLEPLERQAEKAERYRELK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2012 NERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKiaqlkkssESELERQkslvddtVRQRRLVEEEIRILKLNFEkashgkt 2091
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEEL--------EAELEEL-------EAELAELEAELEELRLELE------- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2092 DLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEAr 2171
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2172 rQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQ 2251
Cdd:COG1196 357 -EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2252 EAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKA 2331
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2332 QVEQELTKVKLQLEETDhqksilEEEQQRLKDEVTEAMKQKVQVEEELfkvkvqmeeliKLKTRIEeenkmLITKDKDNM 2411
Cdd:COG1196 516 LAGLRGLAGAVAVLIGV------EAAYEAALEAALAAALQNIVVEDDE-----------VAAAAIE-----YLKAAKAGR 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2412 QKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEkilkekmqAVQEATRLKAEAEVLQKQKDLAQEQ 2491
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD--------TLLGRTLVAARLEAALRRAVTLAGR 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2492 AKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTEL 2571
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2572 ATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEM 2625
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1752-2777 |
1.30e-34 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 147.28 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1752 ITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALR------------LRLQAEEVAHKkalAQEEAEKQKEDAE 1819
Cdd:NF041483 17 LSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRN---AQIQADQLRADAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1820 REARKrSKAEESALRQkELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEV-----ENGEQQRLLLEEELFRLKNEVNE 1894
Cdd:NF041483 94 RELRD-ARAQTQRILQ-EHAEHQARLQAELHTEAVQRRQQLDQELAERRQTVeshvnENVAWAEQLRARTESQARRLLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1895 AvqkRKELEEELAKLRAEMELLLQskaktEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEAT 1974
Cdd:NF041483 172 S---RAEAEQALAAARAEAERLAE-----EARQRLGSEAESARAEAEAILRRARKDAERLLNAASTQAQEATDHAEQLRS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1975 HQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQA-AQHKQDIEEKIAQLKKSSES 2053
Cdd:NF041483 244 STAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAnEQRTRTAKEEIARLVGEATK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2054 ELERQKSLVDDTVRQRRLVEEeiRILKLNFEKA-SHGKTDLELELTRIKQSAEEIQrskEQAEREAEELRQLALEE-ENH 2131
Cdd:NF041483 324 EAEALKAEAEQALADARAEAE--KLVAEAAEKArTVAAEDTAAQLAKAARTAEEVL---TKASEDAKATTRAAAEEaERI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2132 RREAEAKVKKISAAEQEAARQCK-AALEEVERLKAKA----EEARRQKELAEkeserqiQLAQEAAQKRIVAEEKAHLAA 2206
Cdd:NF041483 399 RREAEAEADRLRGEAADQAEQLKgAAKDDTKEYRAKTvelqEEARRLRGEAE-------QLRAEAVAEGERIRGEARREA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2207 VQQKEqellQTRQQEQSILDKLREEAERAK-KAAEDAEFARIKA-EQEAALSRQLVEEAERMKQRAEEEaqtKAKAQEDA 2284
Cdd:NF041483 472 VQQIE----EAARTAEELLTKAKADADELRsTATAESERVRTEAiERATTLRRQAEETLERTRAEAERL---RAEAEEQA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2285 EKLRKEAELEAARRAQAEQAALKQKQL-ADAEMAKHKKFAEQTLrqkAQVEQELTKVKlqlEETDHQKSILEEEQQRLKD 2363
Cdd:NF041483 545 EEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEERL---TAAEEALADAR---AEAERIRREAAEETERLRT 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2364 EVTEAMKQ-KVQVEEELFKVKVQMEE------------LIKLKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAA 2430
Cdd:NF041483 619 EAAERIRTlQAQAEQEAERLRTEAAAdasaaraegenvAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAA 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2431 RLSVEAQ-EAARLRELAEQDLAQQRSLAEkilKEKMQAVQEATRLKAEAevlQKQKDLAQEQAKKLQEDKEQMQLRLAEE 2509
Cdd:NF041483 699 EALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA---RKRVEEAQAEAQRLVEEADRRATELVSA 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2510 AEgfqktlEAERQRQLEITANAERLKVQVTELSLAqakAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQ 2589
Cdd:NF041483 773 AE------QTAQQVRDSVAGLQEQAEEEIAGLRSA---AEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQ 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2590 SDSDAEK--LRKAIADLEQEKEKLKREAELLQQK-----SEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEK 2662
Cdd:NF041483 844 EETEAAKalAERTVSEAIAEAERLRSDASEYAQRvrteaSDTLASAEQDAARTRADAREDANRIRSDAAAQADRLIGEAT 923
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2663 AKLEKLFQEEVNKAQGLKAE-----QERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLA 2737
Cdd:NF041483 924 SEAERLTAEARAEAERLRDEaraeaERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA 1003
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 2069539781 2738 EENQKLR-----EKLEQLQEEQKTALAQTREIMIQTDDLPQEVVA 2777
Cdd:NF041483 1004 AEAERLRteareEADRTLDEARKDANKRRSEAAEQADTLITEAAA 1048
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2097-2763 |
1.66e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 146.24 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2097 LTRIKQSAEEIQRSKEQAEREAEELRQ-LALEEENHRREAEAKVKKISAAEQEAARqckaALEEVERLKAKAEEARRQKE 2175
Cdd:COG1196 188 LERLEDILGELERQLEPLERQAEKAERyRELKEELKELEAELLLLKLRELEAELEE----LEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2176 LAEKESErQIQLAQEAAQKRIvaeekahlAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAAL 2255
Cdd:COG1196 264 ELEAELE-ELRLELEELELEL--------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2256 SRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQ 2335
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2336 ELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENkmlitkdkdnmqkfL 2415
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL--------------A 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2416 AEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLqkqkdLAQEQAKKL 2495
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA-----ALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2496 QEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQE 2575
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2576 KMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQtfrsekdvLLQKE 2655
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE--------EEEER 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2656 RFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKkqlttVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEK- 2734
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE-----LLEEEALEELPEPPDLEELERELERLEREIEALGPv 782
|
650 660 670
....*....|....*....|....*....|.
gi 2069539781 2735 -LLA-EENQKLREKLEQLQEEQKTaLAQTRE 2763
Cdd:COG1196 783 nLLAiEEYEELEERYDFLSEQRED-LEEARE 812
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
178-296 |
2.47e-34 |
|
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: 129.06 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 178 VQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERdvirnlrlprEKGRMRFHKLQNVQI 257
Cdd:cd21215 4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRYN----------KNPKMRVQKLENVNK 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 2069539781 258 ALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 296
Cdd:cd21215 69 ALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
176-294 |
2.89e-34 |
|
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: 128.66 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 176 DRVQKKTFTKWVNKHLLKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPrerdvirnlrlPREKGRMRFHKLQNV 255
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLP-----------KPERGKMRFHKIANV 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 2069539781 256 QIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 294
Cdd:cd21214 67 NKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1508-2537 |
5.76e-34 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 144.97 E-value: 5.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRL--------AEVEAQLEKQRQLAE-----AHARAK-AQAEKEALELQRRMEEEVSRRQLVAVD--AEQQKQTIQQEL 1571
Cdd:NF041483 195 RQRLgseaesarAEAEAILRRARKDAErllnaASTQAQeATDHAEQLRSSTAAESDQARRQAAELSraAEQRMQEAEEAL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1572 SQM-----KLSSDAQIQA--KLKLIEEVEFSR-RKVEEEIrmVRLQLEATERQRAGAEDELQALRDRAEEAErqkRLAQE 1643
Cdd:NF041483 275 REAraeaeKVVAEAKEAAakQLASAESANEQRtRTAKEEI--ARLVGEATKEAEALKAEAEQALADARAEAE---KLVAE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1644 EAERLRKQVkdesqkkreAEDELKHKVQAEQQAAREKQKALEDLQK-LRLQAEEAERRMKQAELEKERQVQLAHEAAQK- 1721
Cdd:NF041483 350 AAEKARTVA---------AEDTAAQLAKAARTAEEVLTKASEDAKAtTRAAAEEAERIRREAEAEADRLRGEAADQAEQl 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1722 --SAEADLQSRRLSFAEktaqlelslqqehitithLQEEAERLKKlqlEAEQSREEADKEVEKWRQKA-NEALRlrlQAE 1798
Cdd:NF041483 421 kgAAKDDTKEYRAKTVE------------------LQEEARRLRG---EAEQLRAEAVAEGERIRGEArREAVQ---QIE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1799 EVAHK------KALAQEEAEKQKEDAEREaRKRSKAEESALRQKELAEQELEKQRklaegtaqqkflAEQELIRLKAEvE 1872
Cdd:NF041483 477 EAARTaeelltKAKADADELRSTATAESE-RVRTEAIERATTLRRQAEETLERTR------------AEAERLRAEAE-E 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1873 NGEQQRLLLEEELFRLKNEVNEAVQKRK-ELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRelAEE 1951
Cdd:NF041483 543 QAEEVRAAAERAARELREETERAIAARQaEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLR--TEA 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1952 AARLRAL----SEEAKRQRQLAEEEATHQRAEAERI-LKEKLVAINEASRLKAEAEIALKEKEAE------------NER 2014
Cdd:NF041483 621 AERIRTLqaqaEQEAERLRTEAAADASAARAEGENVaVRLRSEAAAEAERLKSEAQESADRVRAEaaaaaervgteaAEA 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2015 LRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDT-VRQRRLVEE-EIRILKLNFEKASHGKT- 2091
Cdd:NF041483 701 LAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEAqAEAQRLVEEaDRRATELVSAAEQTAQQv 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2092 ---------DLELELTRIKQSAEEI-QRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAA-----RQCKAA 2156
Cdd:NF041483 781 rdsvaglqeQAEEEIAGLRSAAEHAaERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAkalaeRTVSEA 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2157 LEEVERLKAKAEE-ARRQKELAekeSERQIQLAQEAAQKRIVAEEKAH---LAAVQQKEQELLQTRQQEQSILDKLREEA 2232
Cdd:NF041483 861 IAEAERLRSDASEyAQRVRTEA---SDTLASAEQDAARTRADAREDANrirSDAAAQADRLIGEATSEAERLTAEARAEA 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2233 ERAK-KAAEDAEFARIKA-EQEAALSRQLVEEAERMKQRAeeeAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQ 2310
Cdd:NF041483 938 ERLRdEARAEAERVRADAaAQAEQLIAEATGEAERLRAEA---AETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAR 1014
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2311 lADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDE--------VTEAMKQKVQVEEE---- 2378
Cdd:NF041483 1015 -EEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEaeaqadtmVGAARKEAERIVAEatve 1093
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2379 ----LFKVKVQMEELI--------KLKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEA-ARLREL 2445
Cdd:NF041483 1094 gnslVEKARTDADELLvgarrdatAIRERAEELRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQlAEAEAK 1173
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2446 AEQDLAQQRSLAEKIlkeKMQAVQEATRLKAEAEvlQKQKDLAQEqAKKLQEDKEQMQLRLAEEAegfQKTLEAERQRQL 2525
Cdd:NF041483 1174 AKELVSDANSEASKV---RIAAVKKAEGLLKEAE--QKKAELVRE-AEKIKAEAEAEAKRTVEEG---KRELDVLVRRRE 1244
|
1130
....*....|..
gi 2069539781 2526 EItaNAERLKVQ 2537
Cdd:NF041483 1245 DI--NAEISRVQ 1254
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
311-411 |
7.19e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 127.52 E-value: 7.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDP 390
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2069539781 391 EDVDVPQPDEKSIITYVSSLY 411
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1938-2611 |
1.09e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.54 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1938 LEAEASKLRELAEEAARLRALSEEAkRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRR 2017
Cdd:COG1196 198 LERQLEPLERQAEKAERYRELKEEL-KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2018 LAEDEAYQRRLLEEQAAqhkqdiEEKIAQLKKSSESELERQKSLvddtvrQRRLVEEEIRILKLNFEkashgktdLELEL 2097
Cdd:COG1196 277 EELELELEEAQAEEYEL------LAELARLEQDIARLEERRREL------EERLEELEEELAELEEE--------LEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2098 TRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAE-EARRQKEL 2176
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEaEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2177 AEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALS 2256
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2257 RQLVEEAE---------RMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTL 2327
Cdd:COG1196 497 LEAEADYEgflegvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2328 RQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAmkQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKD 2407
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV--LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2408 KDNMQKFLAEEAEKmkqvAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDL 2487
Cdd:COG1196 655 GGSAGGSLTGGSRR----ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2488 AQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQleitaNAERLKVQVTELS---LAqakAEEEAkrfkkqaEQISQ 2564
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEELPEPPDLEELER-----ELERLEREIEALGpvnLL---AIEEY-------EELEE 795
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2069539781 2565 KLhqTELATQeKMTLVQTLEiqrqqsdsdaeKLRKAIADLEQEKEKL 2611
Cdd:COG1196 796 RY--DFLSEQ-REDLEEARE-----------TLEEAIEEIDRETRER 828
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1933-2764 |
1.49e-33 |
|
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: 143.57 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1933 KSKQILEAEASKLRELAEEAARLR---ALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKE 2009
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRlkrKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2010 AENERLRRLAEDEAYQRRLLEEQAA------QHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNF 2083
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRdeqeeiESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2084 EKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERL 2163
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2164 KAKAEEARRQKELAEKESERQIQLAQEAAQ--------KRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERA 2235
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLElarqledlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2236 KKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAE 2315
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2316 MAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTR 2395
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2396 IEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLK 2475
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2476 AEAE-VLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKR 2554
Cdd:pfam02463 703 KKEQrEKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2555 FKKQAEQISQKLHQTELATQEKMT---------LVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEM 2625
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALeeelkeeaeLLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2626 QTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQ--KQMEQEKKQLTTVLEE 2703
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKeeAEILLKYEEEPEELLL 942
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2704 ARKKQAEAEENVRQKQEELQRLEKQRQK-----------QEKLLAEENQKLREKLEQLQEEQKTALAQTREI 2764
Cdd:pfam02463 943 EEADEKEKEENNKEEEEERNKRLLLAKEelgkvnlmaieEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1899-2486 |
4.31e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 141.61 E-value: 4.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1899 RKELEEELAKLRAEMELLLQSKA-KTEEESRSTSEKSKQILEAEAsKLRELAEEAARLRALSEEAKRQRQLAEEEATHQR 1977
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYRElKEELKELEAELLLLKLRELEA-ELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1978 AEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAY---QRRLLEEQAAQHKQDIEEKIAQLKKSSESE 2054
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEleeELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2055 LERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHgKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRRE 2134
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2135 AEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIV---AEEKAHLAAVQQKE 2211
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLlleAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2212 QELLQTRQQEQSILDKLREEAERAKKAAEDAEFAR---------------IKAEQEAALSRQLVEEAERMKQRAEEEAQT 2276
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAlqnivveddevaaaaIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2277 KAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEE 2356
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2357 EQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELiKLKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEA 2436
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEE-ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2437 QEAARLRELAEQDLAQQRSLAEKILKEK----MQAVQEATRLKAEAEVLQKQKD 2486
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEALgpvnLLAIEEYEELEERYDFLSEQRE 805
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
310-408 |
1.12e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 124.07 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 310 MTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLD 389
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 2069539781 390 PEDVDVPQPDEKSIITYVS 408
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
298-413 |
3.31e-32 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 123.02 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 298 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSV 377
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2069539781 378 AEQDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 413
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
173-298 |
5.47e-32 |
|
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: 122.34 E-value: 5.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 173 DERDRVQKKTFTKWVNKHLLKHWRaeaqRHVNDLYEDLRDGHNLISLLEVLSGDtlprerdvirnlRLPREKGRMRFHKL 252
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQ------------KLVKEKGSTRVHAL 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2069539781 253 QNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 298
Cdd:cd21231 65 NNVNKALQVLQKNNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1508-2289 |
2.98e-31 |
|
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: 135.95 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEevsrrqlvavdAEQQKQTIQQELsqmkLSSDAQIQAKLK 1587
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKEL----YALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAerqkrlaQEEAERLRKQVKDESQKKREAEDELK 1667
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL-------KEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 HKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLElSLQQ 1747
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE-ELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1748 EHITithLQEEAERLKKLQLEAEQSREEADKEVE--KWRQKANEALRLRLQ------AEEVAHKKALA------------ 1807
Cdd:TIGR02168 455 ELER---LEEALEELREELEEAEQALDAAERELAqlQARLDSLERLQENLEgfsegvKALLKNQSGLSgilgvlselisv 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1808 QEEAEKQKEDAEREARKR--SKAEESALRQKE-LAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEE 1884
Cdd:TIGR02168 532 DEGYEAAIEAALGGRLQAvvVENLNAAKKAIAfLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1885 LFRLK------------NEVNEAVQKRKELEEELAKLRAEMELLLQSKAKT---EEESRSTSEKSKQILEAEAsKLRELA 1949
Cdd:TIGR02168 612 PKLRKalsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITggsAKTNSSILERRREIEELEE-KIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1950 EEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLL 2029
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2030 EEqAAQHKQDIEEKIAQLkkssESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQR 2109
Cdd:TIGR02168 771 EE-AEEELAEAEAEIEEL----EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2110 SKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKelaeKESERQIQLAQ 2189
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR----SELRRELEELR 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2190 EaaqkrivaeekaHLAAVQQKEQELlqtRQQEQSILDKLREE----AERAKKAAEDAEFARIKAEQE-AALSRQL----- 2259
Cdd:TIGR02168 922 E------------KLAQLELRLEGL---EVRIDNLQERLSEEysltLEEAEALENKIEDDEEEARRRlKRLENKIkelgp 986
|
810 820 830
....*....|....*....|....*....|....*
gi 2069539781 2260 -----VEEAERMKQRAEEEAQTKAKAQEDAEKLRK 2289
Cdd:TIGR02168 987 vnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
314-415 |
3.40e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 120.06 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 314 EKLLL-WSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED 392
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2069539781 393 VDVPQPDEKSIITYVSSLYDAMP 415
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1812-2398 |
4.90e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 135.06 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1812 EKQKEDAER----EARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFR 1887
Cdd:COG1196 206 ERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1888 LKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALsEEAKRQRQ 1967
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA-EAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1968 LAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQL 2047
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2048 KKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNfekashgkTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALE 2127
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAAL--------AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2128 EENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAV 2207
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2208 QQKEQELLQTRQQEQSILDKLREEAERAkkAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKL 2287
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLG--RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2288 RKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTE 2367
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
570 580 590
....*....|....*....|....*....|.
gi 2069539781 2368 AmkqkvqvEEELFKVKVQMEELIKLKTRIEE 2398
Cdd:COG1196 755 E-------LPEPPDLEELERELERLEREIEA 778
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
310-408 |
6.89e-31 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 119.17 E-value: 6.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 310 MTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLD 389
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 2069539781 390 PEDVDVPQPDEKSIITYVS 408
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1508-2403 |
7.28e-31 |
|
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: 134.71 E-value: 7.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQMKLSSDAQIQAKLK 1587
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELK 1667
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 hkvqAEQQAAREKQKALEDLQKLRLQAEEAERRMKQaELEKERQVQLAHEAAQKSAEADLQSrrlsfAEKTAQLELSLQQ 1747
Cdd:pfam02463 332 ----KEKEEIEELEKELKELEIKREAEEEEEEELEK-LQEKLEQLEEELLAKKKLESERLSS-----AAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1748 EHI-TITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRS 1826
Cdd:pfam02463 402 EEEkEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1827 KAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQ--KRKELEE 1904
Cdd:pfam02463 482 LQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEvsATADEVE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1905 ELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERIL 1984
Cdd:pfam02463 562 ERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1985 KEKL-VAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKI-AQLKKSSESELERQKSLV 2062
Cdd:pfam02463 642 KAKEsGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKkKEQREKEELKKLKLEAEE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2063 DDTVRQRRLVEEEIRILKLNFEKASHGKtdLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKki 2142
Cdd:pfam02463 722 LLADRVQEAQDKINEELKLLKQKIDEEE--EEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLK-- 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2143 sAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQ 2222
Cdd:pfam02463 798 -AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2223 SILDKLREEAERAKKAAEDAEfARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAE 2302
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKE-EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2303 QAALKQKQLADAEMAKHKK-----FAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKdevtEAMKQKVQVEE 2377
Cdd:pfam02463 956 EEEEERNKRLLLAKEELGKvnlmaIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK----EFLELFVSINK 1031
|
890 900
....*....|....*....|....*.
gi 2069539781 2378 ELFKVKVQMEELIKLKTRIEEENKML 2403
Cdd:pfam02463 1032 GWNKVFFYLELGGSAELRLEDPDDPF 1057
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2040-2642 |
1.41e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 133.52 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2040 IEEKIAQLKKsseseLERQKslvdDTVRQRRLVEEEIRILKLnfEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAE 2119
Cdd:COG1196 195 LGELERQLEP-----LERQA----EKAERYRELKEELKELEA--ELLLLKLRELEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2120 ELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEArrQKELAEKESERQIQLAQEAAQKRIVAE 2199
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL--EERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2200 EKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAK 2279
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2280 AQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQ 2359
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2360 RLKDEVTEAmkQKVQVEEELFKVKVQMEELIKLKTRIEEEnkmLITKDKDNMQKFLAEEAEKMKQVAEEAARlsveaQEA 2439
Cdd:COG1196 502 DYEGFLEGV--KAALLLAGLRGLAGAVAVLIGVEAAYEAA---LEAALAAALQNIVVEDDEVAAAAIEYLKA-----AKA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2440 ARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEA 2519
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2520 ERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRfKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRK 2599
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE-RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2069539781 2600 AIADLEQEKEKLKREAELLQQKSEEMQTAQK-EQLRQETQMLQQ 2642
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEELPEPPDlEELERELERLER 774
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
316-411 |
3.67e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 117.06 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 316 LLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED-VD 394
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 2069539781 395 VPQPDEKSIITYVSSLY 411
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
314-416 |
7.06e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 116.57 E-value: 7.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 314 EKLLL-WSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-VENLEQAFSVAEQDLGVTRLLDPE 391
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 2069539781 392 DVDVPQPDEKSIITYVSSLYDAMPR 416
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
165-294 |
1.12e-29 |
|
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: 117.45 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 165 ERAVIR-IADERDRVQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRErdvirnlrlprE 243
Cdd:cd21316 39 ERSRIKaLADEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKP-----------T 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 244 KGRMRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 294
Cdd:cd21316 103 KGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
178-298 |
5.34e-29 |
|
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: 113.92 E-value: 5.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 178 VQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRerdVIRNlrlPRekgrMRFHKLQNVQI 257
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGR---VIKK---PL----NQHQKLENVTL 68
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2069539781 258 ALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 298
Cdd:cd21227 69 ALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
174-300 |
6.18e-29 |
|
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: 113.83 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 174 ERDRVQKKTFTKWVNKHLLKhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGdtlprerdviRNLRLPREKGRMRFHKLQ 253
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSG----------QNLLQEYKPSSHRIFRLN 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2069539781 254 NVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 300
Cdd:cd21191 68 NIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
178-298 |
9.03e-29 |
|
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: 113.18 E-value: 9.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 178 VQKKTFTKWVNKHLLKhwraEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERdvirnlrlprekGRMRFHKLQNVQI 257
Cdd:cd21232 2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKER------------GSTRVHALNNVNR 65
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2069539781 258 ALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 298
Cdd:cd21232 66 VLQVLHQNNVELVNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
177-299 |
1.32e-28 |
|
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: 113.32 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 177 RVQKKTFTKWVNKHLLKhwraeAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERdvirnlrlprEKGRMRFHKLQNVQ 256
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFN----------KRPTFRSQKLENVS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2069539781 257 IALDYLKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 299
Cdd:cd21311 79 VALKFLEEDEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
314-413 |
2.17e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.99 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 314 EKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED- 392
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 2069539781 393 VDVPQPDEKSIITYVSSLYDA 413
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
296-413 |
2.55e-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: 112.49 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 296 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAF 375
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 2069539781 376 SVAEQDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 413
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1789-2723 |
2.93e-28 |
|
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: 126.24 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1789 EALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLK 1868
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1869 AEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRstsekskqileaEASKLREL 1948
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS------------ELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1949 AEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKlvaineasrlkaEAEIALKEKEAENERLRRLAEDEAYQRRL 2028
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL------------EIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2029 LEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQ 2108
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2109 RSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQckAALEEVERLKAKAEEARRQKELAEKESERQIQLA 2188
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQ--KESKARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2189 QEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQlveeaERMKQ 2268
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN-----LAQLD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2269 RAEEEAQTKAKAQEDAEKLRKEAELEAAR--RAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEE 2346
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKesAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2347 TDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEEliklkTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVA 2426
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ-----DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2427 EEAARLSVEaqeaarlRELAEQDLAQQRSLAEKILKEKMQAVQEatrlkaEAEVLQKQKDLAQEQAKKLQEDKEQMQLRL 2506
Cdd:pfam02463 765 EKSELSLKE-------KELAEEREKTEKLKVEEEKEEKLKAQEE------ELRALEEELKEEAELLEEEQLLIEQEEKIK 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2507 AEEAEGFQKTLEAERQRQLEITANAERLKvqvtelslaqakaEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQ 2586
Cdd:pfam02463 832 EEELEELALELKEEQKLEKLAEEELERLE-------------EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2587 RQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLE 2666
Cdd:pfam02463 899 KKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLM 978
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2667 KLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQ 2723
Cdd:pfam02463 979 AIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNK 1035
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1767-2644 |
3.06e-28 |
|
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: 126.24 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1767 LEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQ 1846
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1847 RKLAEGTAQQKflaEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAE--MELLLQSKAKTE 1924
Cdd:pfam02463 243 QELLRDEQEEI---ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLerRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1925 EESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIA 2004
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2005 LKEKEAENERLRRLAEDEAYQRRLLEEQAAqhKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFE 2084
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEEL--EILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2085 KASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLK 2164
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2165 AKAEEA----RRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSiLDKLREEAERAKKAAE 2240
Cdd:pfam02463 558 DEVEERqklvRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK-RAKVVEGILKDTELTK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2241 DAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHK 2320
Cdd:pfam02463 637 LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2321 KFAEQTLRQKaqVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEEN 2400
Cdd:pfam02463 717 LEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2401 KMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLR---ELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAE 2477
Cdd:pfam02463 795 KLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEElalELKEEQKLEKLAEEELERLEEEITKEELLQELLL 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2478 AEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAER--QRQLEITANAERLKVQVTELSLAQAKAEEEAKRF 2555
Cdd:pfam02463 875 KEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEieERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2556 KKQAEQISQKLhqtelatqekmtlvqtleiqRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQ 2635
Cdd:pfam02463 955 KEEEEERNKRL--------------------LLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
....*....
gi 2069539781 2636 ETQMLQQTF 2644
Cdd:pfam02463 1015 TCQRLKEFL 1023
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1708-2722 |
5.18e-28 |
|
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: 125.29 E-value: 5.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1708 KERQVQLAHEAAQKSAE--ADLQSRRLSFAEKTAQLELSLQQEhitiTHLQEEAERL------KKLQLEAEQSREEADKE 1779
Cdd:pfam01576 10 KEEELQKVKERQQKAESelKELEKKHQQLCEEKNALQEQLQAE----TELCAEAEEMrarlaaRKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1780 VEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAER-EARKRSKAEESALRQKELAEQELEKQRKLAEgtaqqkf 1858
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvTTEAKIKKLEEDILLLEDQNSKLSKERKLLE------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1859 laeqelirlkaevengeqqrllleeelfRLKNEVNEAVQKRKELEEELAKLRAEMELL---LQSKAKTEEESRSTSEKSK 1935
Cdd:pfam01576 159 ----------------------------ERISEFTSNLAEEEEKAKSLSKLKNKHEAMisdLEERLKKEEKGRQELEKAK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1936 QILEAEASklrELAEEAARLRALSEEAKRQRQLAEEEathqraeaeriLKEKLVAINEASRLKAEAEIALKEKEAENERL 2015
Cdd:pfam01576 211 RKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLEEETAQKNNALKKIRELEAQISEL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2016 RRLAEDEAYQRrlleEQAAQHKQDIEEKIAQLKKSSESELerqkslvDDTVRQRRLV---EEEIRILK--LNFEKASHgk 2090
Cdd:pfam01576 277 QEDLESERAAR----NKAEKQRRDLGEELEALKTELEDTL-------DTTAAQQELRskrEQEVTELKkaLEEETRSH-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2091 tDLELELTRIKQSA--EEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAE 2168
Cdd:pfam01576 344 -EAQLQEMRQKHTQalEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLS 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2169 EARRQK-ELAEKESERQIQLA------QEAAQKRI-VAEEKAHLAAVQQKEQELLQ--TRQQ------------EQSILD 2226
Cdd:pfam01576 423 ESERQRaELAEKLSKLQSELEsvssllNEAEGKNIkLSKDVSSLESQLQDTQELLQeeTRQKlnlstrlrqledERNSLQ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2227 KLREEAERAKKAAED---------AEFARiKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAAR 2297
Cdd:pfam01576 503 EQLEEEEEAKRNVERqlstlqaqlSDMKK-KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQE 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2298 RAQAEQAALKQKQLADAEMAKHKKF--------------AEQTLRQKAQVEQELTKV---KLQLEETDHQKSILEEEQQR 2360
Cdd:pfam01576 582 LDDLLVDLDHQRQLVSNLEKKQKKFdqmlaeekaisaryAEERDRAEAEAREKETRAlslARALEEALEAKEELERTNKQ 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2361 LKDEVTEAMKQKVQVEE---ELFKVKVQME-ELIKLKTRIEE-ENKMLITKDKD-----NMQKFLA---------EEA-- 2419
Cdd:pfam01576 662 LRAEMEDLVSSKDDVGKnvhELERSKRALEqQVEEMKTQLEElEDELQATEDAKlrlevNMQALKAqferdlqarDEQge 741
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2420 EKMKQVAEEAARLSVEAQEAARLRELA-------EQDLAQQRSLAEKILKEKMQAVQEATRLKA---------------- 2476
Cdd:pfam01576 742 EKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKLQAqmkdlqreleearasr 821
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2477 -----------------EAEVLQKQKDLA-QEQAKK-LQEDKEQMQLRLAEEAEGfqKTLEAERQRQLEitanaERLKVQ 2537
Cdd:pfam01576 822 deilaqskesekklknlEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDEKRRLE-----ARIAQL 894
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2538 VTELSLAQAKAEEEAKRFKKQAEQISQKlhQTELATQEkmTLVQTLEIQRQQSDSDAEKLRKAIADLEQE-KEKLKREAE 2616
Cdd:pfam01576 895 EEELEEEQSNTELLNDRLRKSTLQVEQL--TTELAAER--STSQKSESARQQLERQNKELKAKLQEMEGTvKSKFKSSIA 970
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2617 LLQQKSEEMQtaqkEQLRQETQ-------MLQQTFRSEKDVLLQkerfVEEEKakleklfqeevNKAQGLKAEQERQQKQ 2689
Cdd:pfam01576 971 ALEAKIAQLE----EQLEQESRerqaankLVRRTEKKLKEVLLQ----VEDER-----------RHADQYKDQAEKGNSR 1031
|
1130 1140 1150
....*....|....*....|....*....|...
gi 2069539781 2690 MEQEKKQLTTVLEEARKKQAeaeeNVRQKQEEL 2722
Cdd:pfam01576 1032 MKQLKRQLEEAEEEASRANA----ARRKLQREL 1060
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1809-2562 |
5.69e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.17 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1809 EEAEKQKEDAEREARK--RSKAEESALRQKEL---------AEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQ 1877
Cdd:TIGR02168 196 NELERQLKSLERQAEKaeRYKELKAELRELELallvlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1878 RLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEEsrstsekskqiLEAEASKLRELAEEAARLRA 1957
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ-----------LEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1958 LSEEAKRQRQLAEE---EATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAA 2034
Cdd:TIGR02168 345 KLEELKEELESLEAeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2035 QHKQDIEEkiAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLnFEKASHGKTDLELELTRIKQSAEEIQRSKEQA 2114
Cdd:TIGR02168 425 ELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREE-LEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2115 EREAEELRQLALE-----------------EENHRREAEAKVKKISAA----EQEAARQCKAALEEVERLKAKAEEARRQ 2173
Cdd:TIGR02168 502 EGFSEGVKALLKNqsglsgilgvlselisvDEGYEAAIEAALGGRLQAvvveNLNAAKKAIAFLKQNELGRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2174 KELAEKESERQIQLAQEAAQKRIVAEEKAHLAAvqqkeQELLQTRQQEQSILDKLREEAERAKK---------------- 2237
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL-----RKALSYLLGGVLVVDDLDNALELAKKlrpgyrivtldgdlvr 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2238 -------AAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQ 2310
Cdd:TIGR02168 657 pggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2311 LADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELi 2390
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL- 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2391 klktRIEEENKmliTKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQE 2470
Cdd:TIGR02168 816 ----NEEAANL---RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2471 ATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKtLEAERQRQLEITAN-----AERLKVQVTELSLAQ 2545
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEeysltLEEAEALENKIEDDE 967
|
810
....*....|....*..
gi 2069539781 2546 AKAEEEAKRFKKQAEQI 2562
Cdd:TIGR02168 968 EEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2225-2774 |
1.19e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.89 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2225 LDKLREEAERAKKAAEDAEFARIKAEQEAALS-RQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAEleaarraqaeq 2303
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELE----------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2304 aALKQKQLAdaemakhkkfAEQTLRQKAQVEQELTKvklQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVK 2383
Cdd:COG1196 271 -ELRLELEE----------LELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2384 VQMEELIKLKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKE 2463
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2464 KMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSL 2543
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2544 AQAKAEEE-------AKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSD--SDAEKLRKAIADLEQEKEKLKRE 2614
Cdd:COG1196 497 LEAEADYEgflegvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvvEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2615 AELLQQKSEEMQTAQKEQ------------LRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAE 2682
Cdd:COG1196 577 LPLDKIRARAALAAALARgaigaavdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2683 QERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTR 2762
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570
....*....|..
gi 2069539781 2763 EIMIQTDDLPQE 2774
Cdd:COG1196 737 LLEELLEEEELL 748
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
177-296 |
6.28e-27 |
|
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: 107.95 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 177 RVQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERDvirnlrlprEKGRMRFHKLQNVQ 256
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSYN---------RRPAFQQHYLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2069539781 257 IALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 296
Cdd:cd21183 69 TALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
298-413 |
1.96e-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: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 298 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSV 377
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2069539781 378 AEQDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 413
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
298-413 |
3.99e-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: 106.35 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 298 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSV 377
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2069539781 378 AEQDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 413
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1508-2291 |
6.68e-26 |
|
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: 118.63 E-value: 6.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKeALELQRRMEE----------EVSRRQLVAVDAEQQKQTIQQELSQMKLS 1577
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREyegyellkekEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1578 SDAQ-IQAKLKLIEEVEFS-RRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVkDE 1655
Cdd:TIGR02169 262 ELEKrLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI-EE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1656 SQKKREAEDELKHKVQAEQQAAREKqkaLEDLQKlRLQAEEAERRMKQAELEKERQvqlaheaaqksAEADLQSRRLSFA 1735
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEE---LEDLRA-ELEEVDKEFAETRDELKDYRE-----------KLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1736 EKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQK 1815
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1816 EDAERE---ARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELI---------RLKAEVENGEQQRLLLEE 1883
Cdd:TIGR02169 486 SKLQRElaeAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYAtaievaagnRLNNVVVEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1884 ELFRLKN------EVNEAVQKRKELE-----------------------------------EELAKLRAEM--------- 1913
Cdd:TIGR02169 566 LLKRRKAgratflPLNKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARRLMgkyrmvtle 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1914 -ELLLQSKAKTEEESRSTSEKSKQileaeasklRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAIN 1992
Cdd:TIGR02169 646 gELFEKSGAMTGGSRAPRGGILFS---------RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1993 EASRLKAEAEIALKEKEAENERLRRLAED-EAYQRRLLEEQA-----AQHKQDIEEKIAQLKKSSEsELERQ--KSLVDD 2064
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDlSSLEQEIENVKSelkelEARIEELEEDLHKLEEALN-DLEARlsHSRIPE 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2065 TVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISA 2144
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2145 AEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESER-QIQLAQEAAQKRIVAEEKAHLAAVQQKEQELlqtrQQEQS 2223
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKkRKRLSELKAKLEALEEELSEIEDPKGEDEEI----PEEEL 951
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2224 ILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEA 2291
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1689-2569 |
1.08e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.85 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1689 KLRLQAEEAERRMKQAEL----------EKERQVQLAheaaQKSAEADLQSRRLSFAEKTAQLELSLQQehitITHLQEE 1758
Cdd:TIGR02168 169 KYKERRKETERKLERTREnldrledilnELERQLKSL----ERQAEKAERYKELKAELRELELALLVLR----LEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1759 AERLKKLQLEAEQSREEADKEVEKWRQKANEalrLRLQAEEVAHKKALAQEE----------AEKQKEDAEREARKRSKA 1828
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEE---LRLEVSELEEEIEELQKElyalaneisrLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1829 EESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAK 1908
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1909 LRAEMELLlqskakteEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKL 1988
Cdd:TIGR02168 398 LNNEIERL--------EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1989 VAINEASRLKAEAEIA-LKEKEAENERLRRLAEDEAYQRRlleeQAAQHKQDIEEKIAQLKK--SSESELERQKSLVDDT 2065
Cdd:TIGR02168 470 LEEAEQALDAAERELAqLQARLDSLERLQENLEGFSEGVK----ALLKNQSGLSGILGVLSEliSVDEGYEAAIEAALGG 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2066 VRQRRLVE-EEIRILKLNFEKASHGKTDLELELTRIKqsAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVK---- 2140
Cdd:TIGR02168 546 RLQAVVVEnLNAAKKAIAFLKQNELGRVTFLPLDSIK--GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllg 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2141 --KISAAEQEAARQCKAaLEEVERLKAKAEEARRQKELAEKESERQIQLAQEaaQKRIVAEEKAHLAAVQQKEQELLQTr 2218
Cdd:TIGR02168 624 gvLVVDDLDNALELAKK-LRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE--RRREIEELEEKIEELEEKIAELEKA- 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2219 qqeqsiLDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARR 2298
Cdd:TIGR02168 700 ------LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2299 AQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEE 2378
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2379 LFKVKVQMEELIKLKTRIEEENKMLiTKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRsLAE 2458
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEAL-LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE-LRL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2459 KILKEKMQAVQE--ATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAE--------EAEgfqktLEAERQRQLEIT 2528
Cdd:TIGR02168 932 EGLEVRIDNLQErlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaIEE-----YEELKERYDFLT 1006
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 2069539781 2529 ANAERLKVQVTELSLAQAKAEEEAK-RFKKQAEQISQKLHQT 2569
Cdd:TIGR02168 1007 AQKEDLTEAKETLEEAIEEIDREAReRFKDTFDQVNENFQRV 1048
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2017-2828 |
2.26e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 116.69 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2017 RLAEDEAYQRRLLEEQAA---QHKQDIEEKIAQLKKSSE---------SELERQKSLVDdtvRQRRLVEEEIRIlklnfe 2084
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKETERKLERTREnldrledilNELERQLKSLE---RQAEKAERYKEL------ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2085 KASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCK---AALEEVE 2161
Cdd:TIGR02168 219 KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2162 RLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKahLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAED 2241
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE--LAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2242 AEFARIKAEQEAALSRQLVEEA----ERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQL-ADAEM 2316
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLnneiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEeLQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2317 AKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEvTEAMKQKVQVEEELFKVKVQMEELIKLKtri 2396
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF-SEGVKALLKNQSGLSGILGVLSELISVD--- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2397 EEENKMLITKDKDNMQKFLAEEaekmkqvaEEAARLSVEAQEAARLRELAeqdlaqqrSLAEKILKEKMQAVQEATRLKA 2476
Cdd:TIGR02168 533 EGYEAAIEAALGGRLQAVVVEN--------LNAAKKAIAFLKQNELGRVT--------FLPLDSIKGTEIQGNDREILKN 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2477 EAEVLQKQKDLAqEQAKKLQEDKEQM--QLRLAEEAEGFQKTLEAERQRQLEITANAERLKvqvTELSLAQAKAEEEAKR 2554
Cdd:TIGR02168 597 IEGFLGVAKDLV-KFDPKLRKALSYLlgGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVR---PGGVITGGSAKTNSSI 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2555 FKKQAEqisqklhqtelatqekmtlVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQT------A 2628
Cdd:TIGR02168 673 LERRRE-------------------IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisalrK 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2629 QKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVnKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQ 2708
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAEL 812
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2709 AEAEENVRQKQEELQRLEKQRQKQEKL---LAEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLpQEVVAPSQVPQMK 2785
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-LNERASLEEALAL 891
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 2069539781 2786 AVPNGRDMIDGI----SQNGEAELAFDGIRQKVSAKKLAEAGILSRE 2828
Cdd:TIGR02168 892 LRSELEELSEELreleSKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
316-411 |
4.49e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 102.62 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 316 LLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED-VD 394
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 2069539781 395 VPQPDEKSIITYVSSLY 411
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1579-2432 |
9.41e-25 |
|
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: 114.78 E-value: 9.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1579 DAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEdELQALRDRAEEAERQKRLAQ-EEAERLRKQVKDESQ 1657
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEkEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1658 KKREaedelkhkvqaeqqaarEKQKALEDLQKLRLQAEEAERRMKQAELE-----KERQVQLAHEAAQKSAEADLQSRRL 1732
Cdd:TIGR02169 248 SLEE-----------------ELEKLTEEISELEKRLEEIEQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1733 SFAEKTAQ-LELSLQQEHITITHLQEEAERLKKlQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEA 1811
Cdd:TIGR02169 311 AEKERELEdAEERLAKLEAEIDKLLAEIEELER-EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1812 EKQKEDAEREARKRSKAEESALRQkelaeqelEKQRKlaegtaqqkflaEQELIRLKAEVENGEQQRLLLEEELFRLKNE 1891
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQE--------ELQRL------------SEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1892 VNEAVQKRKELEEELAKLRAEmelLLQSKAKTEEESRSTSEKSKQILEAEASKlRELAEEAARLRALSEEAKRQ------ 1965
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQE---LYDLKEEYDRVEKELSKLQRELAEAEAQA-RASEERVRGGRAVEEVLKASiqgvhg 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1966 --RQLAEEEATHQRAeAERILKEKLVAINEASRLKAEAEIA-LKEKEAENER---LRRLAEDEAYQRRLLEEQAAQHKQD 2039
Cdd:TIGR02169 526 tvAQLGSVGERYATA-IEVAAGNRLNNVVVEDDAVAKEAIElLKRRKAGRATflpLNKMRDERRDLSILSEDGVIGFAVD 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2040 IEEKIAQLKKSSESELeRQKSLVDDTVRQRRLVeEEIRILKLN---FEKA------SHGKTDLELELTRIKQSAEEIQRS 2110
Cdd:TIGR02169 605 LVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLM-GKYRMVTLEgelFEKSgamtggSRAPRGGILFSRSEPAELQRLRER 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2111 KEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARR-----QKELAEKESERQI 2185
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlsslEQEIENVKSELKE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2186 QLAQEAAQKRIVAEEKAHLAAVQQKE-QELLQTRQQEqsiLDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAE 2264
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2265 RmkQRAEEEAQTKAKAQEDAEKLRKEAELeaarraqaeQAALKQKQLADAEM-AKHKKFAEQTLRQKAQ---VEQELTKV 2340
Cdd:TIGR02169 840 E--QRIDLKEQIKSIEKEIENLNGKKEEL---------EEELEELEAALRDLeSRLGDLKKERDELEAQlreLERKIEEL 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2341 KLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEE------LFKVKVQMEELIKLKTRIEEENkMLITKDKDNMQKF 2414
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALEPVN-MLAIQEYEEVLKR 987
|
890
....*....|....*...
gi 2069539781 2415 LAEEAEKMKQVAEEAARL 2432
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAI 1005
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
298-413 |
2.04e-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: 101.30 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 298 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSV 377
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2069539781 378 AEQDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 413
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1318-2175 |
2.19e-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: 113.61 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1318 ERDIDLDRYRERVQQLLERWQAILAQIDLRQRELDQLGRQLRYYRESYDWLIQWIREARQRQEHLQAVpvtnsksvreqL 1397
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-----------L 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1398 LQEKKLLEECDRNREKVEECQcfaKQYIDAIKDYELQLVTYKAQVEPVAspAKKPKVQSASDSVIQEYVDLRTRYSELtt 1477
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELA--EELAELEEKLEELKEELESLEAELEEL-- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1478 ltsqylkfitetlrrleeeekaaeklkeeeRQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVA 1557
Cdd:TIGR02168 364 ------------------------------EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1558 VDAEQQKQTIQQELSQMKLSSDAQIQAKL----KLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEE 1633
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELeeleEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1634 AERQKRLAQEEAERLrKQVKDESQKKREAEDELKHKVQAEQQAAREKQKAL-EDLQKLRLQAEEAERR----MKQAELEK 1708
Cdd:TIGR02168 494 LERLQENLEGFSEGV-KALLKNQSGLSGILGVLSELISVDEGYEAAIEAALgGRLQAVVVENLNAAKKaiafLKQNELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1709 ----------ERQVQLAHEAAQKSAEADLQS-RRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKlQLEAEQSREEAD 1777
Cdd:TIGR02168 573 vtflpldsikGTEIQGNDREILKNIEGFLGVaKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAK-KLRPGYRIVTLD 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1778 KEVEKWRQKANEAlrlRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQK 1857
Cdd:TIGR02168 652 GDLVRPGGVITGG---SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1858 FLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMElLLQSKAKTEEESRSTSEKSKQI 1937
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDE 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1938 LEAEaskLRELAEEAARLRalseeakrqrqlaeeeathQRAEAERilkeklvaiNEASRLKAEAEIALKEKEAENERLRR 2017
Cdd:TIGR02168 808 LRAE---LTLLNEEAANLR-------------------ERLESLE---------RRIAATERRLEDLEEQIEELSEDIES 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2018 LAEDEAYQRRLLEEQAAQHkqdieEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELEL 2097
Cdd:TIGR02168 857 LAAEIEELEELIEELESEL-----EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2098 TRIKQSAEEIQ-RSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKE 2175
Cdd:TIGR02168 932 EGLEVRIDNLQeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKE 1010
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
311-411 |
2.23e-24 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 100.58 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQdLGVTRLLDP 390
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 2069539781 391 EDVDVPQ-PDEKSIITYVSSLY 411
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1328-1916 |
6.84e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 6.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1328 ERVQQLLERWQAILAQIDlrqRELDQLGRQ----LRY--YRESYD-----WLIQWIREARQRQEHLQAVpVTNSKSVREQ 1396
Cdd:COG1196 182 EATEENLERLEDILGELE---RQLEPLERQaekaERYreLKEELKeleaeLLLLKLRELEAELEELEAE-LEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1397 LLQEKKLLE-ECDRNREKVEEcqcfAKQYIDAIKDYELQLVTYKAQVEPVASPAKKpKVQSASDSVIQEYVDLRTRYSEL 1475
Cdd:COG1196 258 LEAELAELEaELEELRLELEE----LELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1476 TTLTSQyLKFITETLRRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQL 1555
Cdd:COG1196 333 EELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1556 VAVDAEQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAE 1635
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1636 RQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQA---EEAERRMKQAELEKE--- 1709
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivvEDDEVAAAAIEYLKAaka 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1710 -RQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKAN 1788
Cdd:COG1196 572 gRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1789 EALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLK 1868
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2069539781 1869 AEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELL 1916
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
310-416 |
9.07e-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: 98.90 E-value: 9.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 310 MTAKEKLLLWSQRMVEGY-QGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNVENLEQAFSVAEQDLGVTR 386
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 2069539781 387 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 416
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2233-2851 |
1.22e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 111.39 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2233 ERAKKAAEDAEFARIK---AEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQK 2309
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEdnrADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2310 QLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEEL 2389
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2390 IKLK-TRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKI-----LKE 2463
Cdd:PTZ00121 1230 KKAEeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkkadeAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2464 KMQAVQEATRLKAEAEVLQKQKDLAQ---EQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTE 2540
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2541 LSLAQaKAEEEAKRFKKQAEQISQKLHQTELATQEKmtlvQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQ 2620
Cdd:PTZ00121 1390 KKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAK----KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2621 KSEEMQTAQKEQLRQEtqmlqqtfrsEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQlttv 2700
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAE----------EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA---- 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2701 leEARKKQAEAE--ENVRQ-----KQEELQRLEKQRQKQEKLLAEE--NQKLR--EKLEQLQEEQKTALAQ--TREIMIQ 2767
Cdd:PTZ00121 1531 --EEAKKADEAKkaEEKKKadelkKAEELKKAEEKKKAEEAKKAEEdkNMALRkaEEAKKAEEARIEEVMKlyEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2768 TDDLPQEVVAPSQVPQMKAVPNGRDMIDGISQNGEAElafdgIRQKVSAKKLAEAGILSRESMEKLA-KGKATVQELSQR 2846
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE-----KKKAEELKKAEEENKIKAAEEAKKAeEDKKKAEEAKKA 1683
|
....*
gi 2069539781 2847 DDIRR 2851
Cdd:PTZ00121 1684 EEDEK 1688
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
177-296 |
1.23e-23 |
|
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: 98.33 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 177 RVQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERDvirnlrlprEKGRMRFHKLQNVQ 256
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKKYN---------KRPTFRQMKLENVS 68
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2069539781 257 IALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 296
Cdd:cd21228 69 VALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
312-411 |
1.83e-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: 98.02 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 312 AKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPE 391
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 2069539781 392 D-VDVPQPDEKSIITYVSSLY 411
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
311-415 |
3.26e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.17 E-value: 3.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYqGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDP 390
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 2069539781 391 EDVDVPQPDEKSIITYVSSLYDAMP 415
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
314-414 |
3.80e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 96.77 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 314 EKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPEDV 393
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 2069539781 394 DVPQPDEKSIITYVSSLYDAM 414
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2068-2739 |
9.90e-23 |
|
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: 108.13 E-value: 9.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2068 QRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQ 2147
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2148 EAARQCKAAlEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSIL-- 2225
Cdd:TIGR00618 275 QEAVLEETQ-ERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHsq 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2226 -DKLREEAERAK-------KAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEE----EAQTKAKAQEDAEKLRKEAEL 2293
Cdd:TIGR00618 354 eIHIRDAHEVATsireiscQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqatiDTRTSAFRDLQGQLAHAKKQQ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2294 EAARRAQAEQAALKQKQLADAEMAK-HKKFAEQTLRQKAQVEQELTKVKLQLEETdhqKSILEEEQQRLKDEVTEAMKQK 2372
Cdd:TIGR00618 434 ELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQTKEQIHLQETRK---KAVVLARLLELQEEPCPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2373 VQVEEELFKVKVqMEELIKLKTRIEEENKMLITKDKdNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQ 2452
Cdd:TIGR00618 511 IHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSEE-DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2453 QRSLAEKILKEkMQAVQEATRLKAEAevLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAE 2532
Cdd:TIGR00618 589 LQNITVRLQDL-TEKLSEAEDMLACE--QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2533 RLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQ----SDSDAEKLRKAIADLEQEK 2608
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienaSSSLGSDLAAREDALNQSL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2609 EKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFvEEEKAKLEKLFQEEVNKAQGLKAEQERQQK 2688
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2689 QMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEE 2739
Cdd:TIGR00618 825 TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
177-299 |
1.28e-22 |
|
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: 96.25 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 177 RVQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERDvirnlrlPREKgrMRFHKLQNVQ 256
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYH-------PRPN--FRQMKLENVS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2069539781 257 IALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 299
Cdd:cd21310 81 VALEFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1755-2508 |
1.36e-22 |
|
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: 107.85 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1755 LQEEAERLKKLQLEAEQSREEADKeVEKWRQKANEALRLRLQAEEVAHKKALAQ-EEAEKQKEDAERE-ARKRSKAEESA 1832
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLER-LRREREKAERYQALLKEKREYEGYELLKEkEALERQKEAIERQlASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1833 LRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAE 1912
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1913 MELL---LQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLR-ALSEEAKRQRQLAEEEATHQRaEAERILKEKL 1988
Cdd:TIGR02169 338 IEELereIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdELKDYREKLEKLKREINELKR-ELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1989 VAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAA------QHKQDIEEKIAQL-----KKSSE-SELE 2056
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlskyeQELYDLKEEYDRVekelsKLQRElAEAE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2057 RQKSLVDDTVRQRRLVEEE------------------------------------------------IRILK-------- 2080
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVlkasiqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakeaIELLKrrkagrat 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2081 ---LNFEKASH---------GKTDLELELTRIKQSAEE----------IQRSKEQAEREAEELRQLALEEENHrrEAEAK 2138
Cdd:TIGR02169 577 flpLNKMRDERrdlsilsedGVIGFAVDLVEFDPKYEPafkyvfgdtlVVEDIEAARRLMGKYRMVTLEGELF--EKSGA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2139 VKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKahLAAVQQKEQELLQTR 2218
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK--IGEIEKEIEQLEQEE 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2219 QQEQSILDKLRE-----EAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAEL 2293
Cdd:TIGR02169 733 EKLKERLEELEEdlsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2294 EAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDhqkSILEEEQQRLKDEVTEAMKQKV 2373
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE---EELEELEAALRDLESRLGDLKK 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2374 QVEEELFKVKVQMEELIKLKTRIEEENKMLITkdkdnMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQ 2453
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSE-----LKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2454 RSLaEKILKEKMQAVQEAtrlkaeAEVLQKQKDLaQEQAKKLQEDKEQMQLRLAE 2508
Cdd:TIGR02169 965 EEI-RALEPVNMLAIQEY------EEVLKRLDEL-KEKRAKLEEERKAILERIEE 1011
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
170-298 |
1.98e-22 |
|
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: 95.60 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 170 RIADERDRVQKKTFTKWVNKHLLKHwraEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRErdvirnlrlprEKGRMRF 249
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRP-----------SRGKMRV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2069539781 250 HKLQNVQIALDYLKHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 298
Cdd:cd21247 78 HFLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2026-2779 |
2.48e-22 |
|
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: 106.69 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2026 RRLLEEQA--AQHKQDIEEKIAQLKKSSESeLERQKSLVD------DTVRQRRLVEEEIRILKLNFEKA-----SHGKTD 2092
Cdd:TIGR02169 156 RKIIDEIAgvAEFDRKKEKALEELEEVEEN-IERLDLIIDekrqqlERLRREREKAERYQALLKEKREYegyelLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2093 LELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARqckaalEEVERLKAKAEEARR 2172
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------EKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2173 QKELAEKESER-QIQLAQEAAQKRIVAEEKAHLAAVQQKEQELlqtRQQEQSILDKLREEAE--RAKKAAEDAEFARIKA 2249
Cdd:TIGR02169 309 SIAEKERELEDaEERLAKLEAEIDKLLAEIEELEREIEEERKR---RDKLTEEYAELKEELEdlRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2250 EQeaalsRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQaalKQKQLADAEMAKHKKFAEQTlRQ 2329
Cdd:TIGR02169 386 EL-----KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA---KINELEEEKEDKALEIKKQE-WK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2330 KAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEEL----------IKLKTRIEEE 2399
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLkasiqgvhgtVAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2400 NKMLITKDKDNMQKFLAEEAEkmkQVAEEAARLsVEAQEAARLRELAEQDLAQQRSLAEKILKEK--------------- 2464
Cdd:TIGR02169 537 YATAIEVAAGNRLNNVVVEDD---AVAKEAIEL-LKRRKAGRATFLPLNKMRDERRDLSILSEDGvigfavdlvefdpky 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2465 -------------MQAVQEATRLKA-------EAEVLQK---------QKDLAQEQAKKLQEDKEQMQLRLAE---EAEG 2512
Cdd:TIGR02169 613 epafkyvfgdtlvVEDIEAARRLMGkyrmvtlEGELFEKsgamtggsrAPRGGILFSRSEPAELQRLRERLEGlkrELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2513 FQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDS 2592
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2593 DAEKLRKAIADLEQEKEKlkreaELLQQKSEEMQTAQKEQLRQETQMlqqtfrSEKDVLLQKERFveeEKAKLEKLFQEE 2672
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSH-----SRIPEIQAELSKLEEEVSRIEARL------REIEQKLNRLTL---EKEYLEKEIQEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2673 VNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEaeenVRQKQEELQRLEKQRQKQEKLLAEENQKLRE------K 2746
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA----LRDLESRLGDLKKERDELEAQLRELERKIEEleaqieK 914
|
810 820 830
....*....|....*....|....*....|...
gi 2069539781 2747 LEQLQEEQKTALAQTREIMIQTDDLPQEVVAPS 2779
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
311-409 |
2.61e-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: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYqgmRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNVENLEQAFSVAEQDLGVTRLLD 389
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 2069539781 390 PEDVDVPQPDEKSIITYVSS 409
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
942-1008 |
3.23e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 92.71 E-value: 3.23e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 942 QLKPRSpsNPVKGRLPLQAVCDYKQMEITVHKGDACTLLSNAQPYKWKVLNAAGSESVVPSICFLVP 1008
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
181-295 |
4.65e-22 |
|
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: 93.53 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 181 KTFTKWVNKHLlkhwRAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPrERDVirnlrlprEKGRMRFHKLQNVQIALD 260
Cdd:smart00033 1 KTLLRWVNSLL----AEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVD-KKKV--------AASLSRFKKIENINLALS 67
|
90 100 110
....*....|....*....|....*....|....*
gi 2069539781 261 YLKHRQVKLVNIRNDDIADGnPKLTLGLIWTIILH 295
Cdd:smart00033 68 FAEKLGGKVVLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
178-298 |
2.03e-21 |
|
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: 91.96 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 178 VQKKTFTKWVNKHLLKhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPrerdvirnlrlPREKGRMRFHKLQNVQI 257
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVD-----------KKKLNKSEFDKLENINL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2069539781 258 ALDYLKHRQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 298
Cdd:pfam00307 68 ALDVAEKKLgVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2479-2791 |
2.24e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2479 EVLQKQKDLAqEQAKKLQEDKEQMQLRLA--------EEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEE 2550
Cdd:COG1196 203 EPLERQAEKA-ERYRELKEELKELEAELLllklreleAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2551 EAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQK 2630
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2631 EQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKlfQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAE 2710
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2711 AEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLPQEVVAPSQVPQMKAVPNG 2790
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
.
gi 2069539781 2791 R 2791
Cdd:COG1196 520 R 520
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
315-412 |
8.40e-21 |
|
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: 90.49 E-value: 8.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 315 KLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLD-PEDV 393
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2069539781 394 DVPQPDEKSIITYVSSLYD 412
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
311-410 |
8.71e-21 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 90.23 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQdLGVTRLLDP 390
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 2069539781 391 ED-VDVPQPDEKSIITYVSSL 410
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1244-1951 |
2.20e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.60 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1244 IRSTQGAEDlIRKYEEQLK--DVQAVPSDLKALEATKAELKRLRGQVEGHQPLFNTLEM----DLAKASEVN--ERMVRG 1315
Cdd:PTZ00121 1130 AEEARKAED-ARKAEEARKaeDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrkaeELRKAEDARkaEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1316 HSERDIDLDRYRERVQQLLERWQAILAQID---LRQRELDQLGRQLRYYRESYDWLIQWIREARQRQEHLQAVPVTNSKS 1392
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDaeeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1393 VRE----QLLQEKKLLEECDRNREKVEECQCFAKQYIDAIKDYELqlVTYKAQVEPVASPAKKPKVQSASDSViqEYVDL 1468
Cdd:PTZ00121 1289 KKKadeaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEA--EAAEE 1364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1469 RTRYSELTTLTSQYLKFITETLRRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAhaRAKAQAEKEALELQRRMEE 1548
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEAKKKAEE 1442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1549 -----EVSRRQLVAVDAEQQKQTIQQELSQMKLSSDAQIQAKL-KLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAED 1622
Cdd:PTZ00121 1443 akkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAdEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1623 ELQALRdRAEEAER--------QKRLAQE--EAERLRK--QVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKL 1690
Cdd:PTZ00121 1523 KADEAK-KAEEAKKadeakkaeEKKKADElkKAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1691 RLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAE 1770
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1771 QSREEADKEVEKWRQKANEALRL----RLQAEEVAHKKALAQEE------AEKQKEDAEREARKRSKAEESALRQKELAE 1840
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAeelkKKEAEEKKKAEELKKAEeenkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1841 QELEKQRKLAEGTAQQKFLAEQEL----IRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEME-- 1914
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELdeedEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKnm 1841
|
730 740 750
....*....|....*....|....*....|....*...
gi 2069539781 1915 LLLQSKAKTEEESRSTSEKSKQI-LEAEASKLRELAEE 1951
Cdd:PTZ00121 1842 QLEEADAFEKHKFNKNNENGEDGnKEADFNKEKDLKED 1879
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1502-2216 |
4.24e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 99.66 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1502 KLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQMKLSSDAQ 1581
Cdd:pfam02463 282 KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1582 IQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKdESQKKRE 1661
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE-EEEESIE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1662 AEDElkhkVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQL 1741
Cdd:pfam02463 441 LKQG----KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1742 E----LSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKA--------------------NEALRLRLQA 1797
Cdd:pfam02463 517 KdgvgGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLvraltelplgarklrllipkLKLPLKSIAV 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1798 EEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQEliRLKAEVENGEQQ 1877
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS--EVKASLSELTKE 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1878 RLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTE---EESRSTSEKSKQILEAEASKLRELAEEAAR 1954
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEllaDRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1955 LRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIA--LKEKEAENERLRRLAEDEAYQRRLLEEQ 2032
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRalEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2033 AAQHKQDIEEKIaQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKE 2112
Cdd:pfam02463 835 LEELALELKEEQ-KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2113 QAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQC-KAALEEVERLKAKAEEARRQKELA--EKESERQIQLAQ 2189
Cdd:pfam02463 914 EKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNkEEEEERNKRLLLAKEELGKVNLMAieEFEEKEERYNKD 993
|
730 740
....*....|....*....|....*..
gi 2069539781 2190 EAAQKRIVAEEKAHLAAVQQKEQELLQ 2216
Cdd:pfam02463 994 ELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
311-411 |
6.08e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 87.78 E-value: 6.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDP 390
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 2069539781 391 EDVDV--PQPDEKSIITYVSSLY 411
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1932-2775 |
8.58e-20 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 98.32 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1932 EKSKQILEAEASKLRELAEEAARlrALSEEAKRQRQLAEEEATHQ---RAEAERILKEKLVAINEASRlKAEAEIALKEK 2008
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAES--ELKELEKKHQQLCEEKNALQeqlQAETELCAEAEEMRARLAAR-KQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2009 EAenerlrRLAEDEAYQRRLLEEQA--AQHKQDIEEKIAqlkkssESELERQKSLVDDTVRQRRL--VEEEIRIL----- 2079
Cdd:pfam01576 81 ES------RLEEEEERSQQLQNEKKkmQQHIQDLEEQLD------EEEAARQKLQLEKVTTEAKIkkLEEDILLLedqns 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2080 KLNFEKA--SHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAArqckaal 2157
Cdd:pfam01576 149 KLSKERKllEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2158 EEVERLKAKAEEARRQkeLAEKESERQiqlaqeAAQKRIvAEEKAHLAAVQQKEQELlqtrqqeQSILDKLREEAERAKK 2237
Cdd:pfam01576 222 EQIAELQAQIAELRAQ--LAKKEEELQ------AALARL-EEETAQKNNALKKIREL-------EAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2238 AAEDAEFARikaeqeaalsRQLVEEAERMKQRAEEEAQTKAKAQEdaEKLRKEAELEAARRAQAEQAALKQKQLADAEMA 2317
Cdd:pfam01576 286 ARNKAEKQR----------RDLGEELEALKTELEDTLDTTAAQQE--LRSKREQEVTELKKALEEETRSHEAQLQEMRQK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2318 KHKKFAEQT--LRQKAQVEQELTKVKLQLE------------------ETDHQKSILEEEQQRLKDEVTEAMKQKVQVEE 2377
Cdd:pfam01576 354 HTQALEELTeqLEQAKRNKANLEKAKQALEsenaelqaelrtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2378 ELFKVKVQMEELIKLKTRIEEENKMLiTKDKDNMQKFLAEE----AEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQ 2453
Cdd:pfam01576 434 KLSKLQSELESVSSLLNEAEGKNIKL-SKDVSSLESQLQDTqellQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2454 RSLAEKILKEKMQAVQEATRLKAEAEVLqkqkDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEI---TAN 2530
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMKKKLEEDAGTL----EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELddlLVD 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2531 AERLKVQVTELSLAQ--------------AKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEK 2596
Cdd:pfam01576 589 LDHQRQLVSNLEKKQkkfdqmlaeekaisARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMED 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2597 LRKAIADLEQEKEKLKREAELLQQKSEEMQTaQKEQLRQETQMLQQT-FRSEKDVLLQKERFVEEEKAKLE------KLF 2669
Cdd:pfam01576 669 LVSSKDDVGKNVHELERSKRALEQQVEEMKT-QLEELEDELQATEDAkLRLEVNMQALKAQFERDLQARDEqgeekrRQL 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2670 QEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEE-------ARKKQAEAEENVRQKQ---EELQR-LEKQRQKQEKLLA- 2737
Cdd:pfam01576 748 VKQVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqidaANKGREEAVKQLKKLQaqmKDLQReLEEARASRDEILAq 827
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 2069539781 2738 -EENQKLREKLE----QLQEEQKTALAQTREIMIQTDDLPQEV 2775
Cdd:pfam01576 828 sKESEKKLKNLEaellQLQEDLAASERARRQAQQERDELADEI 870
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1319-1928 |
1.24e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1319 RDIDLDRYRERVQQLLERWQAILAQIDLRQRELDQLGRQLRYYRESYDWLIQWIREARQRQEHLQAVPVTNSKSVREQLL 1398
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1399 QEKKLLEECDRNREKVEEcqcfakqyidAIKDYELQLVTYKAQVEpvaspakkpKVQSASDSVIQEYVDLRTRYSELTTL 1478
Cdd:COG1196 313 ELEERLEELEEELAELEE----------ELEELEEELEELEEELE---------EAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1479 TSQylkfitetlrrLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAV 1558
Cdd:COG1196 374 LAE-----------AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1559 DAEQQKQTIQQELSQmKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRdRAEEAERQK 1638
Cdd:COG1196 443 ALEEAAEEEAELEEE-EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1639 RLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRL--QAEEAERRMKQAELEKERQVQLAH 1716
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1717 EAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQ 1796
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1797 AEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQ 1876
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1877 QRLLLEEELFRLKNE------VN-------EAVQKRKE-LEEELAKLRAEMELLLQSKAKTEEESR 1928
Cdd:COG1196 761 DLEELERELERLEREiealgpVNllaieeyEELEERYDfLSEQREDLEEARETLEEAIEEIDRETR 826
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1593-2368 |
1.89e-19 |
|
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: 97.35 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1593 EFSRRKVEEEIRMVrLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQA 1672
Cdd:TIGR00618 156 QFLKAKSKEKKELL-MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1673 EQQaareKQKALEDLQKLRLQAEEAERRMKQ-----AELEKERQVQLAHEAAQKsaEADLQSRRLSFAEKTAQLELSLQQ 1747
Cdd:TIGR00618 235 LQQ----TQQSHAYLTQKREAQEEQLKKQQLlkqlrARIEELRAQEAVLEETQE--RINRARKAAPLAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1748 EHITITHLQE-EAERLKKLQLEAEQSREEADkeVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEReARKRS 1826
Cdd:TIGR00618 309 AQRIHTELQSkMRSRAKLLMKRAAHVKQQSS--IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH-IHTLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1827 KAEESALRQKELAEQELEKQRKLAeGTAQQKFLAE----QELIRLKAEVEngeQQRLLLEEELFRLKNEVNEAVQKRKEL 1902
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQ-ATIDTRTSAFrdlqGQLAHAKKQQE---LQQRYAELCAAAITCTAQCEKLEKIHL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1903 EEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEAS----KLRELAEEAARLRALSEEAKRQRQLAEEEATHQRA 1978
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1979 EAERILKEKLVAI-NEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELER 2057
Cdd:TIGR00618 542 TSEEDVYHQLTSErKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2058 QKSLVDDTVRQ-RRLVEEEIRILKLNFEKashgktdleLELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAE 2136
Cdd:TIGR00618 622 QPEQDLQDVRLhLQQCSQELALKLTALHA---------LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQL 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2137 AKVKkisaaeqEAARQCKAALEEVERlkaKAEEARRQKElaekeserQIQLAQEAAQKRIVAEEKAHlaavqqkeqellq 2216
Cdd:TIGR00618 693 TYWK-------EMLAQCQTLLRELET---HIEEYDREFN--------EIENASSSLGSDLAAREDAL------------- 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2217 trqqeQSILDKLREEAERAKKAAEDaefarikaEQEAALSRQLVEEaermkQRAEEEAQTKAKAQ---EDAEKLRKEAEL 2293
Cdd:TIGR00618 742 -----NQSLKELMHQARTVLKARTE--------AHFNNNEEVTAAL-----QTGAELSHLAAEIQffnRLREEDTHLLKT 803
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2294 EAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEA 2368
Cdd:TIGR00618 804 LEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2117-2755 |
3.16e-19 |
|
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: 96.58 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2117 EAEELRQLALEEENHRREAEAKVKKISAAEQ-------EAARQCKAALEEVERLKAKAEEARRQkelaEKESERQIQlaq 2189
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQlltlctpCMPDTYHERKQVLEKELKHLREALQQ----TQQSHAYLT--- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2190 eaaQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQR 2269
Cdd:TIGR00618 247 ---QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2270 AEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQV-------EQELTKVKL 2342
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkttltqkLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2343 QLEETDHQKSILEEEQQRLKDEVTEAMKQ-----------KVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKdkdnm 2411
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQqelqqryaelcAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK----- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2412 QKFLAEEAEKMKQVAEEAARLsveaQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQ 2491
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLEL----QEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2492 AKKLQEDKEQMQLRLAEEAEGFQKtleaeRQRQLEITANAERLKVQVTELSLAQAKAEEeakrfkkqaeQISQKLHQTEL 2571
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQC-----DNRSKEDIPNLQNITVRLQDLTEKLSEAED----------MLACEQHALLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2572 ATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVL 2651
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2652 LQKERFVEEEKAKLE---KLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQ-------EE 2721
Cdd:TIGR00618 700 AQCQTLLRELETHIEeydREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVtaalqtgAE 779
|
650 660 670
....*....|....*....|....*....|....
gi 2069539781 2722 LQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQK 2755
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1891-2745 |
7.22e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.52 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1891 EVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEEsrsTSEKSKQILEAEasklRELAEEAARLRALSEEAKRQRQLAE 1970
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEE---ISELEKRLEEIE----QLLEELNKKIKDLGEEEQLRVKEKI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1971 EEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLkks 2050
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL--- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2051 sESELERQKSLVDdtvrqrRLVEEEIRILKLNFEKASHgKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLAleeen 2130
Cdd:TIGR02169 374 -EEVDKEFAETRD------ELKDYREKLEKLKREINEL-KRELDRLQEELQRLSEELADLNAAIAGIEAKINELE----- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2131 hrREAEAKVKKISAAEQEAaRQCKAALEEVER--LKAKAEEARRQKELAEKESErqiqLAQEAAQKRIVAEEKAHLAAVQ 2208
Cdd:TIGR02169 441 --EEKEDKALEIKKQEWKL-EQLAADLSKYEQelYDLKEEYDRVEKELSKLQRE----LAEAEAQARASEERVRGGRAVE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2209 QKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAaLSRQLVEEAERMK-QRAEEEAQTKAKAQE-DAEK 2286
Cdd:TIGR02169 514 EVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDA-VAKEAIELLKRRKaGRATFLPLNKMRDERrDLSI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2287 LRKEAELEAARraqaeqaalkqkQLADAEmAKHKKFAEQTLRQKAQVE------QELTKVKLQLEETDhqksILEEEQQR 2360
Cdd:TIGR02169 593 LSEDGVIGFAV------------DLVEFD-PKYEPAFKYVFGDTLVVEdieaarRLMGKYRMVTLEGE----LFEKSGAM 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2361 LKDEVTEAMKQKVQVEEElfkvkvqmEELIKLKTRIEEenkmlITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAA 2440
Cdd:TIGR02169 656 TGGSRAPRGGILFSRSEP--------AELQRLRERLEG-----LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2441 RLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLA----EEAEGFQKT 2516
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2517 LEAERQRQLEITANAERlkvqvTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQekmtlVQTLEIQRQQSDSDAEK 2596
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQ-----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-----IENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2597 LRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEqlrQETQMlqQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVN-K 2675
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEE---LEAQI--EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEiP 947
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2676 AQGLKAEQERQQKQ-MEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLRE 2745
Cdd:TIGR02169 948 EEELSLEDVQAELQrVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
307-412 |
1.43e-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: 84.23 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 307 SEDMTAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTR 386
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 2069539781 387 LLDPEDV-DVPQPDEKSIITYVSSLYD 412
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1468-2238 |
1.50e-18 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 94.27 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1468 LRTRYSELTTLTSQYLKFITETLRRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQlaeaharaKAQAEKEALELQRRME 1547
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE--------QLKKQQLLKQLRARIE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1548 EevsRRQLVAVDAEQQKQTIQQelsqmklSSDAQIQAKLKLIEEVEFSRRKVEEEirmvrlqLEATERQRAGAEDELQAL 1627
Cdd:TIGR00618 271 E---LRAQEAVLEETQERINRA-------RKAAPLAAHIKAVTQIEQQAQRIHTE-------LQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1628 RDRAEEAERQKRLAQEeaerlrkQVKDESQKKREAEDELKHKVQAEQQaarekqkaLEDLQKLRLQAEEAERRMKQAELE 1707
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQT-------LHSQEIHIRDAHEVATSIREISCQQ--------HTLTQHIHTLQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1708 KERQVQLAHEAAQksAEADLQSRRlsfaektaqlelsLQQEHITITHLQEEAErLKKLQLEAEQSREEADKEVEKWRQKA 1787
Cdd:TIGR00618 399 CKELDILQREQAT--IDTRTSAFR-------------DLQGQLAHAKKQQELQ-QRYAELCAAAITCTAQCEKLEKIHLQ 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1788 NEALRLRLQAEEVAHKKALAQEEAEKQKedaEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLA-EQELIR 1866
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKEQIHLQETRKKA---VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1867 LKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLR 1946
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1947 ELAEEAARLRALSEEAKRQRQLAEEEAThqraeaerilkeklvaineasrLKAEAEIALKEKEAENERLRRLAEDEAYQR 2026
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTA----------------------LHALQLTLTQERVREHALSIRVLPKELLAS 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2027 RLLEEQAAQHKQdieEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEeirilklnFEKASHG-KTDLELELTRIKQSAE 2105
Cdd:TIGR00618 678 RQLALQKMQSEK---EQLTYWKEMLAQCQTLLRELETHIEEYDREFNE--------IENASSSlGSDLAAREDALNQSLK 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2106 EIQRSKEQAEREAEELRQLALEEENhrrEAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESE-RQ 2184
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNEEVT---AALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQC 823
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2185 IQLAQEAAQ-KRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKA 2238
Cdd:TIGR00618 824 ETLVQEEEQfLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
177-299 |
1.88e-18 |
|
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: 84.36 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 177 RVQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERdvirnlrlpREKGRMRFHKLQNVQ 256
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKY---------HQRPTFRQMQLENVS 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2069539781 257 IALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 299
Cdd:cd21309 82 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1509-2369 |
2.52e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 93.70 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1509 QRLAEVEAQLEkqrqlAEAHARAKAQAEKEALELQ-RRMEEEV------------SRRQLVAVDAEQQKQTIQQE----- 1570
Cdd:pfam01576 103 QHIQDLEEQLD-----EEEAARQKLQLEKVTTEAKiKKLEEDIllledqnsklskERKLLEERISEFTSNLAEEEekaks 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1571 LSQMKLSSDAQI---QAKLKLIE----EVEFSRRKVEEEI-----RMVRLQLEATE--RQRAGAEDELQALRDRAEEAER 1636
Cdd:pfam01576 178 LSKLKNKHEAMIsdlEERLKKEEkgrqELEKAKRKLEGEStdlqeQIAELQAQIAElrAQLAKKEEELQAALARLEEETA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1637 QKRLAQEEAERLRKQVKdesqkkrEAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEA-ERRMKQAELEKERQVQLA 1715
Cdd:pfam01576 258 QKNNALKKIRELEAQIS-------ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTlDTTAAQQELRSKREQEVT 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1716 H-----EAAQKSAEADLQSRRL----SFAEKTAQLE-------------LSLQQEHitiTHLQEEAERLKKLQLEAEQSR 1773
Cdd:pfam01576 331 ElkkalEEETRSHEAQLQEMRQkhtqALEELTEQLEqakrnkanlekakQALESEN---AELQAELRTLQQAKQDSEHKR 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1774 EEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKaEESALRQKELAEQEL---EKQRKLA 1850
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSK-DVSSLESQLQDTQELlqeETRQKLN 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1851 EGTAQQKFLAEQELIRLKAEVE-----NGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQsKAKTEE 1925
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEeeakrNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ-QLEEKA 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1926 ESRSTSEKSKQILEAEaskLRELAEEAARLRAL-SEEAKRQRQ----LAEEEAT-------HQRAEAE------------ 1981
Cdd:pfam01576 566 AAYDKLEKTKNRLQQE---LDDLLVDLDHQRQLvSNLEKKQKKfdqmLAEEKAIsaryaeeRDRAEAEareketralsla 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1982 RILKEKLVAINEASR----LKAEAEIALKEKEA------ENERLRRLAEDEAYQRRL-LEE-----QAAQH-KQDIEEKI 2044
Cdd:pfam01576 643 RALEEALEAKEELERtnkqLRAEMEDLVSSKDDvgknvhELERSKRALEQQVEEMKTqLEEledelQATEDaKLRLEVNM 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2045 AQLKKSSESEL--------ERQKSLvddtVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAER 2116
Cdd:pfam01576 723 QALKAQFERDLqardeqgeEKRRQL----VKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVK 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2117 EAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKE-SERQIQLAQEAAQKR 2195
Cdd:pfam01576 799 QLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQErDELADEIASGASGKS 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2196 IVAEEKAHLAA-VQQKEQELLQTRQQEQSILDKLREEAERA----------KKAAEDAEFARIKAE---QEAALSRQLVE 2261
Cdd:pfam01576 879 ALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRKSTLQVeqlttelaaeRSTSQKSESARQQLErqnKELKAKLQEME 958
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2262 EAERMKQRAEEEAqTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLAdAEMAKHKKFAEQTLRQKAQVEQELTKVK 2341
Cdd:pfam01576 959 GTVKSKFKSSIAA-LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVL-LQVEDERRHADQYKDQAEKGNSRMKQLK 1036
|
970 980 990
....*....|....*....|....*....|.
gi 2069539781 2342 LQLEETDHQKSILEEEQQRLK---DEVTEAM 2369
Cdd:pfam01576 1037 RQLEEAEEEASRANAARRKLQrelDDATESN 1067
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
177-299 |
4.40e-18 |
|
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: 83.60 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 177 RVQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERDvirnlrlprEKGRMRFHKLQNVQ 256
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHN---------QRPTFRQMQLENVS 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2069539781 257 IALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 299
Cdd:cd21308 85 VALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
311-410 |
5.04e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 82.59 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQdLGVTRLLDP 390
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 2069539781 391 ED-VDVPQPDEKSIITYVSSL 410
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2158-2758 |
6.95e-18 |
|
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: 91.71 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2158 EEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQ--QKEQELLQTRQQEQSILDKLREEAERA 2235
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEeiQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2236 KKAAEDAEFARikaEQEAALSRQLVEEAERMKQRAEEeaqtkAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAE 2315
Cdd:pfam05483 168 AEKTKKYEYER---EETRQVYMDLNNNIEKMILAFEE-----LRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2316 makhkKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTR 2395
Cdd:pfam05483 240 -----KQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2396 IEEENKML------ITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQ 2469
Cdd:pfam05483 315 LEEDLQIAtkticqLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2470 EATRLKAEAEV-LQKQKDLAQEQAKKLQEDKEQMqlRLAEEAEGFQKTLEAERQ-RQLEItanaERLKVQVTELSLAQAK 2547
Cdd:pfam05483 395 EMTKFKNNKEVeLEELKKILAEDEKLLDEKKQFE--KIAEELKGKEQELIFLLQaREKEI----HDLEIQLTAIKTSEEH 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2548 AEEEAKRFKKQAEQisQKLHQTELATQEKMTLVQ-----------TLEIQRQQSD-----SDAEKLRKAIADLEQEKEKL 2611
Cdd:pfam05483 469 YLKEVEDLKTELEK--EKLKNIELTAHCDKLLLEnkeltqeasdmTLELKKHQEDiinckKQEERMLKQIENLEEKEMNL 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2612 KRE-----AELLQQ---------KSEE-MQTAQKEQLRQETQM--LQQTFRSEKDVLLQKERFVEE---EKAKLEK---- 2667
Cdd:pfam05483 547 RDElesvrEEFIQKgdevkckldKSEEnARSIEYEVLKKEKQMkiLENKCNNLKKQIENKNKNIEElhqENKALKKkgsa 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2668 ------LFQEEVNKAQgLKAEQERQ---------QKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQR-------- 2724
Cdd:pfam05483 627 enkqlnAYEIKVNKLE-LELASAKQkfeeiidnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaem 705
|
650 660 670
....*....|....*....|....*....|....*....
gi 2069539781 2725 ---LEKQRQKQEKLLAEENQK--LREKLEQLQEEQKTAL 2758
Cdd:pfam05483 706 valMEKHKHQYDKIIEERDSElgLYKNKEQEQSSAKAAL 744
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2128-2753 |
8.44e-18 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 92.20 E-value: 8.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2128 EENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQkeLAEKESERQIQLAQEAAQKRIVAEEKAHlAAV 2207
Cdd:NF041483 13 DDDHLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRS--LASRPAYDGADIGYQAEQLLRNAQIQAD-QLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2208 QQKEQELLQTRQQEQSILDKLREEAERAK-KAAEDAEFARIKAEQEAALSRQLVEE--------AERMKQRAEEEA---- 2274
Cdd:NF041483 90 ADAERELRDARAQTQRILQEHAEHQARLQaELHTEAVQRRQQLDQELAERRQTVEShvnenvawAEQLRARTESQArrll 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2275 -QTKAKAQEDAEKLRKEAEleaarraqAEQAALKQKQLADAEMAKHKkfAEQTL-RQKAQVEQELTKVKLQLEE-TDHQK 2351
Cdd:NF041483 170 dESRAEAEQALAAARAEAE--------RLAEEARQRLGSEAESARAE--AEAILrRARKDAERLLNAASTQAQEaTDHAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2352 -----SILEEEQQRLK-DEVTEAMKQKVQ-VEEELFKVKVQMEELIKLKTriEEENKMLITKDKDNMQkflaeeaeKMKQ 2424
Cdd:NF041483 240 qlrssTAAESDQARRQaAELSRAAEQRMQeAEEALREARAEAEKVVAEAK--EAAAKQLASAESANEQ--------RTRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2425 VAEEAARLSVEA-QEAARLRELAEQDLAQQRSLAEKILKEkmqAVQEATRLKAE--AEVLQKQKDLAQEQAKKLQEDKEQ 2501
Cdd:NF041483 310 AKEEIARLVGEAtKEAEALKAEAEQALADARAEAEKLVAE---AAEKARTVAAEdtAAQLAKAARTAEEVLTKASEDAKA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2502 MQLRLAEEAEGFQKTLEAERQR-QLEITANAERL----KVQVTELSLAQAKAEEEAKRFKKQAEQI-SQKLHQTE-LATQ 2574
Cdd:NF041483 387 TTRAAAEEAERIRREAEAEADRlRGEAADQAEQLkgaaKDDTKEYRAKTVELQEEARRLRGEAEQLrAEAVAEGErIRGE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2575 EKMTLVQTLEiqrQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKeqlRQETQMLQQTfRSEkdvllqK 2654
Cdd:NF041483 467 ARREAVQQIE---EAARTAEELLTKAKADADELRSTATAESERVRTEAIERATTLR---RQAEETLERT-RAE------A 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2655 ERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQE-KKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQR-QKQ 2732
Cdd:NF041483 534 ERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEaAEELTRLHTEAEERLTAAEEALADARAEAERIRREAaEET 613
|
650 660
....*....|....*....|.
gi 2069539781 2733 EKLLAEENQKLREKLEQLQEE 2753
Cdd:NF041483 614 ERLRTEAAERIRTLQAQAEQE 634
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
314-410 |
1.49e-17 |
|
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: 80.82 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 314 EKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----VENLEQAFSVAEQDLGVTRLLD 389
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 2069539781 390 PEDVDVPQPDEKSIITYVSSL 410
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1892-2398 |
2.60e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.10 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1892 VNEAVQKRKELEEELAKLRAEmelllqskaktEEESRSTSEKSKQILEAEASKLRELA---EEAARLRALSEEAKRQRQL 1968
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQ-----------REQARETRDEADEVLEEHEERREELEtleAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1969 AEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKE---AENERLRRLAEDEAYQRRLLEEQA---AQHKQDIEE 2042
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRLEECRVAAQAHNEEAeslREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2043 KIAQLKKSS---ESELERQKSLVDDTVRQRRLVEEEIRILKLNF-------EKASHGKTDLELELTRIKQSAEEIQ---R 2109
Cdd:PRK02224 357 RAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFgdapvdlGNAEDFLEELREERDELREREAELEatlR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2110 SKEQAEREAEELRQLA--------LEEENHRREAEAKVKKISAAEQEAArqckAALEEVERLKAKAEEArrqKELAEKES 2181
Cdd:PRK02224 437 TARERVEEAEALLEAGkcpecgqpVEGSPHVETIEEDRERVEELEAELE----DLEEEVEEVEERLERA---EDLVEAED 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2182 ERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELlqtRQQEQSILDKLREEAERAKKAAEDAEFARIKAeqeAALSRQLVE 2261
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEEL---RERAAELEAEAEEKREAAAEAEEEAEEAREEV---AELNSKLAE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2262 EAERMKQ--RAEEEAQTKAKAQEDAEKLRKeaeleaarraqaeqaalKQKQLADAEMAKHKKFAEQTLRqKAQVEQELTK 2339
Cdd:PRK02224 584 LKERIESleRIRTLLAAIADAEDEIERLRE-----------------KREALAELNDERRERLAEKRER-KRELEAEFDE 645
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2340 VKlqLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEE 2398
Cdd:PRK02224 646 AR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1508-1980 |
2.80e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.10 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAVDAEQqkqtiqqelsqmklsSDAQIQAKLK 1587
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL---------------DDADAEAVEA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELK 1667
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 HKVQAEQQAAREKQKA---LEDLQ--KLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAE-----------ADLQSRR 1731
Cdd:PRK02224 395 ELRERFGDAPVDLGNAedfLEELReeRDELREREAELEATLRTARERVEEAEALLEAGKCPEcgqpvegsphvETIEEDR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1732 lsfaEKTAQLELSLQQEHITITHLQEEAERLKKLQleaeqsreEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEA 1811
Cdd:PRK02224 475 ----ERVEELEAELEDLEEEVEEVEERLERAEDLV--------EAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1812 EKQKEDAEREAR-KRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAeqELIRLKAEVENgEQQRLLLEEELFRLKN 1890
Cdd:PRK02224 543 RERAAELEAEAEeKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE--RIRTLLAAIAD-AEDEIERLREKREALA 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1891 EVNEavqKRKELEEELAKLRAEMELLLQSKAKteEESRSTSEKSKQILEAEASKLRELAEEAARLR----ALSEEAKRQR 1966
Cdd:PRK02224 620 ELND---ERRERLAEKRERKRELEAEFDEARI--EEAREDKERAEEYLEQVEEKLDELREERDDLQaeigAVENELEELE 694
|
490
....*....|....*...
gi 2069539781 1967 QLAEE----EATHQRAEA 1980
Cdd:PRK02224 695 ELRERrealENRVEALEA 712
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1607-2171 |
3.29e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 89.71 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1607 RLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAErlRKQVKDE---SQKKREAEDELKHKVQAEQQAAREKQKA 1683
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESE--LAELDEEierYEEQREQARETRDEADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1684 LEDLQ----KLRLQAEEAER------------RMKQAELEKERQVQLAhEAAQKSAEAD-LQSRRLSFAEKTAQLELSLQ 1746
Cdd:PRK02224 253 LETLEaeieDLRETIAETERereelaeevrdlRERLEELEEERDDLLA-EAGLDDADAEaVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1747 QEHITITHLQEEAERL----KKLQLEAEQSREEADkEVEKWRQKANEALRLRLQAEEVAHKKAlaqEEAEKQKEDAEREa 1822
Cdd:PRK02224 332 ECRVAAQAHNEEAESLredaDDLEERAEELREEAA-ELESELEEAREAVEDRREEIEELEEEI---EELRERFGDAPVD- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1823 rkRSKAEEsalRQKELAEQELEKQRKLAEGTAQQKFLAE--QELIRLKAEvenGEQQRLLLEEELFRLKNEVNEAVQKRK 1900
Cdd:PRK02224 407 --LGNAED---FLEELREERDELREREAELEATLRTARErvEEAEALLEA---GKCPECGQPVEGSPHVETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1901 ELEEELAKLRAEMELL---------LQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEE 1971
Cdd:PRK02224 479 ELEAELEDLEEEVEEVeerleraedLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1972 EATHQRAEAERILKEklvaineasrlKAEAEIALKEKEAENERLRRLAEdeayqrrlLEEQAAQHKQDIEEKIAQLKKSS 2051
Cdd:PRK02224 559 AAAEAEEEAEEAREE-----------VAELNSKLAELKERIESLERIRT--------LLAAIADAEDEIERLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2052 ESELERQKSLVDDTVRQRRLVEeeirilklnfekashgktdlELELTRIKQSAEEIQRSKEQAEREAEELRQlaLEEENH 2131
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEA--------------------EFDEARIEEAREDKERAEEYLEQVEEKLDE--LREERD 677
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2069539781 2132 RREAEAKVKKISAAEQEAARQCKAALEE-VERLKAKAEEAR 2171
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENrVEALEALYDEAE 718
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2042-2714 |
3.38e-17 |
|
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: 89.40 E-value: 3.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2042 EKIAQLKKSSESELERQKSLVDDtvrQRRLVEEEIR-ILKLNFEKAshgKTDLELEltrikqsaEEIQRSKEQAEREAEE 2120
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQE---NRKIIEAQRKaIQELQFENE---KVSLKLE--------EEIQENKDLIKENNAT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2121 LRQLALEEENHRREAEaKVKKISAaEQEAARQCKAALEE--------VERLKAKAEEARRQKELAEKESERQIQLAQEAA 2192
Cdd:pfam05483 154 RHLCNLLKETCARSAE-KTKKYEY-EREETRQVYMDLNNniekmilaFEELRVQAENARLEMHFKLKEDHEKIQHLEEEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2193 QKRIVAEEK-AHLAAVQQKEQE---------LLQTRQQEQSILDKLREEAERAKKAAED-----AEFARIKAEQEAALSR 2257
Cdd:pfam05483 232 KKEINDKEKqVSLLLIQITEKEnkmkdltflLEESRDKANQLEEKTKLQDENLKELIEKkdhltKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2258 Q-LVEEAERMKQRA------EEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEmaKHKKFAEQTLRQK 2330
Cdd:pfam05483 312 QkALEEDLQIATKTicqlteEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE--DQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2331 AQVEQELTKVKLQLE-ETDHQKSILEEEQQRLKDEvteamKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKDKD 2409
Cdd:pfam05483 390 SSELEEMTKFKNNKEvELEELKKILAEDEKLLDEK-----KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKT 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2410 NMQKFLaEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAV-----QEATRLKAEAEVLQKQ 2484
Cdd:pfam05483 465 SEEHYL-KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckkQEERMLKQIENLEEKE 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2485 KDLAQE-----QAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANA-ERLKVQVTELSLAQAKAEEEAKRFKKQ 2558
Cdd:pfam05483 544 MNLRDElesvrEEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcNNLKKQIENKNKNIEELHQENKALKKK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2559 AEQISQKLHQTELATQEkmtLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKE-QLRQET 2637
Cdd:pfam05483 624 GSAENKQLNAYEIKVNK---LELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEiDKRCQH 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2638 QMLQQTFRSEKDVLlQKERFVEEEKAKLeKLFQEEVNKAQGLKAEQERQQKQMEQE----KKQLTTVLEEARKKQAEAEE 2713
Cdd:pfam05483 701 KIAEMVALMEKHKH-QYDKIIEERDSEL-GLYKNKEQEQSSAKAALEIELSNIKAEllslKKQLEIEKEEKEKLKMEAKE 778
|
.
gi 2069539781 2714 N 2714
Cdd:pfam05483 779 N 779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1967-2644 |
3.77e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 89.71 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1967 QLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQhkqdiEEKIAQ 2046
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQ-----REQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2047 LKKSSESELERQkslvddtvRQRRlveEEIrilklnfekashgkTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLAL 2126
Cdd:PRK02224 235 TRDEADEVLEEH--------EERR---EEL--------------ETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2127 EEENHRREAEAKVkKISAAEQEAARQCKAALEE-----VERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRivaEEK 2201
Cdd:PRK02224 290 ELEEERDDLLAEA-GLDDADAEAVEARREELEDrdeelRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR---EEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2202 AHLAAVQQKEQELLQTRQQEQSILDklrEEAERAKKAAEDAEFARIKAEqeaALSRQLVEEAERMKQRaeeEAQTKAKAQ 2281
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELE---EEIEELRERFGDAPVDLGNAE---DFLEELREERDELRER---EAELEATLR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2282 EDAEKLRKEAELEAARRAQAEQAALKQKQLADAemakhkkfaeqtlrqkaqveqeltkvklqLEETDHQKSILEEEQQRL 2361
Cdd:PRK02224 437 TARERVEEAEALLEAGKCPECGQPVEGSPHVET-----------------------------IEEDRERVEELEAELEDL 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2362 KDEVTEamkqkvqVEEELfkvkVQMEELIKLKTRIE--EENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQE- 2438
Cdd:PRK02224 488 EEEVEE-------VEERL----ERAEDLVEAEDRIErlEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEk 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2439 ---AARLRELAEQDLAQQRSLAEKI--LKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEeaegf 2513
Cdd:PRK02224 557 reaAAEAEEEAEEAREEVAELNSKLaeLKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAE----- 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2514 qktlEAERQRQLEITANAERLkvqvtelslaqAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSD 2593
Cdd:PRK02224 632 ----KRERKRELEAEFDEARI-----------EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2594 AEKlRKAIADLEQEKEKLKREAELLQqkseEMQTAQKEQLRQET-----QMLQQTF 2644
Cdd:PRK02224 697 RER-REALENRVEALEALYDEAEELE----SMYGDLRAELRQRNvetleRMLNETF 747
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
315-412 |
3.81e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.92 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 315 KLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLD-PEDV 393
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2069539781 394 DVPQPDEKSIITYVSSLYD 412
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1589-2277 |
3.96e-17 |
|
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: 89.90 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1589 IEEVEFSRRKVEEEIRMVR-LQLEATERQRAGAEDELQALRDRAEEAERQKRLaQEEAERLRKQVKdesQKKREAEDELK 1667
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLEsAELRLSHLHFGYKSDETLIASRQEERQETSAEL-NQLLRTLDDQWK---EKRDELNGELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 hKVQAEQQAAREKQKALEDlQKLRLQAEEAERRmkQAELEKERQVQLAHEAAQKSAEADLQSRRlSFAEKTAQLELSLQQ 1747
Cdd:pfam12128 312 -AADAAVAKDRSELEALED-QHGAFLDADIETA--AADQEQLPSWQSELENLEERLKALTGKHQ-DVTAKYNRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1748 EhitithLQEEAERLKKlqlEAEQSREEADkevekwRQKAneALRLRLQAEEVAHKKALAQE-----EAEKQKEDAEREA 1822
Cdd:pfam12128 387 Q------NNRDIAGIKD---KLAKIREARD------RQLA--VAEDDLQALESELREQLEAGklefnEEEYRLKSRLGEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1823 RKR---SKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQK- 1898
Cdd:pfam12128 450 KLRlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQl 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1899 -----------RKEL---EEELAKLrAEMELLLqskaKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKR 1964
Cdd:pfam12128 530 fpqagtllhflRKEApdwEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1965 QRQLAEEEATHQRAEAERIlKEKLVAIN-EASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEK 2043
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAA-EEQLVQANgELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANER 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2044 IAQLKKSSESELERQKSLVDDTVRQRRlveeEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQ 2123
Cdd:pfam12128 684 LNSLEAQLKQLDKKHQAWLEEQKEQKR----EARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRD 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2124 LA---------LEEENHRREAEAKVKKISAAEQEAAR----QCKAALEEVERLKAKAEEARRqkelaeKESERQIQLAqe 2190
Cdd:pfam12128 760 LAslgvdpdviAKLKREIRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIER------AISELQQQLA-- 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2191 aaqkRIVAEEKAHLAAV--QQKEQELLQTRQQEQsiLDKLREEAERAKKAAEDAEFAriKAEQEAALSRQLVEEAERMKQ 2268
Cdd:pfam12128 832 ----RLIADTKLRRAKLemERKASEKQQVRLSEN--LRGLRCEMSKLATLKEDANSE--QAQGSIGERLAQLEDLKLKRD 903
|
....*....
gi 2069539781 2269 RAEEEAQTK 2277
Cdd:pfam12128 904 YLSESVKKY 912
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1629-2236 |
4.55e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.35 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1629 DRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEK 1708
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1709 ERQVQLAHEaaqksaEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSR---EEADKEVEKWRQ 1785
Cdd:PRK03918 238 EEIEELEKE------LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIklsEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1786 KANEALRLRLQAEEVAHKkalaQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELI 1865
Cdd:PRK03918 312 IEKRLSRLEEEINGIEER----IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1866 RLKAEVENgeqqrllLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAK--------TEEESR--------- 1928
Cdd:PRK03918 388 KLEKELEE-------LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKelleeytae 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1929 -STSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEE-------------EATHQRAEAERILKEKLVAIN-E 1993
Cdd:PRK03918 461 lKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKgE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1994 ASRLKAEAEIA---LKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELErqkslVDDTVRQRR 2070
Cdd:PRK03918 541 IKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE-----LKDAEKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2071 LVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQrsKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAa 2150
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEI- 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2151 rqcKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAhLAAVQQKEQELLQTRQQEQSILDKLRE 2230
Cdd:PRK03918 693 ---KKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERA-LSKVGEIASEIFEELTEGKYSGVRVKA 768
|
....*.
gi 2069539781 2231 EAERAK 2236
Cdd:PRK03918 769 EENKVK 774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1255-2020 |
4.65e-17 |
|
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: 89.35 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1255 RKYEEQLKDVQAVPSDLKaLEATKAELKRLRGQVEGHQPLFNTLEMDLAKASEVNERMVRGHSERDIDLDRYRERVQQLL 1334
Cdd:TIGR02168 216 KELKAELRELELALLVLR-LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1335 ERWQAILAQIDLRQRELDQLGRQLRYYRESydwliqwIREARQRQEHLQAvpvtNSKSVREQLLQekkLLEECDRNREKV 1414
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDELAE----ELAELEEKLEE---LKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1415 EECQCFAKQYIDAIKDYELQLVTYKAQV----EPVASPAKKPKVQSASDSVIQEYVD--LRTRYSELTTLTSQYLKFITE 1488
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVaqleLQIASLNNEIERLEARLERLEDRRErlQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1489 TLRRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHAR--AKAQAEKEALELQRRMEEEVSRR------------- 1553
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERelAQLQARLDSLERLQENLEGFSEGvkallknqsglsg 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1554 ------QLVAVDA--EQQKQTIQQELSQMKLSSDAQIQAK-LKLIEEVEFSRRKVEE-------EIRMVRLQLEATERQR 1617
Cdd:TIGR02168 521 ilgvlsELISVDEgyEAAIEAALGGRLQAVVVENLNAAKKaIAFLKQNELGRVTFLPldsikgtEIQGNDREILKNIEGF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1618 AGAEDEL-------------------------QALRDRAEEAERQkRLAQEEAERLRKQ--------VKDESQKKREAE- 1663
Cdd:TIGR02168 601 LGVAKDLvkfdpklrkalsyllggvlvvddldNALELAKKLRPGY-RIVTLDGDLVRPGgvitggsaKTNSSILERRREi 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1664 DELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLA------HEAAQKSAEADLQSRRLSFAEK 1737
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1738 TAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRlqaeEVAHKKALAQEEAEKQKED 1817
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN----EEAANLRERLESLERRIAA 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1818 AEREARKRSKAEESALRQKELAEQELEKQRKLAEGtaqqkflAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQ 1897
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1898 KRKELEEELAKLRAEMELLLQSKAKTEEESRstsekskQILEAEASKLRELAEEAArlrALSEEAKRQRQLAEEEATHQR 1977
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRID-------NLQERLSEEYSLTLEEAE---ALENKIEDDEEEARRRLKRLE 978
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 2069539781 1978 AEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAE 2020
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2174-2753 |
4.74e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.35 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2174 KELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARikaEQEA 2253
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE---KELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2254 ALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRaqaeqaalkqkqladaEMAKHKKFAEQTLRQKAQV 2333
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE----------------EYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2334 EQELTKVKLQLEETDHQKSILEEEQQR---LKDEVTEAMKQKVQVEE---ELFKVKVQMEELIKLKTRIEEENKMLITKD 2407
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERleeLKKKLKELEKRLEELEErheLYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2408 KDNMQKFLAEEAEKMKQVAEEAARL---------SVEAQEAARL------RELAEQD----LAQQRSLAEKILKEKMQAV 2468
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELkkeikelkkAIEELKKAKGkcpvcgRELTEEHrkelLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2469 QEATRLKAEAE----VLQKQKDLA--QEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELS 2542
Cdd:PRK03918 473 EKERKLRKELRelekVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2543 LAQAKAEEEAKRFKKQAEQISQKLHQTElatQEKMTLVQTLEIQRQQSDSDAEK---LRKAIADLEQEKEKLKREAELLQ 2619
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELE---ELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2620 QKSEEMQTAQK--EQLRQETQMLQQtfrsekdvllqkeRFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQL 2697
Cdd:PRK03918 630 KAFEELAETEKrlEELRKELEELEK-------------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2698 TTvLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEE 2753
Cdd:PRK03918 697 EK-LKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASE 751
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2013-2728 |
4.96e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 89.41 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2013 ERLRRLAEDEAYQ-----RRLLEEQAAQHKQD--IEEKIAQLK-KSSESELERqkslvDDTVRQRRLVEEEIRILKLNFE 2084
Cdd:pfam15921 74 EHIERVLEEYSHQvkdlqRRLNESNELHEKQKfyLRQSVIDLQtKLQEMQMER-----DAMADIRRRESQSQEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2085 KASHgktdlelELTRIKQSAEEIQrskEQAEREAEELRQLALEEENHRRE--------AEAKVKKISAAEQEAA---RQC 2153
Cdd:pfam15921 149 NTVH-------ELEAAKCLKEDML---EDSNTQIEQLRKMMLSHEGVLQEirsilvdfEEASGKKIYEHDSMSTmhfRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2154 KAALEEVER--------LKAKAEEARRQKELAEKESERQIQLAQEAAQKRI---VAEEKAHLAAVQQKEQellQTRQQEQ 2222
Cdd:pfam15921 219 GSAISKILReldteisyLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIeqlISEHEVEITGLTEKAS---SARSQAN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2223 SILDKLREEAERAKKaaEDAEFARIKAEQEAALS--RQLVEEAERMKQRAEEEAQtKAKAQEDAEKLRKEAELEAARRAQ 2300
Cdd:pfam15921 296 SIQSQLEIIQEQARN--QNSMYMRQLSDLESTVSqlRSELREAKRMYEDKIEELE-KQLVLANSELTEARTERDQFSQES 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2301 AEQAALKQKQLADAemakHKKFAEQTLrQKAQVEQELTKVKLQLEETDHQKSILEE---EQQRLkDEVTEAMKQKVQVEE 2377
Cdd:pfam15921 373 GNLDDQLQKLLADL----HKREKELSL-EKEQNKRLWDRDTGNSITIDHLRRELDDrnmEVQRL-EALLKAMKSECQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2378 ELFKVKVQ-----MEELIKLKTRIEEENKMLitkdkdnmqKFLAEEAEKMKQVAEEAAR----LSVEAQEAARLRELAEQ 2448
Cdd:pfam15921 447 ERQMAAIQgknesLEKVSSLTAQLESTKEML---------RKVVEELTAKKMTLESSERtvsdLTASLQEKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2449 DLAQQRSLAEKILKEKMQAVQEATRLK---AEAEVLQKQKDLAQEQAKKLQEDKEQMqLRLAEEAEGFQKTLEAERQrQL 2525
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRnvqTECEALKLQMAEKDKVIEILRQQIENM-TQLVGQHGRTAGAMQVEKA-QL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2526 EITANAERLKVQvtELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLE 2605
Cdd:pfam15921 596 EKEINDRRLELQ--EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2606 QEKEKLKREaelLQQKSEEMQTAQ---KEQLRQETQMLQQTF---------------------------RSEKDVLLQKE 2655
Cdd:pfam15921 674 EDYEVLKRN---FRNKSEEMETTTnklKMQLKSAQSELEQTRntlksmegsdghamkvamgmqkqitakRGQIDALQSKI 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2656 RFVEEE-----------KAKLEKLFQE------EVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQK 2718
Cdd:pfam15921 751 QFLEEAmtnankekhflKEEKNKLSQElstvatEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQ 830
|
810
....*....|
gi 2069539781 2719 QEELQRLEKQ 2728
Cdd:pfam15921 831 EQESVRLKLQ 840
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1900-2761 |
8.92e-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: 8.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1900 KELEEELAKLRAEMELLLQSKA-KTEEESRSTSEKSKQILEAEASKlRELAEEAARLRAlsEEAKRQRQLAEEEATHQRA 1978
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQAlLKEKREYEGYELLKEKEALERQK-EAIERQLASLEE--ELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1979 EAE-RILKEKLVAINEASRLKAEAEIAlkEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSEsELER 2057
Cdd:TIGR02169 271 EQLlEELNKKIKDLGEEEQLRVKEKIG--ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER-EIEE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2058 QKslvddtvRQRRLVEEEIRilklnfekashgktDLELELTRIKQSAEEI----QRSKEQAEREAEELRQLALEEENHRR 2133
Cdd:TIGR02169 348 ER-------KRRDKLTEEYA--------------ELKEELEDLRAELEEVdkefAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2134 EAEAKVKKISAAEQEAArQCKAALEEVERLKAKAEEARRQKELAEKESERQIQlaQEAAQKRIVAEEKAHLAAVQQKEQE 2213
Cdd:TIGR02169 407 ELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE--QLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2214 LLQTRQQEQSILDKLR---EEAERAKKAAEDAEFARIKAEQeaALSRQLVEEAERMKQRAEEEAQTKAKA--QEDAEKLR 2288
Cdd:TIGR02169 484 ELSKLQRELAEAEAQArasEERVRGGRAVEEVLKASIQGVH--GTVAQLGSVGERYATAIEVAAGNRLNNvvVEDDAVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2289 KEAELeaarraqaeqaaLKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDhqksileeeqQRLKDEVTEA 2368
Cdd:TIGR02169 562 EAIEL------------LKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFD----------PKYEPAFKYV 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2369 MKQKVQVEEelfkvkvqMEELIKLKTRIEeenkmLITKDKDNMQK-------FLAEEAEKMKQVAEEAARLSVEAQEAAR 2441
Cdd:TIGR02169 620 FGDTLVVED--------IEAARRLMGKYR-----MVTLEGELFEKsgamtggSRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2442 LRELAeqDLAQQRSLAEKILKEKMQAVQEATR----LKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLaEEAEGFQKTL 2517
Cdd:TIGR02169 687 KRELS--SLQSELRRIENRLDELSQELSDASRkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-ENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2518 EAERQrQLEITANAERLKVQVTELSLAQA----------KAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQR 2587
Cdd:TIGR02169 764 EARIE-ELEEDLHKLEEALNDLEARLSHSripeiqaelsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2588 QQSDSDAEKLRKAIADLEQEKEKLKREAELLQ----QKSEEMQTAQKEQLRQETQM--LQQTFRSEKDVLLQKERFVEEE 2661
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrDLESRLGDLKKERDELEAQLreLERKIEELEAQIEKKRKRLSEL 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2662 KAKLEKLFQEEVNKAQGLKAEQERQQKQM--EQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKlLAEE 2739
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAK-LEEE 1001
|
890 900
....*....|....*....|..
gi 2069539781 2740 NQKLREKLEQLQEEQKTALAQT 2761
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREVFMEA 1023
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1705-2367 |
1.30e-16 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 87.47 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1705 ELEKERQVQLAHEAAQKSAEADLQ-SRRLSFAEKTAQLELSLQQEHITIThLQEEAERLKKLQLEAEQSREEADKEVEKW 1783
Cdd:pfam05483 86 EAEKIKKWKVSIEAELKQKENKLQeNRKIIEAQRKAIQELQFENEKVSLK-LEEEIQENKDLIKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1784 RQKANEALRLRLQAEEVAH----------KKALAQEEAEKQKEDAEREARKRSKAEESALRQ-KELAEQELEKQRKLAEG 1852
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQvymdlnnnieKMILAFEELRVQAENARLEMHFKLKEDHEKIQHlEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1853 TAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSE 1932
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1933 KSKQILEAEASKLRELAEEAA-------RLRALS---EEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAE 2002
Cdd:pfam05483 325 TICQLTEEKEAQMEELNKAKAahsfvvtEFEATTcslEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2003 IALKEKEA----------ENERLRRLAED-EAYQRRLLEEQAAQHKQ--DIEEKIAQLKKSSE---SELERQKSLVDDTV 2066
Cdd:pfam05483 405 VELEELKKilaedeklldEKKQFEKIAEElKGKEQELIFLLQAREKEihDLEIQLTAIKTSEEhylKEVEDLKTELEKEK 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2067 RQRRLVEEEIRILKLNFEKASHGKTDLELELtriKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVK------ 2140
Cdd:pfam05483 485 LKNIELTAHCDKLLLENKELTQEASDMTLEL---KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREefiqkg 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2141 -----KISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQE--AAQKRIVAEEK---AHLAAVQQK 2210
Cdd:pfam05483 562 devkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkALKKKGSAENKqlnAYEIKVNKL 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2211 EQELLQTRQQEQSILDKLREEAERAKKAAEdaefarikaeqeaalsrQLVEEAERMKQRAEEeaQTKAKAQEDAEKLRKE 2290
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDKKISEE-----------------KLLEEVEKAKAIADE--AVKLQKEIDKRCQHKI 702
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2291 AELEAARRAQAEQAAlKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTE 2367
Cdd:pfam05483 703 AEMVALMEKHKHQYD-KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1170-2069 |
1.46e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.80 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1170 QRITDqqqIHQELEGIKKNLGKVSAKTEQVLAQPEQASSAptlhsELDITLQKMDQvyslssiYLEKLKTIHLVIRStqg 1249
Cdd:TIGR02168 189 DRLED---ILNELERQLKSLERQAEKAERYKELKAELREL-----ELALLVLRLEE-------LREELEELQEELKE--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1250 AEDLIRKYEEQLKDVQAVPSDLK-ALEATKAELKRLRGQVEGHQPLFNTLEMDLAKASEVNERMVRGHSErdidLDRYRE 1328
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRlEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE----LEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1329 RVQQLLERWQAILAQIdlrQRELDQLGRQLRYYRESYDWLIQWIREARQRQEHLQAVPVTNSKSVREQLLQEKKLLEECD 1408
Cdd:TIGR02168 327 ELESKLDELAEELAEL---EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1409 RNREKVEecqcfakqyidAIKDYELQLVTYKAQVEPVASPAKKPKVQSASDSVIQEYVDLRTRYSELttltSQYLKFITE 1488
Cdd:TIGR02168 404 RLEARLE-----------RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL----EEALEELRE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1489 TLRRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEK---------EALELQRRMEEEVS-----RRQ 1554
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAIEaalggRLQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1555 LVAVDAEQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDR---- 1630
Cdd:TIGR02168 549 AVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvv 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1631 ---AEEAERQKRLAQEEA------ERLRKQ--------VKDESQKKREAE-DELKHKVQAEQQAAREKQKALEDLQKLRL 1692
Cdd:TIGR02168 629 ddlDNALELAKKLRPGYRivtldgDLVRPGgvitggsaKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1693 QAEEAERRMKQAELEKERQVqlaheaaqKSAEADLQSRRlsfaEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQS 1772
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQI--------SALRKDLARLE----AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1773 REEADKEVEKWRQKANEALRLRLQAEEvahkkalAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKqrklaeg 1852
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALRE-------ALDELRAELTLLNEEAANLRERLESLERRIAATERRLED------- 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1853 TAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMElllqskakteeesrstsE 1932
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR-----------------E 905
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1933 KSKQILEAEAsKLRELAEEAARLRALSEEAKRQR-QLAEEEATHQRAEAERIlkEKLVAINEASRLKAEAEIA-LKEKEA 2010
Cdd:TIGR02168 906 LESKRSELRR-ELEELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLEEA--EALENKIEDDEEEARRRLKrLENKIK 982
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2011 ENERLRRLAEDEAyqrrlleEQAAQHKQDIEEKIAQLKKSSESeLERQKSLVDDTVRQR 2069
Cdd:TIGR02168 983 ELGPVNLAAIEEY-------EELKERYDFLTAQKEDLTEAKET-LEEAIEEIDREARER 1033
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1655-2028 |
2.32e-16 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 86.72 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1655 ESQKKREAEDELKHKVQAEQQAA-REKQKALEDLQKLRLQAEEAErrmKQAELEKERQVQLAHEAAQksAEADLQSRRLS 1733
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSeRQQQEKFEKMEQERLRQEKEE---KAREVERRRKLEEAEKARQ--AEMDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1734 FAEKTAqLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAeevAHKKALAQEEAEK 1813
Cdd:pfam17380 338 EQERMA-MERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA---ARKVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1814 QKEDAEREARKRSKAEESAlRQKELAEQELEKQRKLaEGTAQQKFLAEQELIRLKAEvengeqqrllleeelfrlknevn 1893
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEA-RQREVRRLEEERAREM-ERVRLEEQERQQQVERLRQQ----------------------- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1894 EAVQKRKELEEElaklraemelllqskaKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLA-EEE 1972
Cdd:pfam17380 469 EEERKRKKLELE----------------KEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEE 532
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1973 ATHQRAEAER---ILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRL 2028
Cdd:pfam17380 533 ERRREAEEERrkqQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1926-2760 |
4.94e-16 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 86.16 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1926 ESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRA---------EAERILKEKLVAINEASR 1996
Cdd:PRK04863 297 TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKieryqadleELEERLEEQNEVVEEADE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1997 LKAEAEIALKEKEAENERLR-RLAEdeaYQRRLLEEQ--AAQHKQDIE--EKIAQLKKSSESELERQKSLVDDTVRQRRL 2071
Cdd:PRK04863 377 QQEENEARAEAAEEEVDELKsQLAD---YQQALDVQQtrAIQYQQAVQalERAKQLCGLPDLTADNAEDWLEEFQAKEQE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2072 VEEEIRIL--KLNFEKASHGKTDLELELtrIKQSAEEIQRSkeQAEREAEELrqlaleEENHRREaeakvkKISAAEQEA 2149
Cdd:PRK04863 454 ATEELLSLeqKLSVAQAAHSQFEQAYQL--VRKIAGEVSRS--EAWDVAREL------LRRLREQ------RHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2150 ARQCKAALEEVERLKAKAEEARRQkelAEKESERQIQLAQEAAQKRIVAEEKahLAAVQQKEQELLQTRQQEQSILDKLR 2229
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAE---FCKRLGKNLDDEDELEQLQEELEAR--LESLSESVSEARERRMALRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2230 EEAERAKKAAEDAEFARIKAEQ------EAALSRQLVEEAerMKQRAEEE-AQTKAKAQEDAEKLRKEAELeaarraqae 2302
Cdd:PRK04863 593 ARIQRLAARAPAWLAAQDALARlreqsgEEFEDSQDVTEY--MQQLLERErELTVERDELAARKQALDEEI--------- 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2303 qaaLKQKQLADAEMAKHKKFAEQT--------------------------LRQkAQVEQELTKVKLQLEETDHQKS---I 2353
Cdd:PRK04863 662 ---ERLSQPGGSEDPRLNALAERFggvllseiyddvsledapyfsalygpARH-AIVVPDLSDAAEQLAGLEDCPEdlyL 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2354 LEEEQQRLKDEVTEAmkqkvqveEELFKVKVQMEELIKLK-TRIEEEnKMLITKDKDNMQKFLAEEAEkmkQVAEEAARL 2432
Cdd:PRK04863 738 IEGDPDSFDDSVFSV--------EELEKAVVVKIADRQWRySRFPEV-PLFGRAAREKRIEQLRAERE---ELAERYATL 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2433 SVEAQEAARLRELAEQDLAQQRSLA-----EKILKEKMQAVQEATRlkaeaeVLQKQKDLAQEQAKKLQEDKEQMQL--R 2505
Cdd:PRK04863 806 SFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELER------ALADHESQEQQQRSQLEQAKEGLSAlnR 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2506 LAEEAEGFQKTLEAERQRQLEitanaerlkvqvtelslAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEI 2585
Cdd:PRK04863 880 LLPRLNLLADETLADRVEEIR-----------------EQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQ 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2586 QRQQSDSDAEKLRK---AIADLEQEKEKLK-REAELLQQKSEEMQtaqkEQLRQETQMLQQTFRSEKDVLLQKERFVEEE 2661
Cdd:PRK04863 943 DYQQAQQTQRDAKQqafALTEVVQRRAHFSyEDAAEMLAKNSDLN----EKLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2662 KAKLEKLFQEEVNKAQGLKAEQERqqkqMEQEKKQLTTVLEE-ARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEEN 2740
Cdd:PRK04863 1019 NQVLASLKSSYDAKRQMLQELKQE----LQDLGVPADSGAEErARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLT 1094
|
890 900
....*....|....*....|
gi 2069539781 2741 QKLREKLEQLQEEQKTALAQ 2760
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNA 1114
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1932-2763 |
5.39e-16 |
|
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: 86.25 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1932 EKSKQILEAEASKLRELAEEAARLRALSEEAKRQR-QLAEEEAthQRAEAERILKEKLvaiNEASRLKAEaeiaLKEKEA 2010
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRdQITSKEA--QLESSREIVKSYE---NELDPLKNR----LKEIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2011 ENERLRRLaEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQ--RRLVEEEIRILKLNFEKA-- 2086
Cdd:TIGR00606 260 NLSKIMKL-DNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREkeRELVDCQRELEKLNKERRll 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2087 SHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELR-QLALEEENHRREAEAKVK-----KISAAEQEA--ARQCKAALE 2158
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLAtRLELDGFERGPFSERQIKnfhtlVIERQEDEAktAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2159 EVERLKAKAEEARRQKElaeKESERQIQLAQEAAQKRiVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKA 2238
Cdd:TIGR00606 419 SKERLKQEQADEIRDEK---KGLGRTIELKKEILEKK-QEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2239 AEDAEFARIKAEQ--EAALSRQLVEEAERMKQ-------RAEEEAQTKAKAQEDaEKLRKEAELEAARRAQAEQAALKQK 2309
Cdd:TIGR00606 495 LTETLKKEVKSLQneKADLDRKLRKLDQEMEQlnhhtttRTQMEMLTKDKMDKD-EQIRKIKSRHSDELTSLLGYFPNKK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2310 QLADA--EMAKHKKFAEQTLR----QKAQVEQELTKVKLQLEETDHQKSILEE-------------EQQRLKDEVTEAMK 2370
Cdd:TIGR00606 574 QLEDWlhSKSKEINQTRDRLAklnkELASLEQNKNHINNELESKEEQLSSYEDklfdvcgsqdeesDLERLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2371 QKVQVE------------------------EELFKVKVQMEELIK--------LKTRIEEENKMLITKDK---------- 2408
Cdd:TIGR00606 654 QRAMLAgatavysqfitqltdenqsccpvcQRVFQTEAELQEFISdlqsklrlAPDKLKSTESELKKKEKrrdemlglap 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2409 ------DNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRE--LAEQDLAQQRSLAEKILKEKMQAVQEATRLKAE--A 2478
Cdd:TIGR00606 734 grqsiiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQqaA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2479 EVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEaERQRQLeitanaERLKVQVTELSLAQAKAEEEAKRFKKQ 2558
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ-DQQEQI------QHLKSKTNELKSEKLQIGTNLQRRQQF 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2559 AEQisqklhqtelaTQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEklkreaELLQQKSEEMQTAQkeqlrQETQ 2638
Cdd:TIGR00606 887 EEQ-----------LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE------ELISSKETSNKKAQ-----DKVN 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2639 MLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENV--R 2716
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlR 1024
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2717 QKQEELQRLEKQRQKQEKLLAE--------ENQKLREKLEQLQEEQKTALAQTRE 2763
Cdd:TIGR00606 1025 KRENELKEVEEELKQHLKEMGQmqvlqmkqEHQKLEENIDLIKRNHVLALGRQKG 1079
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1560-1873 |
5.83e-16 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 85.56 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1560 AEQQKQTIQQELSQMKLSsdaqiQAKLKLIEEVEfSRRKVEE--EIRMVRLQLEAT---ERQRAGAEDELQALRDRAEEA 1634
Cdd:pfam17380 285 SERQQQEKFEKMEQERLR-----QEKEEKAREVE-RRRKLEEaeKARQAEMDRQAAiyaEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1635 ERqkrlaqeEAERLRKQ-VKDESQKKREAEdelkhKVQAEQQAAREK-QKALEDLQKLRLQAEEAERRMKQAELEKErQV 1712
Cdd:pfam17380 359 KR-------ELERIRQEeIAMEISRMRELE-----RLQMERQQKNERvRQELEAARKVKILEEERQRKIQQQKVEME-QI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1713 QLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEhITITHLQEEAERLKKLQLEAEQ-SREEADKEVEKWRQKANEAl 1791
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ-VERLRQQEEERKRKKLELEKEKrDRKRAEEQRRKILEKELEE- 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1792 RLRLQAEEVAHKKALAQEEAEKQKEDAEREARKrsKAEESALRQKELAEQE--LEKQRKLAEGTAQQKFLA-EQELIRLK 1868
Cdd:pfam17380 504 RKQAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEMEERRriQEQMRKATEERSRLEAMErEREMMRQI 581
|
....*
gi 2069539781 1869 AEVEN 1873
Cdd:pfam17380 582 VESEK 586
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
313-424 |
6.02e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 76.57 E-value: 6.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 313 KEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED 392
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 2069539781 393 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 424
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2966-3004 |
6.04e-16 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 74.29 E-value: 6.04e-16
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 2966 LLEAQVATGGIIDPVNSHRLPVEVAYKRGYFDEEMQQIL 3004
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
313-412 |
7.31e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 76.16 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 313 KEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED 392
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 2069539781 393 VDV--PQPDEKSIITYVSSLYD 412
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1800-2184 |
8.56e-16 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 84.79 E-value: 8.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1800 VAHKKALAQEEAEKQKEDAEREaRKRSKAEESAlrqkelaeQELEKQRKLAEG-TAQQKFLAEQELIRLKAEvengeqqr 1878
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE-RLRQEKEEKA--------REVERRRKLEEAeKARQAEMDRQAAIYAEQE-------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1879 llleeelfrlknevNEAVQKRKELEeelaklraemelllqsKAKTEEESRSTSEKSKQILEAEASKLRELaEEAARLRAL 1958
Cdd:pfam17380 341 --------------RMAMERERELE----------------RIRQEERKRELERIRQEEIAMEISRMREL-ERLQMERQQ 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1959 SEEAKRQRQLAEEEATHQRAEAERILKEKLVainEASRLKAEAEialkekEAENERLRRLAEDEA--YQRRLLEEQAAQH 2036
Cdd:pfam17380 390 KNERVRQELEAARKVKILEEERQRKIQQQKV---EMEQIRAEQE------EARQREVRRLEEERAreMERVRLEEQERQQ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2037 KQDIEEKIAQLKKSSESELERQKslvddtvRQRRLVEEEIRILklnfekashgktdLELELTRIKQSAEEIQRSKEQAER 2116
Cdd:pfam17380 461 QVERLRQQEEERKRKKLELEKEK-------RDRKRAEEQRRKI-------------LEKELEERKQAMIEEERKRKLLEK 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2117 EAEElRQLALEEENHRREAEAKVKKISAAEQ--EAARQCKAALEEVERLKAKAEEARRQKELAEKESERQ 2184
Cdd:pfam17380 521 EMEE-RQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1305-2081 |
9.60e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.02 E-value: 9.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1305 ASEVNERMVRGHSERDIDLDRYRERVQQLLERWQAILAQIDLRQRELDQLGRQLRYYRESYDWLiqwireaRQRQEHLQA 1384
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL-------TQKREAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1385 vpvtnsKSVREQLLQEKKLLEECDRNREKVEECQcfakqyidaikdyeLQLVTYKAQVEPVASPAKkpKVQSASDSVIQE 1464
Cdd:TIGR00618 255 ------QLKKQQLLKQLRARIEELRAQEAVLEET--------------QERINRARKAAPLAAHIK--AVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1465 YVDLRTRYSELTTLTSQYlkfitetlrrleEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQR 1544
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKR------------AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1545 rmeeevsrrqlvaVDAEQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVR----LQLEATERQRAGA 1620
Cdd:TIGR00618 381 -------------IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKkqqeLQQRYAELCAAAI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1621 EDELQALRDRAEEAERQKRLAQEEAERLrKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAE-- 1698
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQL-QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpl 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1699 -RRMKQAELEKERqvqlaHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEAD 1777
Cdd:TIGR00618 527 tRRMQRGEQTYAQ-----LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1778 KEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQK 1857
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1858 FLAEQELIRLKAEVENGEqqrllleeelfrlkNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQi 1937
Cdd:TIGR00618 682 LQKMQSEKEQLTYWKEML--------------AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK- 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1938 leaeasKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKlvaineaSRLKAEAEIALKEKEAENERLRR 2017
Cdd:TIGR00618 747 ------ELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF-------NRLREEDTHLLKTLEAEIGQEIP 813
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2018 LAEDEayqRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKL 2081
Cdd:TIGR00618 814 SDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
179-296 |
1.21e-15 |
|
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: 75.70 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 179 QKKTFTKWVNKHLLKHwraEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRerdvirnlrlPREKGRMRFHKLQNVQIA 258
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPG----------IHSRPKTRAQKLENIQAC 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 2069539781 259 LDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 296
Cdd:cd21212 68 LQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1603-1980 |
1.30e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 84.40 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1603 IRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKrlaqeEAERLRKQvkDESQKKREAEDELKHKVQAEQQ-AAREKQ 1681
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR-----EVERRRKL--EEAEKARQAEMDRQAAIYAEQErMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1682 KALEdlqklRLQAEEAERrmkqaELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQ-LELSLQ---QEHITITHLQE 1757
Cdd:pfam17380 348 RELE-----RIRQEERKR-----ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeLEAARKvkiLEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1758 EAERLKKLQLEAEQSREEADKEVEKwrQKANEALRLRLQAEEVAHK-KALAQEEAEKQKEDAEREARKRSKAEESALRQK 1836
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1837 ELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENgeqqrllleeelfrlknevneavQKRKELEEElakLRAEMELl 1916
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-----------------------ERRREAEEE---RRKQQEM- 548
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 1917 lqskakteeesrstsEKSKQILEaeasKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEA 1980
Cdd:pfam17380 549 ---------------EERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4202-4240 |
1.41e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 73.13 E-value: 1.41e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 4202 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4240
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
180-294 |
1.46e-15 |
|
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: 75.07 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 180 KKTFTKWVNKHLlkhwRAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRErdvirnlrlpREKGRMRFHKLQNVQIAL 259
Cdd:cd00014 1 EEELLKWINEVL----GEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKI----------NKKPKSPFKKRENINLFL 66
|
90 100 110
....*....|....*....|....*....|....*..
gi 2069539781 260 DYLKHRQV-KLVNIRNDDI-ADGNPKLTLGLIWTIIL 294
Cdd:cd00014 67 NACKKLGLpELDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1508-2280 |
1.85e-15 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 84.24 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVaVDAEQQKQTIQQ---ELSQMKLSSDAQIQA 1584
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLV-QTALRQQEKIERyqaDLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1585 KLKLIEEVEFSRRKV---EEEIRMVRLQL----EATERQ--RAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDE 1655
Cdd:PRK04863 371 VEEADEQQEENEARAeaaEEEVDELKSQLadyqQALDVQqtRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1656 SQKKREAEDELKHKVQAEQQAAREKQKALEDLQKL--RLQAEEAERRMKQAELEKERQVQLA----------HEAAQKSA 1723
Cdd:PRK04863 451 EQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIagEVSRSEAWDVARELLRRLREQRHLAeqlqqlrmrlSELEQRLR 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1724 EADLQSRRLSFAEKTAQLELS-------LQQEH-ITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKA------NE 1789
Cdd:PRK04863 531 QQQRAERLLAEFCKRLGKNLDdedeleqLQEELeARLESLSESVSEARERRMALRQQLEQLQARIQRLAARApawlaaQD 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1790 AL-RLRLQ-AEEVAHKKALaqEEAEKQKEDAEREARKRSkaEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRL 1867
Cdd:PRK04863 611 ALaRLREQsGEEFEDSQDV--TEYMQQLLERERELTVER--DELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVL 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1868 KAEV-------ENGEQQRLLLEEELFRLKNEVNEAVQKRKELE---EELAKLRAEMELLLQSKAKTEEESRSTSEKSKQI 1937
Cdd:PRK04863 687 LSEIyddvsleDAPYFSALYGPARHAIVVPDLSDAAEQLAGLEdcpEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIADR 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1938 lEAEASKLRE--LAEEAARlRALSEEAKRQRQLAEEEATHQRAEAERILK-----EKLVAINEASRLKAEAEIALKEKEA 2010
Cdd:PRK04863 767 -QWRYSRFPEvpLFGRAAR-EKRIEQLRAEREELAERYATLSFDVQKLQRlhqafSRFIGSHLAVAFEADPEAELRQLNR 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2011 E-NERLRRLAEDEAYqrrllEEQAAQHKQDIEEKIAQLKKsseseLERQKSLVDDTVRQRRLVEEEIRILKLNFEKA--- 2086
Cdd:PRK04863 845 RrVELERALADHESQ-----EQQQRSQLEQAKEGLSALNR-----LLPRLNLLADETLADRVEEIREQLDEAEEAKRfvq 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2087 SHGKT--DLELELTRIKQSAEEIQRSKEQAEREAEELRQL-----ALEEENHRRE--AEAKVKKISAAEQEAARQCKAAL 2157
Cdd:PRK04863 915 QHGNAlaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAkqqafALTEVVQRRAhfSYEDAAEMLAKNSDLNEKLRQRL 994
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2158 EEVERLKAKAEEARRQK--ELAEKeSERQIQLAQEAAQKR-IVAEEKAHLAA--VQQKEQELLQTRQQEQSILDKLReeA 2232
Cdd:PRK04863 995 EQAEQERTRAREQLRQAqaQLAQY-NQVLASLKSSYDAKRqMLQELKQELQDlgVPADSGAEERARARRDELHARLS--A 1071
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 2069539781 2233 ERAKKAAEDAEFARIKAEQEAALSRqlVEEAERmKQRAEEEAQTKAKA 2280
Cdd:PRK04863 1072 NRSRRNQLEKQLTFCEAEMDNLTKK--LRKLER-DYHEMREQVVNAKA 1116
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
313-416 |
1.91e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 75.08 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 313 KEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED 392
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 2069539781 393 VDV--PQPDEKSIITYVSSLYDAMPR 416
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
316-411 |
2.51e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 74.70 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 316 LLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEqDLGVTRLLDPED-VD 394
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 2069539781 395 VPQPDEKSIITYVSSLY 411
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1943-2616 |
2.65e-15 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 83.23 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1943 SKLRELAEEAARLRALSEEAKRQRQLAEEEaTHQRAEAERILKEKLVAINEASRLKAEAEIAlkekeaENERLRRLAEDE 2022
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQE-NRKIIEAQRKAIQELQFENEKVSLKLEEEIQ------ENKDLIKENNAT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2023 AYQRRLLEEQAAQHKQdieekiaqlkKSSESELERQKSL-----VDDTVRQRRLVEEEIRILKLNFEKASHGKtdLELEL 2097
Cdd:pfam05483 154 RHLCNLLKETCARSAE----------KTKKYEYEREETRqvymdLNNNIEKMILAFEELRVQAENARLEMHFK--LKEDH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2098 TRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRR-------EAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEA 2170
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKdltflleESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2171 R---RQKELAEKESERQIQLA----------QEAAQKRIVAEEKAHLAAVQQKE------QELLQTRQQE-QSILDKLRE 2230
Cdd:pfam05483 302 KmslQRSMSTQKALEEDLQIAtkticqlteeKEAQMEELNKAKAAHSFVVTEFEattcslEELLRTEQQRlEKNEDQLKI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2231 -EAERAKKAAEDAEFARIKAEQEAALsrqlvEEAERMKQRAEEEAQTKAKAQEDAEKLR-KEAELEAARRAqaeqaalKQ 2308
Cdd:pfam05483 382 iTMELQKKSSELEEMTKFKNNKEVEL-----EELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFLLQA-------RE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2309 KQLADAE--MAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQM 2386
Cdd:pfam05483 450 KEIHDLEiqLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2387 EELIKLKTRIEEENKMLITKDKDNMQKFLAEEAE---KMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKE 2463
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2464 KMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSL 2543
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2544 AQ---------------AKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEK 2608
Cdd:pfam05483 690 LQkeidkrcqhkiaemvALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEK 769
|
....*...
gi 2069539781 2609 EKLKREAE 2616
Cdd:pfam05483 770 EKLKMEAK 777
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1586-2375 |
2.75e-15 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 83.85 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1586 LKLIEEVEFSRRKVEEE----IRMVRlQLEATERQRAGAEDELQALRDR---AEEAERQkrlaQEEAERLRKQVKdesqk 1658
Cdd:PRK04863 289 LELRRELYTSRRQLAAEqyrlVEMAR-ELAELNEAESDLEQDYQAASDHlnlVQTALRQ----QEKIERYQADLE----- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1659 krEAEDELkhkvqAEQQAAREKQkaledlqklRLQAEEAERRMKQAELEKER------QVQLAHEAAQKSAEADLQS-RR 1731
Cdd:PRK04863 359 --ELEERL-----EEQNEVVEEA---------DEQQEENEARAEAAEEEVDElksqlaDYQQALDVQQTRAIQYQQAvQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1732 LSFAEKTAQL-ELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRL-----RLQAEEVAhKKA 1805
Cdd:PRK04863 423 LERAKQLCGLpDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIagevsRSEAWDVA-REL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1806 LaqEEAEKQKEDAEREARKRskAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVEngeqqrllleEEL 1885
Cdd:PRK04863 502 L--RRLREQRHLAEQLQQLR--MRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE----------ARL 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1886 FRLKNEVNEAVQKRKELEEELAKLRAEMelllqskakteeesrstsekskQILEAEASKLRELAEEAARLRALSEEAKRQ 1965
Cdd:PRK04863 568 ESLSESVSEARERRMALRQQLEQLQARI----------------------QRLAARAPAWLAAQDALARLREQSGEEFED 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1966 RQ-LAEEEATHQRAEAERILKEKLVAINEAsRLKAEAEIALKEKEAENERLRRLAED-------EAYQRRLLEE------ 2031
Cdd:PRK04863 626 SQdVTEYMQQLLERERELTVERDELAARKQ-ALDEEIERLSQPGGSEDPRLNALAERfggvllsEIYDDVSLEDapyfsa 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2032 ---------------QAAQHKQD----------IEEKIAQLKKSSESELERQKSLVDDT----VRQRRLVEE-------- 2074
Cdd:PRK04863 705 lygparhaivvpdlsDAAEQLAGledcpedlylIEGDPDSFDDSVFSVEELEKAVVVKIadrqWRYSRFPEVplfgraar 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2075 EIRILKLNFEkashgktdLELELTRIKQSAEEI---QRSKEQAER-------------EAEELRQLALEeenhRREAEAK 2138
Cdd:PRK04863 785 EKRIEQLRAE--------REELAERYATLSFDVqklQRLHQAFSRfigshlavafeadPEAELRQLNRR----RVELERA 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2139 VKKISAAEQEAARQCKAALEEV---------------ERLKAKAEEARRQKELAEkESERQIQ-----LAQEAAQKRIVA 2198
Cdd:PRK04863 853 LADHESQEQQQRSQLEQAKEGLsalnrllprlnlladETLADRVEEIREQLDEAE-EAKRFVQqhgnaLAQLEPIVSVLQ 931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2199 EEKAHLAAVQQKEQELLQTRQQEQSILDKLRE-EAERAKKAAEDAefARIKAEqEAALSRQL---VEEAERMKQRAEEEA 2274
Cdd:PRK04863 932 SDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvVQRRAHFSYEDA--AEMLAK-NSDLNEKLrqrLEQAEQERTRAREQL 1008
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2275 qtKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQL------ADAEMAK----HKKFAEQTLR----QKAQVEQELTKV 2340
Cdd:PRK04863 1009 --RQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELqdlgvpADSGAEEraraRRDELHARLSanrsRRNQLEKQLTFC 1086
|
890 900 910
....*....|....*....|....*....|....*
gi 2069539781 2341 KLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQV 2375
Cdd:PRK04863 1087 EAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAV 1121
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1508-2468 |
2.96e-15 |
|
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: 83.85 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAkaqaekeaLELQRRMEEEVSRRQLVAVDAEqqkqtiqqelsqmkLSSD--AQIQAK 1585
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRL--------VEMARELEELSARESDLEQDYQ--------------AASDhlNLVQTA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1586 LKLIEEVEFSRRKVEEeirmVRLQLEATERQRAGAEDELqalrdraEEAERQKRLAQEEAERLRKQVKDESQkkreAEDE 1665
Cdd:COG3096 343 LRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLADYQQ----ALDV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1666 LKHKVQAEQQAAREKQKALEDLQKLRLQAEEAErrmkqaelekerqvqlAHEAAQKSAEADLQSRRLSFAEKtaqleLSL 1745
Cdd:COG3096 408 QQTRAIQYQQAVQALEKARALCGLPDLTPENAE----------------DYLAAFRAKEQQATEEVLELEQK-----LSV 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1746 QQEHititHLQ-EEAERLKKlQLEAEQSREEADkevekwrQKANEALR----LRLQAEEVAhkkALAQEEAEkqkedAER 1820
Cdd:COG3096 467 ADAA----RRQfEKAYELVC-KIAGEVERSQAW-------QTARELLRryrsQQALAQRLQ---QLRAQLAE-----LEQ 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1821 EARKRSKAEESAlrqkelaeQELEKQrklaegtAQQKFLAEQELIRLKAEVEngeqqrllleEELFRLKNEVNEAVQKRK 1900
Cdd:COG3096 527 RLRQQQNAERLL--------EEFCQR-------IGQQLDAAEELEELLAELE----------AQLEELEEQAAEAVEQRS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1901 ELEEELAKLRAEMelllqskakteeesrstsekskQILEAEASKLRELAEEAARLRALSEEAKRQRQlAEEEATHQRAEA 1980
Cdd:COG3096 582 ELRQQLEQLRARI----------------------KELAARAPAWLAAQDALERLREQSGEALADSQ-EVTAAMQQLLER 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1981 ER---ILKEKLVAINEasRLKAEAEIALKEKEAENERLRRLAE-------DEAYQRRLLEEQA--------AQHK---QD 2039
Cdd:COG3096 639 EReatVERDELAARKQ--ALESQIERLSQPGGAEDPRLLALAErlggvllSEIYDDVTLEDAPyfsalygpARHAivvPD 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2040 IEEKIAQLKKSSESE-----LERQKSLVDDTVRQrrlVEEEirilklnfEKASHGKT-DLELELTRIKQ------SAEEI 2107
Cdd:COG3096 717 LSAVKEQLAGLEDCPedlylIEGDPDSFDDSVFD---AEEL--------EDAVVVKLsDRQWRYSRFPEvplfgrAAREK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2108 QRSKEQAERE--AEELRQLALEEENHRR-------------------EAEAKVKKISAAEQEAARQCKAALEEVERLKAK 2166
Cdd:COG3096 786 RLEELRAERDelAEQYAKASFDVQKLQRlhqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQ 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2167 AEEARRQKELAEKESERQIQLAQEAAQKRIVAEEkAHLAAVQQKEQELLQ---TRQQEQSILDKLREEAErakkaaedaE 2243
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQANLLADETLADRLEELR-EELDAAQEAQAFIQQhgkALAQLEPLVAVLQSDPE---------Q 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2244 FARIKAEQEAALSRQlveeaERMKQRAEEEAQTKAKA-----QEDAEKLRKEAELEAArraqaeqaaLKQkQLADAEMAK 2318
Cdd:COG3096 936 FEQLQADYLQAKEQQ-----RRLKQQIFALSEVVQRRphfsyEDAVGLLGENSDLNEK---------LRA-RLEQAEEAR 1000
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2319 HKkfAEQTLRQKAQVEQELTKVKLQLEETDHQKS-ILEEEQQRLKD-------EVTEAMKQKV-QVEEELFKVKVQMEEL 2389
Cdd:COG3096 1001 RE--AREQLRQAQAQYSQYNQVLASLKSSRDAKQqTLQELEQELEElgvqadaEAEERARIRRdELHEELSQNRSRRSQL 1078
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2390 IKLKTRIEEEnkmlitkdKDNMQKFLAEEAEKMKQVAEEAA----------RLSVEAQEAARL--RELAEQDLAQQRSLA 2457
Cdd:COG3096 1079 EKQLTRCEAE--------MDSLQKRLRKAERDYKQEREQVVqakagwcavlRLARDNDVERRLhrRELAYLSADELRSMS 1150
|
1050
....*....|.
gi 2069539781 2458 EKILKEKMQAV 2468
Cdd:COG3096 1151 DKALGALRLAV 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1474-2179 |
3.50e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.19 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1474 ELTTLTSQYLKFITETLRRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSR- 1552
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKl 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1553 -RQLVAVDAEQQKQTIQQELSQMKLSSDAQIQAKLKL-IEEVEFSRRKVEEEIRMVRLQLEATERQRagaeDELQALRDR 1630
Cdd:TIGR02169 335 lAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAeLEEVDKEFAETRDELKDYREKLEKLKREI----NELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1631 AEEAERQKRlaqEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRlqAEEAERRMKQAELEKER 1710
Cdd:TIGR02169 411 LQEELQRLS---EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE--QELYDLKEEYDRVEKEL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1711 QvQLAHEAAQKSAEAD-LQSRRLSFAEKTAQLELSLQQEHITITHLQEEAE------------RLKKLQLEAEQSREEAD 1777
Cdd:TIGR02169 486 S-KLQRELAEAEAQARaSEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGEryataievaagnRLNNVVVEDDAVAKEAI 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1778 KEVEkwRQKANEA------------LRLRLQAEEVAHKKALAQEEAEKQKEDAER------------EARKRSKAEesaL 1833
Cdd:TIGR02169 565 ELLK--RRKAGRAtflplnkmrderRDLSILSEDGVIGFAVDLVEFDPKYEPAFKyvfgdtlvvediEAARRLMGK---Y 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1834 RQKELAEQELEKQRKLAEGTAQQKFLA------EQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELA 1907
Cdd:TIGR02169 640 RMVTLEGELFEKSGAMTGGSRAPRGGIlfsrsePAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1908 KLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEE-AKRQRQLAEEEATHQRAEAERILKE 1986
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDlHKLEEALNDLEARLSHSRIPEIQAE 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1987 KLVAINEASRLKA---EAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKsSESELERQKSLVD 2063
Cdd:TIGR02169 800 LSKLEEEVSRIEArlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-LEEELEELEAALR 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2064 DTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHrREAEAKVKKIs 2143
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDV- 956
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 2069539781 2144 aaeQEAARQCKAALEEVERLKAKA-----EEARRQKELAEK 2179
Cdd:TIGR02169 957 ---QAELQRVEEEIRALEPVNMLAiqeyeEVLKRLDELKEK 994
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3625-3663 |
4.08e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 4.08e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 3625 LLEAQIATGGIIDPVHSHRLPVEVAYKRGYFDEQMNRTL 3663
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1508-2002 |
4.45e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 82.51 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQ-AEKEALELQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQMKLSSDaQIQAKL 1586
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEElEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1587 KLIEEVEFSRRKVEEEIRMVRLQLEATERQRAgaEDELQALRDRAEEAERqkrlAQEEAERLRKQVKDESQKKREAEDEL 1666
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEE----LQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1667 KhKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADL-QSRRLSFAEKTAQLELSL 1745
Cdd:COG4717 230 E-QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLfLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1746 QQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKR 1825
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1826 SKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENgeqqrllleeelfrLKNEVNEAVQKRKELEEE 1905
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE--------------LEEELEELEEELEELREE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1906 LAKLRAEMELLlqskakteEESRSTSEKSKQILEAEAsKLRELAEEAARLRALSEEAKRQRQLAEEEATHQ-RAEAERIL 1984
Cdd:COG4717 455 LAELEAELEQL--------EEDGELAELLQELEELKA-ELRELAEEWAALKLALELLEEAREEYREERLPPvLERASEYF 525
|
490 500
....*....|....*....|....
gi 2069539781 1985 KE------KLVAINEASRLKAEAE 2002
Cdd:COG4717 526 SRltdgryRLIRIDEDLSLKVDTE 549
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2148-2760 |
4.81e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.66 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2148 EAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAA-VQQKEQELLQTRQQE-QSIL 2225
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAELEElRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2226 DKLREEAERAKKAAEDAEFARIKAEQE-AALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQA 2304
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2305 ALKQ-KQLADAEMAKHKKFAEQ---TLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKvqvEEELF 2380
Cdd:COG4913 385 LRAEaAALLEALEEELEALEEAlaeAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD---EAELP 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2381 KVKvqmeELIKLKTRiEEE-----NKMLitkdkdNMQKF-LAEEAEKMKQVAE----EAARLSVEAQEAARLRELAEQDL 2450
Cdd:COG4913 462 FVG----ELIEVRPE-EERwrgaiERVL------GGFALtLLVPPEHYAAALRwvnrLHLRGRLVYERVRTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2451 AQQRSLAEKiLKEKMQAVQEAtrLKAEaevLQKQKDLAQ-EQAKKLQEDKEQM----QLRLAEEAegFQKTLEAERQRQL 2525
Cdd:COG4913 531 LDPDSLAGK-LDFKPHPFRAW--LEAE---LGRRFDYVCvDSPEELRRHPRAItragQVKGNGTR--HEKDDRRRIRSRY 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2526 EITANA----ERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQ------------Q 2589
Cdd:COG4913 603 VLGFDNraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaeleaelerldA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2590 SDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQT--AQKEQLRQETQMLQQTFRSEKDVLLQ---KERFVEEEKAK 2664
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKelEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDA 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2665 LEKLFQEEvnkaqgLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKL-LAEENQKL 2743
Cdd:COG4913 763 VERELREN------LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDgLPEYEERF 836
|
650
....*....|....*..
gi 2069539781 2744 REKLEQLQEEQKTALAQ 2760
Cdd:COG4913 837 KELLNENSIEFVADLLS 853
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1975-2366 |
6.61e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 82.09 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1975 HQRAEAERILKEKLVAInEASRLKAEAEialkEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQdiEEKIAqlkkssese 2054
Cdd:pfam17380 280 HQKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMA--------- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2055 LERQKSLvdDTVRQrrlvEEEIRilklnfekashgktdlELELTRIKQSAEEIQRSKEQAEREAEELRQlaleEENHRRE 2134
Cdd:pfam17380 344 MEREREL--ERIRQ----EERKR----------------ELERIRQEEIAMEISRMRELERLQMERQQK----NERVRQE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2135 AEAkVKKISAAEQEAARQCKAALEEVERLKAKAEEARrQKELAEKESERQIQLaqeaaqKRIVAEEkahlaavQQKEQEL 2214
Cdd:pfam17380 398 LEA-ARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR-QREVRRLEEERAREM------ERVRLEE-------QERQQQV 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2215 LQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKlRKEAEle 2294
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER-RREAE-- 539
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2295 aarraqaeqaalkQKQLADAEMAKHKKFAEQTLRqkaqVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVT 2366
Cdd:pfam17380 540 -------------EERRKQQEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1686-2279 |
7.32e-15 |
|
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: 81.71 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1686 DLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEadlqsrrlsfaektaqlelslqqehititHLQEEAERLKKL 1765
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKR-----------------------------QLDRESDRNQEL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1766 QLEAEQsREEADKEVEKWRQKANEALRLRLQAEEVAHKKalaQEEAEKQKEDAeREARKRSKAEESALRQK-ELAEQELE 1844
Cdd:pfam05557 54 QKRIRL-LEKREAEAEEALREQAELNRLKKKYLEALNKK---LNEKESQLADA-REVISCLKNELSELRRQiQRAELELQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1845 KQRKLAEGTAQQKFLAEQELIRLKAEVENgeqqrllleeeLFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAktE 1924
Cdd:pfam05557 129 STNSELEELQERLDLLKAKASEAEQLRQN-----------LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKS--E 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1925 EESRSTSEKSKQILEAEASKLRE-------LAEEAARLRA-LSEEAKRQRQLAEEEATHQRAEAEriLKE-KLVAINEAS 1995
Cdd:pfam05557 196 LARIPELEKELERLREHNKHLNEnienkllLKEEVEDLKRkLEREEKYREEAATLELEKEKLEQE--LQSwVKLAQDTGL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1996 RLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQhkQDIEEKIAQLKKSSESE---LERQKSLVDDTVRQRRLV 2072
Cdd:pfam05557 274 NLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRHKALVRRLQRRVLLL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2073 EEEIRILK---------LNFEKASHGKTDLELELTRIKQ----SAEEIQRSKEQAEREAEELRQLALEEEnhrREAEAKV 2139
Cdd:pfam05557 352 TKERDGYRailesydkeLTMSNYSPQLLERIEEAEDMTQkmqaHNEEMEAQLSVAEEELGGYKQQAQTLE---RELQALR 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2140 KKISAAEQEAARQCKAAL-EEVERLKAKAEEARRQKELAEKESERQiQLAQEAAQKRIvaeekahlAAVQQKEQELLQTR 2218
Cdd:pfam05557 429 QQESLADPSYSKEEVDSLrRKLETLELERQRLREQKNELEMELERR-CLQGDYDPKKT--------KVLHLSMNPAAEAY 499
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2219 QQEQSILDKLREEAERAK---KAAEDA--------EFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAK 2279
Cdd:pfam05557 500 QQRKNQLEKLQAEIERLKrllKKLEDDleqvlrlpETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQ 571
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1747-2503 |
7.45e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 82.09 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1747 QEHITIThLQEEAERLKKLQLEAEQSREEADKEVEKWRQ-------KANEALRLRLQAEEVAHKKALAQEEAEKQKEDAE 1819
Cdd:pfam15921 73 KEHIERV-LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlqtKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1820 REARKRSKAEESALRQKELAEQELEKQRKLAEGTAQqkflaEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKR 1899
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ-----EIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKIL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1900 KELEEELAKLRAEM--------ELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEE 1971
Cdd:pfam15921 227 RELDTEISYLKGRIfpvedqleALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1972 EATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQL---- 2047
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladl 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2048 -KKSSESELERQK-----------SLVDDTVRqRRLVEEEIRILKLN-FEKA--SHGKTDLELELTRIK---QSAEEIQR 2109
Cdd:pfam15921 387 hKREKELSLEKEQnkrlwdrdtgnSITIDHLR-RELDDRNMEVQRLEaLLKAmkSECQGQMERQMAAIQgknESLEKVSS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2110 SKEQAEREAEELRQLaLEEENHRR----EAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESE--R 2183
Cdd:pfam15921 466 LTAQLESTKEMLRKV-VEELTAKKmtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDhlR 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2184 QIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQS----ILDKLREEAERAKKAAEDAEFARIKAEQEAALsrql 2259
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTagamQVEKAQLEKEINDRRLELQEFKILKDKKDAKI---- 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2260 veeaERMKQRAEEEAQTKAK-AQEDAEKLRKEAELEAARRAQAEQAALKQKQLADaeMAKHKKFAEQTLRQKAQvEQELT 2338
Cdd:pfam15921 621 ----RELEARVSDLELEKVKlVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNS--LSEDYEVLKRNFRNKSE-EMETT 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2339 KVKLQLEETDHQkSILEEEQQRLKD---EVTEAMKQKVQVEEELFKVKVQMEELiKLKTRIEEENKMLITKDKdnmqKFL 2415
Cdd:pfam15921 694 TNKLKMQLKSAQ-SELEQTRNTLKSmegSDGHAMKVAMGMQKQITAKRGQIDAL-QSKIQFLEEAMTNANKEK----HFL 767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2416 AEEAEKMKQvaeeaaRLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKdlaQEQAK-K 2494
Cdd:pfam15921 768 KEEKNKLSQ------ELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQE---QESVRlK 838
|
810
....*....|.
gi 2069539781 2495 LQE--DKEQMQ 2503
Cdd:pfam15921 839 LQHtlDVKELQ 849
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2211-2773 |
7.65e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.27 E-value: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2211 EQELLQTRQQEQsILDKLREEAERAKKAAEDAEFARI--------KAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQE 2282
Cdd:COG4913 241 HEALEDAREQIE-LLEPIRELAERYAAARERLAELEYlraalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2283 DAEKLRKEAELEAARRAQAEQAALKQkQLADAE------MAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEE 2356
Cdd:COG4913 320 ALREELDELEAQIRGNGGDRLEQLER-EIERLEreleerERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2357 EQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELiklktrieEENKMLITKDKDNMQKFLAEEAekmkQVAEEAARLSVE- 2435
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASL--------ERRKSNIPARLLALRDALAEAL----GLDEAELPFVGEl 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2436 ---AQEAARLRELAEQDLAQQR-SL--AEKILKEKMQAVqEATRLKAEAEVLQKQKDLAQEQAKKLQEDkeqmqlRLAEE 2509
Cdd:COG4913 467 ievRPEEERWRGAIERVLGGFAlTLlvPPEHYAAALRWV-NRLHLRGRLVYERVRTGLPDPERPRLDPD------SLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2510 AE----GFQKTLEAERQRQLEIT--ANAERLKVQVTELSLA-QAKAEEEakRFKKQAEQISQKLHQTELATQEKmtlVQT 2582
Cdd:COG4913 540 LDfkphPFRAWLEAELGRRFDYVcvDSPEELRRHPRAITRAgQVKGNGT--RHEKDDRRRIRSRYVLGFDNRAK---LAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2583 LEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSE------EMQTAQKE--QLRQETQMLqqtfRSEKDVLLQK 2654
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREiaELEAELERL----DASSDDLAAL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2655 ERFVEEEKAKLEKLfQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAE----------AEENVRQKQEELQR 2724
Cdd:COG4913 691 EEQLEELEAELEEL-EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralleerfAAALGDAVERELRE 769
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2725 -LEKQRQKQEKLLAEENQKLREKLEQLQEEQK-------TALAQTREIM-----IQTDDLPQ 2773
Cdd:COG4913 770 nLEERIDALRARLNRAEEELERAMRAFNREWPaetadldADLESLPEYLalldrLEEDGLPE 831
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2307-2775 |
1.03e-14 |
|
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: 81.22 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2307 KQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQM 2386
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2387 EE----LIKLKTRIEEENKML------------ITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDL 2450
Cdd:TIGR04523 197 LKlellLSNLKKKIQKNKSLEsqiselkkqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2451 AQqrslAEKILKEKMQAVQEatrLKAEAEVLQKQKDlaQEQAKKLQEDKEQMQlrlaEEAEGFQKTLEAERQRQLEITAN 2530
Cdd:TIGR04523 277 EQ----NNKKIKELEKQLNQ---LKSEISDLNNQKE--QDWNKELKSELKNQE----KKLEEIQNQISQNNKIISQLNEQ 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2531 AERLKVQVTELSLAQAKAEEEAKRFKKQAEQI----SQKLHQTELATQEKMTLVQTLEIQRQQSdsdaEKLRKAIADLEQ 2606
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenQSYKQEIKNLESQINDLESKIQNQEKLN----QQKDEQIKKLQQ 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2607 EKEKLKREAELLQQKSEEMQ------TAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLK 2680
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNseikdlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2681 aEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQE-----KLLAEENQKLREKLEQLQEEQK 2755
Cdd:TIGR04523 500 -KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfelkkENLEKEIDEKNKEIEELKQTQK 578
|
490 500
....*....|....*....|
gi 2069539781 2756 TALAQTREIMIQTDDLPQEV 2775
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEK 598
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2458-2755 |
1.04e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 81.32 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2458 EKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLR-----LAEEAEGFQKTLEAERQRQLE------ 2526
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRqekeeKAREVERRRKLEEAEKARQAEmdrqaa 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2527 ITANAERLKVQvTELSLAQAKAEEEakrfKKQAEQISQKlhqtELATQ-EKMTLVQTLEIQRQQSD----SDAEKLRKAI 2601
Cdd:pfam17380 335 IYAEQERMAME-RERELERIRQEER----KRELERIRQE----EIAMEiSRMRELERLQMERQQKNervrQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2602 ADLEQEKEKLKREAELLQQKSEEMQTAQKEQLR---------------QETQMLQQTFRSEKDVLLQKERFVEEEKAKLE 2666
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeeraremervrlEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2667 KLFQEEVNKAQGLKAEQERQQKQMEQEKK----------QLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQK--QEK 2734
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEERKrkllekemeeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKatEER 565
|
330 340
....*....|....*....|.
gi 2069539781 2735 LLAEENQKLREKLEQLQEEQK 2755
Cdd:pfam17380 566 SRLEAMEREREMMRQIVESEK 586
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2171-2760 |
1.09e-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: 81.55 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2171 RRQKELAEKESERQIQLAQEAAQKRIVAeekAHLAAVQQKEQELLQtrqqeqsiLDKLREEAERAKKAAEDAEFARIKAE 2250
Cdd:TIGR00618 95 RCTRSHRKTEQPEQLYLEQKKGRGRILA---AKKSETEEVIHDLLK--------LDYKTFTRVVLLPQGEFAQFLKAKSK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2251 QEAALSRQLvEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEaarraqaeqaalkqkqladaemakhKKFAEQTLRQK 2330
Cdd:TIGR00618 164 EKKELLMNL-FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLL-------------------------TLCTPCMPDTY 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2331 AQVEQELTKVKLQLEETDHQKSILEEEQQRLKdevtEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLitkDKDN 2410
Cdd:TIGR00618 218 HERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI---NRAR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2411 MQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELA---EQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDL 2487
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2488 AQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEA-KRFKKQAEQISQKl 2566
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqQRYAELCAAAITC- 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2567 hQTELATQEKMTLVQTleiqRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEmQTAQKEQLRQETQMLQQTFRS 2646
Cdd:TIGR00618 450 -TAQCEKLEKIHLQES----AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDNP 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2647 EKDV-----LLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEArkkqaeaeENVRQKQEE 2721
Cdd:TIGR00618 524 GPLTrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI--------PNLQNITVR 595
|
570 580 590
....*....|....*....|....*....|....*....
gi 2069539781 2722 LQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQ 2760
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL 634
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
313-414 |
1.30e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 73.20 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 313 KEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED 392
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 2069539781 393 -VDVPQPDEKSIITYVSSLYDAM 414
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2257-2775 |
1.73e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2257 RQLVEEAERMKQRAEE-EAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLAdaEMAKHKKFAEQTLRQKAQVEQ 2335
Cdd:PRK03918 175 KRRIERLEKFIKRTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK--ELEELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2336 ELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQK------VQVEEELFKVKVQMEELIKLKTRIEEENKMLITKDKD 2409
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKekaeeyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2410 NMQKflAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKIlkekmqAVQEATRLKAEAEVLQKQKDLAQ 2489
Cdd:PRK03918 333 LEEK--EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL------TGLTPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2490 EQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQ-----RQLEITANAERLKVQVTELSLAQ---AKAEEEAKRFKKQAEQ 2561
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEkelKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2562 ISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEK--------------LKREAELLQQKSE---E 2624
Cdd:PRK03918 485 LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKliklkgeikslkkeLEKLEELKKKLAElekK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2625 MQTAQKEQLRQETQMLQQTFRSEKDVllqkerfvEEEKAKLEKlFQEEVNKAQGLKAEQERQQKQMEQEKkqltTVLEEA 2704
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEEL--------EERLKELEP-FYNEYLELKDAEKELEREEKELKKLE----EELDKA 631
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2705 RKKQAEAEENVRQKQEELQRLEKQRQKQE-KLLAEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLPQEV 2775
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1919-2754 |
3.16e-14 |
|
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: 80.27 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1919 SKAKTEEESRSTSEKSKQILEAEASKLRELAeeaaRLRALSEEAKRQRQLAE-EEATHQRAEAERILKEKLVAIneasrl 1997
Cdd:pfam12128 136 TNLLNTREYRSIIQNDRTLLGRERVELRSLA----RQFALCDSESPLRHIDKiAKAMHSKEGKFRDVKSMIVAI------ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1998 kaeaeIALKEKEAENERLRRlaedEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLvddTVRQRRLVEEEIR 2077
Cdd:pfam12128 206 -----LEDDGVVPPKSRLNR----QQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRL---SHLHFGYKSDETL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2078 ILKLNFEKAShGKTDLELEL----TRIKQSAEEI-QRSKEQAEREAEELRQLALEEENHRREAEAKVKKiSAAEQEAARQ 2152
Cdd:pfam12128 274 IASRQEERQE-TSAELNQLLrtldDQWKEKRDELnGELSAADAAVAKDRSELEALEDQHGAFLDADIET-AAADQEQLPS 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2153 CKAALEEVE-RLKAKAEEAR-------RQKELAEKESERQI------QLAQEAAQKRIVAEEKAHLaavQQKEQELlqtR 2218
Cdd:pfam12128 352 WQSELENLEeRLKALTGKHQdvtakynRRRSKIKEQNNRDIagikdkLAKIREARDRQLAVAEDDL---QALESEL---R 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2219 QQEQSILDKLREEAERAKKAAEDAEF--ARIKAEQEAALS-RQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAElEA 2295
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGELKLrlNQATATPELLLQlENFDERIERAREEQEAANAEVERLQSELRQARKRRD-QA 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2296 ARRAQAEQAALKQKQLADAEmakhkkfAEQTLRQKAQVEQELTKVKLQLEEtDHQKSILEEEQQRLKDEVTEAMKQKVQV 2375
Cdd:pfam12128 505 SEALRQASRRLEERQSALDE-------LELQLFPQAGTLLHFLRKEAPDWE-QSIGKVISPELLHRTDLDPEVWDGSVGG 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2376 EEELFKVKVQMEEL-IKLKTRIEEEnkmlITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQR 2454
Cdd:pfam12128 577 ELNLYGVKLDLKRIdVPEWAASEEE----LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2455 SLAEKILKEKMQAVQEATRLKAEAevlqkqKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKT-LEAERQRQLEITANAER 2533
Cdd:pfam12128 653 LDLRRLFDEKQSEKDKKNKALAER------KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQkREARTEKQAYWQVVEGA 726
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2534 LKVQVTELSLAQAKAEEEAKRFKKQAEqisqKLHQTELAT------------QEKMTLVQTLEiqrqqsdsDAEKLRKAI 2601
Cdd:pfam12128 727 LDAQLALLKAAIAARRSGAKAELKALE----TWYKRDLASlgvdpdviaklkREIRTLERKIE--------RIAVRRQEV 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2602 ADLEQ--------EKEKLKREAELLQQKSEEMQtAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLeKLFQEEV 2673
Cdd:pfam12128 795 LRYFDwyqetwlqRRPRLATQLSNIERAISELQ-QQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGL-RCEMSKL 872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2674 NKaqgLKAEQERQQKQMEQEKKqlTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEklLAEENQKLREKLEQLQEE 2753
Cdd:pfam12128 873 AT---LKEDANSEQAQGSIGER--LAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSG--LAETWESLREEDHYQNDK 945
|
.
gi 2069539781 2754 Q 2754
Cdd:pfam12128 946 G 946
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
311-408 |
3.24e-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: 71.26 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGyqgMRCDNFTTSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnVENLEQAFSVAEQDLGVTR 386
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 2069539781 387 LLDPEDVDVPQPDEKSIITYVS 408
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1509-2057 |
3.49e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1509 QRLAEVEAQLEKQRQLAEAHARAKAQAEKEALE-LQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQMKL----SSDAQIQ 1583
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEaELEELRAELARLEAELERLEARLDALREELDELEAqirgNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1584 AKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQkrlAQEEAERLRKQVKDESQKKREAE 1663
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1664 DELkHKVQAEQQAAREKQKAL-EDLQKLRLQAEEA----ERRMK-QAELekeRQVQLAHEAAQKSAEADLQSRRLS---- 1733
Cdd:COG4913 419 REL-RELEAEIASLERRKSNIpARLLALRDALAEAlgldEAELPfVGEL---IEVRPEEERWRGAIERVLGGFALTllvp 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1734 ---FAEKTA-----QLELSLQQEHITITHLQEEAERLK------KLQLEAEQSREEADKEV------------------- 1780
Cdd:COG4913 495 pehYAAALRwvnrlHLRGRLVYERVRTGLPDPERPRLDpdslagKLDFKPHPFRAWLEAELgrrfdyvcvdspeelrrhp 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1781 ----------------EKWRQKANEAlRLRLQAEEVAHKKALAQEEAEKQKEDAE-REARKRSKAEESALRQKELAEQEL 1843
Cdd:COG4913 575 raitragqvkgngtrhEKDDRRRIRS-RYVLGFDNRAKLAALEAELAELEEELAEaEERLEALEAELDALQERREALQRL 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1844 EKQRKLAEGTAQqkflAEQELIRLKAE---VENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSK 1920
Cdd:COG4913 654 AEYSWDEIDVAS----AEREIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1921 AKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKE-KLVAINEASRLKA 1999
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDA 809
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2000 EAEiALKEKEAeneRLRRLAEDE--AYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELER 2057
Cdd:COG4913 810 DLE-SLPEYLA---LLDRLEEDGlpEYEERFKELLNENSIEFVADLLSKLRRAIREIKER 865
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1995-2760 |
5.47e-14 |
|
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: 79.50 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1995 SRLKAEAEIALKEKEAENERLRRLAEDEAYQRRL--LEEQAAQHKQDIEEKIAQLK----------KSSESELERQKSlv 2062
Cdd:pfam12128 252 TLESAELRLSHLHFGYKSDETLIASRQEERQETSaeLNQLLRTLDDQWKEKRDELNgelsaadaavAKDRSELEALED-- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2063 ddtvRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQrskeQAEREAEELRQLALEEENhrREAEAKVKKI 2142
Cdd:pfam12128 330 ----QHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQ----DVTAKYNRRRSKIKEQNN--RDIAGIKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2143 SAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAqeaaqkriVAEEKAHLAAVQQKEQELLQTRQQeQ 2222
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSR--------LGELKLRLNQATATPELLLQLENF-D 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2223 SILDKLREEAERAKKAAEDA--EFARIKAEQEAAlSRQLVEEAERMKQRAEEEAQTK----AKAQEDAEKLRKEAELEAA 2296
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLqsELRQARKRRDQA-SEALRQASRRLEERQSALDELElqlfPQAGTLLHFLRKEAPDWEQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2297 RRAQAEQAALKQKQLADAEMakhkkfaeqtlrQKAQVEQELT--KVKLQLEETDHQKSILEEEQQRLK-DEVTEAMKQKV 2373
Cdd:pfam12128 550 SIGKVISPELLHRTDLDPEV------------WDGSVGGELNlyGVKLDLKRIDVPEWAASEEELRERlDKAEEALQSAR 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2374 QVEEELfkvkvqmeeliklktrieEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQeaarlrelaeqdlAQQ 2453
Cdd:pfam12128 618 EKQAAA------------------EEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQ-------------SEK 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2454 RSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAqeqakkLQEDKEQMqlrlaeeaegfqktLEAERQRQLEITANAER 2533
Cdd:pfam12128 667 DKKNKALAERKDSANERLNSLEAQLKQLDKKHQAW------LEEQKEQK--------------REARTEKQAYWQVVEGA 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2534 LKVQVTELSLAQAKAEEEAKRFKKQAEqisqKLHQTELATQekmtlvqtleiqrqqsDSDAEKlrkaIADLEQEKEKLKR 2613
Cdd:pfam12128 727 LDAQLALLKAAIAARRSGAKAELKALE----TWYKRDLASL----------------GVDPDV----IAKLKREIRTLER 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2614 EAEllqqkseemqtaQKEQLRQEtqmlqqtfrsekdvLLQKERFveeekakleklfqeevnkaqglkaeqerQQKQMEQE 2693
Cdd:pfam12128 783 KIE------------RIAVRRQE--------------VLRYFDW----------------------------YQETWLQR 808
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2694 KKQLTTVLEEARKKQAEAEENVRQKQEE----LQRLEKQRQKQEKLLAEENQKLR------EKLEQLQEEQKTALAQ 2760
Cdd:pfam12128 809 RPRLATQLSNIERAISELQQQLARLIADtklrRAKLEMERKASEKQQVRLSENLRglrcemSKLATLKEDANSEQAQ 885
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
172-295 |
5.60e-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: 71.16 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 172 ADERDrvqKKTFTKWVNKHLLKHwraeaqrHVNDLYEDLRDGhnlISLLEVLsgDTLprERDVIRNLRLPREKGRMRFHK 251
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKI--QPGCVNWKKVNKPKPLNKFKK 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2069539781 252 LQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 295
Cdd:cd21219 64 VENCNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1804-2275 |
5.70e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 78.66 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1804 KALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENgeqqrLLLEE 1883
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-----LREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1884 ELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAK 1963
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1964 RQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAE----------DEAYQRRLLEEQA 2033
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallallglgGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2034 AQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELtriKQSAEEIQRSKEQ 2113
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL---LDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2114 AEREAEELRQLALEEENHRREAEAKVKKIsaaeqEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQ 2193
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDE-----EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2194 KRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAE-DAEFARIKAEQEAALSRQLVEEA-ERMKQRAE 2271
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQElEELKAELRELAEEWAALKLALELlEEAREEYR 510
|
....
gi 2069539781 2272 EEAQ 2275
Cdd:COG4717 511 EERL 514
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1508-1819 |
6.10e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 79.01 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEA--LELQRRMeeevsrrqlvAVDAEQQKQTIQQELSQMKLSSDAQIQAK 1585
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiYAEQERM----------AMERERELERIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1586 lklieeVEFSRRKVEEEIRMVRLQLEATERQragaedELQALRD-RAEEAERQKRLAQE--EAERLRKQVKDESQKK-RE 1661
Cdd:pfam17380 372 ------MEISRMRELERLQMERQQKNERVRQ------ELEAARKvKILEEERQRKIQQQkvEMEQIRAEQEEARQREvRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1662 AEDELKHKVQAEQQAAREKQKALEdlqklRLQAEEAERRMKQAELEKE-RQVQLAHEAAQKSAEADLQSRRLSFAEKTAQ 1740
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVE-----RLRQQEEERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1741 LELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEAlRLRLQAEEVAHKKALAQEEAEKQKEDAE 1819
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1942-2759 |
6.59e-14 |
|
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: 79.23 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1942 ASKLRELAEEAARLRAlsEEAKRQRQLAEEEATHQR--------AEAERILKEKLVAINEASRLKAEAeIALKEK-EAEN 2012
Cdd:COG3096 277 ANERRELSERALELRR--ELFGARRQLAEEQYRLVEmareleelSARESDLEQDYQAASDHLNLVQTA-LRQQEKiERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2013 ERLRRLAEDEAYQRRLLEEqAAQHKQDIEEKiaqlKKSSESELERQKSLVDDtvRQRRLVEEEIRILKLN-----FEKAS 2087
Cdd:COG3096 354 EDLEELTERLEEQEEVVEE-AAEQLAEAEAR----LEAAEEEVDSLKSQLAD--YQQALDVQQTRAIQYQqavqaLEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2088 HGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQ-LALEEENHRR--EAEAKVKKI------SAAEQEA------ARQ 2152
Cdd:COG3096 427 ALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQkLSVADAARRQfeKAYELVCKIageverSQAWQTArellrrYRS 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2153 CKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELL------------QTRQQ 2220
Cdd:COG3096 507 QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELeeqaaeaveqrsELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2221 EQSILDKLREEAERA---KKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAEleaar 2297
Cdd:COG3096 587 LEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIE----- 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2298 raqaeqaalKQKQLADAEMAKHKKFAEQ--------------------------TLRQkAQVEQELTKVKLQLEETDHQK 2351
Cdd:COG3096 662 ---------RLSQPGGAEDPRLLALAERlggvllseiyddvtledapyfsalygPARH-AIVVPDLSAVKEQLAGLEDCP 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2352 S---ILEEEQQRLKDEVTEAmkqkvqvEEELFKVKVQMEELIKLKTRIEEEnKMLITKDKDNMQKFLAEEAEkmkQVAEE 2428
Cdd:COG3096 732 EdlyLIEGDPDSFDDSVFDA-------EELEDAVVVKLSDRQWRYSRFPEV-PLFGRAAREKRLEELRAERD---ELAEQ 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2429 AARLSVEAQEAARLRELAEQDLAQQRSLA-----EKILKEKMQAVQEATRLkaeaevLQKQKDLAQEQAKKLQEDKEQMQ 2503
Cdd:COG3096 801 YAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELERE------LAQHRAQEQQLRQQLDQLKEQLQ 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2504 L--RLAEEAEGFQKTLEAERQRQLEitanAERLKVQVTELSLAQ-----AKAEEEAKRFKKQAEQISQKLHQTELATQEK 2576
Cdd:COG3096 875 LlnKLLPQANLLADETLADRLEELR----EELDAAQEAQAFIQQhgkalAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQ 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2577 MTLVQTLE-----IQRQQ--SDSDAEKLRKAIADL-EQEKEKLkREAELLQQKSEEMQTAQKEQLRQETQMLQQtFRSEK 2648
Cdd:COG3096 951 RRLKQQIFalsevVQRRPhfSYEDAVGLLGENSDLnEKLRARL-EQAEEARREAREQLRQAQAQYSQYNQVLAS-LKSSR 1028
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2649 DVllqkerfveeeKAKLEKLFQEEVnKAQGLKAEQErqqkqMEqekkqlttvlEEARKKQAEAEENVRQKQEELQRLEKQ 2728
Cdd:COG3096 1029 DA-----------KQQTLQELEQEL-EELGVQADAE-----AE----------ERARIRRDELHEELSQNRSRRSQLEKQ 1081
|
890 900 910
....*....|....*....|....*....|.
gi 2069539781 2729 RQKQEKLLAEENQKLREKLEQLQEEQKTALA 2759
Cdd:COG3096 1082 LTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1253-1930 |
6.79e-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: 78.96 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1253 LIRKYEEQLKDVQAVPSDLKALEATKAELKRLRGQVEghqplfNTLEMDLAKASEVNERMVRGHSERDIDLDR------- 1325
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE------KRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigelea 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1326 -----------YRERVQQLLERWQAILAQIDLRQRELDQLGRQLRYYRESYDWLIQWIREARQRQEHLQAVPVTNSKSVR 1394
Cdd:TIGR02169 302 eiaslersiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1395 EQLLQEKKLLEECDRNREKVEECQCFAKQYIDAIKDYELQLVTYKAQVEpvASPAKKPKVQSASDSVIQEYVDLRTRYSE 1474
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA--GIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1475 LTTLTSQYlkfitetlrrleeeekaaEKLKEEERQRLAEVEAQL-EKQRQLAEAHARAKAQAEKEALELQRRMEEEVSR- 1552
Cdd:TIGR02169 460 LAADLSKY------------------EQELYDLKEEYDRVEKELsKLQRELAEAEAQARASEERVRGGRAVEEVLKASIq 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1553 ------RQLVAVDAEQQ----------------------KQTIQQeLSQMKLSS-------------------------- 1578
Cdd:TIGR02169 522 gvhgtvAQLGSVGERYAtaievaagnrlnnvvveddavaKEAIEL-LKRRKAGRatflplnkmrderrdlsilsedgvig 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1579 --------DAQIQAKLK-------LIEEVEFSRRKVEEeIRMVRLQLEATER----------QRAGA------EDELQAL 1627
Cdd:TIGR02169 601 favdlvefDPKYEPAFKyvfgdtlVVEDIEAARRLMGK-YRMVTLEGELFEKsgamtggsraPRGGIlfsrsePAELQRL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1628 RDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHK------VQAEQQAAREKQKALEDLQKLRLQAEEAERRM 1701
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1702 kQAELEKERQVQLAHEAAQKSAEADLQSR--RLSFAEKTAQLElSLQQEHITITHLQEEAER-LKKLQLE---AEQSREE 1775
Cdd:TIGR02169 760 -LKELEARIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELS-KLEEEVSRIEARLREIEQkLNRLTLEkeyLEKEIQE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1776 ADKEVEKW------RQKANEALRLRLQA-EEVAHKKALAQEEAEKQKEDAEREaRKRSKAEESALRQK-ELAEQELEKQR 1847
Cdd:TIGR02169 838 LQEQRIDLkeqiksIEKEIENLNGKKEElEEELEELEAALRDLESRLGDLKKE-RDELEAQLRELERKiEELEAQIEKKR 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1848 KLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKN------------EVN--------EAVQKRKELEEELA 1907
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAElqrveeeiralePVNmlaiqeyeEVLKRLDELKEKRA 996
|
810 820
....*....|....*....|...
gi 2069539781 1908 KLRAEMELLLQSKAKTEEESRST 1930
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKKREV 1019
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
181-299 |
8.82e-14 |
|
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: 70.73 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 181 KTFTKWVNKhllkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSgdtlPRERDVIRNLRLPREKGRMrFHKLQNVQIALD 260
Cdd:cd21298 9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKIK----PGVVDWSRVNKPFKKLGAN-MKKIENCNYAVE 76
|
90 100 110
....*....|....*....|....*....|....*....
gi 2069539781 261 YLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 299
Cdd:cd21298 77 LGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1820-2509 |
9.71e-14 |
|
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: 78.22 E-value: 9.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1820 REARKRSK---AEESALRQKElaeQELEKQRKLAEGT--AQQKFLAEQELIRLKAEvengeqqrllleeelfrlknevnE 1894
Cdd:pfam05483 85 KEAEKIKKwkvSIEAELKQKE---NKLQENRKIIEAQrkAIQELQFENEKVSLKLE-----------------------E 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1895 AVQKRKELEEELAKLRAEMELLLQSKAKTEEESRS---TSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEE 1971
Cdd:pfam05483 139 EIQENKDLIKENNATRHLCNLLKETCARSAEKTKKyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1972 EATHQRAEAERILKEKlvaINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEE----QAAQHKQDIEEK---- 2043
Cdd:pfam05483 219 EDHEKIQHLEEEYKKE---INDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEktklQDENLKELIEKKdhlt 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2044 --IAQLKKSSESELERQKSLVDDTVRQRRLV-----EEEIRILKLNFEKASHGKTDLELELTRIkqSAEEIQRSKEQA-E 2115
Cdd:pfam05483 296 keLEDIKMSLQRSMSTQKALEEDLQIATKTIcqlteEKEAQMEELNKAKAAHSFVVTEFEATTC--SLEELLRTEQQRlE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2116 REAEELRQLALEEENHRREAEA-------------KVKKISAAEQEAARQCKAALEEVERLKAKAEE-----ARRQKELA 2177
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEmtkfknnkeveleELKKILAEDEKLLDEKKQFEKIAEELKGKEQElifllQAREKEIH 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2178 EKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELlqtrqqeQSILDKLREEAERAKKAAEDAEFaRIKAEQEAALSR 2257
Cdd:pfam05483 454 DLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL-------TAHCDKLLLENKELTQEASDMTL-ELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2258 QlvEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKfaeqtlrQKAQVEQEL 2337
Cdd:pfam05483 526 K--KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK-------QMKILENKC 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2338 TKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELiklKTRIEE--ENKMLITKDKDNMQKFL 2415
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA---KQKFEEiiDNYQKEIEDKKISEEKL 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2416 AEEAEKMKQVAEEAARLSVE-----AQEAARLRELAEQDLAQQRSLAEK------ILKEKMQAVQ--------EATRLKA 2476
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKEidkrcQHKIAEMVALMEKHKHQYDKIIEErdselgLYKNKEQEQSsakaaleiELSNIKA 753
|
730 740 750
....*....|....*....|....*....|...
gi 2069539781 2477 EAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEE 2509
Cdd:pfam05483 754 ELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2152-2749 |
9.91e-14 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 78.30 E-value: 9.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2152 QCKAALEEVERLKAKAEEARRQkelaekeSERQIQLAQEAAQKrIVAEEKAHLAAVQQKEQELLQTRQQeqsilDKLREE 2231
Cdd:PRK10246 192 QHKSARTELEKLQAQASGVALL-------TPEQVQSLTASLQV-LTDEEKQLLTAQQQQQQSLNWLTRL-----DELQQE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2232 AERAKKAAEDAEFARIKAE-QEAALS-----RQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAeqaa 2305
Cdd:PRK10246 259 ASRRQQALQQALAAEEKAQpQLAALSlaqpaRQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHA---- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2306 LKQKQLADAEM-------AKHKKFA---------EQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLK-DEVTEA 2368
Cdd:PRK10246 335 AKQSAELQAQQqslntwlAEHDRFRqwnnelagwRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTaDEVAAA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2369 MKQKVQ---VEEELFKVKVQMEELIKLKTRIEEenkmlitkdkdNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLREL 2445
Cdd:PRK10246 415 LAQHAEqrpLRQRLVALHGQIVPQQKRLAQLQV-----------AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTI 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2446 AEQ-----DLAQQRSL------------AEKILKEKMQAV-------------QEATRLKAEAEVLQKQKDLAQEQakkL 2495
Cdd:PRK10246 484 CEQearikDLEAQRAQlqagqpcplcgsTSHPAVEAYQALepgvnqsrldaleKEVKKLGEEGAALRGQLDALTKQ---L 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2496 QEDKEQMQlRLAEEaegfQKTLEAERQrqlEITANaerlkvqvteLSLAQAKAEE------EAKRFKKQAEQISQKLH-Q 2568
Cdd:PRK10246 561 QRDESEAQ-SLRQE----EQALTQQWQ---AVCAS----------LNITLQPQDDiqpwldAQEEHERQLRLLSQRHElQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2569 TELA--TQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKL---KREAELLQQKSEEMQTAQkEQLRQETQMLQ-- 2641
Cdd:PRK10246 623 GQIAahNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQ-NRIQQLTPLLEtl 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2642 ----QTFRSEKDVLLQKERFVEEEKAKLEKLFQeevnkAQGLKAEQERQQKQmeQEKKQLTTVLEEARKKQAEA------ 2711
Cdd:PRK10246 702 pqsdDLPHSEETVALDNWRQVHEQCLSLHSQLQ-----TLQQQDVLEAQRLQ--KAQAQFDTALQASVFDDQQAflaall 774
|
650 660 670
....*....|....*....|....*....|....*....
gi 2069539781 2712 -EENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQ 2749
Cdd:PRK10246 775 dEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQH 813
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
179-296 |
1.03e-13 |
|
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: 70.02 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 179 QKKTFTKWVNKHLLKHwraEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPrerDVIRNlrlPREKGRMRfhklQNVQIA 258
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLP---GIDWN---PTTDAERK----ENVEKV 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 2069539781 259 LDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 296
Cdd:cd21213 68 LQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1509-2186 |
1.10e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1509 QRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEevsrrqlvavdaeqqkqtiqqelsqmklssdaqIQAKLKL 1588
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEE---------------------------------IEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1589 IEEVEFSRRKVEEEIRmvrlqleATERQRAGAEDELQALRDRAEEAERQKRLAqEEAERLRKQVKDESQKKREAEDELKH 1668
Cdd:PRK03918 247 LESLEGSKRKLEEKIR-------ELEERIEELKKEIEELEEKVKELKELKEKA-EEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1669 KvqaeQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKER---QVQLAHEAAQKSAEADLQSRRLSfaektaqlelsl 1745
Cdd:PRK03918 319 L----EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleeRHELYEEAKAKKEELERLKKRLT------------ 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1746 qqehitithlQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEalrlrLQAEEVAHKKALAQEEAEKQK---------E 1816
Cdd:PRK03918 383 ----------GLTPEKLEKELEELEKAKEEIEEEISKITARIGE-----LKKEIKELKKAIEELKKAKGKcpvcgreltE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1817 DAEREARKRSKAEESALRqKELAEQELEKQRKLAEGTAQQKFLA-EQELIRLKaevengeqqrllleeelfrlknevnEA 1895
Cdd:PRK03918 448 EHRKELLEEYTAELKRIE-KELKEIEEKERKLRKELRELEKVLKkESELIKLK-------------------------EL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1896 VQKRKELEEELAKLRAEmELllqskAKTEEESRSTSEKSKQiLEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEath 1975
Cdd:PRK03918 502 AEQLKELEEKLKKYNLE-EL-----EKKAEEYEKLKEKLIK-LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE--- 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1976 qRAEAERILKEKlvaineasrlkaeaeiALKEKEAENERLRRLaedEAYQRRLLEEQAAQHKQDIEEKiaqLKKSSESEL 2055
Cdd:PRK03918 572 -LAELLKELEEL----------------GFESVEELEERLKEL---EPFYNEYLELKDAEKELEREEK---ELKKLEEEL 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2056 ERQKSLVDDTVRQRRLVEEEIRILKLNF-----EKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRqlalEEEN 2130
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK----EELE 704
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2131 HRREAEAKVKKIsaaeqeaarqcKAALEEVERLKakaEEARRQKELAEKESERQIQ 2186
Cdd:PRK03918 705 EREKAKKELEKL-----------EKALERVEELR---EKVKKYKALLKERALSKVG 746
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3549-3587 |
1.14e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.74 E-value: 1.14e-13
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 3549 LLEAQAATGFMVDPVRNQRLPVHEAVKAGFVGPELHEKL 3587
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3294-3332 |
1.15e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 67.74 E-value: 1.15e-13
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 3294 LLDAQLATGGIIDPANSHRLPLDVACKRGYFSEEMNKAL 3332
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1174-1729 |
1.15e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1174 DQQQIHQELEGIKKNLGKVSAKTEQVLAQPEQASSAptlHSELDITLQKMDQVYSLSSIYLEKLKT--IHLVIRSTQGAE 1251
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLE---LEELELELEEAQAEEYELLAELARLEQdiARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1252 DLIRKYEEQLKDVQAVPSDLKALEATKAELKRLRGQVEghqplfnTLEMDLAKASEVNERMVRGHSERDIDLDRYRERVQ 1331
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1332 QLLERWQAILAQI-DLRQRELDQLGRQLRYYREsydwliqwIREARQRQEHLQAVPVTNSKSVREQLLQEKKLLEECDRN 1410
Cdd:COG1196 390 EALRAAAELAAQLeELEEAEEALLERLERLEEE--------LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1411 REKVEECQCFAKQYIDAIKDYELQLVTYKAQVEPVASPAKKPKVQSASDSVIQEYVDLRTRYSELTTLTSQYLKFITETL 1490
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1491 RRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAVDAEQQKQTIQQE 1570
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1571 LsQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELqaLRDRAEEAERQKRLAQEEAERLRK 1650
Cdd:COG1196 622 L-LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL--LEAEAELEELAERLAEEELELEEA 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1651 QVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAH-EAAQKSAEADLQS 1729
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEElERELERLEREIEA 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2323-2752 |
1.36e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2323 AEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFK--------------VKVQMEE 2388
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaeaglddadaeaVEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2389 LIKLKTRIEE--ENKMLITKDKDNMQKFLAEEAEKMKQVA----EEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILK 2462
Cdd:PRK02224 319 LEDRDEELRDrlEECRVAAQAHNEEAESLREDADDLEERAeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2463 EKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAE-----------------EAEGFQKTLEAERQRQL 2525
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHVETIEEDRERVE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2526 EITANAERLKVQVTELS--LAQA----KAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRK 2599
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEerLERAedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2600 AIADLEQEKEKLKREAELLQQKSEEMqTAQKEQLRqetqmlqqTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGL 2679
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAEL-KERIESLE--------RIRTLLAAIADAEDEIERLREKREALAELNDERRERL 629
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2680 KAEQERQQkqmEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLA------EENQKLREKLEQLQE 2752
Cdd:PRK02224 630 AEKRERKR---ELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGavenelEELEELRERREALEN 705
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1569-2276 |
1.36e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 77.84 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1569 QELSQMKLSSDAQIQAKLKLIEEvefSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQeeaeRL 1648
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQE---NRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN----LL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1649 RKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEadlq 1728
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN---- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1729 srrlsfaEKTAQLELSLQQehitithLQEEAERLKKLQLEAEQSREEADKEVEKwrqkanealrLRLQAE---EVAHKKA 1805
Cdd:pfam05483 237 -------DKEKQVSLLLIQ-------ITEKENKMKDLTFLLEESRDKANQLEEK----------TKLQDEnlkELIEKKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1806 LAQEEAEKQKEDAEREARKRSKAEE----------SALRQKELAEQELEKQR---KLAEGTAQQKFLAEQELIRLKAE-V 1871
Cdd:pfam05483 293 HLTKELEDIKMSLQRSMSTQKALEEdlqiatkticQLTEEKEAQMEELNKAKaahSFVVTEFEATTCSLEELLRTEQQrL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1872 ENGEQQRLLLEEELFRLKNEVNEAVQ--KRKELE-EELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLREL 1948
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKfkNNKEVElEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEI 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1949 AEEAARLRALSeeAKRQRQLAEEEATHQRAEAERILKEKLVAinEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRL 2028
Cdd:pfam05483 453 HDLEIQLTAIK--TSEEHYLKEVEDLKTELEKEKLKNIELTA--HCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2029 lEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQ 2108
Cdd:pfam05483 529 -EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2109 RSKEQAEREAEELRQLALEEENHRREAEAKVKKI----SAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQ 2184
Cdd:pfam05483 608 KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLelelASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2185 IQLAQEAAQK--RIVAEEKAHLAAVQQKEQELLQTRQQEQSiLDKLREEAERAKKAAEDAEFARIKAEQeAALSRQL--- 2259
Cdd:pfam05483 688 VKLQKEIDKRcqHKIAEMVALMEKHKHQYDKIIEERDSELG-LYKNKEQEQSSAKAALEIELSNIKAEL-LSLKKQLeie 765
|
730
....*....|....*..
gi 2069539781 2260 VEEAERMKQRAEEEAQT 2276
Cdd:pfam05483 766 KEEKEKLKMEAKENTAI 782
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
311-411 |
1.38e-13 |
|
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: 70.10 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQdLGVTRLLDP 390
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 2069539781 391 ED-VDVPQPDEKSIITYVSSLY 411
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1623-2046 |
1.41e-13 |
|
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: 77.75 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1623 ELQALRDRAEEAERQKrlAQEEAERLRKQVKDESQKKREAEDELKHKV-QAEQQAAREKQKALEDL-----QKLRLQAEE 1696
Cdd:NF033838 103 ELNVLKEKSEAELTSK--TKKELDAAFEQFKKDTLEPGKKVAEATKKVeEAEKKAKDQKEEDRRNYptntyKTLELEIAE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1697 AERRMKQAELE--KERQVQLAHEAAQKSAEADLQSRrlsfaektaqlelslqqehitithlQEEAERLKKLQLEAEQSRE 1774
Cdd:NF033838 181 SDVEVKKAELElvKEEAKEPRDEEKIKQAKAKVESK-------------------------KAEATRLEKIKTDREKAEE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1775 EADKEVEKWRQKANEALRLRLQAEEVAH--KKALAQEEA--EKQKEDAerearkrsKAEESALRQKELAEQELEKQRKLA 1850
Cdd:NF033838 236 EAKRRADAKLKEAVEKNVATSEQDKPKRraKRGVLGEPAtpDKKENDA--------KSSDSSVGEETLPSPSLKPEKKVA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1851 EgtAQQKFLAEQEliRLKAEVEngeqqrllleeelfrlKNEVNEAVQKRKELEEELAKL-----RAEMELLLQSKAKTEE 1925
Cdd:NF033838 308 E--AEKKVEEAKK--KAKDQKE----------------EDRRNYPTNTYKTLELEIAESdvkvkEAELELVKEEAKEPRN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1926 EsrstsEKSKQILEAEASKLrelaEEAARLralsEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIAL 2005
Cdd:NF033838 368 E-----EKIKQAKAKVESKK----AEATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPK 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2069539781 2006 KEKEAENERLRRLAEDEA---YQRRLLEE--QAAQHKQDIEEKIAQ 2046
Cdd:NF033838 435 PEKPAEQPKAEKPADQQAeedYARRSEEEynRLTQQQPPKTEKPAQ 480
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2324-2648 |
1.75e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 77.47 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2324 EQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQ---------RL---KDEVTEAMKQKVQVEEelfKVKVQMEELIK 2391
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQekfekmeqeRLrqeKEEKAREVERRRKLEE---AEKARQAEMDR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2392 LKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAArlsveAQEAARLRELAEQDLAQQRSlaEKILKEKMQAVQEA 2471
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEI-----AMEISRMRELERLQMERQQK--NERVRQELEAARKV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2472 TRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEgfQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEE 2551
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2552 aKRFKKQAEQISQKLHQTELATQEKMTLVQtlEIQRQQSDSDAEKLRKAIADLEQ-----EKEKLKREAELLQQKSEEMQ 2626
Cdd:pfam17380 483 -KRDRKRAEEQRRKILEKELEERKQAMIEE--ERKRKLLEKEMEERQKAIYEEERrreaeEERRKQQEMEERRRIQEQMR 559
|
330 340
....*....|....*....|....*..
gi 2069539781 2627 TAQKEQLR-----QETQMLQQTFRSEK 2648
Cdd:pfam17380 560 KATEERSRleameREREMMRQIVESEK 586
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2329-2764 |
1.84e-13 |
|
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: 77.37 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2329 QKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKD-------EVTEAMKQKVQVEEELFKVKVQMEELIKLKTriEEENK 2401
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKqlsekqkELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2402 ML------ITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLK 2475
Cdd:TIGR04523 311 ELkselknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2476 AEAEVLQKQKDLAQEQAKKLQEDKEQMQlrlaEEAEGFQKtlEAERQRQLEITANAE--RLKVQVTELSLAQakaeEEAK 2553
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELLEK--EIERLKETIIKNNSEikDLTNQDSVKELII----KNLD 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2554 RFKKQAEQisqklhQTELATQEKMTLVQTLEIQRQQSD---SDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMqTAQK 2630
Cdd:TIGR04523 461 NTRESLET------QLKVLSRSINKIKQNLEQKQKELKskeKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL-ESEK 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2631 EQLRQETQMLQQTFRSEKDVLlqkerfveeEKAKLEKLFQEEVNKAQGLKAEQ---ERQQKQMEQEKKQLTTVLEEARKK 2707
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFEL---------KKENLEKEIDEKNKEIEELKQTQkslKKKQEEKQELIDQKEKEKKDLIKE 604
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2708 QAEAEENVRQKQEELQRLEKQRQK---QEKLLAEENQKLREKLEQLQEEQKTALAQTREI 2764
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKlssIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2541-2764 |
1.98e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 75.57 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2541 LSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQ 2620
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2621 KSEEMQTAQKEQLRQETQMLQQTFRSEK----DVLLQKERFveEEKAKLEKLFQEevnkaqgLKAEQERQQKQMEQEKKQ 2696
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDF--LDAVRRLQYLKY-------LAPARREQAEELRADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2697 LTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREI 2764
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1747-2389 |
1.99e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1747 QEHI-TITHLQEEAERLKKlQLEA-EQSREEADKEVEKWRQKA-NEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREAR 1823
Cdd:COG4913 231 VEHFdDLERAHEALEDARE-QIELlEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1824 KRSKAEEsALRQKELAEQELEKQRKLAEGtaqqkflaeQELIRLKAEVENgeqqrllleeelfrLKNEVNEAVQKRKELE 1903
Cdd:COG4913 310 ELERLEA-RLDALREELDELEAQIRGNGG---------DRLEQLEREIER--------------LERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1904 EELAKLRAEMELllqskakTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERI 1983
Cdd:COG4913 366 ALLAALGLPLPA-------SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1984 ---LKEKLVAINEASRLKAEA--------EIALKEKEAEN--ER-LRRLAedeayqRRLLEEQaaQHKQDIEEKIAQLKK 2049
Cdd:COG4913 439 parLLALRDALAEALGLDEAElpfvgeliEVRPEEERWRGaiERvLGGFA------LTLLVPP--EHYAAALRWVNRLHL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2050 SSESELERQKSLVDDTVRQR----RLVEeeirilKLNFEKASHGKTdLELELTRIK-----QSAEEIQRSKEQAERE--- 2117
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRldpdSLAG------KLDFKPHPFRAW-LEAELGRRFdyvcvDSPEELRRHPRAITRAgqv 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2118 --AEELRQLALEEENHRR-----EAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEK---ESERQIQL 2187
Cdd:COG4913 584 kgNGTRHEKDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeYSWDEIDV 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2188 AQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMK 2267
Cdd:COG4913 664 ASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2268 QRAEEEAQTKAKAQEDAEKLRKE--AELEAARRAQAEQAALKQKQLADAeMAKHKK---FAEQTLRQKAQVEQELTKVKL 2342
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERElrENLEERIDALRARLNRAEEELERA-MRAFNRewpAETADLDADLESLPEYLALLD 822
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2343 QLEETDhqksiLEEEQQRLKDEVTEAMKQKV-----QVEEELFKVKVQMEEL 2389
Cdd:COG4913 823 RLEEDG-----LPEYEERFKELLNENSIEFVadllsKLRRAIREIKERIDPL 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1675-2243 |
2.85e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1675 QAAREKQKALEDLQKLRLQAEEAERRMKQaeLEKERQVQLAHEAAQKSAEAdLQSRRLSFAEKTAQLELSLQQEHitITH 1754
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL--LEPIRELAERYAAARERLAE-LEYLRAALRLWFAQRRLELLEAE--LEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1755 LQEEAERLKKLQLEAEQSREEADKEVekwrqkanEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREaRKRSKAEEsALR 1834
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREEL--------DELEAQIRGNGGDRLEQLEREIERLERELEERE-RRRARLEA-LLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1835 QKELA----EQELEKQRKLAEGTAQQkflAEQELIRLkaevengeqqrllleeelfrlKNEVNEAVQKRKELEEELAKLR 1910
Cdd:COG4913 370 ALGLPlpasAEEFAALRAEAAALLEA---LEEELEAL---------------------EEALAEAEAALRDLRRELRELE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1911 AEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAE---------------EAA----RLRALSEEAKRQRQLAEE 1971
Cdd:COG4913 426 AEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGElievrpeeerwrgaiERVlggfALTLLVPPEHYAAALRWV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1972 EATHQRAE------AERILKEKLVAINEASRLkaeAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKiA 2045
Cdd:COG4913 506 NRLHLRGRlvyervRTGLPDPERPRLDPDSLA---GKLDFKPHPFRAWLEAELGRRFDYVCVDSPEELRRHPRAITRA-G 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2046 QLKKSSE-------SELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAERE- 2117
Cdd:COG4913 582 QVKGNGTrhekddrRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEi 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2118 -----AEELRQLaleeENHRREAEAKVKKISAAEQEAArQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAA 2192
Cdd:COG4913 662 dvasaEREIAEL----EAELERLDASSDDLAALEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2193 QKRIVAEEKAHLAAVQQKEQELLQtRQQEQSILDKLREEAERAKKAAEDAE 2243
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALG-DAVERELRENLEERIDALRARLNRAE 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1590-2236 |
3.10e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1590 EEVEFSRRKVE--EEIRMVRLQLEATERQRAGAEDELQALRdrAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELK 1667
Cdd:COG4913 242 EALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 hkvqAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEkerqvqlaheaaqksaeaDLQSRRLSFAEKTAQLELSlqq 1747
Cdd:COG4913 320 ----ALREELDELEAQIRGNGGDRLEQLEREIERLERELE------------------ERERRRARLEALLAALGLP--- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1748 ehitithLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEvahkkalaqEEAEKQKEDAEREARKRSK 1827
Cdd:COG4913 375 -------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR---------ELRELEAEIASLERRKSNI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1828 AEESALRQKELAEQelekqrkLAEGTAQQKFLAeqELIRLKAE--------------------VENGEQqrllleeelfr 1887
Cdd:COG4913 439 PARLLALRDALAEA-------LGLDEAELPFVG--ELIEVRPEeerwrgaiervlggfaltllVPPEHY----------- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1888 lkNEVNEAVQKRKeLEEELAKLRAEMELLLQSKAKTEEesRSTSEKskqiLEAEASKLR-----ELAEEAARLRALSEEA 1962
Cdd:COG4913 499 --AAALRWVNRLH-LRGRLVYERVRTGLPDPERPRLDP--DSLAGK----LDFKPHPFRawleaELGRRFDYVCVDSPEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1963 -----------------------KRQRQLAEE-----EATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENER 2014
Cdd:COG4913 570 lrrhpraitragqvkgngtrhekDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2015 LRRLAEDEAYQRRLleEQAAQHKQDIEEKIAQLKKSSeSELERQKSLVDDTVRQRRLVEEEIrilklnfEKASHGKTDLE 2094
Cdd:COG4913 650 LQRLAEYSWDEIDV--ASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEEL-------DELKGEIGRLE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2095 LELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVE-RLKAKAEEARRQ 2173
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEeELERAMRAFNRE 799
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2174 KELAEKESERQIQLAQEAAQ--KRIVAEekaHLAAVQQKEQELLqTRQQEQSILD---KLREEAERAK 2236
Cdd:COG4913 800 WPAETADLDADLESLPEYLAllDRLEED---GLPEYEERFKELL-NENSIEFVADllsKLRRAIREIK 863
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2083-2493 |
3.52e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 76.32 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2083 FEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVK-KISAAEQEAARQCKaaleeve 2161
Cdd:pfam17380 233 YEKMERRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQeKFEKMEQERLRQEK------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2162 rlKAKAEEARRQKELAEKESERQIQLAQEAAqkrIVAEekaHLAAVQQKEQELLQTRQQEQsildklREEAERAKKAAED 2241
Cdd:pfam17380 306 --EEKAREVERRRKLEEAEKARQAEMDRQAA---IYAE---QERMAMERERELERIRQEER------KRELERIRQEEIA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2242 AEFARIKAEQEAALSRQlvEEAERMKQraEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLAdaemakhkk 2321
Cdd:pfam17380 372 MEISRMRELERLQMERQ--QKNERVRQ--ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR--------- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2322 faeqtlRQKAQVEQELTKVKLQLEETDHQKSILEeeqqrlkdevteamkqkvQVEEELFKVKVQMEELIKLKTRIEEENK 2401
Cdd:pfam17380 439 ------RLEEERAREMERVRLEEQERQQQVERLR------------------QQEEERKRKKLELEKEKRDRKRAEEQRR 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2402 MLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQ-AVQEATRLKA---E 2477
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRkATEERSRLEAmerE 574
|
410
....*....|....*.
gi 2069539781 2478 AEVLQKQKDLAQEQAK 2493
Cdd:pfam17380 575 REMMRQIVESEKARAE 590
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2108-2334 |
4.38e-13 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 74.46 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2108 QRSKEQAEREAEELRQLALEEENHRREAEAKvkKISAAEQeaarqckaaleeverlKAKAEEARRQKELAEKESERQIQL 2187
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEKE--RLAAQEQ----------------KKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2188 AQEAAQKRIVAEEKAHLAAVQQKEQELlqtrqqeqsildKLREEAERAKKAAEDAefariKAEQEAALSRQLVEEAermK 2267
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAEA------------KKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEA---K 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2268 QRAEEEAQTKAKAqEDAEKLRKEAELEAARRaqaeqaalKQKQLADAEMAKHKKFAEQTLRQKAQVE 2334
Cdd:PRK09510 201 KKAEAEAKKKAAA-EAKKKAAAEAKAAAAKA--------AAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1760-2742 |
6.29e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 75.85 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1760 ERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRlqaeevahkkalAQEEAEKQKEDAEREARKRSKAEESAL--RQKE 1837
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR------------DQITSKEAQLESSREIVKSYENELDPLknRLKE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1838 LAE-----QELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFrlKNEVNEAVQKRKELEEELAKLRAE 1912
Cdd:TIGR00606 257 IEHnlskiMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH--QRTVREKERELVDCQRELEKLNKE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1913 MELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARL-----------------------RALSEEAKRQRQLA 1969
Cdd:TIGR00606 335 RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgfergpfserqiknfhtlviERQEDEAKTAAQLC 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1970 EEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKK 2049
Cdd:TIGR00606 415 ADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2050 SSESELERQKSLVD---DTVRQRRLVEEEIrilklnfEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLAL 2126
Cdd:TIGR00606 495 LTETLKKEVKSLQNekaDLDRKLRKLDQEM-------EQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2127 EEENhrreaeakvKKISAAEQEAARQCKAALEEverlkakaEEARRQKELAEKESErqiqlaqeaaQKRIVAEEKAHLAA 2206
Cdd:TIGR00606 568 YFPN---------KKQLEDWLHSKSKEINQTRD--------RLAKLNKELASLEQN----------KNHINNELESKEEQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2207 VQQKEQELLQ--TRQQEQSILDKLREEAERAKKaaeDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDA 2284
Cdd:TIGR00606 621 LSSYEDKLFDvcGSQDEESDLERLKEEIEKSSK---QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFI 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2285 EKLRKEAELEAArraqaeqaalKQKQLaDAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDE 2364
Cdd:TIGR00606 698 SDLQSKLRLAPD----------KLKST-ESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2365 VTEAMKQKVQVEEElfkvkvqmeeliklktriEEENKMLITkDKDNMQKFLAEEAEKMKQVAEEAARLsveaqeaarlre 2444
Cdd:TIGR00606 767 IEEQETLLGTIMPE------------------EESAKVCLT-DVTIMERFQMELKDVERKIAQQAAKL------------ 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2445 laeQDLAQQRSLAEkILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQ 2524
Cdd:TIGR00606 816 ---QGSDLDRTVQQ-VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2525 LEITanaeRLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADl 2604
Cdd:TIGR00606 892 ELST----EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQD- 966
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2605 EQEKEKLKREAEL--LQQKSEEMQTaQKEQLRQETQMLQQTFRSEKdvllQKERFVEEEKAKL---EKLFQEEVNKAQGL 2679
Cdd:TIGR00606 967 GKDDYLKQKETELntVNAQLEECEK-HQEKINEDMRLMRQDIDTQK----IQERWLQDNLTLRkreNELKEVEEELKQHL 1041
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2680 KAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQK 2742
Cdd:TIGR00606 1042 KEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYR 1104
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
311-411 |
9.72e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 67.36 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQdLGVTRLLDP 390
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 2069539781 391 ED-VDVPQPDEKSIITYVSSLY 411
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3959-3997 |
9.93e-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: 9.93e-13
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 3959 LLDAQLATGGIIDPHLGFHLPLETAYQRGYFNRETYERL 3997
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2068-2774 |
1.23e-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: 74.99 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2068 QRRLVEEEIRILKLNFEKASHG--KTDLELELtrikQSAEEIQRSKEQAEREAE--ELRQLALEEENHR-REAEAKVKKI 2142
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSarESDLEQDY----QAASDHLNLVQTALRQQEkiERYQEDLEELTERlEEQEEVVEEA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2143 SAAEQEAARQCKAALEEVERLKAKAeeARRQKELAEKESeRQIQLaQEAAQKRIVAEEKAHLA--AVQQKEQELLQTRQQ 2220
Cdd:COG3096 374 AEQLAEAEARLEAAEEEVDSLKSQL--ADYQQALDVQQT-RAIQY-QQAVQALEKARALCGLPdlTPENAEDYLAAFRAK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2221 EQSILDKLREEAERAkkaaEDAEFARIKAEQEAALSRQLVEEAERmkqraeEEAQTKAKAQedaekLRKEAELEAARRAQ 2300
Cdd:COG3096 450 EQQATEEVLELEQKL----SVADAARRQFEKAYELVCKIAGEVER------SQAWQTAREL-----LRRYRSQQALAQRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2301 AEQaalkQKQLADAEmakhkkfaeQTLRQKAQVEQELTKVKLQL-------EETDHQKSILEEEQQRLKDEVTEAMKQKV 2373
Cdd:COG3096 515 QQL----RAQLAELE---------QRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2374 QVEEELFKVKVQMEEL-------IKLKTRIE--EENKMLITKDKDNMQKFLAEEAEKMKQVAEE-----AARLSVEAQ-- 2437
Cdd:COG3096 582 ELRQQLEQLRARIKELaarapawLAAQDALErlREQSGEALADSQEVTAAMQQLLEREREATVErdelaARKQALESQie 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2438 --------EAARLRELAEQdlaqqrsLAEKILKEKMQ--AVQEATRLKA------EAEVLQkqkDL--AQEQAKKLQEDK 2499
Cdd:COG3096 662 rlsqpggaEDPRLLALAER-------LGGVLLSEIYDdvTLEDAPYFSAlygparHAIVVP---DLsaVKEQLAGLEDCP 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2500 EQMQLRLAEEAEGFQKTLEAERQRQLEITANAERlKVQVTELS----LAQAKAEEEAKRFKKQAEQISQKLHQTELATQE 2575
Cdd:COG3096 732 EDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDR-QWRYSRFPevplFGRAAREKRLEELRAERDELAEQYAKASFDVQK 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2576 KMTLVQTLE--IQRQQSDSDAEKLRKAIADLEQEKEKLkrEAELLQQKSEEMQTAQK-EQLRQETQMLQ----------- 2641
Cdd:COG3096 811 LQRLHQAFSqfVGGHLAVAFAPDPEAELAALRQRRSEL--ERELAQHRAQEQQLRQQlDQLKEQLQLLNkllpqanllad 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2642 -------QTFRSEKDVLLQKERFVEEEKAKLEKLfQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVleearKKQAEAEEN 2714
Cdd:COG3096 889 etladrlEELREELDAAQEAQAFIQQHGKALAQL-EPLVAVLQSDPEQFEQLQADYLQAKEQQRRL-----KQQIFALSE 962
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2715 VRQKQEELQRLEKQRQKQEKllAEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLPQE 2774
Cdd:COG3096 963 VVQRRPHFSYEDAVGLLGEN--SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQV 1020
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2243-2956 |
1.54e-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: 74.62 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2243 EFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKF 2322
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2323 AEQTLRQ------KAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRI 2396
Cdd:pfam02463 225 YLLYLDYlklneeRIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2397 EEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKA 2476
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2477 EAEVLQKQKDLAQEQA-KKLQEDKEQMQLR------LAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAE 2549
Cdd:pfam02463 385 RLSSAAKLKEEELELKsEEEKEAQLLLELArqledlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2550 EEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAI---------------ADLEQEKEKLKRE 2614
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIkdgvggriisahgrlGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2615 AELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEK 2694
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2695 KQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLPQE 2774
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2775 VVAPSQVPQMKAVPNGRDMIDGISQNGEAELAFDGIRQKVSAKKLAEAGILSRESMEKLAKGKATVQELSQRDDIRRYLR 2854
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2855 GTSSIAGLLLKPSNEKMSIYSAMKQQLLSPGTALILLEAQAASGFVIDPVRNRTLSVSEAVKEGVVGPELHNKLLSAERA 2934
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
730 740
....*....|....*....|..
gi 2069539781 2935 VTGYKDPYTGEKISLFQAMTKD 2956
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKD 886
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
176-292 |
1.55e-12 |
|
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: 66.79 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 176 DRVQKKTFTKWVNKHLLKhwRAEAQrhVNDLYEDLRDGHNLISLLEVLSGDTLPRERDVirnlrlpreKGRMRFHKLQNV 255
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK--RGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKFDL---------EPKNRIQMIQNL 68
|
90 100 110
....*....|....*....|....*....|....*...
gi 2069539781 256 QIALDYL-KHRQVKLVNIRNDDIADGNPKLTLGLIWTI 292
Cdd:cd21225 69 HLAMLFIeEDLKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2268-2763 |
2.03e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 74.10 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2268 QRAEEEAQTKAKAQEDAEKLRK-EAELEAARRAQAEQAALKQKQL-ADAEMAKHKKFAEQTLRQK-----AQVEQELTKV 2340
Cdd:pfam12128 234 AGIMKIRPEFTKLQQEFNTLESaELRLSHLHFGYKSDETLIASRQeERQETSAELNQLLRTLDDQwkekrDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2341 KLQLEETDHQKSILEEEQQRLKDEVTEAMKQKvqvEEELFKVKVQMEELiklktriEEENKMLITKDKDNMQKFLAEEAE 2420
Cdd:pfam12128 314 DAAVAKDRSELEALEDQHGAFLDADIETAAAD---QEQLPSWQSELENL-------EERLKALTGKHQDVTAKYNRRRSK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2421 KMKQVAEEAARLSVEA----QEAARLRELAEQDLAQQrslaEKILKEKMQAVqeatrlKAEAEVLQKQKDLAQEQAKkLQ 2496
Cdd:pfam12128 384 IKEQNNRDIAGIKDKLakirEARDRQLAVAEDDLQAL----ESELREQLEAG------KLEFNEEEYRLKSRLGELK-LR 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2497 EDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLkvqvtelslaqakaEEEAKRFKKQAEQISQKLHQTELATQEK 2576
Cdd:pfam12128 453 LNQATATPELLLQLENFDERIERAREEQEAANAEVERL--------------QSELRQARKRRDQASEALRQASRRLEER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2577 MTLVQTLEIQ-RQQSDSDAEKLRKAIADLEQEKEKLKREAEL--------------------------LQQKSEEMQTAQ 2629
Cdd:pfam12128 519 QSALDELELQlFPQAGTLLHFLRKEAPDWEQSIGKVISPELLhrtdldpevwdgsvggelnlygvkldLKRIDVPEWAAS 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2630 KEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQK---QMEQEKKQLTTVLEEARK 2706
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRlfdEKQSEKDKKNKALAERKD 678
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2707 KqaeAEENVRQKQEELQRLEKQRQ----KQEKLLAEENQKLREKLEQLQEEQKTALAQTRE 2763
Cdd:pfam12128 679 S---ANERLNSLEAQLKQLDKKHQawleEQKEQKREARTEKQAYWQVVEGALDAQLALLKA 736
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4471-4509 |
2.15e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.89 E-value: 2.15e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 4471 LLEAQACTGGIIDPATGEKFSVADAVNKGLVDKIMVDRI 4509
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3218-3256 |
2.37e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.89 E-value: 2.37e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 3218 LLEAQAATGYMVDPVRNEQLPVDDAVRSGMVGPELHEKL 3256
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
198-293 |
3.29e-12 |
|
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: 66.08 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 198 EAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERdvirnLRLPREkGRMRfhKLQNVQIALDYLKHRQV----KLVNIR 273
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSK-----LRVPAI-SRLQ--KLHNVEVALKALKEAGVlrggDGGGIT 92
|
90 100
....*....|....*....|
gi 2069539781 274 NDDIADGNPKLTLGLIWTII 293
Cdd:cd21223 93 AKDIVDGHREKTLALLWRII 112
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
180-293 |
3.30e-12 |
|
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: 66.06 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 180 KKTFTKWVNKHL-----LKHWRAEAQrHVNDLYEDLRDGHNLISLLEVLSGDTLPrerdvIRNLRLPREKGRmrFHKLQN 254
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDP-DGDDLFEALRDGVLLCKLINKIVPGTID-----ERKLNKKKPKNI--FEATEN 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 2069539781 255 VQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 293
Cdd:cd21217 75 LNLALNAAKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2395-2753 |
3.35e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 73.45 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2395 RIEEENKMLItkdkDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRElAEQDLAQQRSLAekilKEKMQAVQEATRl 2474
Cdd:PRK04863 276 RHANERRVHL----EEALELRRELYTSRRQLAAEQYRLVEMARELAELNE-AESDLEQDYQAA----SDHLNLVQTALR- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2475 kaeaevlqkqkdlAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLE--AERQRQLEIT-ANAERLKVQ----VTELSLAQAK 2547
Cdd:PRK04863 346 -------------QQEKIERYQADLEELEERLEEQNEVVEEADEqqEENEARAEAAeEEVDELKSQladyQQALDVQQTR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2548 AEE--EAKRFKKQAEQISQKLH---------QTELATQEKMTLVQTLEIQRQQSDSDAEK---------LRKAIADLEQE 2607
Cdd:PRK04863 413 AIQyqQAVQALERAKQLCGLPDltadnaedwLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfeqayqlVRKIAGEVSRS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2608 KEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDV--LLQK---------------ERFVEEEKAKLEKLfQ 2670
Cdd:PRK04863 493 EAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAerLLAEfckrlgknlddedelEQLQEELEARLESL-S 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2671 EEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAE---ENVRQKQEELQRLEKQRQ---KQEKLLAEENQKLR 2744
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALArlrEQSGEEFEDSQDVTEYMQqllERERELTVERDELA 651
|
....*....
gi 2069539781 2745 EKLEQLQEE 2753
Cdd:PRK04863 652 ARKQALDEE 660
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2416-2765 |
3.46e-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: 73.45 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2416 AEEAEKMKQVAEEAARLSVEAQEAARLRElAEQDLAQQRSLAEKILKEKMQAVQEA---TRLKAEAEVLQKQKDLAQEQA 2492
Cdd:COG3096 292 RELFGARRQLAEEQYRLVEMARELEELSA-RESDLEQDYQAASDHLNLVQTALRQQekiERYQEDLEELTERLEEQEEVV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2493 KKLQEDKE--QMQLRLAEEAEGFQKTLEAERQRQLEIT--------------ANAERLkVQVTELSLAQAKAEEEAkrFK 2556
Cdd:COG3096 371 EEAAEQLAeaEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqalEKARAL-CGLPDLTPENAEDYLAA--FR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2557 KQAEQISQKLhqteLATQEKMTLVqtlEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQE 2636
Cdd:COG3096 448 AKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLRAQ 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2637 TQMLQQTFRSEKDVLLQKERFVeeekakleKLFQEEVNKAQGLKAEQERQQKQmeqekkqlttvLEEARKKQAEAEENVR 2716
Cdd:COG3096 521 LAELEQRLRQQQNAERLLEEFC--------QRIGQQLDAAEELEELLAELEAQ-----------LEELEEQAAEAVEQRS 581
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2069539781 2717 QKQEELQRLeKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREIM 2765
Cdd:COG3096 582 ELRQQLEQL-RARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT 629
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1943-2290 |
3.58e-12 |
|
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: 72.62 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1943 SKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDE 2022
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2023 AYQRRLLEEQAAQHKQDIEE------KIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELE 2096
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2097 LTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKI-SAAEQEAARQCKAALEEVERLKAKAEEARRQKE 2175
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELrSLQERLNASERKVEGLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2176 LAE---KESERQIQLAQEAAQKRivaEEKAHLAavqQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQE 2252
Cdd:pfam07888 274 LHQarlQAAQLTLQLADASLALR---EGRARWA---QERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2069539781 2253 AALSR--QLVEEAERMKQRAEEEAQTKAkAQEDAEKLRKE 2290
Cdd:pfam07888 348 LGREKdcNRVQLSESRRELQELKASLRV-AQKEKEQLQAE 386
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1753-2428 |
3.79e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 73.22 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1753 THLQEEAERLKKLQLEAEQSREEADKEVEKWR-------------QKANEALRLRLQAEEVAHKKALAQEEAEKQ----- 1814
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQENRkiieaqrkaiqelQFENEKVSLKLEEEIQENKDLIKENNATRHlcnll 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1815 KEDAEREARKRSKAEesalrqkelAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEvengeqqrllleEELFRLKNEVNE 1894
Cdd:pfam05483 161 KETCARSAEKTKKYE---------YEREETRQVYMDLNNNIEKMILAFEELRVQAE------------NARLEMHFKLKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1895 AVQKRKELEEELAKLRAEME-----LLLQSKAKTE---------EESRSTSEKSKQILEAEASKLRELAEEAARLRALSE 1960
Cdd:pfam05483 220 DHEKIQHLEEEYKKEINDKEkqvslLLIQITEKENkmkdltfllEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1961 EAK--RQRQLAEEEATHQRAEAE-----RILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQA 2033
Cdd:pfam05483 300 DIKmsLQRSMSTQKALEEDLQIAtkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2034 A------QHKQDIEEKIAQLKKSSESELERQK-------SLVDDTVRQRRLVEE------EIRILKLNFEKASHgktDLE 2094
Cdd:pfam05483 380 KiitmelQKKSSELEEMTKFKNNKEVELEELKkilaedeKLLDEKKQFEKIAEElkgkeqELIFLLQAREKEIH---DLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2095 LELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQK 2174
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2175 E-LAEKESERQIQLA---QEAAQKRivAEEKAHLAAVQQK----EQELLQTRQQEQSILDK---LREEAERAKKAAED-A 2242
Cdd:pfam05483 537 EnLEEKEMNLRDELEsvrEEFIQKG--DEVKCKLDKSEENarsiEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEElH 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2243 EFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKF 2322
Cdd:pfam05483 615 QENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEI 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2323 AEQTLRQKAQVEQELTKVKLQLEEtdhqksILEEEQQRL---KDEVTEAMKQKVQVEEELFKVKvqmEELIKLKTRIEEE 2399
Cdd:pfam05483 695 DKRCQHKIAEMVALMEKHKHQYDK------IIEERDSELglyKNKEQEQSSAKAALEIELSNIK---AELLSLKKQLEIE 765
|
730 740
....*....|....*....|....*....
gi 2069539781 2400 NkmlitkdkdnmqkflaEEAEKMKQVAEE 2428
Cdd:pfam05483 766 K----------------EEKEKLKMEAKE 778
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
767-956 |
4.19e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 68.63 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 767 LQAFVVAATKELMWLNEKEEEEVNYDWTERNSNMVAKKESYSGLMRELEQRERKIKEIQSTGDRLLQEDHPAKQAVEAFQ 846
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 847 AALQTQWSWMLQMCCCIEAHLKENTAYFQFFSDLKEAEEFLcktQETMRKKFMCDRSVTVTRLEDLLQDSLDEKEHLTEY 926
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWL---EEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 2069539781 927 QGHVAGLAKRAKAIVQLKPRSPSNPVKGRL 956
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1938-2444 |
4.28e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1938 LEAEASKLRELAEEAARLRALSEEAKRQR-QLAEEEATHQRAEAERILKEKLVAINEASRLKAeAEIALKEKEAENERLR 2016
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIeLLEPIRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2017 RLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELE 2096
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2097 LTRI-KQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQ------EAARQCKAALEEveRLKAKAEE 2169
Cdd:COG4913 382 FAALrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnipARLLALRDALAE--ALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2170 ARRQKELAE-KESERQIQLAQEAA---QKR--IVAEEkaHLAA------------------VQQKEQELLQTRQQEQSIL 2225
Cdd:COG4913 460 LPFVGELIEvRPEEERWRGAIERVlggFALtlLVPPE--HYAAalrwvnrlhlrgrlvyerVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2226 DKLREEAERAKKAAED---AEFARIKAEQEAALSR------------------------------QLVEEAERMKQRAEE 2272
Cdd:COG4913 538 GKLDFKPHPFRAWLEAelgRRFDYVCVDSPEELRRhpraitragqvkgngtrhekddrrrirsryVLGFDNRAKLAALEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2273 EAQ----TKAKAQEDAEKLrkEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQ---ELTKVKLQLE 2345
Cdd:COG4913 618 ELAeleeELAEAEERLEAL--EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2346 ETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEEN--KMLITKDKDNMQKFLAEEAEkmK 2423
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVERELRENLE--E 773
|
570 580
....*....|....*....|.
gi 2069539781 2424 QVAEEAARLSVEAQEAARLRE 2444
Cdd:COG4913 774 RIDALRARLNRAEEELERAMR 794
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1555-1780 |
7.75e-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: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1555 LVAVDAEQQKQTIQQELSQMKlssdAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEA 1634
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1635 ERQKRLAQEEAERLRKQVKDE--SQKKREAEDELKHKVQAE--QQAARE----KQKALEDLQKLR-LQAEEAERRMKQAE 1705
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPEdfLDAVRRlqylKYLAPARREQAEeLRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 1706 LEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEV 1780
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4126-4164 |
7.95e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.95e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 4126 LLEAQAATGYVVDPIKGLKLTVEEAVRMGIVGPEFKDKL 4164
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2890-2928 |
8.34e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 8.34e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 2890 LLEAQAASGFVIDPVRNRTLSVSEAVKEGVVGPELHNKL 2928
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2023-2770 |
8.36e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.30 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2023 AYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLvDDTVRQRRLVEEEIRILKLNFEKASHGKTDLEleltRIKQ 2102
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMAREL-AELNEAESDLEQDYQAASDHLNLVQTALRQQE----KIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2103 SAEEIQRSKEQAErEAEELRQLALEE----ENHRREAEAKVKKISA----------AEQEAA---RQCKAALEEVERLKA 2165
Cdd:PRK04863 353 YQADLEELEERLE-EQNEVVEEADEQqeenEARAEAAEEEVDELKSqladyqqaldVQQTRAiqyQQAVQALERAKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2166 KAEEArrqkelAEKESERQIQL---AQEAAQKRIVAEEK--AHLAAVQQKEQELlqtrQQEQSILDKL-REEAER-AKKA 2238
Cdd:PRK04863 432 LPDLT------ADNAEDWLEEFqakEQEATEELLSLEQKlsVAQAAHSQFEQAY----QLVRKIAGEVsRSEAWDvAREL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2239 AEDAEFARIKAEQEAALSRQLVEeaerMKQRAEEeaqtkakaQEDAEKLRKEAELEAarraqaeqaalkQKQLADAEmak 2318
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSE----LEQRLRQ--------QQRAERLLAEFCKRL------------GKNLDDED--- 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2319 hkkFAEQTLrqkAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQ--------------KVQVEEELFKvKV 2384
Cdd:PRK04863 555 ---ELEQLQ---EELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaqdalarlREQSGEEFED-SQ 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2385 QMEELIKlkTRIEEENKMLITKDkdnmqkflaEEAEKMKQVAEEAARLS-VEAQEAARLRELAEQ-------DLAQQRSL 2456
Cdd:PRK04863 628 DVTEYMQ--QLLERERELTVERD---------ELAARKQALDEEIERLSqPGGSEDPRLNALAERfggvllsEIYDDVSL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2457 A-----EKILKEKMQA--VQEatrLKAEAEVLQKQKDLAqEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITa 2529
Cdd:PRK04863 697 EdapyfSALYGPARHAivVPD---LSDAAEQLAGLEDCP-EDLYLIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYS- 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2530 naerlkvQVTELSLAQAKAEEE-AKRFKKQAEQISQKLHQTELATQEKMTLVQTLeiqrqqSDSDAEKLRKA-IADLEQE 2607
Cdd:PRK04863 772 -------RFPEVPLFGRAAREKrIEQLRAEREELAERYATLSFDVQKLQRLHQAF------SRFIGSHLAVAfEADPEAE 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2608 KEKLKR-----EAELLQQKSEEMQTAQK-EQLRQETQMLQQTFRSEKdvLLQKERFVEEekakLEKLfQEEVNKAQGLKA 2681
Cdd:PRK04863 839 LRQLNRrrvelERALADHESQEQQQRSQlEQAKEGLSALNRLLPRLN--LLADETLADR----VEEI-REQLDEAEEAKR 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2682 EQERQQKQMEQEKKQLTtVLEEARKKQAEAEENVRQKQEELQRLEKQ-------RQKQE--------KLLAEE---NQKL 2743
Cdd:PRK04863 912 FVQQHGNALAQLEPIVS-VLQSDPEQFEQLKQDYQQAQQTQRDAKQQafaltevVQRRAhfsyedaaEMLAKNsdlNEKL 990
|
810 820
....*....|....*....|....*..
gi 2069539781 2744 REKLEQLQEEQKTALAQTREIMIQTDD 2770
Cdd:PRK04863 991 RQRLEQAEQERTRAREQLRQAQAQLAQ 1017
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2119-2745 |
8.75e-12 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 72.14 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2119 EELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARrqkelaekeserqIQLAQEAAQKRiva 2198
Cdd:PRK10246 230 DEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQLAA-------------LSLAQPARQLR--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2199 eekAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAefARIKAEQEAALSR--QLVEEAERMKQ-------- 2268
Cdd:PRK10246 294 ---PHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHA--AKQSAELQAQQQSlnTWLAEHDRFRQwnnelagw 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2269 RAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAeMAKHKKfaEQTLRQKAQVEQE----LTKVKLQL 2344
Cdd:PRK10246 369 RAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAA-LAQHAE--QRPLRQRLVALHGqivpQQKRLAQL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2345 EETDHQksiLEEEQQRLKDEVTEAMKQKVQVEEELFKVKV--QMEELIKlktRIEEENKMLIT----------------- 2405
Cdd:PRK10246 446 QVAIQN---VTQEQTQRNAALNEMRQRYKEKTQQLADVKTicEQEARIK---DLEAQRAQLQAgqpcplcgstshpavea 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2406 ----KDKDNMQKFLAEEAEKmKQVAEEAARLSveaqeaARLRELAEQdLAQQRSLAEKILKEKMQAVQEATRLKAEAEV- 2480
Cdd:PRK10246 520 yqalEPGVNQSRLDALEKEV-KKLGEEGAALR------GQLDALTKQ-LQRDESEAQSLRQEEQALTQQWQAVCASLNIt 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2481 LQKQKDLAQEQAKklQEDKEQmQLRLAEEAEGFQKTLEA----ERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFK 2556
Cdd:PRK10246 592 LQPQDDIQPWLDA--QEEHER-QLRLLSQRHELQGQIAAhnqqIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLA 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2557 KQAEQISQ-KLHQTELAT-QEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQE--KEKLKREAE---LLQQKSEEMQTAQ 2629
Cdd:PRK10246 669 TRQQEAQSwQQRQNELTAlQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQvhEQCLSLHSQlqtLQQQDVLEAQRLQ 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2630 KEQLRQETQMLQQTFRSEKDVLlqKERFVEEEKAKLEKLFQ---EEVNKAQGLKAEQERQQ-----------------KQ 2689
Cdd:PRK10246 749 KAQAQFDTALQASVFDDQQAFL--AALLDEETLTQLEQLKQnleNQRQQAQTLVTQTAQALaqhqqhrpdgldltvtvEQ 826
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2690 MEQEKKQLTTVLEEARKKQAEAEENVRQKQEelqrlekQRQKQEKLLAEENQKLRE 2745
Cdd:PRK10246 827 IQQELAQLAQQLRENTTRQGEIRQQLKQDAD-------NRQQQQALMQQIAQATQQ 875
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1949-2292 |
8.88e-12 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 71.05 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1949 AEEAARLRALSEEAKRQRQLAEEEATHQraEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEayQRRL 2028
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQ--VTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERR--QKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2029 LEEQAAQHKQDieEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEirilklnfekashgKTDLELELTRIKQSAEEIQ 2108
Cdd:pfam02029 80 QEALERQKEFD--PTIADEKESVAERKENNEEEENSSWEKEEKRDSR--------------LGRYKEEETEIREKEYQEN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2109 RSKEQAEREAEELRqlalEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQkelaekeSERQIQLA 2188
Cdd:pfam02029 144 KWSTEVRQAEEEGE----EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGH-------PEVKSQNG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2189 QEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQsilDKLREEAERAKKAAEDAEFARIKAEQ-EAALS----------- 2256
Cdd:pfam02029 213 EEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEA---EQKLEELRRRRQEKESEEFEKLRQKQqEAELEleelkkkreer 289
|
330 340 350
....*....|....*....|....*....|....*.
gi 2069539781 2257 RQLVEEAERmkQRAEEEAQTKAKAQEDAEKLRKEAE 2292
Cdd:pfam02029 290 RKLLEEEEQ--RRKQEEAERKLREEEEKRRMKEEIE 323
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
313-412 |
1.12e-11 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 64.28 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 313 KEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---VENLEQAFSVAEQ-DLGVTRLL 388
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 2069539781 389 DPEDVdVPQPDEKSIITYVSSLYD 412
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1634-1844 |
1.45e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 69.84 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1634 AERQKRLAQEEAERLRKQVKDESQKKREAEdELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAElekerqvQ 1713
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ-------K 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1714 LAHEAAQKSAE-----ADLQSRRLSFAEKTAQLELSLQQehitithlQEEAERLKKLQLEAEQSREEADKEVEKWRQKAN 1788
Cdd:PRK09510 133 QAEEAAAKAAAaakakAEAEAKRAAAAAKKAAAEAKKKA--------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1789 EALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELE 1844
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1678-1857 |
1.46e-11 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 70.29 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1678 REKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAhEAAQKSAEADLQSRRlsfaektaqlelslqqEHITITHLQE 1757
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQER----------------EIETARIAEA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1758 EAERLKK---LQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALR 1834
Cdd:COG2268 243 EAELAKKkaeERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
170 180
....*....|....*....|...
gi 2069539781 1835 QKELAEQELEKQRKLAEGTAQQK 1857
Cdd:COG2268 323 AEAEAEAEAIRAKGLAEAEGKRA 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2528-2761 |
1.64e-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: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2528 TANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQrqqsdsdaeKLRKAIADLEQE 2607
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR---------ALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2608 KEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQtfrSEKDVLLQKERFVEEEK--AKLEKLFQEEVNKAQGLKAEQER 2685
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRLGRQ---PPLALLLSPEDFLDAVRrlQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2686 ---QQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAE---ENQKLREKLEQLQEEQKTALA 2759
Cdd:COG4942 162 laaLRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAAAE 241
|
..
gi 2069539781 2760 QT 2761
Cdd:COG4942 242 RT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2097-2558 |
1.71e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2097 LTRIKQSAEEIQR-SKEQAEREAEELRQLALEeenhRREAEAKVKKISAAEQEAARqckaALEEVERLKAKAEEARRQKE 2175
Cdd:COG4717 48 LERLEKEADELFKpQGRKPELNLKELKELEEE----LKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2176 LAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQeqsiLDKLREEAERAKKAAEdAEFARIKAEQEAAL 2255
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELE-ELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2256 sRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKE-AELEAARRAQAEQAALKQKQ--------LADAEMAKHKKFAEQT 2326
Cdd:COG4717 195 -QDLAEELEELQQRLAELEEELEEAQEELEELEEElEQLENELEAAALEERLKEARlllliaaaLLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2327 LRQKAQV-------------EQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLK 2393
Cdd:COG4717 274 TIAGVLFlvlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2394 TRIEE-ENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILkekmqAVQEAT 2472
Cdd:COG4717 354 REAEElEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2473 RLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGfqKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEA 2552
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506
|
....*.
gi 2069539781 2553 KRFKKQ 2558
Cdd:COG4717 507 EEYREE 512
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
313-413 |
1.79e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 63.91 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 313 KEKLLLWSQRMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPED 392
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 2069539781 393 VdVPQPDEKSIITYVSSLYDA 413
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2019-2248 |
2.03e-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: 69.41 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2019 AEDEAYQRRLLEEQAAQHKQDIEEKIAQlKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELT 2098
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2099 RIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKE--L 2176
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEalL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2177 AEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIK 2248
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3883-3921 |
2.13e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.19 E-value: 2.13e-11
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 3883 LLEAQAATGFIVDPIKNEMLTVDEAVRKAVVGPEMHDRL 3921
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
313-408 |
2.18e-11 |
|
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: 63.56 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 313 KEKLLLWSQRMVEGyqgMRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNVENLEQAFSVAEQDLGVTRLLDPE 391
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 2069539781 392 DVDVPQPDEKSIITYVS 408
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1677-2605 |
2.76e-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: 70.75 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1677 AREKQKALEDLQKLRlqAEEAERRMKQAElEKERQVQLAHEAAQKSA-----EADLQSrrlsfAEKTAQLELSLQQEHIT 1751
Cdd:COG3096 277 ANERRELSERALELR--RELFGARRQLAE-EQYRLVEMARELEELSAresdlEQDYQA-----ASDHLNLVQTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1752 ITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEA------LRLRL----QAEEVAHKKALAQEEAEKQKEDAERe 1821
Cdd:COG3096 349 IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAeeevdsLKSQLadyqQALDVQQTRAIQYQQAVQALEKARA- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1822 arkrsKAEESALRQKELAEQELEKQRKLAEGTAqqkflaeqelirlkaevengeqqrllleeelfrlknEVNEAVQKRKE 1901
Cdd:COG3096 428 -----LCGLPDLTPENAEDYLAAFRAKEQQATE------------------------------------EVLELEQKLSV 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1902 LEEELAKLRAEMELLlqsKAKTEEESRSTS-EKSKQILEaeasKLRELAEEAARLRALseeakrQRQLAE-EEATHQRAE 1979
Cdd:COG3096 467 ADAARRQFEKAYELV---CKIAGEVERSQAwQTARELLR----RYRSQQALAQRLQQL------RAQLAElEQRLRQQQN 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1980 AERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEeqaaQHKQDIEEKIAQLKKSSESELERQK 2059
Cdd:COG3096 534 AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR----QQLEQLRARIKELAARAPAWLAAQD 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2060 SLVddtvrqrRLVEEEIRILKLNFEKASHGKTDLELElTRIKQSAEEIQRSKEQAEREAEELRQLALEEENH-RREAEA- 2137
Cdd:COG3096 610 ALE-------RLREQSGEALADSQEVTAAMQQLLERE-REATVERDELAARKQALESQIERLSQPGGAEDPRlLALAERl 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2138 ----------KVKKISAAEQEA----ARQC------KAALEEVERLK--------------AKAEEARRQKELAE----K 2179
Cdd:COG3096 682 ggvllseiydDVTLEDAPYFSAlygpARHAivvpdlSAVKEQLAGLEdcpedlyliegdpdSFDDSVFDAEELEDavvvK 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2180 ESERQI------------------QLAQEAAQKRIVAEEKAHLAAVQQKEQELLQtrQQEQSILDKLrEEAERAKKAAED 2241
Cdd:COG3096 762 LSDRQWrysrfpevplfgraarekRLEELRAERDELAEQYAKASFDVQKLQRLHQ--AFSQFVGGHL-AVAFAPDPEAEL 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2242 AEFARikaeQEAALSRQLVEEAERMKQRAEEEAQTKAkAQEDAEKLRKEAELEAARRAQAEQAALKQkQLADAEMAKHkk 2321
Cdd:COG3096 839 AALRQ----RRSELERELAQHRAQEQQLRQQLDQLKE-QLQLLNKLLPQANLLADETLADRLEELRE-ELDAAQEAQA-- 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2322 FAEQTLRQKAQVEQELTKVK---LQLEETDHQKSILEEEQQRLKDEVtEAMKQKVQveeelfkvkvqmeeliklktriee 2398
Cdd:COG3096 911 FIQQHGKALAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQI-FALSEVVQ------------------------ 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2399 enkmlitkdkdNMQKFLAEEAEKMkqvAEEAARLSVEAQEaaRLRElAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEA 2478
Cdd:COG3096 966 -----------RRPHFSYEDAVGL---LGENSDLNEKLRA--RLEQ-AEEARREAREQLRQAQAQYSQYNQVLASLKSSR 1028
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2479 EVlqkqkdlAQEQAKKLQEDKEQMQLRLAEEAEgfQKTLEAERQRQLEITANAERL-----KVQVTELSLAQA-----KA 2548
Cdd:COG3096 1029 DA-------KQQTLQELEQELEELGVQADAEAE--ERARIRRDELHEELSQNRSRRsqlekQLTRCEAEMDSLqkrlrKA 1099
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2549 EEEAKRFKKQAEQ----------------ISQKLHQTELATQEKMTLvqtleiqRQQSDSDAEKLRKAIADLE 2605
Cdd:COG3096 1100 ERDYKQEREQVVQakagwcavlrlardndVERRLHRRELAYLSADEL-------RSMSDKALGALRLAVADNE 1165
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2094-2330 |
3.21e-11 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 68.33 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2094 ELELTRIKQSAEEIQRSKEqAEREAEELRQLALEEENHRREAEAKVK--KISAAEQEAARQCKAALEEVERLKAKAEEAR 2171
Cdd:TIGR02794 54 RIQQQKKPAAKKEQERQKK-LEQQAEEAEKQRAAEQARQKELEQRAAaeKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2172 RQKELAEKEserqiQLAQEAAQKRIVAEEKAHLAAVQQKEQEllqtrqqeqsildKLREEAERAKKAAEDAEfARIKAEQ 2251
Cdd:TIGR02794 133 KAKAEAEAE-----RKAKEEAAKQAEEEAKAKAAAEAKKKAE-------------EAKKKAEAEAKAKAEAE-AKAKAEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2252 EAALSRQLVEEAE---RMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLR 2328
Cdd:TIGR02794 194 AKAKAEAAKAKAAaeaAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQ 273
|
..
gi 2069539781 2329 QK 2330
Cdd:TIGR02794 274 QN 275
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1640-1857 |
3.44e-11 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 68.33 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1640 LAQEEAERLRKQVKDESQKKREAEDEL-KHKVQAEQQAAREKQKALEdlQKLRLQAEEAERRMKQAELEKERQVQLAHEA 1718
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLeQQAEEAEKQRAAEQARQKE--LEQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1719 AQKSAeadlqsrrlsfAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRlRLQAE 1798
Cdd:TIGR02794 125 KAKQA-----------AEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 1799 EVAHKKalaqeEAEKQKEDAE--REARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQK 1857
Cdd:TIGR02794 193 EAKAKA-----EAAKAKAAAEaaAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1624-1857 |
3.59e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 68.64 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1624 LQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQ 1703
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1704 AELEKERQVQLAHE---AAQKSAEADLQSRRLSfAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEV 1780
Cdd:COG4942 95 LRAELEAQKEELAEllrALYRLGRQPPLALLLS-PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1781 EKWRQ--KANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQK 1857
Cdd:COG4942 174 AELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1629-2611 |
3.93e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.99 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1629 DRAEEAERQKRLAQEEAErlrkqvkdESQKKReaeDELKHKVQAEQ--------QAAREKQKALEdlQKLRLQAEEAERR 1700
Cdd:PRK04863 233 QDMEAALRENRMTLEAIR--------VTQSDR---DLFKHLITESTnyvaadymRHANERRVHLE--EALELRRELYTSR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1701 mKQAELEKERQVQLAHE-AAQKSAEADLQSRRLSFAEKTAQLELSL-QQEHIT--ITHLQEEAERLKklqlEAEQSREEA 1776
Cdd:PRK04863 300 -RQLAAEQYRLVEMARElAELNEAESDLEQDYQAASDHLNLVQTALrQQEKIEryQADLEELEERLE----EQNEVVEEA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1777 DKEVEKWRQKANEA----LRLRLQ------AEEVAHKKAL-------AQEEAEKQKEDAEREARKRSK-AEESALRQKEL 1838
Cdd:PRK04863 375 DEQQEENEARAEAAeeevDELKSQladyqqALDVQQTRAIqyqqavqALERAKQLCGLPDLTADNAEDwLEEFQAKEQEA 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1839 AEQELEKQRKL--AEGTAQQKFLAEQELIRLKAEVENgeqqrllleeelfrlknevNEAVQKRKELEEELAKLRA----- 1911
Cdd:PRK04863 455 TEELLSLEQKLsvAQAAHSQFEQAYQLVRKIAGEVSR-------------------SEAWDVARELLRRLREQRHlaeql 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1912 --------EMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAE------EEATHQR 1977
Cdd:PRK04863 516 qqlrmrlsELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMalrqqlEQLQARI 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1978 AEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLlEEQAAQHKQDIEEKIAQLKKSSESELER 2057
Cdd:PRK04863 596 QRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE-RDELAARKQALDEEIERLSQPGGSEDPR 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2058 QKSLVDDtvrqrrlveeeirilkLNFEKASHGKTDLELE-----LTRIKQSAEEI-----QRSKEQAEREAEELRQLALE 2127
Cdd:PRK04863 675 LNALAER----------------FGGVLLSEIYDDVSLEdapyfSALYGPARHAIvvpdlSDAAEQLAGLEDCPEDLYLI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2128 E------ENHRREAEAKVKKISAaeQEAARQCK-AALEEVERLKAKAEEARrqkeLAEKESERQiqlaqeaaqkrIVAEE 2200
Cdd:PRK04863 739 EgdpdsfDDSVFSVEELEKAVVV--KIADRQWRySRFPEVPLFGRAAREKR----IEQLRAERE-----------ELAER 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2201 KAHLAAVQQKEQELLQtrQQEQSILDKLrEEAERAKKAAEDAEFARIKAEQEAALSrQLVEEAERMKQRAEeeaqtKAKA 2280
Cdd:PRK04863 802 YATLSFDVQKLQRLHQ--AFSRFIGSHL-AVAFEADPEAELRQLNRRRVELERALA-DHESQEQQQRSQLE-----QAKE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2281 QEDA-EKLRKEAELEAARRAQAEQAALkQKQLADAEMAkhKKFAEQTLRQKAQVEQELTkvKLQLEETDHqksileeeqQ 2359
Cdd:PRK04863 873 GLSAlNRLLPRLNLLADETLADRVEEI-REQLDEAEEA--KRFVQQHGNALAQLEPIVS--VLQSDPEQF---------E 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2360 RLKDEVTEAMKQKVQVEEELFKVKvqmeELIKLKTRI--EEENKMLiTKDKDNMQKFLA--EEAEKMKQVAEEAARlsve 2435
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFALT----EVVQRRAHFsyEDAAEML-AKNSDLNEKLRQrlEQAEQERTRAREQLR---- 1009
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2436 aQEAARLRELAE--QDLAQQRSLAEKILKEKMQAVQEatrlkaeaevLQKQKDLAQEQAKKLQEDKEQMQLRlaeeaEGF 2513
Cdd:PRK04863 1010 -QAQAQLAQYNQvlASLKSSYDAKRQMLQELKQELQD----------LGVPADSGAEERARARRDELHARLS-----ANR 1073
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2514 QKTLEAERQRQLeITANAERLKVQVTelslaqaKAEEEAKRFKKQAEQ----------------ISQKLHQTELATQEKM 2577
Cdd:PRK04863 1074 SRRNQLEKQLTF-CEAEMDNLTKKLR-------KLERDYHEMREQVVNakagwcavlrlvkdngVERRLHRRELAYLSAD 1145
|
1050 1060 1070
....*....|....*....|....*....|....
gi 2069539781 2578 TLvqtleiqRQQSDSDAEKLRKAIADLEQEKEKL 2611
Cdd:PRK04863 1146 EL-------RSMSDKALGALRLAVADNEHLRDVL 1172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2323-2752 |
7.18e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2323 AEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVtEAMKQKVQVEEELFKVKVQMEELIKLKTRIEE-ENK 2401
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-EKLEKLLQLLPLYQELEALEAELAELPERLEElEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2402 MLITKDKDNMQKFLAEEAEKMKQVAEEAARlSVEAQEAARLRELAEQdlaqqrslAEKILKEKMQAVQEATRLKAEAEVL 2481
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLE-QLSLATEEELQDLAEE--------LEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2482 QKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITAN-AERLKVQVTELSLAQAKAEEEAKRFKKQAE 2560
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2561 QISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQ---EKEKLKREAELLQQKSEE------------- 2624
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEllrEAEELEEELQLEELEQEIaallaeagvedee 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2625 ------MQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEE--KAKLEKLfQEEVNKAQGLKAEQERQQKQMEQEKKQ 2696
Cdd:COG4717 386 elraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEEL-EEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2697 LTT--VLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAE-ENQKLREKLEQLQE 2752
Cdd:COG4717 465 LEEdgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEyREERLPPVLERASE 523
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1271-1718 |
8.09e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1271 LKALEATKAELKRLRGQVEGHQPLFNTLEMDLAKASEVNERmvRGHSERDIDLDRYRERVQQLLERWQAILAQIDLRQRE 1350
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE--LEELREELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1351 LDQLGRQLRYYRE---SYDWLIQWIREARQR-QEHLQAVPVTNSKSVREQLLQEKKLLEECDRNREKVEECQCFAKQYID 1426
Cdd:COG4717 148 LEELEERLEELREleeELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1427 AIKDYELQLVTYKAQvEPVASPAKKPKVQSASDSVIQEYVDLRTRYSE----------LTTLTSQYLKFITETLRRLEEE 1496
Cdd:COG4717 228 ELEQLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1497 EKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLvavdaEQQKQTIQQELSQMKL 1576
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-----EELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1577 SSDAQIQAKLKLIEEvefsRRKVEEEIRMVRLQLEA--TERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKD 1654
Cdd:COG4717 382 EDEEELRAALEQAEE----YQELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1655 ESQKKREAE--DELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKqaELEKERQVQLAHEA 1718
Cdd:COG4717 458 LEAELEQLEedGELAELLQELEELKAELRELAEEWAALKLALELLEEARE--EYREERLPPVLERA 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1840-2292 |
8.81e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1840 EQELEKQR-KLAEGTAQQKFLAEQELIRLKAEVEngeqQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLlq 1918
Cdd:COG4717 48 LERLEKEAdELFKPQGRKPELNLKELKELEEELK----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1919 SKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEakrQRQLAEEEATHQRAEAERILKEKLVAINEASRLK 1998
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE---LEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1999 AEAEIALKEKEAENERLRRL-AEDEAYQRRLLEEQAAQHKQDIEEKIAQLKksseSELERQKSLVDDTVRQRRLVEEEIR 2077
Cdd:COG4717 199 EELEELQQRLAELEEELEEAqEELEELEEELEQLENELEAAALEERLKEAR----LLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2078 ILKLNFekASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQ-EAARQCKAA 2156
Cdd:COG4717 275 IAGVLF--LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELlDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2157 LEEVERLKAKAEEARRQKELAEK------ESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLRE 2230
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALlaeagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2231 EAERAKKAAED---------AEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAK-------AQEDAEKLRKEAE 2292
Cdd:COG4717 433 ELEELEEELEEleeeleelrEELAELEAELEQLEEDGELAELLQELEELKAELRELAEewaalklALELLEEAREEYR 510
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
174-290 |
1.07e-10 |
|
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: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 174 ERDRvQKKTFTKWVNKhllkhwrAEAQRHVNDLYEDLRDGhnLIsLLEVLSGdTLPRERDVIRNLRLPREKGRMRFHKLQ 253
Cdd:cd21300 4 EGER-EARVFTLWLNS-------LDVEPAVNDLFEDLRDG--LI-LLQAYDK-VIPGSVNWKKVNKAPASAEISRFKAVE 71
|
90 100 110
....*....|....*....|....*....|....*..
gi 2069539781 254 NVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIW 290
Cdd:cd21300 72 NTNYAVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1508-2131 |
2.38e-10 |
|
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: 67.05 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKqrqLAEAHARAKAQAEKEALELQRRMEEEVSRRQlvAVDAEQQKQTiqqelsqmklsSDAQIQAKLK 1587
Cdd:pfam05483 182 RQVYMDLNNNIEK---MILAFEELRVQAENARLEMHFKLKEDHEKIQ--HLEEEYKKEI-----------NDKEKQVSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEVEfsrrkVEEEIRMVRLQLEATerqragaedelqalRDRAEEAERQKRLaqeEAERLRKQVKDESQKKREAEDelk 1667
Cdd:pfam05483 246 LIQITE-----KENKMKDLTFLLEES--------------RDKANQLEEKTKL---QDENLKELIEKKDHLTKELED--- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 hkVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQ 1747
Cdd:pfam05483 301 --IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQ 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1748 EHITITHLQE---EAERLKKLQLEAEQSREE-----ADKEVEKWRQKANEALRLRLQAEEvaHKKALAQEEAEKQKEDAE 1819
Cdd:pfam05483 379 LKIITMELQKkssELEEMTKFKNNKEVELEElkkilAEDEKLLDEKKQFEKIAEELKGKE--QELIFLLQAREKEIHDLE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1820 REARKRSKAEESALRQKELAEQELEKQR-KLAEGTAQQKFL----------AEQELIRLKAEVENGEQQRLLLEEELFRL 1888
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLllenkeltqeASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1889 KNEVNEAVQKRKELE---EELAKLRAEMELLL---QSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAAR-LRALSEE 1961
Cdd:pfam05483 537 ENLEEKEMNLRDELEsvrEEFIQKGDEVKCKLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnIEELHQE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1962 AKRQRQlaEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERL--RRLAEdEAYQRRLLEEQAAQHKQD 2039
Cdd:pfam05483 617 NKALKK--KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKIseEKLLE-EVEKAKAIADEAVKLQKE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2040 IEEKIAQLKKSSESELERQKSLVDDTVRQRrlvEEEIRILKLNFEKASHGKTDLELELTRIKQsaeEIQRSKEQAEREAE 2119
Cdd:pfam05483 694 IDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKA---ELLSLKKQLEIEKE 767
|
650
....*....|..
gi 2069539781 2120 ELRQLALEEENH 2131
Cdd:pfam05483 768 EKEKLKMEAKEN 779
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2093-2777 |
2.77e-10 |
|
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: 67.08 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2093 LELELTR-IKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAeqeaARQCKAALEEVERLKAKAEEAR 2171
Cdd:pfam07111 53 LELEGSQaLSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDAL----AVAEKAGQAEAEGLRAALAGAE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2172 RQKELAEKESERQIQLAQEAAQKRIVAEEKAHlaavqqkeqellqtrqqeQSILDKLREEAERAKKAAEDAEFARIKAEQ 2251
Cdd:pfam07111 129 MVRKNLEEGSQRELEEIQRLHQEQLSSLTQAH------------------EEALSSLTSKAEGLEKSLNSLETKRAGEAK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2252 EAALSRQLVEEAERMKQRAEEEAQTKAKAqedAEKLRKEAELEAARRAQAEQAALKQKQLADAemAKHKkfaeQTLRQKA 2331
Cdd:pfam07111 191 QLAEAQKEAELLRKQLSKTQEELEAQVTL---VESLRKYVGEQVPPEVHSQTWELERQELLDT--MQHL----QEDRADL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2332 QVEQELTKVKLQleETDHQKSILEEEQQR-------LKDEVTEAMKQKVQV-EEELFKVKVQM--------EELIKLKTR 2395
Cdd:pfam07111 262 QATVELLQVRVQ--SLTHMLALQEEELTRkiqpsdsLEPEFPKKCRSLLNRwREKVFALMVQLkaqdlehrDSVKQLRGQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2396 IEEENKMLITKDKDN--MQKFLAEEAEKMKQVAEEAARLSVE---AQEAARLRElaeqdlaQQRSLAEKILKEKMQAVQe 2470
Cdd:pfam07111 340 VAELQEQVTSQSQEQaiLQRALQDKAAEVEVERMSAKGLQMElsrAQEARRRQQ-------QQTASAEEQLKFVVNAMS- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2471 ATRLKAEAEVLQKQKDLAQEQAkklQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEE 2550
Cdd:pfam07111 412 STQIWLETTMTRVEQAVARIPS---LSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLRE 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2551 EAKRFKKQAeQISQKLHQTELATQekmtlvqtleiqRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQK 2630
Cdd:pfam07111 489 ERNRLDAEL-QLSAHLIQQEVGRA------------REQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2631 EQlRQETQMLQQTFRSEKDVLLQKerfVEEEKAKLEKlfqeevnkaqglkaeqeRQQKQMEQEKKQLTtvleEARKKQAE 2710
Cdd:pfam07111 556 ES-TEEAASLRQELTQQQEIYGQA---LQEKVAEVET-----------------RLREQLSDTKRRLN----EARREQAK 610
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2711 AEENVRQKQ----EELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLPQEVVA 2777
Cdd:pfam07111 611 AVVSLRQIQhratQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLA 681
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1511-1813 |
3.98e-10 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 64.94 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1511 LAEVEAQL-EKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQMKLSSDAQIQAKLKLI 1589
Cdd:pfam13868 21 NKERDAQIaEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1590 EEVEFSRRKVEEEIRMVRLQLEatERQRAGAEDELQALRDRAEEAERQKRLAQEEAERL---------RKQVKDESQKKR 1660
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKL--EKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIleylkekaeREEEREAEREEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1661 EAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQ 1740
Cdd:pfam13868 179 EEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAER 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1741 LE------LSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEK 1813
Cdd:pfam13868 259 EEeefermLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2233-2631 |
4.89e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2233 ERAKKAAEDAEFARIKAEQEAALsrqlvEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQaeqaalkQKQLA 2312
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKAL-----EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAL-------LKEKR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2313 DAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEEtdhqksiLEEEQQRLKDEVTEAMKQKVQVEEELfkVKVQMEELIKL 2392
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEK-------LTEEISELEKRLEEIEQLLEELNKKI--KDLGEEEQLRV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2393 KTRIEEenkmlITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEAT 2472
Cdd:TIGR02169 293 KEKIGE-----LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2473 RLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAE---EAEGFQKTLEAERQRQLEITANAERLKVQVTELslaQAKAE 2549
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINElkrELDRLQEELQRLSEELADLNAAIAGIEAKINEL---EEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2550 EEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLeiqrqqsdsdaEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQ 2629
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY-----------DRVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
|
..
gi 2069539781 2630 KE 2631
Cdd:TIGR02169 514 EV 515
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1629-1980 |
5.77e-10 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 65.27 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1629 DRAEEAERQK-RLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKL--RLQAEEaERRMKQAE 1705
Cdd:pfam02029 2 EDEEEAARERrRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFldRTAKRE-ERRQKRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1706 LEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTaqlelSLQQEHITITHLQEEAErlkklqlEAEQSREEADKEvEKWRQ 1785
Cdd:pfam02029 81 EALERQKEFDPTIADEKESVAERKENNEEEENS-----SWEKEEKRDSRLGRYKE-------EETEIREKEYQE-NKWST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1786 KANEAlrlrlqAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESaLRQKELAEQELEKQRKLAEGTAQQkflAEQELI 1865
Cdd:pfam02029 148 EVRQA------EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE-KKVKYESKVFLDQKRGHPEVKSQN---GEEEVT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1866 RLKAEvENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKL-RAEMELLLQSKAKTE---EESRSTSEKSKQILEAE 1941
Cdd:pfam02029 218 KLKVT-TKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKeSEEFEKLRQKQQEAElelEELKKKREERRKLLEEE 296
|
330 340 350
....*....|....*....|....*....|....*....
gi 2069539781 1942 asKLRELAEEAARLRALSEEAKRQRqlaeEEATHQRAEA 1980
Cdd:pfam02029 297 --EQRRKQEEAERKLREEEEKRRMK----EEIERRRAEA 329
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4547-4585 |
5.97e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 56.95 E-value: 5.97e-10
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 4547 FLEVQYLTGGLIEPEVTGRVSLDEALQKGTIDARTAQKL 4585
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1630-2290 |
6.89e-10 |
|
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: 65.61 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1630 RAEEAER------QKRLAQEEAERLRKQVKdESQKKREAEDELKHKVQAEQQAAR----------------------EKQ 1681
Cdd:pfam10174 48 RKEEAARisvlkeQYRVTQEENQHLQLTIQ-ALQDELRAQRDLNQLLQQDFTTSPvdgedkfstpelteenfrrlqsEHE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1682 KALEDLQKLRLQAEEAERRM---KQAELEKERQVQLAHEAAQ-----KSAEADLQSRRLSFAEKTAQ---LELSLQQEHI 1750
Cdd:pfam10174 127 RQAKELFLLRKTLEEMELRIetqKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRRIAEAEMQlghLEVLLDQKEK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1751 TITHLQEEAERlkKLQLEAEQSREEADKEVEKWRQKANEALR-----LRLQAEEVAHKKALAQEEAEKQKEDAErEARKR 1825
Cdd:pfam10174 207 ENIHLREELHR--RNQLQPDPAKTKALQTVIEMKDTKISSLErnirdLEDEVQMLKTNGLLHTEDREEEIKQME-VYKSH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1826 SKAEESALRQkelAEQELEKQrklaegtaqqkflaEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEE 1905
Cdd:pfam10174 284 SKFMKNKIDQ---LKQELSKK--------------ESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1906 LAKLR---AEMELLLQSKAK-----TEEESRSTSEKS--KQILEAEASKLRELAEeaaRLRALSEEAK-RQRQLAEeeat 1974
Cdd:pfam10174 347 VDALRlrlEEKESFLNKKTKqlqdlTEEKSTLAGEIRdlKDMLDVKERKINVLQK---KIENLQEQLRdKDKQLAG---- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1975 hqraeaeriLKEKLVAINEASRLKAEA----EIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQL--- 2047
Cdd:pfam10174 420 ---------LKERVKSLQTDSSNTDTAlttlEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALqpe 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2048 ---KKSSESEL-ERQKSLVDDTVRQrrlvEEEIRILKLNFEKASHGKTDLELELTRIKQSAE-----------------E 2106
Cdd:pfam10174 491 lteKESSLIDLkEHASSLASSGLKK----DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEavrtnpeindrirlleqE 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2107 IQRSKEQAER---EAEELRQLALEEENhrrEAEAKVKKISAAEQEAARQCKAALEEVERLKAK-AEEARRQKELAEKESE 2182
Cdd:pfam10174 567 VARYKEESGKaqaEVERLLGILREVEN---EKNDKDKKIAELESLTLRQMKEQNKKVANIKHGqQEMKKKGAQLLEEARR 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2183 RQIQLAQEAAQKRIvaEEKahLAAVQQKEQELLQTRQQEQSILDKLREeaerakkaaEDAEFARIKAEQeaalsRQLVEE 2262
Cdd:pfam10174 644 REDNLADNSQQLQL--EEL--MGALEKTRQELDATKARLSSTQQSLAE---------KDGHLTNLRAER-----RKQLEE 705
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 2069539781 2263 AERMKQRA---------------EEEAQTKAKAQEDAEKLRKE 2290
Cdd:pfam10174 706 ILEMKQEAllaaisekdaniallELSSSKKKKTQEEVMALKRE 748
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1550-2097 |
7.05e-10 |
|
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: 65.43 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1550 VSRRQLVavdaEQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEeirmVRLQLEaterqragaedelqalrd 1629
Cdd:pfam05701 34 VERRKLV----ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLE------------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1630 RAEEAERQkrlAQEEAERLRKQVKDESQKkreAEDELKHKVQAEQQAAREK-QKALEDLQKLRLQAEEAERRMKQAELEK 1708
Cdd:pfam05701 88 RAQTEEAQ---AKQDSELAKLRVEEMEQG---IADEASVAAKAQLEVAKARhAAAVAELKSVKEELESLRKEYASLVSER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1709 ERQVQLAHEAAQKSAEADLQSRRLSfAEKTAQLElSLQQEHitITHLQEEAERLK--------KLQLEAEQsrEEADKEV 1780
Cdd:pfam05701 162 DIAIKRAEEAVSASKEIEKTVEELT-IELIATKE-SLESAH--AAHLEAEEHRIGaalareqdKLNWEKEL--KQAEEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1781 EKWRQK------------ANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREarkRSKAEESALRQKELAEQELEKQRK 1848
Cdd:pfam05701 236 QRLNQQllsakdlkskleTASALLLDLKAELAAYMESKLKEEADGEGNEKKTS---TSIQAALASAKKELEEVKANIEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1849 LAEGTAqQKFLAEQelirLKAEVEngeqqrllleeelfrlKNEVNEAVQKRKE---------LEEELAKLRAEMElLLQS 1919
Cdd:pfam05701 313 KDEVNC-LRVAAAS----LRSELE----------------KEKAELASLRQREgmasiavssLEAELNRTKSEIA-LVQA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1920 KAKteeESRstsEKSKQIleaeASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEA-------ERILKEkLVAIN 1992
Cdd:pfam05701 371 KEK---EAR---EKMVEL----PKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAAstvesrlEAVLKE-IEAAK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1993 EASRLKAEAEIALKEKEAENE--------RLRRLAEDEAY----QRRLLEEQAaqhKQDIEEKIAQLKKSSESELERQKS 2060
Cdd:pfam05701 440 ASEKLALAAIKALQESESSAEstnqedspRGVTLSLEEYYelskRAHEAEELA---NKRVAEAVSQIEEAKESELRSLEK 516
|
570 580 590
....*....|....*....|....*....|....*..
gi 2069539781 2061 LvDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELEL 2097
Cdd:pfam05701 517 L-EEVNREMEERKEALKIALEKAEKAKEGKLAAEQEL 552
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2026-2491 |
7.61e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2026 RRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSlvddTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAE 2105
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEE----ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2106 EIQRSKEQAE--REAEELRQLALEEENHRREAEAKVKKIsaaeQEAARQCKAALEEVERLKAKAEEARRQKELAEKESER 2183
Cdd:COG4717 120 KLEKLLQLLPlyQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2184 QIQLAQEAAQKRIVAEEKAhlaaVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFA------------------ 2245
Cdd:COG4717 196 DLAEELEELQQRLAELEEE----LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2246 --RIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKkfA 2323
Cdd:COG4717 272 ilTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE--L 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2324 EQTLRQKAQVEQELTKVKLQleetDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELfkvkvqmEELIKLKTRIEEENK-- 2401
Cdd:COG4717 350 QELLREAEELEEELQLEELE----QEIAALLAEAGVEDEEELRAALEQAEEYQELK-------EELEELEEQLEELLGel 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2402 --MLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEA-ARLRELAEQDLAQQRSLAEKILKEKMQ-AVQEATRLKAE 2477
Cdd:COG4717 419 eeLLEALDEEELEEELEELEEELEELEEELEELREELAELeAELEQLEEDGELAELLQELEELKAELReLAEEWAALKLA 498
|
490
....*....|....
gi 2069539781 2478 AEVLQKQKDLAQEQ 2491
Cdd:COG4717 499 LELLEEAREEYREE 512
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2120-2764 |
8.30e-10 |
|
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: 65.23 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2120 ELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALeeverlkaKAEEARRqkelaeKESERQIQLAQEaaQKRIVAE 2199
Cdd:pfam10174 4 QLRDLQRENELLRRELDIKESKLGSSMNSIKTFWSPEL--------KKERALR------KEEAARISVLKE--QYRVTQE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2200 EKAHLAAVQQKEQELLQTR-------QQEQSILDKLREEAERAKKAAEDaEFARIKAEQ-----EAALSRQLVEEaerMK 2267
Cdd:pfam10174 68 ENQHLQLTIQALQDELRAQrdlnqllQQDFTTSPVDGEDKFSTPELTEE-NFRRLQSEHerqakELFLLRKTLEE---ME 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2268 QRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKH--------KKFAEQTLRQ----KAQVEQ 2335
Cdd:pfam10174 144 LRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGhlevlldqKEKENIHLREelhrRNQLQP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2336 ELTKVK-LQ--LEETDHQKSILEEEQQRLKDEV----TEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKDK 2408
Cdd:pfam10174 224 DPAKTKaLQtvIEMKDTKISSLERNIRDLEDEVqmlkTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2409 D------------NMQKFLAEEAEKMKQ--VAEE--AARLSVEAqEAARLR-ELAEQDLAQQRSLAEKILKEKMQAVQEA 2471
Cdd:pfam10174 304 EllalqtkletltNQNSDCKQHIEVLKEslTAKEqrAAILQTEV-DALRLRlEEKESFLNKKTKQLQDLTEEKSTLAGEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2472 TRLKAEAEVLQKQKDLAQEQAKKLQE---DKEQMQLRLAEEAEGFQK----------TLE---AERQRQLeitanaERLK 2535
Cdd:pfam10174 383 RDLKDMLDVKERKINVLQKKIENLQEqlrDKDKQLAGLKERVKSLQTdssntdtaltTLEealSEKERII------ERLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2536 VQVTelSLAQAKAEEEAKrFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEK----- 2610
Cdd:pfam10174 457 EQRE--REDRERLEELES-LKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQkkeec 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2611 LKREAELLQQKSEEMQTAQKEQLRQETQMLQQTF----------RSEKDVLLQKERFVEEEK-------AKLEKLFQEEV 2673
Cdd:pfam10174 534 SKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVarykeesgkaQAEVERLLGILREVENEKndkdkkiAELESLTLRQM 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2674 nKAQGLKAEQERQQKQmeQEKKQLTTVLEEARKKQAEAEENVRQKQ--EELQRLEKQRQKQE---KLLAEENQKLREK-- 2746
Cdd:pfam10174 614 -KEQNKKVANIKHGQQ--EMKKKGAQLLEEARRREDNLADNSQQLQleELMGALEKTRQELDatkARLSSTQQSLAEKdg 690
|
730
....*....|....*....
gi 2069539781 2747 -LEQLQEEQKTALAQTREI 2764
Cdd:pfam10174 691 hLTNLRAERRKQLEEILEM 709
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
671-860 |
8.36e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.08 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 671 LRYLQDLLAWVEENQRRIGAAEWGVDLPTVESQLGSHRGLHQSIEEFRAKIERARADETQL---SPGPRSAYRDCLSKLD 747
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 748 LQYAKLLTSSKARLRHLE---SLQAFVVAATKELMWLNEKEEEEVNYDWTERNSNMVAKKESYSGLMRELEQRERKIKEI 824
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 2069539781 825 QSTGDRLLQEDHPAKQA-VEAFQAALQTQWSWMLQMC 860
Cdd:cd00176 166 NELAEELLEEGHPDADEeIEEKLEELNERWEELLELA 202
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
311-413 |
8.42e-10 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 59.31 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 311 TAKEKLLLWSQRMVEGyqgMRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNVENLEQAFSVAEQDLGVTRLLD 389
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 2069539781 390 PEDVDVPQPDEKSIITYVSSLYDA 413
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1271-2256 |
8.98e-10 |
|
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: 65.45 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1271 LKALEATKAELKRLRGQVEGHQPLFNTLEMDLAKASEVNERMVRGH----SERDI------DLDRYRERVQQLLERWQAI 1340
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEaqleSSREIvksyenELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1341 ------LAQIDLRQRELDQLGRQLRYYRES------------YDWLIQWIREARQRQEHLQAVPVTNSKSVREQLLQEKK 1402
Cdd:TIGR00606 265 mkldneIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1403 LLEECDRNREKVEECQCFAKQYIDAIKDYELQLVTYKAQVEPVaspakkpkvqsaSDSVIQEYVDLRTRYSELTTLTSQY 1482
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPF------------SERQIKNFHTLVIERQEDEAKTAAQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1483 LKFITETLRRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEV--SRRQLVAVDA 1560
Cdd:TIGR00606 413 LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELrkAERELSKAEK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1561 EQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEeirmvRLQLEATERQRAGAEDELQALRDRAEEAERQ--- 1637
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTT-----RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllg 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1638 ----KRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLR--------LQAEEAERRMKQAE 1705
Cdd:TIGR00606 568 yfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgSQDEESDLERLKEE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1706 LEKERQvqlahEAAQKSAEADLQSRRLSFAEKTAQLELSL-QQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWR 1784
Cdd:TIGR00606 648 IEKSSK-----QRAMLAGATAVYSQFITQLTDENQSCCPVcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1785 QKANEALRL-RLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQE 1863
Cdd:TIGR00606 723 KRRDEMLGLaPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1864 LIRLKAEvengeqqRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLlqskakteeesRSTSEKSKQILEAEAS 1943
Cdd:TIGR00606 803 DVERKIA-------QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELN-----------RKLIQDQQEQIQHLKS 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1944 KLRELAEEAARLralsEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKE---AENERLRRLAE 2020
Cdd:TIGR00606 865 KTNELKSEKLQI----GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEeliSSKETSNKKAQ 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2021 DEAYQRRLLEEQAAQHKQDIEEKIAQ----LKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELE 2096
Cdd:TIGR00606 941 DKVNDIKEKVKNIHGYMKDIENKIQDgkddYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDN 1020
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2097 LTRIKQSAE--EIQRSKEQAEREAEELRQLALEEENHRREAEakVKKISAAEQEAARQCKAALEEVERLKAKAeearRQK 2174
Cdd:TIGR00606 1021 LTLRKRENElkEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN--IDLIKRNHVLALGRQKGYEKEIKHFKKEL----REP 1094
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2175 ELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVqqkEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAA 2254
Cdd:TIGR00606 1095 QFRDAEEKYREMMIVMRTTELVNKDLDIYYKTL---DQAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADEN 1171
|
..
gi 2069539781 2255 LS 2256
Cdd:TIGR00606 1172 VS 1173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2558-2780 |
9.51e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.08 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2558 QAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQet 2637
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2638 QMLQQTFRSEKDVLLQKERFVE-----EEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAE 2712
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2713 ENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLPQEVVAPSQ 2780
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2084-2511 |
1.13e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 64.53 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2084 EKASHGK---TDLELELTRikqsAEEIQRSKEQAEREAEELRQlALEEENHRREAEAKVKKisAAEQEAARQCKAALEEV 2160
Cdd:pfam07888 10 EEESHGEeggTDMLLVVPR----AELLQNRLEECLQERAELLQ-AQEAANRQREKEKERYK--RDREQWERQRRELESRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2161 ERLKAKAEEAR-RQKELAEKESERQIQLAQEAAQKRIVAEEKA-HLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKA 2238
Cdd:pfam07888 83 AELKEELRQSReKHEELEEKYKELSASSEELSEEKDALLAQRAaHEARIRELEEDIKTLTQRVLERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2239 AedAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARraqaeqaalkqkqladaemak 2318
Cdd:pfam07888 163 G--AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT--------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2319 hkkfaeQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEEL------IKL 2392
Cdd:pfam07888 220 ------QKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLtlqladASL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2393 KTRieeENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEat 2472
Cdd:pfam07888 294 ALR---EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQE-- 368
|
410 420 430
....*....|....*....|....*....|....*....
gi 2069539781 2473 rLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAE 2511
Cdd:pfam07888 369 -LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1497-2274 |
1.22e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.14 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1497 EKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRME---EEVSRRQLVAVDAEQQKQTIQQELSQ 1573
Cdd:pfam15921 98 NELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvHELEAAKCLKEDMLEDSNTQIEQLRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1574 MKLSSDAQIQA-KLKLIEEVEFSRRKVEEE------------------IRMVRLQLEATERQRAGAEDELQALrdRAEEA 1634
Cdd:pfam15921 178 MMLSHEGVLQEiRSILVDFEEASGKKIYEHdsmstmhfrslgsaiskiLRELDTEISYLKGRIFPVEDQLEAL--KSESQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1635 ERQKRLAQEEAERLRKQVK----------DESQKKREAEDELKHKVQAEQQAAREKQ----KALEDLQ----KLRLQAEE 1696
Cdd:pfam15921 256 NKIELLLQQHQDRIEQLISeheveitgltEKASSARSQANSIQSQLEIIQEQARNQNsmymRQLSDLEstvsQLRSELRE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1697 AERRMKQAELEKERQVQLAHeaaqkSAEADLQSRRLSFAEKTAQLELSLQQehititHLQEEAERLKKLQLEAEQSREEA 1776
Cdd:pfam15921 336 AKRMYEDKIEELEKQLVLAN-----SELTEARTERDQFSQESGNLDDQLQK------LLADLHKREKELSLEKEQNKRLW 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1777 DkevekwRQKANEALRLRLQAEevahkkaLAQEEAEKQKEDAEREARKrSKAEESALRQKELAEQELEKQRKLAEGTAQQ 1856
Cdd:pfam15921 405 D------RDTGNSITIDHLRRE-------LDDRNMEVQRLEALLKAMK-SECQGQMERQMAAIQGKNESLEKVSSLTAQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1857 KFLAEQelirLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELE---EELAKLRAEMELLLQ--SKAKTEEESRSTS 1931
Cdd:pfam15921 471 ESTKEM----LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnAEITKLRSRVDLKLQelQHLKNEGDHLRNV 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1932 EKskqilEAEASKLrELAEEAARLRALSEEAKRQRQLAEEEATH------QRAEAERILKEKLVAINEASRLKAEAEIAL 2005
Cdd:pfam15921 547 QT-----ECEALKL-QMAEKDKVIEILRQQIENMTQLVGQHGRTagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKI 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2006 KEKEAenerlrRLAEDEAYQRRLLEEQAAQHK--QDIEEKIAQL---KKSSESELERqkslvddtvrqrrlVEEEIRILK 2080
Cdd:pfam15921 621 RELEA------RVSDLELEKVKLVNAGSERLRavKDIKQERDQLlneVKTSRNELNS--------------LSEDYEVLK 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2081 LNFEKASHgktDLELELTRIKQSAEEIQRSKEQAEreaEELRQLALEEENHRREAEAKVKKISAAEQeaarQCKAALEEV 2160
Cdd:pfam15921 681 RNFRNKSE---EMETTTNKLKMQLKSAQSELEQTR---NTLKSMEGSDGHAMKVAMGMQKQITAKRG----QIDALQSKI 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2161 ERLKAKAEEARRQKELAEKESERqiqLAQEAAQkriVAEEKAHLAAVqqkeqellqtrqqeqsiLDKLREEAERAKKAAE 2240
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNK---LSQELST---VATEKNKMAGE-----------------LEVLRSQERRLKEKVA 807
|
810 820 830
....*....|....*....|....*....|....
gi 2069539781 2241 DAEFARIKAEQEAAlsrqlveEAERMKQRAEEEA 2274
Cdd:pfam15921 808 NMEVALDKASLQFA-------ECQDIIQRQEQES 834
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4469-4506 |
1.28e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 55.95 E-value: 1.28e-09
10 20 30
....*....|....*....|....*....|....*...
gi 2069539781 4469 QRLLEAQACTGGIIDPATGEKFSVADAVNKGLVDKIMV 4506
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1678-2127 |
1.31e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1678 REKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQE 1757
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1758 EAERLKKLQ------LEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEES 1831
Cdd:COG4717 144 LPERLEELEerleelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1832 ALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEElfrlknevneavqkrkeleeELAKLRA 1911
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA--------------------GVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1912 EMELLLqskakteeesRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAI 1991
Cdd:COG4717 284 GLLALL----------FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1992 NEASRLKAEAEIALKEKEAENERLRRLAEDEA--YQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQR 2069
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGVEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2070 -RLVEEEIRILKLNFEKASHGKTDLELELTRIKQSaEEIQRSKEQAEREAEELRQLALE 2127
Cdd:COG4717 434 lEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEE 491
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1598-1859 |
1.35e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.33 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1598 KVEEEIRMVRLQLEATERQragAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDEsQKKREAEDELKHKVQAEQQAA 1677
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKK---EQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE-KAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1678 REKQKALEDlqklRLQAEEAERRMKQAElekerqvqlaheAAQKSAEADlqsrrlsfAEKTAQLELSLQQEHITithLQE 1757
Cdd:TIGR02794 123 EAKAKQAAE----AKAKAEAEAERKAKE------------EAAKQAEEE--------AKAKAAAEAKKKAEEAK---KKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1758 EAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKE 1837
Cdd:TIGR02794 176 EAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGA 255
|
250 260
....*....|....*....|..
gi 2069539781 1838 LAEQELEKQRKLAEGTAQQKFL 1859
Cdd:TIGR02794 256 AAGSEVDKYAAIIQQAIQQNLY 277
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2581-2774 |
1.39e-09 |
|
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: 64.20 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2581 QTLEIQRQQSDSDAEKLRkaiadlEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQM-----LQQTFRSEkDVLLQKE 2655
Cdd:pfam15709 322 KALLEKREQEKASRDRLR------AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMreeleLEQQRRFE-EIRLRKQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2656 RFVEEEKAKLEklfqEEVNKAQGLKAEQERQQKQMEQEKKQLttvLEEARKKQAE-----AEENVRQKQEELQ------- 2723
Cdd:pfam15709 395 RLEEERQRQEE----EERKQRLQLQAAQERARQQQEEFRRKL---QELQRKKQQEeaeraEAEKQRQKELEMQlaeeqkr 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2724 --------RLEKQRQKQEkllAEENQKLREKLEQLQEEQKTALAQtREIMIQTDDLPQE 2774
Cdd:pfam15709 468 lmemaeeeRLEYQRQKQE---AEEKARLEAEERRQKEEEAARLAL-EEAMKQAQEQARQ 522
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
306-408 |
1.59e-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: 58.64 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 306 QSEDMTAKEKLLLWSQRMVEGyqgMRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNVENLEQAFSVAEQDLGV 384
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 2069539781 385 TRLLDPEDVDVPQPDEKSIITYVS 408
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2333-2763 |
1.65e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2333 VEQELTKVKLQLEETDHQksILEEEQQRLKDEVTEAMKQKVQVEEELfkvkvqmEELiklktrieEENKMLITKDKDNMQ 2412
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQ--IEEKEEKDLHERLNGLESELAELDEEI-------ERY--------EEQREQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2413 KFLAEEAEKMKQ---VAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDlaq 2489
Cdd:PRK02224 241 EVLEEHEERREEletLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE--- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2490 eqakKLQEDKEQMQLRLAEE---AEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKL 2566
Cdd:PRK02224 318 ----ELEDRDEELRDRLEECrvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2567 HQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLE---QEKEKLKREAELLQ------------------------ 2619
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlRTARERVEEAEALLeagkcpecgqpvegsphvetieed 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2620 -QKSEEMqTAQKEQLRQETQMLQQTFRSEKDvLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQkQMEQEKKQLT 2698
Cdd:PRK02224 474 rERVEEL-EAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE-ELRERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2699 TVLEEARKKQAEAEENVRQKQEELQRLEKQRQ----------KQEKLLA------EENQKLREKLEQLQE---EQKTALA 2759
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAelkeriesleRIRTLLAaiadaeDEIERLREKREALAElndERRERLA 630
|
....
gi 2069539781 2760 QTRE 2763
Cdd:PRK02224 631 EKRE 634
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1508-1822 |
1.72e-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: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRM---EEEVSRRQLVAVDAEQQKQTIQQELSQMKlssdaqiqa 1584
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELkelEARIEELEEDLHKLEEALNDLEARLSHSR--------- 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1585 klklIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAED 1664
Cdd:TIGR02169 793 ----IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1665 ELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELE----KERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQ 1740
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQiekkRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1741 LELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKevekwRQKANEALRLRLQAEEVAHKKALaqEEAEKQKEDAER 1820
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLK-----RLDELKEKRAKLEEERKAILERI--EEYEKKKREVFM 1021
|
..
gi 2069539781 1821 EA 1822
Cdd:TIGR02169 1022 EA 1023
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1611-1844 |
1.81e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 63.29 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1611 EATERQRAGAEDELQAlrdraEEAERQKRLAQEEAERLRKQvkdesQKKREAEDELKHKVQAEQQAAREKQKALEDLQ-K 1689
Cdd:PRK09510 79 EQRKKKEQQQAEELQQ-----KQAAEQERLKQLEKERLAAQ-----EQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKaK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1690 LRLQAEEAERRMKQAELEKERQvqlAHEAAQKSAEADlqsrrlsfAEKTAqlelslqqehitithlqeEAERLKKLQLEA 1769
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKKK---AEAEAAKKAAAE--------AKKKA------------------EAEAAAKAAAEA 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 1770 EQSREEADKEvekwrqkanealrlrlQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELE 1844
Cdd:PRK09510 200 KKKAEAEAKK----------------KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2154-2337 |
2.08e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 62.94 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2154 KAALEEVERLKAKAEEARRQKELAEKESERQiqlAQEAAQKRivAEEKAHLAAVQQKEQELLQTRQQEQ---SILDKLRE 2230
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ---AEEAEKQR--AAEQARQKELEQRAAAEKAAKQAEQaakQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2231 EAERAKKAAEDAefariKAEQEAALSRQLVEEAERmkqRAEEEAqtKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQ 2310
Cdd:TIGR02794 121 AEEAKAKQAAEA-----KAKAEAEAERKAKEEAAK---QAEEEA--KAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAK 190
|
170 180
....*....|....*....|....*....
gi 2069539781 2311 --LADAEMAKHKKFAEQTLRQKAQVEQEL 2337
Cdd:TIGR02794 191 aeEAKAKAEAAKAKAAAEAAAKAEAEAAA 219
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1906-2364 |
2.19e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1906 LAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQlAEEEATHQRAEAERiLK 1985
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-ELEELREELEKLEK-LL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1986 EKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAyQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDT 2065
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2066 VRQRRLVEEEIRILKLNFEKASHgktdlELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKV------ 2139
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEE-----ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILtiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2140 ----------------KKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESE-----RQIQLAQEAAQKRIVA 2198
Cdd:COG4717 280 flvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEllellDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2199 EEKAHLAAVQQKEQELLQTRQQEqsildklrEEAERAKKAAEDAEFARIKAEQEaALSRQLVEEAERMKQRAE--EEAQT 2276
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGVE--------DEEELRAALEQAEEYQELKEELE-ELEEQLEELLGELEELLEalDEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2277 KAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQK-AQVEQELTKVKLQLEetdhqksILE 2355
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAElRELAEEWAALKLALE-------LLE 503
|
....*....
gi 2069539781 2356 EEQQRLKDE 2364
Cdd:COG4717 504 EAREEYREE 512
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2140-2290 |
2.30e-09 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 63.64 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2140 KKISAAEQEAARQCKAALEEVERLKAKA-----EEARRQKELAEKES-ERQIQLAQeaAQKRIVAEEKA---HLAAVQQK 2210
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEAlleakEEIHKLRNEFEKELrERRNELQK--LEKRLLQKEENldrKLELLEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2211 EQELLQTRQ---QEQSILDKLREEAERAKKAAEDaefariKAEQEAALSRqlvEEA-----ERMKQRAEEEA-----QTK 2277
Cdd:PRK12704 109 EEELEKKEKeleQKQQELEKKEEELEELIEEQLQ------ELERISGLTA---EEAkeillEKVEEEARHEAavlikEIE 179
|
170
....*....|...
gi 2069539781 2278 AKAQEDAEKLRKE 2290
Cdd:PRK12704 180 EEAKEEADKKAKE 192
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1508-1836 |
2.35e-09 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 63.35 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRqlaeaharakaqaekealelQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQMKLssdaqiqaklk 1587
Cdd:pfam02029 61 EEAFLDRTAKREERR--------------------QKRLQEALERQKEFDPTIADEKESVAERKENNEE----------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 liEEVEFSRRKVEEEIRMVRLQLEATE-RQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQV-KDESQKKREAEDE 1665
Cdd:pfam02029 110 --EENSSWEKEEKRDSRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENfAKEEVKDEKIKKE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1666 LKHKvqaeqqaarEKQKALEDLQKLRlqaeeAERRMKQAELEKERqvqlaHEAAQKSAEADLQSRRLSFAEKTAQLELSL 1745
Cdd:pfam02029 188 KKVK---------YESKVFLDQKRGH-----PEVKSQNGEEEVTK-----LKVTTKRRQGGLSQSQEREEEAEVFLEAEQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1746 QQEHITITHLQ---EEAERLKKLQLEAEQSREEADKEVEkWRQKANEALRLRLQAEEvAHKKALAQEEAEKQKEDAEREa 1822
Cdd:pfam02029 249 KLEELRRRRQEkesEEFEKLRQKQQEAELELEELKKKRE-ERRKLLEEEEQRRKQEE-AERKLREEEEKRRMKEEIERR- 325
|
330
....*....|....
gi 2069539781 1823 rkrsKAEESALRQK 1836
Cdd:pfam02029 326 ----RAEAAEKRQK 335
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1323-1973 |
2.85e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1323 LDRYRERVQQLLERWQAILAQIDLRQRELDQLGRQLRYYRESYDWLIQWIREARQRQEHLQA--VPVTNSKSVREQLLQE 1400
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1401 KKLLEECDRNREKveecqcfakqyidAIKDYELQLVTYKAQVEPVASpakkpkvqsasdsvIQEYVDlrtRYSELTTLTS 1480
Cdd:PRK03918 254 KRKLEEKIRELEE-------------RIEELKKEIEELEEKVKELKE--------------LKEKAE---EYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1481 QYLKfitetlrrleeEEKAAEKLKEEERQRLAEVEAQLEKqrqlAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAvDA 1560
Cdd:PRK03918 304 EYLD-----------ELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYE-EA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1561 EQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRA--------- 1631
Cdd:PRK03918 368 KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelte 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1632 EEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKhkvqaEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEkerq 1711
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE---- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1712 vqlahEAAQKSAEADLQSRRLSFAEKTAqleLSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEAL 1791
Cdd:PRK03918 519 -----ELEKKAEEYEKLKEKLIKLKGEI---KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1792 RLRLQAEEVAHKKALAQEEAEKQKEDAEREarkrskaeesalrqKELAEQELEKQRKLAEGTaqqkflaEQELIRLKAEV 1871
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAEKELEREEKE--------------LKKLEEELDKAFEELAET-------EKRLEELRKEL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1872 EngeqqrlllEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLlqskakteEESRSTSEKSKQILEAEASKLRELAEE 1951
Cdd:PRK03918 650 E---------ELEKKYSEEEYEELREEYLELSRELAGLRAELEEL--------EKRREEIKKTLEKLKEELEEREKAKKE 712
|
650 660
....*....|....*....|....*....
gi 2069539781 1952 A-------ARLRALSEEAKRQRQLAEEEA 1973
Cdd:PRK03918 713 LeklekalERVEELREKVKKYKALLKERA 741
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2501-2770 |
4.24e-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: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2501 QMQLRLAEEAEGFQKTLEA--ERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQklHQTELATQEKMT 2578
Cdd:pfam17380 214 QMSTVAPKEVQGMPHTLAPyeKMERRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQ--HQKAVSERQQQE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2579 LVQTLEIQRqqsdsdaeklrkaiadLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQT-FRSEKDVLLQKERf 2657
Cdd:pfam17380 292 KFEKMEQER----------------LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQErMAMERERELERIR- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2658 VEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLA 2737
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
250 260 270
....*....|....*....|....*....|....*..
gi 2069539781 2738 EENQKLRE----KLEQLQEEQKTALAQTREIMIQTDD 2770
Cdd:pfam17380 435 REVRRLEEerarEMERVRLEEQERQQQVERLRQQEEE 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2204-2675 |
4.29e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2204 LAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQED 2283
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2284 AEKLRKEAELEAARRAQAEQ-AALKQKQLADAEMAKHKKFAEQTLRQKAQ------------VEQELTKVKLQLEETDHQ 2350
Cdd:COG4717 128 LPLYQELEALEAELAELPERlEELEERLEELRELEEELEELEAELAELQEeleelleqlslaTEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2351 KSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQmEELIKLKTRIEEENKMLItkdkdnmqkFLAEEAEKMKQVAEEAA 2430
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLA---------LLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2431 RLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQlRLAEEA 2510
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ-ELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2511 EGFQKTLEAERQRQlEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQqs 2590
Cdd:COG4717 357 EELEEELQLEELEQ-EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE-- 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2591 dsdAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQK-EQLRQETQMLQQTFRS-EKDVLLQK--ERFVEEEKAKLE 2666
Cdd:COG4717 434 ---LEELEEELEELEEELEELREELAELEAELEQLEEDGElAELLQELEELKAELRElAEEWAALKlaLELLEEAREEYR 510
|
....*....
gi 2069539781 2667 KLFQEEVNK 2675
Cdd:COG4717 511 EERLPPVLE 519
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2430-2763 |
4.42e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2430 ARLSVEAQEAARlRELAEQDLAQQRSLAEKILKEKMQAV-QEATRLKAEAEVLQKQKDLAQEQAKKLQ------EDKEQM 2502
Cdd:PRK02224 174 ARLGVERVLSDQ-RGSLDQLKAQIEEKEEKDLHERLNGLeSELAELDEEIERYEEQREQARETRDEADevleehEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2503 QLRLAEEAEGFQKTL-EAERQRQlEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQklHQTELATQEKmTLVQ 2581
Cdd:PRK02224 253 LETLEAEIEDLRETIaETERERE-ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEA--RREELEDRDE-ELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2582 TLEIQR---QQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTA------QKEQLRQETQMLQQTF-------- 2644
Cdd:PRK02224 329 RLEECRvaaQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAvedrreEIEELEEEIEELRERFgdapvdlg 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2645 ---------RSEKDVLLQKERfveEEKAKLEKLfQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENV 2715
Cdd:PRK02224 409 naedfleelREERDELREREA---ELEATLRTA-RERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2716 RQKQEELQRLEKQRQKQEKL--LAEENQKLREK---LEQLQEEQKTALAQTRE 2763
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLveAEDRIERLEERredLEELIAERRETIEEKRE 537
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2117-2291 |
4.76e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 62.20 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2117 EAEELRQLA-LEEENHRREAEAkvkkisaaEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLA---QEAA 2192
Cdd:COG2268 187 DALGRRKIAeIIRDARIAEAEA--------ERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAeerREAE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2193 QKRIVAEEKAHLAAV---QQKEQELLQTRQQEQSILDKLREEAERAKKAAE-----DAEFARIKAEQEAalsrqlveEAE 2264
Cdd:COG2268 259 TARAEAEAAYEIAEAnaeREVQRQLEIAEREREIELQEKEAEREEAELEADvrkpaEAEKQAAEAEAEA--------EAE 330
|
170 180
....*....|....*....|....*..
gi 2069539781 2265 RMKQRAEEEAQTKAKAQEDAEKLRKEA 2291
Cdd:COG2268 331 AIRAKGLAEAEGKRALAEAWNKLGDAA 357
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
174-298 |
5.22e-09 |
|
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: 57.70 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 174 ERDRVQKKTFTKWVNKhllkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSgdtLPRERDVIRNLRLPREKGRMRfhKLQ 253
Cdd:cd21331 18 EGETREERTFRNWMNS-------LGVNPHVNHLYGDLQDALVILQLYEKIK---VPVDWNKVNKPPYPKLGANMK--KLE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2069539781 254 NVQIALDYLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 298
Cdd:cd21331 86 NCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2411-2753 |
5.60e-09 |
|
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: 61.47 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2411 MQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQE 2490
Cdd:pfam13868 33 RIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2491 QAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEitanAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTE 2570
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE----EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2571 LATQEkmtlvqtLEIQRQQSDSDAEKLRKAIADLE-QEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQqtfrsekd 2649
Cdd:pfam13868 189 LRAQQ-------EKAQDEKAERDELRAKLYQEEQErKERQKEREEAEKKARQRQELQQAREEQIELKERRLA-------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2650 vllqkerfveeEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQlttvlEEARKKQAEAEENVRQKQEELQRLEKQR 2729
Cdd:pfam13868 254 -----------EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL-----EHRRELEKQIEEREEQRAAEREEELEEG 317
|
330 340
....*....|....*....|....
gi 2069539781 2730 QKQEKLLAEENQKLREKLEQLQEE 2753
Cdd:pfam13868 318 ERLREEEAERRERIEEERQKKLKE 341
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1534-1967 |
5.63e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.53 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1534 QAEKEALELqrRMEEE---VSRRQLVAVDAEQQKQTIQQELSQMKLSSDAQ------IQAKLKLIEEVEFSRRKVEEEI- 1603
Cdd:pfam10174 344 QTEVDALRL--RLEEKesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKerkinvLQKKIENLQEQLRDKDKQLAGLk 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1604 -RMVRLQLEATERQRAgaedeLQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQK 1682
Cdd:pfam10174 422 eRVKSLQTDSSNTDTA-----LTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKES 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1683 ALEDLQK----LRLQAEEAERRMKQAELEKERQV------QLAHEAAQKSAEAdlQSRRLSFAEKTAQLELSLQQEHITI 1752
Cdd:pfam10174 497 SLIDLKEhassLASSGLKKDSKLKSLEIAVEQKKeecsklENQLKKAHNAEEA--VRTNPEINDRIRLLEQEVARYKEES 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1753 THLQEEAERLKKLQLEAEQSREEADKEVEKWRQKAneALRLRLQAEEVAHKKALAQEEAEKQKEDAErEARKRSKAEESA 1832
Cdd:pfam10174 575 GKAQAEVERLLGILREVENEKNDKDKKIAELESLT--LRQMKEQNKKVANIKHGQQEMKKKGAQLLE-EARRREDNLADN 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1833 LRQKELAE--QELEKQRKLAEGTAQ-----QKFLAEQE--LIRLKAEvengeqqrllleeelfrlknevneavqKRKELE 1903
Cdd:pfam10174 652 SQQLQLEElmGALEKTRQELDATKArlsstQQSLAEKDghLTNLRAE---------------------------RRKQLE 704
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1904 EELaklraEMelllqskaKTEEESRSTSEKSKQI--LEAEASKLRELAEEAARLR----ALSEEAKRQRQ 1967
Cdd:pfam10174 705 EIL-----EM--------KQEALLAAISEKDANIalLELSSSKKKKTQEEVMALKrekdRLVHQLKQQTQ 761
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1800-2048 |
5.71e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1800 VAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENgeqqrl 1879
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1880 lleeelfrLKNEVNEAVQKRKELEEELAKL---------RAEMELLLQSKAKTEEESRSTSEKS-KQILEAEASKLRELA 1949
Cdd:COG4942 88 --------LEKEIAELRAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1950 EEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEdeayqrRLL 2029
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA------RLE 233
|
250
....*....|....*....
gi 2069539781 2030 EEQAAQHKQDIEEKIAQLK 2048
Cdd:COG4942 234 AEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2174-2636 |
5.73e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2174 KELAEKESERQiqlaqeaaqkrivaEEKAHLAAVQQKEQELLQTRQQEQSiLDKLREEAERAKKAAEDAEFARIKAEQEA 2253
Cdd:COG4717 71 KELKELEEELK--------------EAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2254 ALSRQLVEEAERMkQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQtlrQKAQV 2333
Cdd:COG4717 136 ALEAELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ---RLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2334 EQELTKVKLQLEETDHQKSILEEEQQRLKD-EVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKDKDNMQ 2412
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2413 KFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQdLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQa 2492
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAA-LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2493 kklQEDKEQMQLRLAEEAEGFQKTLEAERQRQlEITANAERLKVQvtelsLAQAKAEEEAKRFKKQAEQISQKLHQtela 2572
Cdd:COG4717 370 ---QEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQ-----LEELLGELEELLEALDEEELEEELEE---- 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2573 tqekmtlvqtLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSE-EMQTAQKEQLRQE 2636
Cdd:COG4717 437 ----------LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQElEELKAELRELAEE 491
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2151-2368 |
6.02e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 62.66 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2151 RQCKAALEEVERLKAKAEEAR-----RQKELAEKESERQIQLAQEAAQKRIVAEE--KAHLAAVQQKEQELLQTRQQEQS 2223
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKarfeaRQARLEREKAAREARHKKAAEARAAKDKDavAAALARVKAKKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2224 ILDKLRE--EAERAKKAAEDAEFARIKAEQEAALSRQLVEEA-ERMKQRAEEEAQTKAKAQED----------------A 2284
Cdd:PRK05035 512 ARPDNSAviAAREARKAQARARQAEKQAAAAADPKKAAVAAAiARAKAKKAAQQAANAEAEEEvdpkkaavaaaiarakA 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2285 EKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQ--------KAQVEQELTKVKLQLEETDHQKSILEE 2356
Cdd:PRK05035 592 KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEpeepvdprKAAVAAAIARAKARKAAQQQANAEPEE 671
|
250
....*....|..
gi 2069539781 2357 EQQRLKDEVTEA 2368
Cdd:PRK05035 672 AEDPKKAAVAAA 683
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2106-2725 |
6.10e-09 |
|
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: 62.45 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2106 EIQRSKEQAEREAEELRQLALEEENHRREAEAKVkkisaaeQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQI 2185
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKA-------SALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2186 QLAQEAAQkrivaEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAaeDAEFARIKAEQEaALSRQLVEEAER 2265
Cdd:pfam05557 76 ELNRLKKK-----YLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA--ELELQSTNSELE-ELQERLDLLKAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2266 MKQRAEEEAQTKAKAQEDAEKLRKEAELEAARraqaeqaalkQKQLADAEMAKHKKfaeQTLRQKAQVEQELTKVKL--- 2342
Cdd:pfam05557 148 ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEI----------QSQEQDSEIVKNSK---SELARIPELEKELERLREhnk 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2343 QLEETDHQKSILEEEQQRLK---DEVTEAMKQKVQVEEELFKVKVQMEELIKLktriEEENKMLITKDKDNMQKFLAEEA 2419
Cdd:pfam05557 215 HLNENIENKLLLKEEVEDLKrklEREEKYREEAATLELEKEKLEQELQSWVKL----AQDTGLNLRSPEDLSRRIEQLQQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2420 EKMKQVAEEAARLSVEAQEAARLRELaEQDLAQQRSlaeKILKEKMqavqEATRLKAEAEVLQKQKDLAQEQAKKLQEDK 2499
Cdd:pfam05557 291 REIVLKEENSSLTSSARQLEKARREL-EQELAQYLK---KIEDLNK----KLKRHKALVRRLQRRVLLLTKERDGYRAIL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2500 EQMQLRLAEEAEGFQKTleaerQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEqisqklhqtelatqekmTL 2579
Cdd:pfam05557 363 ESYDKELTMSNYSPQLL-----ERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQ-----------------TL 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2580 VQTLEIQRQQSD-SDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMqtaqkeQLRQETQMLQQTFRSEKDVLLQKE--- 2655
Cdd:pfam05557 421 ERELQALRQQESlADPSYSKEEVDSLRRKLETLELERQRLREQKNEL------EMELERRCLQGDYDPKKTKVLHLSmnp 494
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2656 --RFVEEEKAKLEKLfQEEVnkaQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRL 2725
Cdd:pfam05557 495 aaEAYQQRKNQLEKL-QAEI---ERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRL 562
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1515-1747 |
6.70e-09 |
|
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: 61.89 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1515 EAQLEKQRQLAEAHARAKAQAEKealelQRRMEEEVSRRQlvavdAEQQKQTIQQELSQMKlssdaqiqaklKLIEEVEF 1594
Cdd:pfam15709 322 KALLEKREQEKASRDRLRAERAE-----MRRLEVERKRRE-----QEEQRRLQQEQLERAE-----------KMREELEL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1595 SRRKVEEEIRMVRLQLEaTERQRAGAEDELQALRDRAeeAERQKRLAQEEaerLRKQVKDESQKKREAEDElkhKVQAEQ 1674
Cdd:pfam15709 381 EQQRRFEEIRLRKQRLE-EERQRQEEEERKQRLQLQA--AQERARQQQEE---FRRKLQELQRKKQQEEAE---RAEAEK 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 1675 QAAREKQKALEDLQKLRLQAEEAERrmkqaeLEKERQVQLAHEAAQKSAEADLQ----SRRLSFAEKTAQLELSLQQ 1747
Cdd:pfam15709 452 QRQKELEMQLAEEQKRLMEMAEEER------LEYQRQKQEAEEKARLEAEERRQkeeeAARLALEEAMKQAQEQARQ 522
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
306-413 |
7.79e-09 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 56.25 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 306 QSEDMTAKEKLLLWSQRMVEGyqgMRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNVENLEQAFSVAEQDLGV 384
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 2069539781 385 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 413
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2569-2764 |
9.75e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.17 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2569 TELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEqlrqetqmlqqtfrsek 2648
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2649 dvllqKERFVEEEKAKLEKLfQEEVNKAQGLKaEQERQQKQMEQEKKQLttvlEEARKKQAEAEENVRQKQEELQRLEKQ 2728
Cdd:COG1579 64 -----LELEIEEVEARIKKY-EEQLGNVRNNK-EYEALQKEIESLKRRI----SDLEDEILELMERIEELEEELAELEAE 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 2069539781 2729 RQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREI 2764
Cdd:COG1579 133 LAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1599-2285 |
1.01e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 62.13 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1599 VEEEIRMVRLQLEATERQRAGA-----------EDELQALRDRAEEAERQKRLAQEEAERLRKQvkdesqkkreaeDELK 1667
Cdd:PRK10246 189 VFEQHKSARTELEKLQAQASGValltpeqvqslTASLQVLTDEEKQLLTAQQQQQQSLNWLTRL------------DELQ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 HKVQAEQQAAREKQKALEDlqklrlqaeeaerrmKQAELEKerqVQLAHEAAQksaeadLQSRRLSFAEKTAQLELSLQQ 1747
Cdd:PRK10246 257 QEASRRQQALQQALAAEEK---------------AQPQLAA---LSLAQPARQ------LRPHWERIQEQSAALAHTRQQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1748 EHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKAL-AQEEAEKQKEDAEREARKRS 1826
Cdd:PRK10246 313 IEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQfSQQTSDREQLRQWQQQLTHA 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1827 KAEESALRQKELAEQELEKQRKLAEGTAQ----QKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNE-VNEAVQKRKE 1901
Cdd:PRK10246 393 EQKLNALPAITLTLTADEVAAALAQHAEQrplrQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAaLNEMRQRYKE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1902 LEEELAKLRAEMEllLQSKAKTEEESRSTSEKSK----------------QILEAEASKLR---------ELAEEAARLR 1956
Cdd:PRK10246 473 KTQQLADVKTICE--QEARIKDLEAQRAQLQAGQpcplcgstshpaveayQALEPGVNQSRldalekevkKLGEEGAALR 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1957 ALSEEAKRQRQLAEEEATHQRAEAERILKE-KLVAINEASRLKAEAEIA--LKEKEAENERLRRLAedeayQRRLLEEQA 2033
Cdd:PRK10246 551 GQLDALTKQLQRDESEAQSLRQEEQALTQQwQAVCASLNITLQPQDDIQpwLDAQEEHERQLRLLS-----QRHELQGQI 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2034 AQHKQDIEEKIAQLKksseselERQKSLVDDTVRQRRLVEEEirilklnfEKASHGKTDLELELTRIKQSAEEIQRSKEQ 2113
Cdd:PRK10246 626 AAHNQQIIQYQQQIE-------QRQQQLLTALAGYALTLPQE--------DEEASWLATRQQEAQSWQQRQNELTALQNR 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2114 AEREAEELRQLALEEENHRREAEAkvkkISAAEQEAARQCKAALEEVERLKakaeearrQKELAEKESERQIQLAQEAA- 2192
Cdd:PRK10246 691 IQQLTPLLETLPQSDDLPHSEETV----ALDNWRQVHEQCLSLHSQLQTLQ--------QQDVLEAQRLQKAQAQFDTAl 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2193 QKRIVAEEKAHLAA---------VQQKEQELLQTRQQEQSILDKLREEAERAKKAA----EDAEFARIKAEQEAALSRQL 2259
Cdd:PRK10246 759 QASVFDDQQAFLAAlldeetltqLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRpdglDLTVTVEQIQQELAQLAQQL 838
|
730 740 750
....*....|....*....|....*....|...
gi 2069539781 2260 VEEAER-------MKQRAEEEAQTKAKAQEDAE 2285
Cdd:PRK10246 839 RENTTRqgeirqqLKQDADNRQQQQALMQQIAQ 871
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2336-2753 |
1.02e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2336 ELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQME-------ELIKLKTRIEEENKMLItKDK 2408
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnnkynDLKKQKEELENELNLLE-KEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2409 DNMQKFLAEEAekmKQVAEEAARLSVEAQEAARLRELAEQ--DLAQQRSLAEKILKEKMQAVQEatrLKAEAEVLQKQ-K 2485
Cdd:TIGR04523 183 LNIQKNIDKIK---NKLLKLELLLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQlN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2486 DLAQEQakklQEDKEQMQlrlaeeaegfQKTLEAERQRQL--EITANAERLKVQVTELslaqakaeeeakrfKKQAEQIS 2563
Cdd:TIGR04523 257 QLKDEQ----NKIKKQLS----------EKQKELEQNNKKikELEKQLNQLKSEISDL--------------NNQKEQDW 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2564 QKLHQTELATQEKmtlvqtleiQRQQSDSDAEKLRKAIADLEQEKEKLKREaelLQQKSEEMQTAQKEqlrqetqmlqqt 2643
Cdd:TIGR04523 309 NKELKSELKNQEK---------KLEEIQNQISQNNKIISQLNEQISQLKKE---LTNSESENSEKQRE------------ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2644 frsekdvllqkerfVEEEKAKLEKLFQEEVNKAQGLKaeqerqqkQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQ 2723
Cdd:TIGR04523 365 --------------LEEKQNEIEKLKKENQSYKQEIK--------NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
410 420 430
....*....|....*....|....*....|
gi 2069539781 2724 RLEKQRQKqeklLAEENQKLREKLEQLQEE 2753
Cdd:TIGR04523 423 LLEKEIER----LKETIIKNNSEIKDLTNQ 448
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2453-2789 |
1.16e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.57 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2453 QRSLAEKILKEKMQAVQEATRLKAEAEVLqKQKDLAQEQAKKLQEDKEQMQLRLAEE--AEGFQKTLEAERQRQ---LEI 2527
Cdd:COG3206 62 EPQSSDVLLSGLSSLSASDSPLETQIEIL-KSRPVLERVVDKLNLDEDPLGEEASREaaIERLRKNLTVEPVKGsnvIEI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2528 TANAE--RLKVQVTE----------LSLAQAKAEEEAKRFKKQAEQISQKLHQTELAtqekmtlVQTLEIQRQQSDSDAE 2595
Cdd:COG3206 141 SYTSPdpELAAAVANalaeayleqnLELRREEARKALEFLEEQLPELRKELEEAEAA-------LEEFRQKNGLVDLSEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2596 K--LRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEkdvLLQKERFVEEEKAKLEKLFQEEV 2673
Cdd:COG3206 214 AklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARYTPNH 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2674 NKAQGLKAEQERQQKQMEQEKKQlttVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQkLREKLEQLQEE 2753
Cdd:COG3206 291 PDVIALRAQIAALRAQLQQEAQR---ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVAREL 366
|
330 340 350
....*....|....*....|....*....|....*...
gi 2069539781 2754 QKTALAQTREIMIQTDDLPQ--EVVAPSQVPQMKAVPN 2789
Cdd:COG3206 367 YESLLQRLEEARLAEALTVGnvRVIDPAVVPLKPVSPK 404
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2405-2622 |
1.18e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2405 TKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQK- 2483
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2484 ---QKDLAQEQAKKLQEDKEQMQLRL---AEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKK 2557
Cdd:COG4942 99 leaQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2558 QAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKS 2622
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1893-2286 |
1.19e-08 |
|
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: 61.57 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1893 NEAVQKRKELEEELAKLRAEMELLL-QSKAKTEEESRSTSEKSKQILEAEaSKLRELAEEAARLRALSEEAKRQRQLAEE 1971
Cdd:NF033838 103 ELNVLKEKSEAELTSKTKKELDAAFeQFKKDTLEPGKKVAEATKKVEEAE-KKAKDQKEEDRRNYPTNTYKTLELEIAES 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1972 EATHQRAEAERILKEKLVAINEASRLKAEAEIalKEKEAENERLRRLAEDeayqrRLLEEQAAQHKQDIEEKIAQLKKSS 2051
Cdd:NF033838 182 DVEVKKAELELVKEEAKEPRDEEKIKQAKAKV--ESKKAEATRLEKIKTD-----REKAEEEAKRRADAKLKEAVEKNVA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2052 ESELERQKSLVDDTVRQRRLVEEEirilKLNFEKASH---GKTDLELELTRIKQSAEEIQRSKEQAEREAEelrqlALEE 2128
Cdd:NF033838 255 TSEQDKPKRRAKRGVLGEPATPDK----KENDAKSSDssvGEETLPSPSLKPEKKVAEAEKKVEEAKKKAK-----DQKE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2129 ENHR---------------------REAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESErqiql 2187
Cdd:NF033838 326 EDRRnyptntyktleleiaesdvkvKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEE----- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2188 aqEAaqKRIVAEEKahlaAVQQKEQELLQTRQQEQSildklREEAERAKKAAEDAEFARIKAEQ-EAALSRQLVEEAERM 2266
Cdd:NF033838 401 --EA--KRKAAEED----KVKEKPAEQPQPAPAPQP-----EKPAPKPEKPAEQPKAEKPADQQaEEDYARRSEEEYNRL 467
|
410 420
....*....|....*....|
gi 2069539781 2267 KQraEEEAQTKAKAQEDAEK 2286
Cdd:NF033838 468 TQ--QQPPKTEKPAQPSTPK 485
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2326-2735 |
1.21e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.06 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2326 TLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKT-------RIEE 2398
Cdd:pfam07888 8 TLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRelesrvaELKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2399 ENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELaEQDLaqqRSLAEKILKEKMqavqEATRLKAEA 2478
Cdd:pfam07888 88 ELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDI---KTLTQRVLERET----ELERMKERA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2479 EVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTleaeRQRQLEITANAERLKVQVTELSLAQAKAEeeakrfkkq 2558
Cdd:pfam07888 160 KKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL----RNSLAQRDTQVLQLQDTITTLTQKLTTAH--------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2559 aeqisQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKR---EAELLQQKSEEMQTAQKE---Q 2632
Cdd:pfam07888 227 -----RKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALREgraR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2633 LRQETQMLQQTFRSEKDVLLQkerfVEEEKAKLEKLFQEEVNKAQGLKAEQERQQK----QMEQEKKQLTTVLEEARKKQ 2708
Cdd:pfam07888 302 WAQERETLQQSAEADKDRIEK----LSAELQRLEERLQEERMEREKLEVELGREKDcnrvQLSESRRELQELKASLRVAQ 377
|
410 420
....*....|....*....|....*..
gi 2069539781 2709 AEAEENVRQKQEELQRLEKQRQKQEKL 2735
Cdd:pfam07888 378 KEKEQLQAEKQELLEYIRQLEQRLETV 404
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2435-2748 |
1.36e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 61.04 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2435 EAQEAARLREL-AEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVL--QKQKDLAQEQA--KKLQEDKEQMQLRLAEE 2509
Cdd:pfam02029 3 DEEEAARERRRrAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELkpSGQGGLDEEEAflDRTAKREERRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2510 AEGfQKTLEAERQRQLEITANAERlKVQVTELSLA---------QAKAEEEAKRFKKQAEQiSQKLHQTELATQEKMTLV 2580
Cdd:pfam02029 83 LER-QKEFDPTIADEKESVAERKE-NNEEEENSSWekeekrdsrLGRYKEEETEIREKEYQ-ENKWSTEVRQAEEEGEEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2581 Q--TLEIQRQQSDSDA------EKLRKAIADLEQEKEKLKREAELLQQKS---EEMQTAQKEQLRQETQMLQQTFRSEKD 2649
Cdd:pfam02029 160 EdkSEEAEEVPTENFAkeevkdEKIKKEKKVKYESKVFLDQKRGHPEVKSqngEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2650 VllqkERFVEEEKAKleklfqEEVNKAQGLKAEQERQQKQMEQEKKQLTtvLEEARKKQaeaEENVRQKQEELQRLEKQR 2729
Cdd:pfam02029 240 A----EVFLEAEQKL------EELRRRRQEKESEEFEKLRQKQQEAELE--LEELKKKR---EERRKLLEEEEQRRKQEE 304
|
330
....*....|....*....
gi 2069539781 2730 QKQEKLLAEENQKLREKLE 2748
Cdd:pfam02029 305 AERKLREEEEKRRMKEEIE 323
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2465-2610 |
1.66e-08 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 61.19 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2465 MQAVQEATRlkaeaEVLQKQKDLAQEQAKKLQEDKEQMQ-LRLAEEAEG------FQKTLEAERQRQLEITANAERLKVQ 2537
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAIEITTKSQEAAARHQaELLEQEARGrlerqkMHDKAKAEEQRTKLLELQAESAAVE 712
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2538 VTELSLAQAKAEEEAKRFKKQAEqisqkLHQTEL-ATQEKMTLVQTLEIQRQQSDSDAEKlRKAIADLEQEKEK 2610
Cdd:PTZ00491 713 SSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2543-2751 |
1.93e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2543 LAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEiQRQQSDSDAEKLRKAIADLEQEKEKLKREAELL-QQK 2621
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLeKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2622 SEEMQTAQKEQLRQETQMLQQtfrsEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVL 2701
Cdd:COG4717 126 QLLPLYQELEALEAELAELPE----RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2702 EEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLaeENQKLREKLEQLQ 2751
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEAR 249
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1617-1854 |
2.24e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 60.73 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1617 RAGAEDELQALRDRAEEAERQKRLAQEEAE---RLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQ 1693
Cdd:PRK05035 439 RAIEQEKKKAEEAKARFEARQARLEREKAAreaRHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSA 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1694 AEEAERRMKQAELEKERQVQLAHEAAQKSAE-----ADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLE 1768
Cdd:PRK05035 519 VIAAREARKAQARARQAEKQAAAAADPKKAAvaaaiARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQA 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1769 AEQSREEADKEVEKwRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRK 1848
Cdd:PRK05035 599 ASAEPEEQVAEVDP-KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKK 677
|
....*.
gi 2069539781 1849 LAEGTA 1854
Cdd:PRK05035 678 AAVAAA 683
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1632-1988 |
2.46e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 59.55 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1632 EEAERQKRLAQEEAERLRKQVKDESQKKREAEdelkhkvqaEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQ 1711
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEE---------EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1712 VQLAHEAAQKSAEADLQSRRLSFAEKTAqlelsLQQEHITITHLQEEAERLKKLQLEAEQSR-EEADKEVEKwRQKANEA 1790
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQ-----LREEIDEFNEEQAEWKELEKEEEREEDERiLEYLKEKAE-REEEREA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1791 LRLRLQAEEVAHKKALAQEEAEKQKEDAEREArkrskaeesaLRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAE 1870
Cdd:pfam13868 174 EREEIEEEKEREIARLRAQQEKAQDEKAERDE----------LRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1871 vengeqqrllleeelfrlknevnEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAE 1950
Cdd:pfam13868 244 -----------------------QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIE 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 2069539781 1951 EAARLRALSEEAKRQ-RQLAEEEATHQRAEAERILKEKL 1988
Cdd:pfam13868 301 EREEQRAAEREEELEeGERLREEEAERRERIEEERQKKL 339
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1610-2207 |
2.58e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 60.64 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1610 LEATERQRAgaedeLQALRDRAEEAERqkRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAARekqkaLEDLQK 1689
Cdd:COG3899 696 NRAGERDRA-----ARLLLRAARRALA--RGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALYL-----AGRFEE 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1690 LRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLqqehitithlqeeAERLKKLQLEA 1769
Cdd:COG3899 764 AEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALAL-------------AERLGDRRLEA 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1770 EQSREEAdkEVEKWRQKANEALRLRLQAEEVahkkalaqeeAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKL 1849
Cdd:COG3899 831 RALFNLG--FILHWLGPLREALELLREALEA----------GLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLA 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1850 AEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRs 1929
Cdd:COG3899 899 AAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA- 977
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1930 tsekskqiLEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKE 2009
Cdd:COG3899 978 --------AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAAL 1049
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2010 AENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLkkssESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHG 2089
Cdd:COG3899 1050 AAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAA----LAAALAAAALAAAAAAALALAAALAALALAAALAALAL 1125
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2090 KTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEE 2169
Cdd:COG3899 1126 AAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAAR 1205
|
570 580 590
....*....|....*....|....*....|....*...
gi 2069539781 2170 ARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAV 2207
Cdd:COG3899 1206 LAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1753-2293 |
2.77e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 60.04 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1753 THLQEEAERLKKLQLEAEQSREEADKevekwrqkanealrLRLQAEEVAHKKALAQEEAEKQK---EDAEREARKRSKAE 1829
Cdd:pfam05701 28 AHRIQTVERRKLVELELEKVQEEIPE--------------YKKQSEAAEAAKAQVLEELESTKrliEELKLNLERAQTEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1830 ESALRQKELAEQELEKqrklaegtaQQKFLAEQELIRLKAEVENgeqqrllleeelfrLKNEVNEAVQKRKELEEELAKL 1909
Cdd:pfam05701 94 AQAKQDSELAKLRVEE---------MEQGIADEASVAAKAQLEV--------------AKARHAAAVAELKSVKEELESL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1910 RAEMELLLQSKAKTEEESRSTSEKSKQI------LEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQ------R 1977
Cdd:pfam05701 151 RKEYASLVSERDIAIKRAEEAVSASKEIektveeLTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNwekelkQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1978 AEAE-RILKEKLVA-------INEASR----LKAE----AEIALKEKEAENERLRRLAedeayqrRLLEEQAAQHKQDIE 2041
Cdd:pfam05701 231 AEEElQRLNQQLLSakdlkskLETASAllldLKAElaayMESKLKEEADGEGNEKKTS-------TSIQAALASAKKELE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2042 EKIAQLKK-------------SSESELERQKSLVdDTVRQRRlveeeirilklnfEKASHGKTDLELELTRIKQSAEEIQ 2108
Cdd:pfam05701 304 EVKANIEKakdevnclrvaaaSLRSELEKEKAEL-ASLRQRE-------------GMASIAVSSLEAELNRTKSEIALVQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2109 rSKEQAEReaEELRQLALEEENHRREAE-AKVKKISAAE-----QEAARQCKAALEEVE-RLKAKAEEArrqkeLAEKES 2181
Cdd:pfam05701 370 -AKEKEAR--EKMVELPKQLQQAAQEAEeAKSLAQAAREelrkaKEEAEQAKAAASTVEsRLEAVLKEI-----EAAKAS 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2182 ERqiqLAQEAAQkrivaeekahlaAVQQKEQELLQTRQ-----------QEQSILDKLREEAERAKKAAEDAEFARIKAE 2250
Cdd:pfam05701 442 EK---LALAAIK------------ALQESESSAESTNQedsprgvtlslEEYYELSKRAHEAEELANKRVAEAVSQIEEA 506
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2069539781 2251 QEAALS--RQLVEEAERMKQRAE--EEAQTKAKAQEDaEKLRKEAEL 2293
Cdd:pfam05701 507 KESELRslEKLEEVNREMEERKEalKIALEKAEKAKE-GKLAAEQEL 552
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1515-1837 |
3.47e-08 |
|
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: 60.03 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1515 EAQLEKQRQLAEAHARAKAQAEKE----------ALELQR-RMEEEVSRRQLVAVDAEQQKQTIQQELSQMKLSSDAQiQ 1583
Cdd:NF033838 139 KKVAEATKKVEEAEKKAKDQKEEDrrnyptntykTLELEIaESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESK-K 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1584 AKLKLIEEVEFSRRKVEEeirmvrlqlEATERQRAGAEDELQALRDRAEEAERQKR----LAQEEAERLRKQVKDESQKK 1659
Cdd:NF033838 218 AEATRLEKIKTDREKAEE---------EAKRRADAKLKEAVEKNVATSEQDKPKRRakrgVLGEPATPDKKENDAKSSDS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1660 REAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQ-KSAEADL------QSRRl 1732
Cdd:NF033838 289 SVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKvKEAELELvkeeakEPRN- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1733 sfAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAE 1812
Cdd:NF033838 368 --EEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAE 445
|
330 340
....*....|....*....|....*.
gi 2069539781 1813 K-QKEDAEREARKRSKAEESALRQKE 1837
Cdd:NF033838 446 KpADQQAEEDYARRSEEEYNRLTQQQ 471
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1998-2284 |
3.67e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 59.96 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1998 KAE-AEIALKEKEAENERLRRlaedEAYQRRLLEEQAAQ---HKQDIEEKIAQLKKSSESELERQKSlvddtvrqrrlve 2073
Cdd:PRK05035 435 KAEiRAIEQEKKKAEEAKARF----EARQARLEREKAARearHKKAAEARAAKDKDAVAAALARVKA------------- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2074 eeirilklnfEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRRE------AEAKVKKisaAEQ 2147
Cdd:PRK05035 498 ----------KKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAavaaaiARAKAKK---AAQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2148 EAARQckAALEEVERLKAKAEEA-----RRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTrqqeq 2222
Cdd:PRK05035 565 QAANA--EAEEEVDPKKAAVAAAiarakAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEP----- 637
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2223 sildklrEEAERAKKAAEDAEFARIKA---EQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDA 2284
Cdd:PRK05035 638 -------EEPVDPRKAAVAAAIARAKArkaAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1596-1918 |
3.76e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.78 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1596 RRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQ 1675
Cdd:pfam13868 54 ERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1676 AAREKQKALEDLQKLRLQAEEaERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSfaektAQLELSLQQehitithl 1755
Cdd:pfam13868 134 EFNEEQAEWKELEKEEEREED-ERILEYLKEKAEREEEREAEREEIEEEKEREIARLR-----AQQEKAQDE-------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1756 QEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRL-QAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEEsalr 1834
Cdd:pfam13868 200 KAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQaREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE---- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1835 qKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVEngeqqrllleeelfrlknEVNEAVQKRKELEEELAKLRAEME 1914
Cdd:pfam13868 276 -IEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREE------------------ELEEGERLREEEAERRERIEEERQ 336
|
....
gi 2069539781 1915 LLLQ 1918
Cdd:pfam13868 337 KKLK 340
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
315-410 |
3.85e-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: 55.00 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 315 KLLL-WSQrMVEGYQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-----------------------VEN 370
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTqtvdraqdeaedfwvaefspstgDSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 371 LEQAFSVAE-----------QDLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 410
Cdd:cd21224 82 LSSELLANEkrnfklvqqavAELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2544-2781 |
3.95e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 60.07 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2544 AQAKAEEEAKRFKKQAEQiSQKLHQTElATQEKMTLVQTLEiQRQQSDSDAEKLRKAIADLEqekeKLKREaeLLQQKSE 2623
Cdd:PRK10929 20 ATAPDEKQITQELEQAKA-AKTPAQAE-IVEALQSALNWLE-ERKGSLERAKQYQQVIDNFP----KLSAE--LRQQLNN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2624 EMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFqEEVNKAQGLKAEQERQQKQMEQEKKQL---TTV 2700
Cdd:PRK10929 91 ERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARRQLNEIERRLQTLgtpNTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2701 LEEARKKQAEAEENVRQ-KQEEL----------QRLEKQR----QKQEKLLAEENQKLREKL-EQLQEEQKTALAQTREI 2764
Cdd:PRK10929 170 LAQAQLTALQAESAALKaLVDELelaqlsannrQELARLRselaKKRSQQLDAYLQALRNQLnSQRQREAERALESTELL 249
|
250
....*....|....*..
gi 2069539781 2765 MIQTDDLPQEVVAPSQV 2781
Cdd:PRK10929 250 AEQSGDLPKSIVAQFKI 266
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2414-2636 |
4.75e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2414 FLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAK 2493
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2494 KLQEDKEQMQLRLAEEAEGFQKTleaERQRQLEITANAERLKVQVTELSLAQAKAE---EEAKRFKKQAEQISQKLHQTE 2570
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRL---GRQPPLALLLSPEDFLDAVRRLQYLKYLAParrEQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2571 LATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQE 2636
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1935-2121 |
4.97e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 59.41 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1935 KQILEAEASKLRELAE---EAARLRAlsEEAKRQRQL-AEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEA 2010
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEA--EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2011 ENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKssesELERQKSLVDDTVRQRRL--VEEEIRIlklnfEKASH 2088
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEILLekVEEEARH-----EAAVL 174
|
170 180 190
....*....|....*....|....*....|...
gi 2069539781 2089 gktdleleltrIKQSAEEiqrSKEQAEREAEEL 2121
Cdd:PRK12704 175 -----------IKEIEEE---AKEEADKKAKEI 193
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1098-1666 |
5.23e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1098 DDRLQVEREYSACTQKYELLLRSLEKGEQEESLCRNFISQLKDIRLQLEgcesrtihkirlpldkdpaKECAQRITDQQQ 1177
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE-------------------EELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1178 IHQELEGIKKNLGKVSAKTEQVLAQPEQASSAptlhsELDITLQKMDQVYSLSSIYLEKLKTIHLVIRSTQGAEDLIRKY 1257
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1258 EEQLKDVQAVPSDLKALEATKAELKRLRGQVEGHQplfntlemdLAKASEVNERMVRGHSERDIDLDRYRERVQQLLERW 1337
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEAL---------EEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1338 QAILAQIDLRQRELDQLGRQLRYYRESYDWLIQWIREARQRQEHLQAVPVTNSKSVrEQLLQEKKLLEECDRNREKVEEc 1417
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-EAALEAALAAALQNIVVEDDEV- 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1418 qcfAKQYIDAIKDYELQLVT-YKAQVEPVASPAKKPKVQSASDSVIQEYVDLRTRYSELTTLTSQYLKFITETLRRLEEE 1496
Cdd:COG1196 559 ---AAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1497 EKAAEKLKEEERQRLAEVEAQLEKQRqLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQMKL 1576
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGS-LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1577 SSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQ-KRL------AQEEAERLR 1649
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREiEALgpvnllAIEEYEELE 794
|
570 580
....*....|....*....|
gi 2069539781 1650 KQVKD-ESQKK--REAEDEL 1666
Cdd:COG1196 795 ERYDFlSEQREdlEEARETL 814
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4200-4236 |
5.64e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 51.33 E-value: 5.64e-08
10 20 30
....*....|....*....|....*....|....*..
gi 2069539781 4200 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4236
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2374-2759 |
6.05e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2374 QVEEELFKVKVQMEELIKLKTRIEEENKMLitkdkdnmqkflaEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQ 2453
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEEL-------------EELEAELEELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2454 RSLAEKI--LKEKMQAVQEA--TRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQlRLAEEAEGFQKTLEAERQRQLEITA 2529
Cdd:COG4717 142 AELPERLeeLEERLEELRELeeELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2530 NAERLKVQVTELSLAQAKAEEEAKRFKKQ----------------AEQISQKLHQTELAT-----------------QEK 2576
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARlllliaaallallglgGSLLSLILTIAGVLFlvlgllallflllarekASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2577 MTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKER 2656
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2657 FVEEE----KAKLEKLFQEEVNKAQGLKAE-----QERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEK 2727
Cdd:COG4717 381 VEDEEelraALEQAEEYQELKEELEELEEQleellGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430
....*....|....*....|....*....|....
gi 2069539781 2728 QRQKQEK--LLAEENQKLREKLEQLQEEQKTALA 2759
Cdd:COG4717 461 ELEQLEEdgELAELLQELEELKAELRELAEEWAA 494
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2526-2749 |
6.07e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2526 EITANAERLKVQVTELSlaqaKAEEEAKRFKKQAEQISQ--KLHQTELATQEKMTLVQTL---------EIQRQQSDSDA 2594
Cdd:COG4913 222 DTFEAADALVEHFDDLE----RAHEALEDAREQIELLEPirELAERYAAARERLAELEYLraalrlwfaQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2595 EKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVN 2674
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2675 KAQGLKAEQER---QQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRqkqeKLLAEENQKLREKLEQ 2749
Cdd:COG4913 378 SAEEFAALRAEaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK----SNIPARLLALRDALAE 451
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1587-1691 |
6.26e-08 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 59.39 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1587 KLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDR--------AEEAERQKRLAQEEAERLRKQVKDESQK 1658
Cdd:COG1193 518 KLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEkeeilekaREEAEEILREARKEAEELIRELREAQAE 597
|
90 100 110
....*....|....*....|....*....|....*....
gi 2069539781 1659 KREAE------DELKHKVQAEQQAAREKQKALEDLQKLR 1691
Cdd:COG1193 598 EEELKearkklEELKQELEEKLEKPKKKAKPAKPPEELK 636
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2439-2682 |
7.59e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 58.87 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2439 AARLRELAEqDLAQQRSLAE--KILKEKMQAVQEatrlkaEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKT 2516
Cdd:PHA02562 149 APARRKLVE-DLLDISVLSEmdKLNKDKIRELNQ------QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2517 LEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQteLATQEKM--------TLVQTLEiqrq 2588
Cdd:PHA02562 222 YDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQ--FQKVIKMyekggvcpTCTQQIS---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2589 QSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKE------QLRQETQMLQQTFRSEKDV-----LLQKERF 2657
Cdd:PHA02562 296 EGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKllelknKISTNKQSLITLVDKAKKVkaaieELQAEFV 375
|
250 260
....*....|....*....|....*.
gi 2069539781 2658 V-EEEKAKLEKLFQEEVNKAQGLKAE 2682
Cdd:PHA02562 376 DnAEELAKLQDELDKIVKTKSELVKE 401
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1519-1726 |
8.01e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.89 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1519 EKQRQlAEAHARAKAQAEKEALELQRRMEEEVSRRQlvavDAEQQKQTIQQElsqmKLSSDAQIQAKLKLIEEVEFSRRK 1598
Cdd:PRK09510 78 EEQRK-KKEQQQAEELQQKQAAEQERLKQLEKERLA----AQEQKKQAEEAA----KQAALKQKQAEEAAAKAAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1599 VEEEIRmvrlQLEATERQragAEDELQAlRDRAEEAERQKRLAQEEAERLRKQ-VKDESQKKREAEDELKHKVQAEQQAA 1677
Cdd:PRK09510 149 AEAEAK----RAAAAAKK---AAAEAKK-KAEAEAAKKAAAEAKKKAEAEAAAkAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2069539781 1678 REKQKAledlqklrlQAEEAERRMKQAELEKERQVQLAHEAAQKSAEAD 1726
Cdd:PRK09510 221 AEAKAA---------AAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1509-1866 |
8.17e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 59.04 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1509 QRLAEVEAQLEKQRQLAEAHARAKAQAekeaLELQRRMEEEVSRRQlvAVDAEQQKQTIQQELSQMKLSSDAQIQAKLKL 1588
Cdd:PRK10246 409 DEVAAALAQHAEQRPLRQRLVALHGQI----VPQQKRLAQLQVAIQ--NVTQEQTQRNAALNEMRQRYKEKTQQLADVKT 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1589 IEEVEFSRRKVEEEirmvRLQLEA---------TERQRAGAED--ELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQ 1657
Cdd:PRK10246 483 ICEQEARIKDLEAQ----RAQLQAgqpcplcgsTSHPAVEAYQalEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTK 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1658 KKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAE-------EAERRMKQAELEKER---QVQLA-HEAAQKSAEAD 1726
Cdd:PRK10246 559 QLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDdiqpwldAQEEHERQLRLLSQRhelQGQIAaHNQQIIQYQQQ 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1727 LQSRRLSFAEKTAQLELSL--------------------QQEHITITHLQEEAERLK----KLQLEAEQSREEADKEVEK 1782
Cdd:PRK10246 639 IEQRQQQLLTALAGYALTLpqedeeaswlatrqqeaqswQQRQNELTALQNRIQQLTplleTLPQSDDLPHSEETVALDN 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1783 WRQKANEALRLR-----LQAEEVAHKKALAQEEAE-----KQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEG 1852
Cdd:PRK10246 719 WRQVHEQCLSLHsqlqtLQQQDVLEAQRLQKAQAQfdtalQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQT 798
|
410
....*....|....
gi 2069539781 1853 TAQQkflAEQELIR 1866
Cdd:PRK10246 799 LVTQ---TAQALAQ 809
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2307-2511 |
8.63e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2307 KQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQM 2386
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2387 EELIKLKTRIEEENKMLITKDKDNMQKF-------------LAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQ 2453
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2454 RSLAEKILKEKMQAVQeatRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAE 2511
Cdd:COG4942 187 RAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2445-2727 |
8.69e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.35 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2445 LAEQDLAQQRSLAEKILKEKMQAVqeATRLKAEaEVLQKQKDLAQEQAKKLQEDKEQMQLRLA-------EEAEGFqktL 2517
Cdd:COG2268 113 FLGRDPEEIEELAEEKLEGALRAV--AAQMTVE-ELNEDREKFAEKVQEVAGTDLAKNGLELEsvaitdlEDENNY---L 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2518 EAERQRQL-EITANAErlkvqvtelslaqaKAEEEAKRfkKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQsdsdaek 2596
Cdd:COG2268 187 DALGRRKIaEIIRDAR--------------IAEAEAER--ETEIAIAQANREAEEAELEQEREIETARIAEAE------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2597 lrkaiADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERfVEEEKAKLEklfqeevnKA 2676
Cdd:COG2268 244 -----AELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE-AEREEAELE--------AD 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2677 QGLKAEQERQQKQMEQE-----KKQLTTVLEEARKKQAEAEENVRQKQEELQRLEK 2727
Cdd:COG2268 310 VRKPAEAEKQAAEAEAEaeaeaIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEK 365
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1889-2557 |
1.04e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1889 KNEVNEAVQKRKELEEELAKLRAEM---ELLLQS--KAKTEEESRSTSEKSK-QILEAEAS-----------KLRELAEE 1951
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELknkEKELKNldKNLNKDEEKINNSNNKiKILEQQIKdlndklkknkdKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1952 AARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEaeiaLKEKEAENERLRRLAEDEAYQRRLLEE 2031
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2032 QaaqhKQDIEEKIAQLKK----------SSESELERQKSLVDDTVRqrrlVEEEIRILKLNFEKASHGKTDLELELTR-- 2099
Cdd:TIGR04523 181 E----KLNIQKNIDKIKNkllklelllsNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNtq 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2100 -----IKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKI-SAAEQEAARQCKAALEEVERLKAKAEEARRQ 2173
Cdd:TIGR04523 253 tqlnqLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnNQKEQDWNKELKSELKNQEKKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2174 KELAEKESERQI-QLAQEAAQKRIVAEEKAHlaAVQQKEQELLQTRQQEQSILDKLreeaERAKKAAEDAEFARIKAEQE 2252
Cdd:TIGR04523 333 NNKIISQLNEQIsQLKKELTNSESENSEKQR--ELEEKQNEIEKLKKENQSYKQEI----KNLESQINDLESKIQNQEKL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2253 AALSRQLVEEAERMKQRAEEEAQ----TKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKfAEQTLR 2328
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIErlkeTIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK-IKQNLE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2329 QKaqvEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEaMKQKvqvEEELFKVKVQMEEliKLKTRIEEENKMLITKDK 2408
Cdd:TIGR04523 486 QK---QKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-LKEK---IEKLESEKKEKES--KISDLEDELNKDDFELKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2409 DNMQKFLAEEAEKMKQVAEEAARLSVEAQEaarLRELAEQDLAQQRSLAEKILKEKMQAVQeatrLKAEAEVLQKQKDLA 2488
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEE---KQELIDQKEKEKKDLIKEIEEKEKKISS----LEKELEKAKKENEKL 629
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2489 QEQAKKLQEDKEqmqlRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEA-KRFKK 2557
Cdd:TIGR04523 630 SSIIKNIKSKKN----KLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELsLHYKK 695
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1509-2171 |
1.04e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1509 QRLAEVEAQLEKQRQLAEAHARAKAQAekeaLELQRRMEEEVSRRQL--VAVDAEQQKQTIQQELSQMklssdAQIQAKL 1586
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAHSQFEQA----YQLVRKIAGEVSRSEAwdVARELLRRLREQRHLAEQL-----QQLRMRL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1587 KLIEevefsrRKVEEEIRMVRLQLEATERQRAG--AEDELQALrdrAEEAERQKRLAQEEAERLRKQVKDESQKkreaED 1664
Cdd:PRK04863 523 SELE------QRLRQQQRAERLLAEFCKRLGKNldDEDELEQL---QEELEARLESLSESVSEARERRMALRQQ----LE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1665 ELKHKVQAEQQAAREKQKALEDLQKLRLQAEEA----ERRMK--QAELEKERQVQLAH-EAAQKSAEADLQSRRLS---- 1733
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQDALARLREQSGEEfedsQDVTEymQQLLERERELTVERdELAARKQALDEEIERLSqpgg 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1734 --------FAEKTAQLELSLQQEHITI-------------------THLQEEAERLKKLQ--------LEAEQSR----- 1773
Cdd:PRK04863 670 sedprlnaLAERFGGVLLSEIYDDVSLedapyfsalygparhaivvPDLSDAAEQLAGLEdcpedlylIEGDPDSfddsv 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1774 ---EEADKEV------EKWR-----------QKANEAL--RLRLQAEEVAHKkaLAQEEAEKQKEDAEREARKRSKAE-- 1829
Cdd:PRK04863 750 fsvEELEKAVvvkiadRQWRysrfpevplfgRAAREKRieQLRAEREELAER--YATLSFDVQKLQRLHQAFSRFIGShl 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1830 --------ESALRQKELAEQELEKQRKLAEGTAQQkflAEQELIRLKAEVengeqqrllleeeLFRLKNEVNEAVQKRKE 1901
Cdd:PRK04863 828 avafeadpEAELRQLNRRRVELERALADHESQEQQ---QRSQLEQAKEGL-------------SALNRLLPRLNLLADET 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1902 LEEELAKLRAEMELLLQSKAKTEEESRSTSEkskqiLEAEASKLRELAEEAARLRALSEEAKRQRQLAEeeathQRAEAe 1981
Cdd:PRK04863 892 LADRVEEIREQLDEAEEAKRFVQQHGNALAQ-----LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAK-----QQAFA- 960
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1982 riLKEkLVAINEAsrLKAEAEIALKEKEAE-NERLR-RLAEDEAyQRRLLEEQAAQHKQDIEEKIaQLKKSSESELERQK 2059
Cdd:PRK04863 961 --LTE-VVQRRAH--FSYEDAAEMLAKNSDlNEKLRqRLEQAEQ-ERTRAREQLRQAQAQLAQYN-QVLASLKSSYDAKR 1033
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2060 SLVDDTvrQRRLVEEEIRILKLNFEKASHGKTDLELEL--TRIKQSAEEIQRSKEQAEREAEELRQLALEEENH--RREA 2135
Cdd:PRK04863 1034 QMLQEL--KQELQDLGVPADSGAEERARARRDELHARLsaNRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHemREQV 1111
|
730 740 750
....*....|....*....|....*....|....*..
gi 2069539781 2136 E-AKVKKISAAEQEAARQCKAALEEVERLKAKAEEAR 2171
Cdd:PRK04863 1112 VnAKAGWCAVLRLVKDNGVERRLHRRELAYLSADELR 1148
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2055-2271 |
1.14e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2055 LERQKSLVDDTVRQRRLVEEEiRILKLNFEKASHGKTDLELELTRIKQsaeeiQRSKEQAEREAeelrQLALEEEnhRRE 2134
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ-QAEELQQKQAAEQERLKQLEKERLAA-----QEQKKQAEEAA----KQAALKQ--KQA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2135 AEAKVKKISAAEQEAARQCKAAleevERLKAKAEEARRQKELAEKESErqiqlAQEAAQKRIVAEEKAHLAAVQQKEQEL 2214
Cdd:PRK09510 135 EEAAAKAAAAAKAKAEAEAKRA----AAAAKKAAAEAKKKAEAEAAKK-----AAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2215 LQTRQQEQsiLDKLREEAERAKKAAEDAEFARIKAEQEAAlsRQLVEEAERMKQRAE 2271
Cdd:PRK09510 206 EAKKKAAA--EAKKKAAAEAKAAAAKAAAEAKAAAEKAAA--AKAAEKAAAAKAAAE 258
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2349-2784 |
1.19e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.21 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2349 HQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEEliklktriEEENKMLITKDKDNMQKFLAEEAEKMKQVAEE 2428
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDR--------ESDRNQELQKRIRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2429 AARLSVEAQEAARLRELAEQDLAQQRSLAEKILKE-------KMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQ 2501
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNElselrrqIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2502 MQLRLAEEAEGFQKTLEAERQRQL-----EITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQIsqklhqtELATQEK 2576
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSqeqdsEIVKNSKSELARIPELEKELERLREHNKHLNENIENK-------LLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2577 MTLVQTLEIQrqqsdsdaEKLRKAIADLEQEKEKLkrEAELLQQKSEEMQTAQK----EQLRQETQMLQQTfrsekdvll 2652
Cdd:pfam05557 231 EDLKRKLERE--------EKYREEAATLELEKEKL--EQELQSWVKLAQDTGLNlrspEDLSRRIEQLQQR--------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2653 qkerfveeekaklEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQ 2732
Cdd:pfam05557 292 -------------EIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGY 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2733 EKLL---------AEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLPQEVVAPSQVPQM 2784
Cdd:pfam05557 359 RAILesydkeltmSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQT 419
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1508-1845 |
1.32e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 57.35 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQlvavdaeQQKQTIQQElsqmklssdaqiqAKLK 1587
Cdd:pfam15558 38 RRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADR-------REKQVIEKE-------------SRWR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEVEFSRRKveEEIRMVRLQLEATERQragaedelQALRDRAEEAERQKRLAQEEAERLRKQVKDEsQKKREAEDELK 1667
Cdd:pfam15558 98 EQAEDQENQRQ--EKLERARQEAEQRKQC--------QEQRLKEKEEELQALREQNSLQLQERLEEAC-HKRQLKEREEQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 HKVQAEQQAAREKQKALEDLQKLRLQAEEAerrMKQAELEKErqvqlaHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQ 1747
Cdd:pfam15558 167 KKVQENNLSELLNHQARKVLVDCQAKAEEL---LRRLSLEQS------LQRSQENYEQLVEERHRELREKAQKEEEQFQR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1748 EHITIT-HLQEEAERLKKLQLEAEQSREEADKEVEKW-RQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREA-RK 1824
Cdd:pfam15558 238 AKWRAEeKEEERQEHKEALAELADRKIQQARQVAHKTvQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAiKK 317
|
330 340
....*....|....*....|.
gi 2069539781 1825 RSKAEESALRQKELAEQELEK 1845
Cdd:pfam15558 318 KEQRSEQISREKEATLEEARK 338
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1250-1771 |
1.40e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1250 AEDLIRKYEEQLKDVQAVPSDLKALEATKAELKRLRGqveghqplfntlemdlAKASEVNERmvrghserdidldryRER 1329
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERERE----------------ELAEEVRDL---------------RER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1330 VQQLLERWQAILAQIDLRQRELDQLGRQLRYYRESYDWLIQWIREARQRQEHLQAVPVTNSKSVREQLLQEKKLLEECDR 1409
Cdd:PRK02224 288 LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1410 NREKVEECQCFAKQYIDAIKDYELQLVTYKAQVEpvASPAKKPKVQSASDSVIQEYVDLRTRYSELTTLTSQYLKFITET 1489
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFG--DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1490 LRRLEE----------EEKAAEKLKEEERQRLAEVEAQLEkqrQLAEAHARAKAQAE--KEALELQRRMEEEVSRRQLVA 1557
Cdd:PRK02224 446 EALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELE---DLEEEVEEVEERLEraEDLVEAEDRIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1558 VDAEQQKQTIQQELSQMKlSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQ 1637
Cdd:PRK02224 523 ELIAERRETIEEKRERAE-ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAI 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1638 KRLAqEEAERLRKQVKDESQKKREAEDELKHKvqaeqqaaREKQKALED-LQKLRLqaEEAERRMKQAElekERQVQLAH 1716
Cdd:PRK02224 602 ADAE-DEIERLREKREALAELNDERRERLAEK--------RERKRELEAeFDEARI--EEAREDKERAE---EYLEQVEE 667
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1717 EAAQKSAEAD-LQSRRLSFAEKTAQLElSLQQEHitiTHLQEEAERLKKLQLEAEQ 1771
Cdd:PRK02224 668 KLDELREERDdLQAEIGAVENELEELE-ELRERR---EALENRVEALEALYDEAEE 719
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2085-2441 |
1.42e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 57.65 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2085 KASHGKTDLELELTRiKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAArqckaaleEVERLK 2164
Cdd:pfam15709 211 KSRESKAEKKSELIS-KGKKTGAKRKRTQKERNLEVAAELSGPDVINSKETEDASERGAFSSDSVV--------EDPWLS 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2165 AKAEEARRQKELAEKESERQIQLAQEAAQKRivaEEKAHlaavQQKEQELLQTRQQEQSILDKLReeAERAKKAAEDAEF 2244
Cdd:pfam15709 282 SKYDAEESQVSIDGRSSPTQTFVVTGNMESE---EERSE----EDPSKALLEKREQEKASRDRLR--AERAEMRRLEVER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2245 ARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAkaqeDAEKLRKEaeleaarraqaeqaALKQKQLADAEMAKHKKFAE 2324
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRF----EEIRLRKQ--------------RLEEERQRQEEEERKQRLQL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2325 QTLRQKAQVEQELTKVKLQLeetdhqksiLEEEQQRLKDEVTEAMKQKVQVEEElfkvkvQMEELIKLKTRIEEENKMLI 2404
Cdd:pfam15709 415 QAAQERARQQQEEFRRKLQE---------LQRKKQQEEAERAEAEKQRQKELEM------QLAEEQKRLMEMAEEERLEY 479
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2069539781 2405 TKDKDNMQKFLAEEAEKMKQVAEEAARLSVE-----AQEAAR 2441
Cdd:pfam15709 480 QRQKQEAEEKARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
179-295 |
1.43e-07 |
|
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: 52.89 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 179 QKKTFTKWVNKhllkhwrAEAQRHVNDLYEDLRDGhnlISLLEVLsgDTLprERDVIRNLRLPREKGRMRFHKLQNVQIA 258
Cdd:cd21299 5 EERCFRLWINS-------LGIDTYVNNVFEDVRDG---WVLLEVL--DKV--SPGSVNWKHANKPPIKMPFKKVENCNQV 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 2069539781 259 LDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 295
Cdd:cd21299 71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2164-2344 |
1.55e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.58 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2164 KAKAEEARRQKELAEKESERQIQLAQEAAQKrivaeekahlaavQQKEQELLQtrQQEQSILDKLREEAERAKKAAE--- 2240
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANR-------------EAEEAELEQ--EREIETARIAEAEAELAKKKAEerr 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2241 DAEFARIKAEQEAALSRqlvEEAERMKQRAEEEA-QTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAE---- 2315
Cdd:COG2268 256 EAETARAEAEAAYEIAE---ANAEREVQRQLEIAeREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEaeai 332
|
170 180
....*....|....*....|....*....
gi 2069539781 2316 MAKHKKFAEqTLRQKAQVEQELTKVKLQL 2344
Cdd:COG2268 333 RAKGLAEAE-GKRALAEAWNKLGDAAILL 360
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2134-2879 |
1.56e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2134 EAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQkeLAEKEserqiqlAQEAAQKRIVAEEKAHLAAVQQKEQE 2213
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQ--ITSKE-------AQLESSREIVKSYENELDPLKNRLKE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2214 LLQTRQQEQSILDKLREEAERAKKAAED-AEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAE 2292
Cdd:TIGR00606 257 IEHNLSKIMKLDNEIKALKSRKKQMEKDnSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2293 LeaarraqaeqaaLKQKqladaemakhkkfaeqtlrqKAQVEQELTKVKLQLEEtdHQKSILEEEQQRLKDevteAMKQK 2372
Cdd:TIGR00606 337 L------------LNQE--------------------KTELLVEQGRLQLQADR--HQEHIRARDSLIQSL----ATRLE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2373 VQVEEELFKVKVQMEELIKLKTRIEEENKMLITKDkdnmqkfLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQ 2452
Cdd:TIGR00606 379 LDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL-------CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2453 QRSLAEKILKEKMQAVQEATR-LKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANA 2531
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRiLELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2532 ERLKvQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKL 2611
Cdd:TIGR00606 532 TTRT-QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHI 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2612 KREAEllqqKSEEMQTAQKEQLRQETQmlQQTFRSEKDVLLQKERFVEEEKAKL-------EKLFQEEVNKAQGLKAEQE 2684
Cdd:TIGR00606 611 NNELE----SKEEQLSSYEDKLFDVCG--SQDEESDLERLKEEIEKSSKQRAMLagatavySQFITQLTDENQSCCPVCQ 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2685 RqqkqMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQ-----------------KQEKLLAEENQKLREKL 2747
Cdd:TIGR00606 685 R----VFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDemlglapgrqsiidlkeKEIPELRNKLQKVNRDI 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2748 EQLQ---EEQKTALAQTREIMIQTDDLPQEVVAPSQV-PQMKAVPNGRDMIDGISQNGEAELAFDGIRQKVSAK------ 2817
Cdd:TIGR00606 761 QRLKndiEEQETLLGTIMPEEESAKVCLTDVTIMERFqMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKqheldt 840
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2818 ---KLAEAGILSRESMEKLAKGKATVQEL-SQRDDIRRYLRGTSSIAGLLLKPSNEKMSIYSAMKQ 2879
Cdd:TIGR00606 841 vvsKIELNRKLIQDQQEQIQHLKSKTNELkSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2439-2763 |
1.63e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.04 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2439 AARLRELAEQDLAQQRSLAEKilKEKMQAVQEA-TRLKAEAEVLQ-KQKDLAQE-QAKKLQEDKEQMQLRLAEEAEGFQK 2515
Cdd:COG3096 277 ANERRELSERALELRRELFGA--RRQLAEEQYRlVEMARELEELSaRESDLEQDyQAASDHLNLVQTALRQQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2516 TLEaerqrqlEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKL--HQTELATQekmtlvQTLEIQRQQsdsd 2593
Cdd:COG3096 355 DLE-------ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadYQQALDVQ------QTRAIQYQQ---- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2594 aeklrkAIADLEQEKEkLKREAELLQQKSEEMQTAQKEQLRQETQMLQQtfrsekdvLLQKERFVEEEKAKLEKLFQeev 2673
Cdd:COG3096 418 ------AVQALEKARA-LCGLPDLTPENAEDYLAAFRAKEQQATEEVLE--------LEQKLSVADAARRQFEKAYE--- 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2674 nKAQGLKAEQERQQKQmeQEKKQLttvLEEAR--KKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQK--------- 2742
Cdd:COG3096 480 -LVCKIAGEVERSQAW--QTAREL---LRRYRsqQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRigqqldaae 553
|
330 340
....*....|....*....|..
gi 2069539781 2743 -LREKLEQLQEEQKTALAQTRE 2763
Cdd:COG3096 554 eLEELLAELEAQLEELEEQAAE 575
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1559-1842 |
1.67e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1559 DAEQQKQTIQQELSQMKlsSDAQIQA---KLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAG-------------AED 1622
Cdd:COG3206 75 SLSASDSPLETQIEILK--SRPVLERvvdKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNvieisytspdpelAAA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1623 ELQALRD--RAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDEL-----KHKV---QAEQQAAREKQKALED-LQKLR 1691
Cdd:COG3206 153 VANALAEayLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALeefrqKNGLvdlSEEAKLLLQQLSELESqLAEAR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1692 LQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKK-LQLEAE 1770
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAqLQQEAQ 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 1771 QSREEADKEVEKWRQKANEalrlrLQAEEVAHKKALAQE-EAEKQKEDAEREARKRSKAEESAL-RQKELAEQE 1842
Cdd:COG3206 313 RILASLEAELEALQAREAS-----LQAQLAQLEARLAELpELEAELRRLEREVEVARELYESLLqRLEEARLAE 381
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1890-2123 |
1.82e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1890 NEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKskqiLEAEASKLRELAEEAARLRALSEEAKRQRQLA 1969
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1970 EEEATHQRAEaeriLKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEdeaYQRRLLEEQAAQHKQDIEEkIAQLKK 2049
Cdd:COG4942 96 RAELEAQKEE----LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK---YLAPARREQAEELRADLAE-LAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2050 SSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQ 2123
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1855-2292 |
1.91e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.44 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1855 QQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEEL-AKLRAEMELLLQSKAKTEEESRSTSEK 1933
Cdd:pfam05557 16 NEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAeEALREQAELNRLKKKYLEALNKKLNEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1934 SKQILEAEASKLrELAEEAARLRalseeakRQRQLAEEEATHQRAEAERI---LKEKLVAINEASRLKAEAEIALKEKEA 2010
Cdd:pfam05557 96 ESQLADAREVIS-CLKNELSELR-------RQIQRAELELQSTNSELEELqerLDLLKAKASEAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2011 ENERLRRLAedeayQRRLLEEQAAQHKQDIEEKIAQLKKsSESELERQK---SLVDDTVRQRRLVEEEIRILKLN---FE 2084
Cdd:pfam05557 168 AEQRIKELE-----FEIQSQEQDSEIVKNSKSELARIPE-LEKELERLRehnKHLNENIENKLLLKEEVEDLKRKlerEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2085 KASHGKTDLELELTRIKQSAEEIQ----------RSKEQAEREAEELRQ--LALEEENHrrEAEAKVKKISAAEQEAARQ 2152
Cdd:pfam05557 242 KYREEAATLELEKEKLEQELQSWVklaqdtglnlRSPEDLSRRIEQLQQreIVLKEENS--SLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2153 CKAALEEVERLKAKAEearRQKELAEKESERQIQLAQEAAQKRIVAEEkahlaavQQKEQELLQTRQQEQSILDKLREEA 2232
Cdd:pfam05557 320 LAQYLKKIEDLNKKLK---RHKALVRRLQRRVLLLTKERDGYRAILES-------YDKELTMSNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2233 ERAKKAAEDAEFARIKAEQEAALSRQLVE--EAERMKQRAEEEAQTKAKAQEDAEKLRKEAE 2292
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQtlERELQALRQQESLADPSYSKEEVDSLRRKLE 451
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1855-2405 |
2.11e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.34 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1855 QQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEE------SR 1928
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNidkiknKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1929 STSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEaeiaLKEK 2008
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ----LSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2009 EAENERLRRLAEDeayqrrlLEEQAAQHKQDIE----EKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFE 2084
Cdd:TIGR04523 273 QKELEQNNKKIKE-------LEKQLNQLKSEISdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2085 KASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAAleeverlk 2164
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL-------- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2165 akaeearrQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEF 2244
Cdd:TIGR04523 418 --------QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2245 ARIKAEQE-AALSRQLVEEAERMKQRAEEEAQTKAKAQE-DAEKLRKEAELEAARRA-QAEQAALKQKQLADAEMAKHKK 2321
Cdd:TIGR04523 490 ELKSKEKElKKLNEEKKELEEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDElNKDDFELKKENLEKEIDEKNKE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2322 FAEQTLRQKAqveqeLTKVKLQLEETDHQKsilEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENK 2401
Cdd:TIGR04523 570 IEELKQTQKS-----LKKKQEEKQELIDQK---EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
....
gi 2069539781 2402 MLIT 2405
Cdd:TIGR04523 642 KLKQ 645
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2392-2775 |
2.50e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2392 LKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQ--DLAQQRSLAEKILKEKMQAVQ 2469
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEleELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2470 ------EATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSL 2543
Cdd:COG4717 127 llplyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2544 AQAKAEEEAKRFKKQAEQISQKLHQTElATQEKMTLVQTLEIQRQQ--------------------SDSDAEKLRKAIAD 2603
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERLKEARLLlliaaallallglggsllslILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2604 LEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKErFVEEEKAKLEKLFQEEVNKAqglKAEQ 2683
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE-ELLELLDRIEELQELLREAE---ELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2684 ERQQKQMEQEKKQLTTVL----EEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLreKLEQLQEEQKTALA 2759
Cdd:COG4717 362 ELQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEE 439
|
410
....*....|....*.
gi 2069539781 2760 QTREIMIQTDDLPQEV 2775
Cdd:COG4717 440 ELEELEEELEELREEL 455
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1561-1821 |
2.65e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.88 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1561 EQQKQTIQQELSQMKLSSDA--QIQAKLKLIEeVEFSRRKVEEEIRMVRLQLEATERQRAgaedELqalrdraeEAERQK 1638
Cdd:pfam15709 318 EDPSKALLEKREQEKASRDRlrAERAEMRRLE-VERKRREQEEQRRLQQEQLERAEKMRE----EL--------ELEQQR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1639 RLaqeEAERLRKQVKDESQKKREAEDELKH-KVQAEQQAA-REKQKALEDLQKL--RLQAEEAERrmkqAELEKERQvql 1714
Cdd:pfam15709 385 RF---EEIRLRKQRLEEERQRQEEEERKQRlQLQAAQERArQQQEEFRRKLQELqrKKQQEEAER----AEAEKQRQ--- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1715 aheaaqksaeadlqsrrlsfaektAQLELSLQQEHITITHLQEEaERLKKLQlEAEQSREEADKEVEKWRQKANEALRlr 1794
Cdd:pfam15709 455 ------------------------KELEMQLAEEQKRLMEMAEE-ERLEYQR-QKQEAEEKARLEAEERRQKEEEAAR-- 506
|
250 260
....*....|....*....|....*..
gi 2069539781 1795 lqaeevahkkaLAQEEAEKQKEDAERE 1821
Cdd:pfam15709 507 -----------LALEEAMKQAQEQARQ 522
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1508-2059 |
2.70e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.06 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQR----QLAEAHARAKAQAEKEALELQRRMEEEVSRRQlvavdaEQQKQtiqqelsqMKLSSDAQIQ 1583
Cdd:pfam05557 1 RAELIESKARLSQLQnekkQMELEHKRARIELEKKASALKRQLDRESDRNQ------ELQKR--------IRLLEKREAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1584 AKLKLIEEVEFSRRKVEEEIRMVRLQLEaTERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKqvkdESQKKREAE 1663
Cdd:pfam05557 67 AEEALREQAELNRLKKKYLEALNKKLNE-KESQLADAREVISCLKNELSELRRQIQRAELELQSTNS----ELEELQERL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1664 DELKHKVQAeqqaAREKQKALEDLQKLRLqaeEAERRMKQAELEKERQVQLAHEAaqksaeADLQSRRLSFAEktAQLEL 1743
Cdd:pfam05557 142 DLLKAKASE----AEQLRQNLEKQQSSLA---EAEQRIKELEFEIQSQEQDSEIV------KNSKSELARIPE--LEKEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1744 SLQQEHI--------TITHLQEEAERLKKLQLEAEQSREEADK---EVEKWRQKAN----------------EALRLR-- 1794
Cdd:pfam05557 207 ERLREHNkhlnenieNKLLLKEEVEDLKRKLEREEKYREEAATlelEKEKLEQELQswvklaqdtglnlrspEDLSRRie 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1795 -LQAEEVAHKkalAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQ-ELEKQRKLAEGTAQQKFLAEQELIRLKAEVE 1872
Cdd:pfam05557 287 qLQQREIVLK---EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNkKLKRHKALVRRLQRRVLLLTKERDGYRAILE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1873 NGEQQRLLLEEELFRLKnEVNEAVQKRKELEEELAKLRAEMElLLQSKAKTEEESRSTSEKSKQIL--EAEASKLRELAE 1950
Cdd:pfam05557 364 SYDKELTMSNYSPQLLE-RIEEAEDMTQKMQAHNEEMEAQLS-VAEEELGGYKQQAQTLERELQALrqQESLADPSYSKE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1951 EAARLRALSEEAKRQRQLAEEEATHQRAEAER--------ILKEKLVAINEASRLKAEAEIA--LKEKEAENERLRRLAE 2020
Cdd:pfam05557 442 EVDSLRRKLETLELERQRLREQKNELEMELERrclqgdydPKKTKVLHLSMNPAAEAYQQRKnqLEKLQAEIERLKRLLK 521
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2069539781 2021 DEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSES-ELERQK 2059
Cdd:pfam05557 522 KLEDDLEQVLRLPETTSTMNFKEVLDLRKELESaELKNQR 561
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2655-2758 |
3.25e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.71 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2655 ERFVEEEKAKLEKLFQEEVNKAqglKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEK 2734
Cdd:PRK12704 41 KRILEEAKKEAEAIKKEALLEA---KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100
....*....|....*....|....*..
gi 2069539781 2735 LLAEENQ---KLREKLEQLQEEQKTAL 2758
Cdd:PRK12704 118 ELEQKQQeleKKEEELEELIEEQLQEL 144
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2068-2364 |
3.83e-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: 55.70 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2068 QRRLVEEEIRILKLNFEKASHGKTDLELEltrIKQSAEEIQRSKEQAEREAEELRQL---ALEEENHRREAEAKVKKISA 2144
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQ---IEEREQKRQEEYEEKLQEREQMDEIverIQEEDQAEAEEKLEKQRQLR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2145 AEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQEllQTRQQEQSI 2224
Cdd:pfam13868 130 EEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQD--EKAERDELR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2225 LDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQA 2304
Cdd:pfam13868 208 AKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2305 ALKQKQLADAEMakhkkfAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDE 2364
Cdd:pfam13868 288 RLEHRRELEKQI------EEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2452-2767 |
4.04e-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: 55.70 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2452 QQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEaegfQKTLEAERQRQLEITANA 2531
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKR----QEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2532 ERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTElATQEKMTLVQTLEIQRQQSDSDAEKlrkaiadlEQEKEKL 2611
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE-KEEEREEDERILEYLKEKAEREEER--------EAEREEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2612 KREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLL-QKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQM 2690
Cdd:pfam13868 179 EEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKErQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAER 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2691 E-QEKKQLTTVLEEARKKQAEAEENVRQKQ----EELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREIM 2765
Cdd:pfam13868 259 EeEEFERMLRKQAEDEEIEQEEAEKRRMKRlehrRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
..
gi 2069539781 2766 IQ 2767
Cdd:pfam13868 339 LK 340
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2042-2274 |
4.23e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.03 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2042 EKIAQLKKSS---ESELERqkslvddtvrqrrlvEEEIRILKLNFEKA-SHGKTDLELELTRIKQSAEEIQRSKEQAERE 2117
Cdd:COG2268 192 RKIAEIIRDAriaEAEAER---------------ETEIAIAQANREAEeAELEQEREIETARIAEAEAELAKKKAEERRE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2118 AEELRQLAlEEENHRREAEAKvKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAekESERQIQLAQEAAQKRIV 2197
Cdd:COG2268 257 AETARAEA-EAAYEIAEANAE-REVQRQLEIAEREREIELQEKEAEREEAELEADVRKPA--EAEKQAAEAEAEAEAEAI 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2198 AEEKAHLAAVQQKEQELLQTRQQEQ---SILDKLREEAERAKKAAEDAEFARI--KAEQEAALSRQLVEEAERMKQRAEE 2272
Cdd:COG2268 333 RAKGLAEAEGKRALAEAWNKLGDAAillMLIEKLPEIAEAAAKPLEKIDKITIidGGNGGNGAGSAVAEALAPLLESLLE 412
|
..
gi 2069539781 2273 EA 2274
Cdd:COG2268 413 ET 414
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1252-1854 |
4.76e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.77 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1252 DLIRKYEEQLKDVQAVPSDLKALEATKAELKRLRGQVEGHQPLFNTLEmdlakaSEVNERMVRGHSERDIDLDRYRERVQ 1331
Cdd:pfam12128 231 QAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQ------EERQETSAELNQLLRTLDDQWKEKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1332 QLLERWQAILAQIDLRQRELDQLGRQLRYYR----ESY----DWLIQWIREARQRQEHLQAVPVTNSKSVREQLLQEKKL 1403
Cdd:pfam12128 305 ELNGELSAADAAVAKDRSELEALEDQHGAFLdadiETAaadqEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1404 LEECDRNREKVEECQcfakqyiDAIKD-YELQLVTYKAQVEPVASPAKKPKVQSASDSVIQEYvDLRTRYSELTTLTSQy 1482
Cdd:pfam12128 385 KEQNNRDIAGIKDKL-------AKIREaRDRQLAVAEDDLQALESELREQLEAGKLEFNEEEY-RLKSRLGELKLRLNQ- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1483 LKFITETLRRLEEEEKAAEKLKEEERQRLAEVEA---QLEKQRQLAEAHARAKAQAEKEALELQRRMEE--EVSRRQLVA 1557
Cdd:pfam12128 456 ATATPELLLQLENFDERIERAREEQEAANAEVERlqsELRQARKRRDQASEALRQASRRLEERQSALDEleLQLFPQAGT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1558 VDAEQQKQTIQQELSQMKLSSDAQIqAKLKLIEEVEFSRRKVEEEIRMVRLQLEATE------------RQRAGAEDELQ 1625
Cdd:pfam12128 536 LLHFLRKEAPDWEQSIGKVISPELL-HRTDLDPEVWDGSVGGELNLYGVKLDLKRIDvpewaaseeelrERLDKAEEALQ 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1626 ALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKH--------KVQAEQQAAREKQKALEDLQKLRLQAEEA 1697
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRlfdekqseKDKKNKALAERKDSANERLNSLEAQLKQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1698 ERRMKQA--------------------ELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLEL-SLQQEHITITHLQ 1756
Cdd:pfam12128 695 DKKHQAWleeqkeqkreartekqaywqVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLaSLGVDPDVIAKLK 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1757 EEAERLKKLQLEAEQSREEAdKEVEKWRQK--ANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALR 1834
Cdd:pfam12128 775 REIRTLERKIERIAVRRQEV-LRYFDWYQEtwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEK 853
|
650 660
....*....|....*....|
gi 2069539781 1835 QKELAEQELEKQRKLAEGTA 1854
Cdd:pfam12128 854 QQVRLSENLRGLRCEMSKLA 873
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1560-1740 |
5.33e-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: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1560 AEQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRmvrlqleaTERQRAGAEDELQAlrdrAEEAERQKR 1639
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK--------ELEQRAAAEKAAKQ----AEQAAKQAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1640 LAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQ-KALEDLQKlrlQAEEAERRMKQ-AELEKERQVQLAHE 1717
Cdd:TIGR02794 116 EKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKaKAAAEAKK---KAEEAKKKAEAeAKAKAEAEAKAKAE 192
|
170 180
....*....|....*....|...
gi 2069539781 1718 AAQKSAEADLQSRRLSFAEKTAQ 1740
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEA 215
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2242-2667 |
5.37e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2242 AEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQtkakaQEDAEKLRKEAELEAARRAQAEQaalkQKQLADAEMAKhkk 2321
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELRRELYTSRRQLAAE-----QYRLVEMARELAELNEAESDLEQ----DYQAASDHLNL--- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2322 fAEQTLRQKAQVEQ---ELTKVKLQLEEtdhQKSILEEEQqrlkDEVTEAMKQKVQVEEELFKVKVQmeeLIKLKTRIEE 2398
Cdd:PRK04863 340 -VQTALRQQEKIERyqaDLEELEERLEE---QNEVVEEAD----EQQEENEARAEAAEEEVDELKSQ---LADYQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2399 ENKMLItkdKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEA--ARLRELAEQ--DLAQQRSLAEKILKEKMQAVQEATRL 2474
Cdd:PRK04863 409 QQTRAI---QYQQAVQALERAKQLCGLPDLTADNAEDWLEEfqAKEQEATEEllSLEQKLSVAQAAHSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2475 KAEAEVLQkqkdlAQEQAKKLQEDKEQMQLrLAEEAEGFQKTLeAERQRQLEITANAERLkvqvtelsLAQAKaeeeakr 2554
Cdd:PRK04863 486 AGEVSRSE-----AWDVARELLRRLREQRH-LAEQLQQLRMRL-SELEQRLRQQQRAERL--------LAEFC------- 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2555 fkkqaeqisQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQK--EQ 2632
Cdd:PRK04863 544 ---------KRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDalAR 614
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2069539781 2633 LRQE-----------TQMLQQTFRSEKDVLLQKERfVEEEKAKLEK 2667
Cdd:PRK04863 615 LREQsgeefedsqdvTEYMQQLLERERELTVERDE-LAARKQALDE 659
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
172-296 |
5.41e-07 |
|
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: 51.43 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 172 ADERDRVQKKTFTKWVNKHLlkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPrerdvirnLRLPREKGRMRFHK 251
Cdd:cd21222 10 APEKLAEVKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVP--------LHEYHLTPSTDDEK 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2069539781 252 LQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 296
Cdd:cd21222 77 LHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2073-2367 |
5.52e-07 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 55.76 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2073 EEEIRILKLNFEKASHGKTDLELELTRiKQSAEEIQRSKEQAEREA--EELRQLALEEENHRREAEAKVKKISAAEQEAA 2150
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVA-KHGAEISKLEEENREKEKalPKNDDMTIEEAKRRAAAAAKAKAAALAKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2151 RQCKAALEEVErlKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLRE 2230
Cdd:PRK07735 81 GTEEVTEEEKA--KAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2231 EAERAKKAAEDAEFARIKAeqeAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQ 2310
Cdd:PRK07735 159 ETDKEKAKAKAAAAAKAKA---AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2311 LADAEMAKHKKfAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTE 2367
Cdd:PRK07735 236 KAKAIAAAKAK-AAAAARAKTKGAEGKKEEEPKQEEPSVNQPYLNKYVEVIKEKLGE 291
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4303-4331 |
5.53e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.86 E-value: 5.53e-07
10 20
....*....|....*....|....*....
gi 2069539781 4303 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4331
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2411-2791 |
6.40e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.67 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2411 MQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQE 2490
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2491 QAKKLQEDKEQMQLRLaEEAEGFQKTLEaerQRQLEITANAERLKVQVtELSLAQAKAEEEAKrfkkqaEQISQKLHQTE 2570
Cdd:pfam07888 116 EKDALLAQRAAHEARI-RELEEDIKTLT---QRVLERETELERMKERA-KKAGAQRKEEEAER------KQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2571 LATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQkEQLRQETQMLQQTFRSEKDV 2650
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ-ERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2651 LLQKERFVEE-EKAKLEkLFQEEVNKAQ-GLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEenVRQKQEELQRLEKQ 2728
Cdd:pfam07888 264 AAQRDRTQAElHQARLQ-AAQLTLQLADaSLALREGRARWAQERETLQQSAEADKDRIEKLSAE--LQRLEERLQEERME 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2729 RQKQEKLLAEEN--------------QKLREKLEQLQEEQKTALAQTREIMIQTDDLPQ--EVVAPSQVPQMKAVPNGR 2791
Cdd:pfam07888 341 REKLEVELGREKdcnrvqlsesrrelQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQrlETVADAKWSEAALTSTER 419
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2346-2771 |
6.84e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 55.73 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2346 ETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLktRIEEENKMLITKDKDNMQKFLAEEAEKM--K 2423
Cdd:COG5185 129 EIVALKDELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQN--LKKLEIFGLTLGLLKGISELKKAEPSGTvnS 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2424 QVAEEAARLSVE-----AQEAARLRELAEQDLAQQRSLAEKI------LKEKMQAVQE--ATRLKAEAEVLQKQKDLAQE 2490
Cdd:COG5185 207 IKESETGNLGSEstlleKAKEIINIEEALKGFQDPESELEDLaqtsdkLEKLVEQNTDlrLEKLGENAESSKRLNENANN 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2491 QAKKLQEDKEQMQlRLAEEAEGFQKTLEAERQ-RQLEITANAERLKVQVT--------ELSLAQAKAEEEAKRFKKQAEQ 2561
Cdd:COG5185 287 LIKQFENTKEKIA-EYTKSIDIKKATESLEEQlAAAEAEQELEESKRETEtgiqnltaEIEQGQESLTENLEAIKEEIEN 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2562 ISQkLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAEllqQKSEEMQTAQKEQLRQETQMLQ 2641
Cdd:COG5185 366 IVG-EVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD---RQIEELQRQIEQATSSNEEVSK 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2642 QTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEE 2721
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQ 521
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2722 LQRLEK---QRQKQEKLLAEEN-QKLREKLEQLQEE--QKTALAQTREIMIQTDDL 2771
Cdd:COG5185 522 VAESLKdfmRARGYAHILALENlIPASELIQASNAKtdGQAANLRTAVIDELTQYL 577
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2394-2721 |
9.88e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 54.66 E-value: 9.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2394 TRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEA-ARLRELAEQDLAQQRSLAEKILKEKMQAVQEAT 2472
Cdd:pfam15558 15 ARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQeQWQAEKEQRKARLGREERRRADRREKQVIEKES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2473 RLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQ-LRLAEEAEGFQKTLEAERQRQLEITANAERLKVQvtelslaQAKAEEE 2551
Cdd:pfam15558 95 RWREQAEDQENQRQEKLERARQEAEQRKQCQeQRLKEKEEELQALREQNSLQLQERLEEACHKRQL-------KEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2552 AKRFKKQAEQISQKLHQTELATQEKMTLVQ---TLEIQRQQSDSDAEKLRKAiaDLEQEKEKLKREAELLQQ------KS 2622
Cdd:pfam15558 168 KVQENNLSELLNHQARKVLVDCQAKAEELLrrlSLEQSLQRSQENYEQLVEE--RHRELREKAQKEEEQFQRakwraeEK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2623 EEMQTAQKEQLRQETQ--MLQQTFRSEKDVLLQKERFVE--EEKAKLEKLFQEEVNKA-----QGLKAEQERQQKQMEQE 2693
Cdd:pfam15558 246 EEERQEHKEALAELADrkIQQARQVAHKTVQDKAQRARElnLEREKNHHILKLKVEKEekchrEGIKEAIKKKEQRSEQI 325
|
330 340
....*....|....*....|....*...
gi 2069539781 2694 KKQLTTVLEEARKKqAEAEENVRQKQEE 2721
Cdd:pfam15558 326 SREKEATLEEARKT-ARASFHMREKVRE 352
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2017-2291 |
1.07e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 55.34 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2017 RLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLkksseselERQKslvddtvrqrrlVEEEIRILKLNFEKASHGKTDLELE 2096
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARFEARQARL--------EREK------------AAREARHKKAAEARAAKDKDAVAAA 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2097 LTRIK-QSAEEIQRSKEQAEREAEELRQLALEEEnhrREAEAKVKKISAAEQEAARQCKAALEE-VERlkAKAEEARRQK 2174
Cdd:PRK05035 492 LARVKaKKAAATQPIVIKAGARPDNSAVIAAREA---RKAQARARQAEKQAAAAADPKKAAVAAaIAR--AKAKKAAQQA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2175 ELAEKESERQIQLAQEAAQkriVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAK--KAAEDAEFARI----- 2247
Cdd:PRK05035 567 ANAEAEEEVDPKKAAVAAA---IARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKakKAEQQANAEPEepvdp 643
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2069539781 2248 -KAEQEAALSRqlveeaERMKQRAEEEAQTKAKAQEDAEKLRKEA 2291
Cdd:PRK05035 644 rKAAVAAAIAR------AKARKAAQQQANAEPEEAEDPKKAAVAA 682
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1758-1978 |
1.16e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 54.08 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1758 EAERLKKL-----QLEAEQSREEADKEVEKWRQKANEALRlrlQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESA 1832
Cdd:TIGR02794 66 EQERQKKLeqqaeEAEKQRAAEQARQKELEQRAAAEKAAK---QAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAER 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1833 LRQKELAEQELEKQRKLAEGTAQQKflaeQELIRLKAEVEngeqqrllleeelfrlKNEVNEAVQKRKeleEELAKLRAE 1912
Cdd:TIGR02794 143 KAKEEAAKQAEEEAKAKAAAEAKKK----AEEAKKKAEAE----------------AKAKAEAEAKAK---AEEAKAKAE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1913 melllQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRA 1978
Cdd:TIGR02794 200 -----AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2662-2764 |
1.20e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.78 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2662 KAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKkqLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQ 2741
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100
....*....|....*....|...
gi 2069539781 2742 KLREKLEQLQEEQKTALAQTREI 2764
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQEL 126
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1894-2179 |
1.20e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.87 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1894 EAVQKRKELEEELAKLRAEMELllQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQL----- 1968
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEP--NEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFdptia 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1969 ------AEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAEN--ERLRRLAEDEAYQRRLLEEQAAQHKQDI 2040
Cdd:pfam02029 95 dekesvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKwsTEVRQAEEEGEEEEDKSEEAEEVPTENF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2041 ------EEKIAQLKKSSESEL--ERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSA----EEIQ 2108
Cdd:pfam02029 175 akeevkDEKIKKEKKVKYESKvfLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAeqklEELR 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2109 RSK-EQAEREAEELRQ------LALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEK 2179
Cdd:pfam02029 255 RRRqEKESEEFEKLRQkqqeaeLELEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1577-1790 |
1.23e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1577 SSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKD-- 1654
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1655 -ESQKKREAEDELK------------HKVQAEQQAAREKQKALEDLQKLRLQAEEaerrmKQAELEKERQVQLAHEAAQK 1721
Cdd:COG3883 93 rALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEA-----KKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1722 SAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEA 1790
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2327-2855 |
1.28e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.91 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2327 LRQKAQVEQ-ELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEEliklKTRIEEEnkmliT 2405
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM----KNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2406 KDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQK 2485
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2486 DlAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEaerqrqleitaNAERLKvqvtelslaqAKAEEEAKRFKKQAEQISQK 2565
Cdd:PRK01156 339 N-DYIKKKSRYDDLNNQILELEGYEMDYNSYLK-----------SIESLK----------KKIEEYSKNIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2566 LHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQ--------------QKSEEMQTAQKE 2631
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttlgeEKSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2632 QLRQETQMLQQTFRSEKDVLLQKerfvEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTvLEEARKKQAEA 2711
Cdd:PRK01156 477 KKSRLEEKIREIEIEVKDIDEKI----VDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINE-LKDKHDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2712 EEnvRQKQEELQRLEKQRQKQEKLLAEEN----QKLREKLEQLQEEQKTALAQTREIMIQTDDLpqEVVAPSQVPQMK-A 2786
Cdd:PRK01156 552 KN--RYKSLKLEDLDSKRTSWLNALAVISlidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDD--KSYIDKSIREIEnE 627
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2787 VPNGRDMIDGISQNgeaELAFDGIRQKVSAKKLAEAGILSREsmeklaKGKATVQ-ELSQRDDIRRYLRG 2855
Cdd:PRK01156 628 ANNLNNKYNEIQEN---KILIEKLRGKIDNYKKQIAEIDSII------PDLKEITsRINDIEDNLKKSRK 688
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2171-2544 |
1.30e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 54.76 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2171 RRQKELAEKESERQIQLAQEAAQKRIVAEEKA---HLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARI 2247
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEAtkdAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2248 KAEQEAALS-RQLVEEAERMKQRAEEEAQTKAKAQedAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQT 2326
Cdd:pfam09731 157 QAVKAHTDSlKEASDTAEISREKATDSALQKAEAL--AEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2327 LRQKAQVEQELTKVKlQLEETDHQksILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQmeeliKLKTRIEEENKMLITK 2406
Cdd:pfam09731 235 VEKAQSLAKLVDQYK-ELVASERI--VFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIA-----HAHREIDQLSKKLAEL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2407 dKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEkiLKEKMQAVQEATRLKAEAEVLQKQKD 2486
Cdd:pfam09731 307 -KKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREE--IRESYEEKLRTELERQAEAHEEHLKD 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2487 LAQEQAKKLQEDKEQ-MQLRLAEEAEGFQKTLEA------ERQRQLEITANAERLKVQVTELSLA 2544
Cdd:pfam09731 384 VLVEQEIELQREFLQdIKEKVEEERAGRLLKLNEllanlkGLEKATSSHSEVEDENRKAQQLWLA 448
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2089-2292 |
1.30e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 54.62 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2089 GKTDLELELTRIKQSA--EEIQRSKEQAEREAEELRQLALEEENHRREAeAKVKKISAaeQEAARQCKAALEEVERLKAK 2166
Cdd:pfam05262 152 GKTQIVIPLKKNILSGnvSDVDTDSISDKKVVEALREDNEKGVNFRRDM-TDLKERES--QEDAKRAQQLKEELDKKQID 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2167 AEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAhlAAVQQKEQELLQTRQqeqsildklREEAERAKKAAEDAEFAR 2246
Cdd:pfam05262 229 ADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPA--DTSSPKEDKQVAENQ---------KREIEKAQIEIKKNDEEA 297
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2069539781 2247 IKAEQEAALS-RQLVEEAERMKQRAEEEAQTKAK-AQEDAEKLRKEAE 2292
Cdd:pfam05262 298 LKAKDHKAFDlKQESKASEKEAEDKELEAQKKREpVAEDLQKTKPQVE 345
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1889-2241 |
1.30e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.52 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1889 KNEVNEAVQKRKELEEELAKLRAEMELLLQskaKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQL 1968
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESRVA---ELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1969 AEEEATHQRAEAERILKEKLvainEASRLKAEAEIA---LKEKEAENERLR-RLAEDEAYQRRL-LEEQAAQHKQDIEEK 2043
Cdd:pfam07888 131 IRELEEDIKTLTQRVLERET----ELERMKERAKKAgaqRKEEEAERKQLQaKLQQTEEELRSLsKEFQELRNSLAQRDT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2044 IAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQ 2123
Cdd:pfam07888 207 QVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2124 LALEEENHRREAEAKVKKISAAEQEAARQCKAALE----EVERLKAKAEEARRQKELAEKE--SERQIQLAQEAAQKRIV 2197
Cdd:pfam07888 287 QLADASLALREGRARWAQERETLQQSAEADKDRIEklsaELQRLEERLQEERMEREKLEVElgREKDCNRVQLSESRREL 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2069539781 2198 AEEKAHLaAVQQKEQELLQTRQQEqsILDKLREEAERAKKAAED 2241
Cdd:pfam07888 367 QELKASL-RVAQKEKEQLQAEKQE--LLEYIRQLEQRLETVADA 407
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1718-1954 |
1.47e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.11 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1718 AAQKSAEaDLQSRRLSFAEK---TAQLELS---LQQEHITITHLQEEA--------ERLKKLQLEAEQSREEADKEVEKW 1783
Cdd:COG2268 137 AAQMTVE-ELNEDREKFAEKvqeVAGTDLAkngLELESVAITDLEDENnyldalgrRKIAEIIRDARIAEAEAERETEIA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1784 RQKANEALRL-RLQAEEVAHKKALAQEEAEKQKEDAEREA---RKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKfL 1859
Cdd:COG2268 216 IAQANREAEEaELEQEREIETARIAEAEAELAKKKAEERReaeTARAEAEAAYEIAEANAEREVQRQLEIAEREREIE-L 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1860 AEQELIRlkaevengeqqrllLEEELFRLKNEVNEAVQKRKELEE--ELAKLRAEMELLLQSKAKTEEESRSTSEksKQI 1937
Cdd:COG2268 295 QEKEAER--------------EEAELEADVRKPAEAEKQAAEAEAeaEAEAIRAKGLAEAEGKRALAEAWNKLGD--AAI 358
|
250
....*....|....*..
gi 2069539781 1938 LEAEASKLRELAEEAAR 1954
Cdd:COG2268 359 LLMLIEKLPEIAEAAAK 375
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1699-2020 |
1.52e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1699 RRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHitithlqeeAERLKKLQLEAEQSREEADK 1778
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI---------EEREQKRQEEYEEKLQEREQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1779 EVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEgtAQQKF 1858
Cdd:pfam13868 103 MDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER--EEIEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1859 LAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRsTSEKSKQIL 1938
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKER-RLAEEAERE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1939 EAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRL 2018
Cdd:pfam13868 260 EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
..
gi 2069539781 2019 AE 2020
Cdd:pfam13868 340 KE 341
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
181-292 |
1.54e-06 |
|
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: 49.64 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 181 KTFTKWVNKHLLKhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPRERDVirnlrlPREKGRMrfhkLQNVQIALD 260
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGC------PRSQSQM----IENVDVCLS 69
|
90 100 110
....*....|....*....|....*....|..
gi 2069539781 261 YLKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 292
Cdd:cd21286 70 FLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2035-2378 |
1.57e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 54.34 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2035 QHKQDIEEKIAQLKKSSeSELERQKSLVDDTVRQRRLVEEEIRILKlnfekashgKTDLELELTRIKQSAEEI---QRSK 2111
Cdd:pfam03528 1 QPDEDLQQRVAELEKEN-AEFYRLKQQLEAEFNQKRAKFKELYLAK---------EEDLKRQNAVLQEAQVELdalQNQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2112 EQAEREAEELRQLALEEENHRREAEAKVKKisaaeqeaarqckAALEEVERLKAKAEEARRqkelaEKESERQIQLAQEA 2191
Cdd:pfam03528 71 ALARAEMENIKAVATVSENTKQEAIDEVKS-------------QWQEEVASLQAIMKETVR-----EYEVQFHRRLEQER 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2192 AQ----KRIVAEEKAHLaavqqkeQELLQTRQQEQSILDKLreeaeraKKAAEDAEFAR---IKAEQE-AALSRQLVEEA 2263
Cdd:pfam03528 133 AQwnqyRESAEREIADL-------RRRLSEGQEEENLEDEM-------KKAQEDAEKLRsvvMPMEKEiAALKAKLTEAE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2264 ERMKQ-------------RAEEEAQT------------KAKAQEDAEKLRKEAEleaARRAQAEQAALKQKQLADAEMAK 2318
Cdd:pfam03528 199 DKIKEleaskmkelnhylEAEKSCRTdlemyvavlntqKSVLQEDAEKLRKELH---EVCHLLEQERQQHNQLKHTWQKA 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2319 HKKFAEQT---LRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEvteamKQKVQVEEE 2378
Cdd:pfam03528 276 NDQFLESQrllMRDMQRMESVLTSEQLRQVEEIKKKDQEEHKRARTHKE-----KETLKSDRE 333
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1618-1855 |
1.78e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1618 AGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEA 1697
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1698 ERRMKQAElekerqvqlaheAAQKSAEADLQSRRLS-FAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEA 1776
Cdd:COG3883 92 ARALYRSG------------GSVSYLDVLLGSESFSdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1777 DKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQ 1855
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3623-3659 |
1.79e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 1.79e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2069539781 3623 IRLLEAQIATGGIIDPVHSHRLPVEVAYKRGYFDEQM 3659
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2184-2506 |
1.89e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 54.67 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2184 QIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILD--KLREEAeRAKKAAEDAEFARIKAEQEAA------- 2254
Cdd:PRK10929 34 QAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNfpKLSAEL-RQQLNNERDEPRSVPPNMSTDaleqeil 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2255 --------LSRQLVEEAERMKQRAEEEAQTKAKaQEDAEKLRKEAElEAARRAQAEQAALKQKQLADAEMakhkkfaeQT 2326
Cdd:PRK10929 113 qvssqlleKSRQAQQEQDRAREISDSLSQLPQQ-QTEARRQLNEIE-RRLQTLGTPNTPLAQAQLTALQA--------ES 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2327 LRQKAQVEQ-ELTkvklQLEETDHQksileeEQQRLKDEVteAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLIT 2405
Cdd:PRK10929 183 AALKALVDElELA----QLSANNRQ------ELARLRSEL--AKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2406 KDKDNMQKFLAEEaekMKQVAEEAARLSVEAQE----AARLRELAEQDLAQQRSLAekILKEKMQAVQEATRLkaeAEVL 2481
Cdd:PRK10929 251 EQSGDLPKSIVAQ---FKINRELSQALNQQAQRmdliASQQRQAASQTLQVRQALN--TLREQSQWLGVSNAL---GEAL 322
|
330 340
....*....|....*....|....*
gi 2069539781 2482 QKQKDLAQEQAKKLQEDKEQMQLRL 2506
Cdd:PRK10929 323 RAQVARLPEMPKPQQLDTEMAQLRV 347
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1893-2253 |
2.05e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 54.19 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1893 NEAVQKRKELEE--ELAKLRAEMELLLQSKAKTEEESRSTSEK-----SKQILEAEASKLRELAEEAARLRALSEEAKRQ 1965
Cdd:COG5185 170 QELNQNLKKLEIfgLTLGLLKGISELKKAEPSGTVNSIKESETgnlgsESTLLEKAKEIINIEEALKGFQDPESELEDLA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1966 RQLAE-EEATHQRAEaerILKEKLVAINEAS-RLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEK 2043
Cdd:COG5185 250 QTSDKlEKLVEQNTD---LRLEKLGENAESSkRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2044 IAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEkASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQ 2123
Cdd:COG5185 327 LEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQ 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2124 LALEEEN-----HRREAEAKVKKISAAE---QEAARQCKAALEEVERLKAKAEEARRQK-ELAEKESERQIQLAQEAAQK 2194
Cdd:COG5185 406 EILATLEdtlkaADRQIEELQRQIEQATssnEEVSKLLNELISELNKVMREADEESQSRlEEAYDEINRSVRSKKEDLNE 485
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2195 RIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEA 2253
Cdd:COG5185 486 ELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENL 544
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1557-1725 |
2.18e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.66 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1557 AVDAEQQKQTIQQELSQMKLSSDAQIQAKLKLIEEvefsrrkveEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAER 1636
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK---------ERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1637 QKRLAQEEAERLrkqvkDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAE-----EAERRMKQAELEKERQ 1711
Cdd:PRK09510 145 AKAKAEAEAKRA-----AAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEakkkaEAEAKKKAAAEAKKKA 219
|
170
....*....|....
gi 2069539781 1712 VQLAHEAAQKSAEA 1725
Cdd:PRK09510 220 AAEAKAAAAKAAAE 233
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2345-2775 |
2.20e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 53.92 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2345 EETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEenkmlitkdkdnmqkfLAEEAEKMkQ 2424
Cdd:pfam05622 17 HELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQ----------------LQEENFRL-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2425 VAEEAARLSVEAQEaarlRELAEQDLAQQrslaekilkEKMQAVQEATRLKAEAEVLQKQKDLAQ------EQAKKLQED 2498
Cdd:pfam05622 80 TARDDYRIKCEELE----KEVLELQHRNE---------ELTSLAEEAQALKDEMDILRESSDKVKkleatvETYKKKLED 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2499 ----KEQMQLRLAEEAEGFQKT--LEAERQRQLEITANAERLKVQVTELslaQAKAEEEAKRFKKQAEQISQKlhqtela 2572
Cdd:pfam05622 147 lgdlRRQVKLLEERNAEYMQRTlqLEEELKKANALRGQLETYKRQVQEL---HGKLSEESKKADKLEFEYKKL------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2573 tQEKMTLVQtleiqrqqsdsdaeklrkaiadleQEKEKLKREAELLQQKSEEMQTAQKEQ--LRQETQMLQQTFRSEKDv 2650
Cdd:pfam05622 217 -EEKLEALQ------------------------KEKERLIIERDTLRETNEELRCAQLQQaeLSQADALLSPSSDPGDN- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2651 lLQKERFVEEEKAKLEKLFQEevNKAQGLKAEQERQQKQMEqekkqLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQ 2730
Cdd:pfam05622 271 -LAAEIMPAEIREKLIRLQHE--NKMLRLGQEGSYRERLTE-----LQQLLEDANRRKNELETQNRLANQRILELQQQVE 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2731 KQEKLLAEENQK------LREKLEQLQEEQKTALAQTREIMIQTDDLPQEV 2775
Cdd:pfam05622 343 ELQKALQEQGSKaedsslLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ 393
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4086-4123 |
2.22e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.22e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2069539781 4086 KKFLEGTSCIAGVYVDSTKERLSVYQAMKKGIIRPGTA 4123
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2416-2760 |
2.24e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 54.29 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2416 AEEAEKMKQVAEEAARLSVE-AQEAARLRE--------LAEQDLAQQ-RSLAEKILKEKMQAVQEATRLKAEAEVLQKqk 2485
Cdd:PRK10929 64 LERAKQYQQVIDNFPKLSAElRQQLNNERDeprsvppnMSTDALEQEiLQVSSQLLEKSRQAQQEQDRAREISDSLSQ-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2486 dLAQEQ--AKKLQEDKEQmqlRLaeEAEGFQKTLEAERQRQLeITANAERLKVQVTELSLAQAKA--EEEAKR-----FK 2556
Cdd:PRK10929 142 -LPQQQteARRQLNEIER---RL--QTLGTPNTPLAQAQLTA-LQAESAALKALVDELELAQLSAnnRQELARlrselAK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2557 KQAEQISQKLHQtelatqekmtLVQTLEIQRQQSDSDA----EKLRKAIADLEQ---EKEKLKRE-AELLQQKSEEMQ-- 2626
Cdd:PRK10929 215 KRSQQLDAYLQA----------LRNQLNSQRQREAERAlestELLAEQSGDLPKsivAQFKINRElSQALNQQAQRMDli 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2627 TAQKEQLRQETQMLQQ---TFRSEKDVLLQKERFVEEEKAKLEKLfqEEVNKAQglkaeqerqqkQMEQEKKQLttvlee 2703
Cdd:PRK10929 285 ASQQRQAASQTLQVRQalnTLREQSQWLGVSNALGEALRAQVARL--PEMPKPQ-----------QLDTEMAQL------ 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2704 aRKKQAEAEEnvrqKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQ 2760
Cdd:PRK10929 346 -RVQRLRYED----LLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRELLNSLLS 397
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1509-1771 |
2.31e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 54.29 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1509 QRLAEVEAQL-EKQRQLAEAHARAKAQAEKEALELQRRMEeevSRRQLVavDAEQQKQTIQQELSQMKLSSDAQIQAKL- 1586
Cdd:PRK10929 109 QEILQVSSQLlEKSRQAQQEQDRAREISDSLSQLPQQQTE---ARRQLN--EIERRLQTLGTPNTPLAQAQLTALQAESa 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1587 ---KLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDR--------AEEA-ERQKRLAQEEAErLRKQVKD 1654
Cdd:PRK10929 184 alkALVDELELAQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQlnsqrqreAERAlESTELLAEQSGD-LPKSIVA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1655 ESQKKREAEDELKHKVQ-----AEQQ--AAREKQKALEDLQKLRLQAE---------EAERRMKQAELEKERQVQLAHEA 1718
Cdd:PRK10929 263 QFKINRELSQALNQQAQrmdliASQQrqAASQTLQVRQALNTLREQSQwlgvsnalgEALRAQVARLPEMPKPQQLDTEM 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 1719 AQksaeadLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQ 1771
Cdd:PRK10929 343 AQ------LRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQR 389
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1609-2015 |
2.31e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 53.76 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1609 QLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQ 1688
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1689 KLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLE 1768
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1769 AEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRK 1848
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1849 LAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESR 1928
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1929 STSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEK 2008
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
....*..
gi 2069539781 2009 EAENERL 2015
Cdd:COG5278 511 AAAEAAL 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1508-1700 |
2.46e-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: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEvsRRQLVAVDAEQQKQTIQQELSQMKLSSDA-QIQAKL 1586
Cdd:COG4942 61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ--KEELAELLRALYRLGRQPPLALLLSPEDFlDAVRRL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1587 KLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAeeaerqkrlaQEEAERLRKQVKDesqkKREAEDEL 1666
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL----------EEERAALEALKAE----RQKLLARL 204
|
170 180 190
....*....|....*....|....*....|....*.
gi 2069539781 1667 KHKVQAEQQAAREKQKALEDLQKL--RLQAEEAERR 1700
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALiaRLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2191-2431 |
2.50e-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: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2191 AAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAErmKQRA 2270
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--KEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2271 EEEAQTKAKAQEDAEKLRKeaeLEAARRAQAEQAALKQKQLADAE--MAKHKKFAEQTLRQKAQVE---QELTKVKLQLE 2345
Cdd:COG4942 94 ELRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRadlAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2346 ETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKdkdnMQKFLAEEAEKMKQV 2425
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR----LEAEAAAAAERTPAA 246
|
....*.
gi 2069539781 2426 AEEAAR 2431
Cdd:COG4942 247 GFAALK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2019-2215 |
2.55e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.27 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2019 AEDEAYQRRLLEEQAA---QHKQDIE-EKIAQLKKSSESELERQKSLVDdtvrQRRLVEEEirilklnfEKASHGKTDLE 2094
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAeelQQKQAAEqERLKQLEKERLAAQEQKKQAEE----AAKQAALK--------QKQAEEAAAKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2095 LELTRIKQSAEEiQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQK 2174
Cdd:PRK09510 142 AAAAKAKAEAEA-KRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2069539781 2175 ELAEKESERQIQLAQEAAQKRivAEEKAHLAAVQQKEQELL 2215
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKA--AAAKAAEKAAAAKAAAEV 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2312-2552 |
2.56e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2312 ADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIK 2391
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2392 -LKTRIEEENKMLITKDKDNMQKFLaEEAEKMKQVAEEAARLsVEAQEAARlrelaeQDLAQQRSLAEKILKEKMQAVQE 2470
Cdd:COG3883 94 aLYRSGGSVSYLDVLLGSESFSDFL-DRLSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2471 ATRLKAEaevLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEE 2550
Cdd:COG3883 166 LEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
..
gi 2069539781 2551 EA 2552
Cdd:COG3883 243 AA 244
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1595-1946 |
2.76e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 53.72 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1595 SRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQ 1674
Cdd:pfam02029 32 VTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1675 QAAREKQKALEDlQKLRLQAEEAERRMKQAELEKERQVQLAHE-----AAQKSAEADLQSRRLSFAEKTAQLELSLQQEH 1749
Cdd:pfam02029 112 NSSWEKEEKRDS-RLGRYKEEETEIREKEYQENKWSTEVRQAEeegeeEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1750 ITITHLQEEAERLKklqleAEQSREEADKEVEKWRQKANEALRLRLQAEEvahkkalAQEEAEKQKEdAERearkrsKAE 1829
Cdd:pfam02029 191 KYESKVFLDQKRGH-----PEVKSQNGEEEVTKLKVTTKRRQGGLSQSQE-------REEEAEVFLE-AEQ------KLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1830 ESALRQKELAEQELEKQRklaegtaQQKFLAEQELIRLKAEVEngeqqrllleeelfrlknevneavQKRKELEEELAKL 1909
Cdd:pfam02029 252 ELRRRRQEKESEEFEKLR-------QKQQEAELELEELKKKRE------------------------ERRKLLEEEEQRR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2069539781 1910 RAEMElllQSKAKTEEESRstseKSKQILE---AEASKLR 1946
Cdd:pfam02029 301 KQEEA---ERKLREEEEKR----RMKEEIErrrAEAAEKR 333
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2476-2723 |
2.82e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 54.07 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2476 AEAEVlQKQKDLAQEQAKklQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERlKVQVTELSLAQAKAEEEAKRF 2555
Cdd:NF012221 1536 ATSES-SQQADAVSKHAK--QDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQS-QLESTDQNALETNGQAQRDAI 1611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2556 KKQAEQIsqklhqtelaTQEKMTLVQTLEIQRQQSDSDAE---KLRKAIAD--LEQEKEKLKREAELLQQKSEEMQTAQK 2630
Cdd:NF012221 1612 LEESRAV----------TKELTTLAQGLDALDSQATYAGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHV 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2631 EQLRQetqmlqqtfrsEKDVLLQKERFV---EEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKK 2707
Cdd:NF012221 1682 DNQQK-----------VKDAVAKSEAGVaqgEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSR 1750
|
250 260
....*....|....*....|
gi 2069539781 2708 ----QAEAEENVRQKQEELQ 2723
Cdd:NF012221 1751 geqdASAAENKANQAQADAK 1770
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2587-2756 |
2.83e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 53.68 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2587 RQQSDSDAEKLRKAIADLEQekekLKREAEllqQKSEEMqtaqkEQLRQETQMLQQtfrsekDVLLQKERFVEEEKAKLE 2666
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEE----LERELE---QKAEEA-----EALLKEAEKLKE------ELEEKKEKLQEEEDKLLE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2667 KLfQEEVNKA-QGLKAEQERQQKQM-EQEKKQLTTV----LEEARKKQAEAEENV-------RQKQEELQ-----RLEKQ 2728
Cdd:PRK00409 570 EA-EKEAQQAiKEAKKEADEIIKELrQLQKGGYASVkaheLIEARKRLNKANEKKekkkkkqKEKQEELKvgdevKYLSL 648
|
170 180 190
....*....|....*....|....*....|....*..
gi 2069539781 2729 RQKQEKLLAEENQ---------KLREKLEQLQEEQKT 2756
Cdd:PRK00409 649 GQKGEVLSIPDDKeaivqagimKMKVPLSDLEKIQKP 685
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2086-2292 |
3.39e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2086 ASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLaleeenhRREAEAKVKKISAAEQEAARQCKAALEEVERLKA 2165
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-------LAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2166 KAEEARRQKELAEKESERQIQLAQEA------------------------------AQKRIVAEEKAHLAAVQQKEQELL 2215
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLgrqpplalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2216 QTRQQEQSILDKLREEAERAKKAAEDaefariKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAE 2292
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAE------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4088-4126 |
3.46e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 46.55 E-value: 3.46e-06
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 4088 FLEGTSCIAGVYVDSTKERLSVYQAMKKGIIRPGTAFEL 4126
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
2558-2728 |
3.54e-06 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 53.51 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2558 QAEQI--SQKLHQTELATQEKMTLVQTLEIQRQQSDSDaeklrkaIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQ 2635
Cdd:pfam10168 539 RATQVfrEEYLKKHDLAREEIQKRVKLLKLQKEQQLQE-------LQSLEEERKSLSERAEKLAEKYEEIKDKQEKLMRR 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2636 ETQMLQQtFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEK---KQLTTVLEEARKKQaeAE 2712
Cdd:pfam10168 612 CKKVLQR-LNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAKKKMNYQRYQIAKSQsirKKSSLSLSEKQRKT--IK 688
|
170
....*....|....*.
gi 2069539781 2713 ENVRQKQEELQRLEKQ 2728
Cdd:pfam10168 689 EILKQLGSEIDELIKQ 704
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1515-2149 |
3.57e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 53.65 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1515 EAQLEKQRQLAEAHARAKAQAEKEALELQRrmeeevSRRQLVAVDAEQQKQTIQQELSQMKLSS-DAQIQAKLKLieeve 1593
Cdd:PRK10246 258 EASRRQQALQQALAAEEKAQPQLAALSLAQ------PARQLRPHWERIQEQSAALAHTRQQIEEvNTRLQSTMAL----- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1594 fsRRkveeEIRmvrlqlEATERQRAGAEDELQALRDRAEEAERQKRLAQEEA---ERLRKQVKDESQKKREAE--DELKH 1668
Cdd:PRK10246 327 --RA----RIR------HHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAgwrAQFSQQTSDREQLRQWQQqlTHAEQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1669 KVQA-----------EQQAAREKQKALEDLQK--LRLQAEEAERRMKQAELEKERQvqlAHEAAQKSAEADLQSRRLSFA 1735
Cdd:PRK10246 395 KLNAlpaitltltadEVAAALAQHAEQRPLRQrlVALHGQIVPQQKRLAQLQVAIQ---NVTQEQTQRNAALNEMRQRYK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1736 EKtaqlelslQQEHITITHLQEEAERLKKlqLEAEQSREEADKEVEkwrqkanealrLRLQAEEVAHKKALAQEEAEKQK 1815
Cdd:PRK10246 472 EK--------TQQLADVKTICEQEARIKD--LEAQRAQLQAGQPCP-----------LCGSTSHPAVEAYQALEPGVNQS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1816 EDAEREARKRSKAEESALRQKELaeQELEKQRKLAEGTAQQKFLAEQELIRLKAEVengeqqrLLLEEELFRLKNEVNEA 1895
Cdd:PRK10246 531 RLDALEKEVKKLGEEGAALRGQL--DALTKQLQRDESEAQSLRQEEQALTQQWQAV-------CASLNITLQPQDDIQPW 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1896 VQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTS--EKSKQILEAE----ASKLRELAEEAARLRALSEEAKRQRQLA 1969
Cdd:PRK10246 602 LDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQqiEQRQQQLLTAlagyALTLPQEDEEASWLATRQQEAQSWQQRQ 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1970 EEEATHQ-------------------RAEAERILKEKLVAINEASrLKAEAEIALKEKEAENERLR-------------- 2016
Cdd:PRK10246 682 NELTALQnriqqltplletlpqsddlPHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEAQRlqkaqaqfdtalqa 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2017 -RLAEDEAYQRRLLEEQAAQhkqdieeKIAQLKKSSESELERQKSLVDDTVRQrrlVEEEIRILKLNFEKASHGKTdLEL 2095
Cdd:PRK10246 761 sVFDDQQAFLAALLDEETLT-------QLEQLKQNLENQRQQAQTLVTQTAQA---LAQHQQHRPDGLDLTVTVEQ-IQQ 829
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2096 ELTRIKqsaeeiQRSKEQAEREAEELRQLALEEENhRREAEAKVKKISAAEQEA 2149
Cdd:PRK10246 830 ELAQLA------QQLRENTTRQGEIRQQLKQDADN-RQQQQALMQQIAQATQQV 876
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2964-3000 |
3.59e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.59e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2069539781 2964 IRLLEAQVATGGIIDPVNSHRLPVEVAYKRGYFDEEM 3000
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1598-1764 |
3.69e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1598 KVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKhkvqaEQQAA 1677
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-----NVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1678 REKQKALEDLQKLRLQAEEAERRMKQAELEKErqvqlAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQE 1757
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERIE-----ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*..
gi 2069539781 1758 EAERLKK 1764
Cdd:COG1579 164 EREELAA 170
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2355-2564 |
4.06e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2355 EEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKML---ITKDKDNMQKFLAEEAEKMKQVAEEAAR 2431
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALqaeIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2432 LSVEAQEAARLRELAE----QDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLA 2507
Cdd:COG3883 95 LYRSGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2508 EEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQ 2564
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
306-413 |
4.27e-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: 48.65 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 306 QSEDMTAKEKLLLWSQRMVEGyqgMRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNVENLEQAFSVAEQDLGV 384
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 2069539781 385 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 413
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2002-2447 |
4.35e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.99 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2002 EIALKEKEAENERLRRLAEDEAYQRRLLE--EQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRIL 2079
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2080 KLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEE 2159
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2160 VERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAA 2239
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2240 EDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKH 2319
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2320 KKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEE 2399
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2069539781 2400 NKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAE 2447
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2104-2438 |
4.66e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.95 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2104 AEEIQRSKEQAEREA-EELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLK---AKAEEARRQKelaek 2179
Cdd:pfam02029 4 EEEAARERRRRAREErRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLdrtAKREERRQKR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2180 eserqiqlAQEAAQKRIVAEEKAHLAAVQQKEQElLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQL 2259
Cdd:pfam02029 79 --------LQEALERQKEFDPTIADEKESVAERK-ENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2260 VEEAER--MKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQK--------QLADAEMAKHKKFAEQTLRQ 2329
Cdd:pfam02029 150 RQAEEEgeEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKrghpevksQNGEEEVTKLKVTTKRRQGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2330 KAQVEQELTKVKLQLeETDHQKSILEEEQQRLKDEVTEAMKQKVQ-VEEELFKVKVQMEEliKLKTRIEEENKmlitKDK 2408
Cdd:pfam02029 230 LSQSQEREEEAEVFL-EAEQKLEELRRRRQEKESEEFEKLRQKQQeAELELEELKKKREE--RRKLLEEEEQR----RKQ 302
|
330 340 350
....*....|....*....|....*....|
gi 2069539781 2409 DNMQKFLAEEAEKmKQVAEEAARLSVEAQE 2438
Cdd:pfam02029 303 EEAERKLREEEEK-RRMKEEIERRRAEAAE 331
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1897-2046 |
4.69e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.57 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1897 QKRKELEEELAKLRAEMELLLQSKAKTE-------EESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLA 1969
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEaelakkkAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1970 EEEATHQRAEAERILK-----EKLVAINEAsrlKAEAEIALKEKEAENERLRRLAE-DEAYQRRLLEEQAAQHKQDIEEK 2043
Cdd:COG2268 296 EKEAEREEAELEADVRkpaeaEKQAAEAEA---EAEAEAIRAKGLAEAEGKRALAEaWNKLGDAAILLMLIEKLPEIAEA 372
|
...
gi 2069539781 2044 IAQ 2046
Cdd:COG2268 373 AAK 375
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2022-2236 |
4.80e-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: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2022 EAYQRRLLE---EQAAQHKQDIEEKIAQLKK---SSESELE--RQKSLVDDTVRQRRLVEEEIRILKLNFEKAshgktdl 2093
Cdd:COG3206 159 EAYLEQNLElrrEEARKALEFLEEQLPELRKeleEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEA------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2094 ELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEE--NHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEaR 2171
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ-E 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2172 RQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQ-TRQQE--QSILDKLREEAERAK 2236
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEvaRELYESLLQRLEEAR 378
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3845-3883 |
5.22e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.78 E-value: 5.22e-06
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 3845 YLYGSGCIAGIYIPSSKQKLNVYQALKRGLITPEVARPL 3883
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
206-293 |
5.58e-06 |
|
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: 48.60 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 206 LYEDLRDGHNLISLLEVLSGDTLPrerDVIRNLRLPREKGRMRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLT 285
Cdd:cd21294 38 LFDECKDGLVLSKLINDSVPDTID---ERVLNKPPRKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLI 114
|
....*...
gi 2069539781 286 LGLIWTII 293
Cdd:cd21294 115 LGLIWQII 122
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2425-2786 |
5.83e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 52.42 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2425 VAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKIL--KEKMQAVQEATRLKAEAEVLQKQKDLAQEQAkklqEDKEQM 2502
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYlaKEEDLKRQNAVLQEAQVELDALQNQLALARA----EMENIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2503 QLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTE------LSLAQAKAEeeAKRFKKQAEQISQKLHQTELATQEK 2576
Cdd:pfam03528 82 AVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVREyevqfhRRLEQERAQ--WNQYRESAEREIADLRRRLSEGQEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2577 mtlvQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQL----------RQETQMLQQTFRS 2646
Cdd:pfam03528 160 ----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELnhyleaekscRTDLEMYVAVLNT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2647 EKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQER-------QQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQ 2719
Cdd:pfam03528 236 QKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKandqfleSQRLLMRDMQRMESVLTSEQLRQVEEIKKKDQEE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2720 EELQRLEKQRQKQeKLLAEENQKLREKLEQLQEEQKTALAQTREIMIQT----DDLPQEVVAPSQVPQMKA 2786
Cdd:pfam03528 316 HKRARTHKEKETL-KSDREHTVSIHAVFSPAGVETSAPLSNVEEQINSAhgsvHSLDTDVVLGAGDSFNKQ 385
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1808-2064 |
5.98e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1808 QEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRklaegtaQQKFLAEQELIRLKAEVENgeqqrllleeelfr 1887
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQL-------EKERLAAQEQKKQAEEAAK-------------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1888 lknevnEAVQKRKELEEELAKLRAemelllQSKAKTEEESRSTSEKSKQIlEAEASKLrelAEEAARLRAlSEEAKRQrq 1967
Cdd:PRK09510 126 ------QAALKQKQAEEAAAKAAA------AAKAKAEAEAKRAAAAAKKA-AAEAKKK---AEAEAAKKA-AAEAKKK-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1968 lAEEEAThQRAEAErilkeklvaineaSRLKAEAEIALKEKEAENERLRRLAEDEAyqrrlleEQAAQHKQDIEEKIAQL 2047
Cdd:PRK09510 187 -AEAEAA-AKAAAE-------------AKKKAEAEAKKKAAAEAKKKAAAEAKAAA-------AKAAAEAKAAAEKAAAA 244
|
250
....*....|....*..
gi 2069539781 2048 KKSSESELERQKSLVDD 2064
Cdd:PRK09510 245 KAAEKAAAAKAAAEVDD 261
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2143-2346 |
6.63e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2143 SAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQE--AAQKRIVAEEKAHLAAVQQKEQELLQTRQQ 2220
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2221 EQSILDKLREE-AERAKKA--------------AEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAE 2285
Cdd:COG4942 95 LRAELEAQKEElAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2286 KLRK-EAELEAARRAQAEQAALKQKQLADAEmaKHKKFAEQTLRQKAQVEQELTKVKLQLEE 2346
Cdd:COG4942 175 ELEAlLAELEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEA 234
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2258-2413 |
6.86e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.45 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2258 QLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAAL-KQKQLADAEMAKHKKFAEQT---LRQKAQV 2333
Cdd:COG1193 518 KLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILeKAREEAEEILREARKEAEELireLREAQAE 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2334 EQELTKVKLQLEETDHQksiLEEEQQRLKD--------------------------EVTEAMKQK-VQVEEELFKVKVQM 2386
Cdd:COG1193 598 EEELKEARKKLEELKQE---LEEKLEKPKKkakpakppeelkvgdrvrvlslgqkgEVLEIPKGGeAEVQVGILKMTVKL 674
|
170 180
....*....|....*....|....*..
gi 2069539781 2387 EELIKLKTRIEEENKMLITKDKDNMQK 2413
Cdd:COG1193 675 SDLEKVEKKKPKKPKKRPAGVSVSVSK 701
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1319-1821 |
7.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1319 RDIDLDRYRERVQQLLERWQAILAQIDLRQRELDQLGRQLRYYRESYDWLIQWIREARQRQEHLQAVpvtnsksvREQLL 1398
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE--------LEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1399 QEKKLLEECDRNREKVEECQCFAKQyidaIKDYELQLVTYKAQVEPVASpaKKPKVQSASDSVIQEYVDLRTRYSELTTL 1478
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAE----LAELPERLEELEERLEELRE--LEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1479 TSQYLKFITETLRRLEEEEKAAEKLKEEERQRLAEVEAQLEkqrqlaeaharaKAQAEKEALELQRRMEEEvsRRQLVAV 1558
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE------------QLENELEAAALEERLKEA--RLLLLIA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1559 DAEQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQK 1638
Cdd:COG4717 256 AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1639 RLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLahea 1718
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQL---- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1719 aqksAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERL--KKLQLEAEQSREEADKEVEKWRQKANEALRLRLQ 1796
Cdd:COG4717 412 ----EELLGELEELLEALDEEELEEELEELEEELEELEEELEELreELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
490 500
....*....|....*....|....*
gi 2069539781 1797 AEEVAHKKALAQEEAEKQKEDAERE 1821
Cdd:COG4717 488 LAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2592-2765 |
7.31e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2592 SDAEKLRKAI-ADLEQEKEKLKREAEL-LQQKSEEMQTAQKEQLRQETQMLQQTFRSekdvLLQKERFVEEEKAKLEKlf 2669
Cdd:PRK12704 34 KEAEEEAKRIlEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKR----LLQKEENLDRKLELLEK-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2670 qeevnkaqglkaeqerQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLekqrqkqEKLLAEENQKlrEKLEQ 2749
Cdd:PRK12704 108 ----------------REEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-------SGLTAEEAKE--ILLEK 162
|
170
....*....|....*..
gi 2069539781 2750 LQEEQKTALAQT-REIM 2765
Cdd:PRK12704 163 VEEEARHEAAVLiKEIE 179
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1596-1999 |
7.35e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 52.45 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1596 RRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQ-------KKREAEDELKH 1668
Cdd:pfam09731 33 RDFFEEYIPYGEEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQsgvssevAEEEKEATKDA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1669 KVQAEQQ--AAREKQKALEDLQKLRL-QAEEAERRMKQAELEKERQVQLAHEAAQ---KSAEADLQSRRLSFAEKTAQLE 1742
Cdd:pfam09731 113 AEAKAQLpkSEQEKEKALEEVLKEAIsKAESATAVAKEAKDDAIQAVKAHTDSLKeasDTAEISREKATDSALQKAEALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1743 LSLQQEHITITHLQEEA--ERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEK-----QK 1815
Cdd:pfam09731 193 EKLKEVINLAKQSEEEAapPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSifpdiIP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1816 EDAEREARKRSKAE---ESALR-----QKELAEQELEKQRKLAEGTAQQKF----LAEQELIRLKAEVENgeqqrlllee 1883
Cdd:pfam09731 273 VLKEDNLLSNDDLNsliAHAHReidqlSKKLAELKKREEKHIERALEKQKEeldkLAEELSARLEEVRAA---------- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1884 elfrlknevnEAVQKRKELEEELAKLRAEMELLLQSKAKTEEEsrSTSEKSKQILEAEASKLRELAEEAARLRALSEEAK 1963
Cdd:pfam09731 343 ----------DEAQLRLEFEREREEIRESYEEKLRTELERQAE--AHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAG 410
|
410 420 430
....*....|....*....|....*....|....*.
gi 2069539781 1964 RQRQLAeeEATHQRAEAERILKEKLVAINEASRLKA 1999
Cdd:pfam09731 411 RLLKLN--ELLANLKGLEKATSSHSEVEDENRKAQQ 444
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1780-2042 |
7.83e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 52.26 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1780 VEKWRQKANEalrLRLQAEEvAHKKALAQE--EAEKQ---KEDAEREARKRSKAEESAlrqkelAEQELEKQRKLAEGTA 1854
Cdd:PRK05035 428 VQYYRQAKAE---IRAIEQE-KKKAEEAKArfEARQArleREKAAREARHKKAAEARA------AKDKDAVAAALARVKA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1855 QQKflAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMElllQSKAKTEEESRSTSEKS 1934
Cdd:PRK05035 498 KKA--AATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA---RAKAKKAAQQAANAEAE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1935 KQILEAEAsklrelAEEAARLRAlseEAKRQRQLAEEEATHQRAEAERILKEKLVA-INEASRLKAEAEIALKEKEAENE 2013
Cdd:PRK05035 573 EEVDPKKA------AVAAAIARA---KAKKAAQQAASAEPEEQVAEVDPKKAAVAAaIARAKAKKAEQQANAEPEEPVDP 643
|
250 260 270
....*....|....*....|....*....|
gi 2069539781 2014 RLRRLAEDEAYQR-RLLEEQAAQHKQDIEE 2042
Cdd:PRK05035 644 RKAAVAAAIARAKaRKAAQQQANAEPEEAE 673
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
174-299 |
8.05e-06 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 48.06 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 174 ERDRVQKKTFTKWVNKhllkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSgdtLPRERDVIRNLRLPREKGRMRfhKLQ 253
Cdd:cd21329 2 EGESSEERTFRNWMNS-------LGVNPYVNHLYSDLCDALVIFQLYEMTR---VPVDWGHVNKPPYPALGGNMK--KIE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2069539781 254 NVQIALDYLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 299
Cdd:cd21329 70 NCNYAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
768-860 |
8.65e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 768 QAFVVAATKELMWLNEKEEEEVNYDWTERNSNMVAKKESYSGLMRELEQRERKIKEIQSTGDRLLQEDHPAKQAVEAFQA 847
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 2069539781 848 ALQTQWSWMLQMC 860
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3957-3994 |
1.01e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 1.01e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2069539781 3957 LRLLDAQLATGGIIDPHLGFHLPLETAYQRGYFNRETY 3994
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
317-410 |
1.03e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 46.91 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 317 LLWSQRMVegyQGMRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNVENLEQAFSVAEQdLGVTRLLDPEDVDVP 396
Cdd:cd21185 7 LRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADP 82
|
90
....*....|....
gi 2069539781 397 QPDEKSIITYVSSL 410
Cdd:cd21185 83 EVEHLGIMAYAAQL 96
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1259-1441 |
1.07e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 49.75 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1259 EQLKDVQAVPSDLKALEATKAELKRLRGQVEGHQPLFNTLEmdlakasEVNERMVRGHSErdiDLDRYRERVQQLLERWQ 1338
Cdd:cd00176 20 EELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALN-------ELGEQLIEEGHP---DAEEIQERLEELNQRWE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1339 AILAQIDLRQRELDQLGRQLRYYRESYDwLIQWIREARQRQEHLQavPVTNSKSVREQLLQEKKLLEECDRNREKVEECQ 1418
Cdd:cd00176 90 ELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLN 166
|
170 180
....*....|....*....|...
gi 2069539781 1419 CFAKQYIDAIKDYELQLVTYKAQ 1441
Cdd:cd00176 167 ELAEELLEEGHPDADEEIEEKLE 189
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4545-4582 |
1.21e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.21e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2069539781 4545 QRFLEVQYLTGGLIEPEVTGRVSLDEALQKGTIDARTA 4582
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1893-2591 |
1.24e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1893 NEAVQKRKELEEELAKlraeMELLLQSKAKTEE---ESRSTSEKskqiLEAEASKLRELAEEA-----ARLRALSEEAKR 1964
Cdd:PRK10246 163 NAKPKERAELLEELTG----TEIYGQISAMVFEqhkSARTELEK----LQAQASGVALLTPEQvqsltASLQVLTDEEKQ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1965 Q--RQLAEEEATH---QRAEAERILKEKLVAINEA--SRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLeeqaAQHK 2037
Cdd:PRK10246 235 LltAQQQQQQSLNwltRLDELQQEASRRQQALQQAlaAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAAL----AHTR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2038 QDIEEKIAQLkkssESELERQKSLVDDTVRQRRLVEEEIRILKLNFekASHGKTDL---ELELTRI---KQSAEEIQRSK 2111
Cdd:PRK10246 311 QQIEEVNTRL----QSTMALRARIRHHAAKQSAELQAQQQSLNTWL--AEHDRFRQwnnELAGWRAqfsQQTSDREQLRQ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2112 EQAEREAEELRQLALEEENHRREAEAKVKKISA-AEQEAARQCKAALEE--VERLKAKAEEARRQKELAEKESERQIQLA 2188
Cdd:PRK10246 385 WQQQLTHAEQKLNALPAITLTLTADEVAAALAQhAEQRPLRQRLVALHGqiVPQQKRLAQLQVAIQNVTQEQTQRNAALN 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2189 QEAAQKRIVAEEKAHLAAVQQKEQE---LLQTRQQEQS----------------ILDKLREEAERAKKAAEDAEFARIKa 2249
Cdd:PRK10246 465 EMRQRYKEKTQQLADVKTICEQEARikdLEAQRAQLQAgqpcplcgstshpaveAYQALEPGVNQSRLDALEKEVKKLG- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2250 eQEAALSRQLVEEAERMKQRAEEEAQTKAkaqEDAEKLRKEAE-------------------LEAARRAQAEQAALKQKQ 2310
Cdd:PRK10246 544 -EEGAALRGQLDALTKQLQRDESEAQSLR---QEEQALTQQWQavcaslnitlqpqddiqpwLDAQEEHERQLRLLSQRH 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2311 LADAEMAKH----KKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEqqrlkdevteamkqkvqvEEELFKVKVQM 2386
Cdd:PRK10246 620 ELQGQIAAHnqqiIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATR------------------QQEAQSWQQRQ 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2387 EELIKLKTRIEEENKMLITKDKDNMQKFLAE--EAEKMKQVAEEAarLSVEAQeaarLRELAEQDLAQQRSLAEKIlkEK 2464
Cdd:PRK10246 682 NELTALQNRIQQLTPLLETLPQSDDLPHSEEtvALDNWRQVHEQC--LSLHSQ----LQTLQQQDVLEAQRLQKAQ--AQ 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2465 MQAVQEATRLKAEAEVLQKQKDLAQ----EQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTE 2540
Cdd:PRK10246 754 FDTALQASVFDDQQAFLAALLDEETltqlEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQ 833
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2541 LslaqakAEEEAKRFKKQAEqISQKLHQTELATQEKMTLVQTLEIQRQQSD 2591
Cdd:PRK10246 834 L------AQQLRENTTRQGE-IRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1508-1739 |
1.42e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEK-QRQLAEAHARAkAQAEKEALELQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQM-KLSSDAQIQAK 1585
Cdd:COG3883 22 QKELSELQAELEAaQAELDALQAEL-EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1586 LKLIEEVEFSRRKVEEEIRMVRLQLEATERQRagaeDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDE 1665
Cdd:COG3883 101 SVSYLDVLLGSESFSDFLDRLSALSKIADADA----DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 1666 LKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTA 1739
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2433-2717 |
1.49e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.11 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2433 SVEAQEAARLRELAEQDLAQQRSLAEKILKEKMqavqEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEG 2512
Cdd:pfam15709 316 SEEDPSKALLEKREQEKASRDRLRAERAEMRRL----EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2513 FQKTLEAERQRQLEitanaerlkvqvtelslaqakaEEEAKRFKKQAEQISQKLHQTELATqekmtlvQTLEIQRQQsds 2592
Cdd:pfam15709 392 RKQRLEEERQRQEE----------------------EERKQRLQLQAAQERARQQQEEFRR-------KLQELQRKK--- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2593 daeklrkaiadleQEKEKLKREAELLQQKSEEMQTAQKEQLRQEtqmlqqtfrsekdvllqkerFVEEEKAKLEKLFQEE 2672
Cdd:pfam15709 440 -------------QQEEAERAEAEKQRQKELEMQLAEEQKRLME--------------------MAEEERLEYQRQKQEA 486
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2069539781 2673 VNKAQgLKAEQERQqkqmeQEKKQLTTVLEEARKkqaEAEENVRQ 2717
Cdd:pfam15709 487 EEKAR-LEAEERRQ-----KEEEAARLALEEAMK---QAQEQARQ 522
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2035-2214 |
1.52e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.61 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2035 QHKQDIEEKIAQLKKSSESELERQKSLvddtvRQRRLVEEEIRilklNFEKASHGKTDLELELTRIKQSAEEIQRSKEQA 2114
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKEL-----EQRAAAEKAAK----QAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2115 EREaeelrQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVE-----RLKAKAEEARRQKELAEKESerqiqlAQ 2189
Cdd:TIGR02794 139 EAE-----RKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKakaeaEAKAKAEEAKAKAEAAKAKA------AA 207
|
170 180
....*....|....*....|....*
gi 2069539781 2190 EAAQKRIVAEEKAHLAAVQQKEQEL 2214
Cdd:TIGR02794 208 EAAAKAEAEAAAAAAAEAERKADEA 232
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1785-2077 |
1.58e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.61 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1785 QKANEALRLRLQAEEVAHKKALAQEEAEKQKEdaerEARKRSKAEEsalrqkelaeqelEKQRKLAEGTAQQKFLAEQEL 1864
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAE----EAEKQRAAEQ-------------ARQKELEQRAAAEKAAKQAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1865 IRLKAEvengeqqrllleeelfrlknevneavQKRKELEEELAKLRAEmellLQSKAKTEEESRSTSEKSKQileAEASK 1944
Cdd:TIGR02794 110 AAKQAE--------------------------EKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEEAAKQ---AEEEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1945 LRELAEEAARlralseEAKRQRQLAEEEAThQRAEAERILK-EKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEA 2023
Cdd:TIGR02794 157 KAKAAAEAKK------KAEEAKKKAEAEAK-AKAEAEAKAKaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2024 YQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIR 2077
Cdd:TIGR02794 230 DEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQNLYDDPSFR 283
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1508-1925 |
1.61e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.06 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEkealELQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQMKLSSDAQIQAKLK 1587
Cdd:COG5278 117 DQWLAELEQVIALRRAGGLEAALALVRSG----EGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELK 1667
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 HKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQ 1747
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1748 EHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSK 1827
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1828 AEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELA 1907
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAA 512
|
410
....*....|....*...
gi 2069539781 1908 KLRAEMELLLQSKAKTEE 1925
Cdd:COG5278 513 AEAALAAALAAALASAEL 530
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1936-2292 |
1.63e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 51.45 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1936 QILEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALK--EKEAENE 2013
Cdd:pfam15964 300 QTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKErlEKELASQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2014 RLRRLAEDEAYQRRLLEEQ--AAQHKQDIEEKIAQLkkssESELERqkslvddtvrqrrlVEEEIRILKLNFEKASHGKT 2091
Cdd:pfam15964 380 QEKRAQEKEALRKEMKKEReeLGATMLALSQNVAQL----EAQVEK--------------VTREKNSLVSQLEEAQKQLA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2092 DLELELTRI----KQSAEEIQRSKEQAEREAEELRQLALeeenhrREAEAKVKKISAAEQEAArQCKAALEEVERLKAKA 2167
Cdd:pfam15964 442 SQEMDVTKVcgemRYQLNQTKMKKDEAEKEHREYRTKTG------RQLEIKDQEIEKLGLELS-ESKQRLEQAQQDAARA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2168 -EEARRQKELAeKESERQIQLA---QEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAErAKKAAEDAE 2243
Cdd:pfam15964 515 rEECLKLTELL-GESEHQLHLTrleKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQY-SLLTSQNTF 592
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2069539781 2244 FARIKaEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAE 2292
Cdd:pfam15964 593 IAKLK-EECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNE 640
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3255-3291 |
1.74e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.74e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2069539781 3255 KLLSAEKAVTGYRDPYTGQVVSLFQALQKGLIPKDAG 3291
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2406-2560 |
1.80e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2406 KDKDNMQKFLAE--EAEKMKQVAEEAARLSVEAQEAARLRELAEQ--DLAQQRSLAEKILKEKMQAVQEATRLKAEAEVL 2481
Cdd:PRK09510 75 KRAEEQRKKKEQqqAEELQQKQAAEQERLKQLEKERLAAQEQKKQaeEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2482 QKQKDLAQEQAKKLQEDKEQMQLRLAEEAegfQKTLEAERQRQL--EITANAERLKVQVTElSLAQAKAEEEAKRFKKQA 2559
Cdd:PRK09510 155 RAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAaaEAKKKAEAEAKKKAA-AEAKKKAAAEAKAAAAKA 230
|
.
gi 2069539781 2560 E 2560
Cdd:PRK09510 231 A 231
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2187-2502 |
1.98e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2187 LAQEAAQK--RIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEaalsrqLVEEAE 2264
Cdd:pfam05667 209 LERNAAELaaAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQD------LAELLS 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2265 RMKQRAEEEAQ-TKAKAQEDAEKLrkeaeleaarraqaeqaALKQKQLADAEMAKHKKFAEQTLRQkaQVEQELTKVKLQ 2343
Cdd:pfam05667 283 SFSGSSTTDTGlTKGSRFTHTEKL-----------------QFTNEAPAATSSPPTKVETEEELQQ--QREEELEELQEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2344 LEETDHQKSILEEEQQRLKDEVTeamkqkvQVEEELFKVKVQMEELIKlKTRIEEENKMLITKDKDNM---QKFLAEEAE 2420
Cdd:pfam05667 344 LEDLESSIQELEKEIKKLESSIK-------QVEEELEELKEQNEELEK-QYKVKKKTLDLLPDAEENIaklQALVDASAQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2421 KMKQVAE--EAARLSVeAQEAARLREL-AEQDLAQQRSLAE-KILKEKMQAVQEATRLKAEaevLQKQkdlaqeqakkLQ 2496
Cdd:pfam05667 416 RLVELAGqwEKHRVPL-IEEYRALKEAkSNKEDESQRKLEEiKELREKIKEVAEEAKQKEE---LYKQ----------LV 481
|
....*.
gi 2069539781 2497 EDKEQM 2502
Cdd:pfam05667 482 AEYERL 487
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2100-2196 |
2.21e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 47.05 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2100 IKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKI-----SAAEQEAARQCKAALEEVERLKAKA-EEARRQ 2173
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIieearKEAEKIKEEILAEAKEEAERILEQAkAEIEQE 107
|
90 100
....*....|....*....|....
gi 2069539781 2174 KELAEKESERQI-QLAQEAAQKRI 2196
Cdd:cd06503 108 KEKALAELRKEVaDLAVEAAEKIL 131
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1758-1955 |
2.30e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1758 EAERLKKLQLEAEQSREEADKEVEkwRQKANEALRLRLQAE----EVAHKKA-LAQEEAEKQKEDAEREARKrsKAEESA 1832
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEQE--RLKQLEKERLAAQEQkkqaEEAAKQAaLKQKQAEEAAAKAAAAAKA--KAEAEA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1833 LRQKELAEQELEKQRKLAEGTAQQKFLAEQeliRLKAEVEngeqqrllleeelfRLKNEVNEAVQKRKELEEELAKLRAE 1912
Cdd:PRK09510 154 KRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAE--------------AAAKAAAEAKKKAEAEAKKKAAAEAK 216
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2069539781 1913 MELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARL 1955
Cdd:PRK09510 217 KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2447-2775 |
2.35e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2447 EQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKklQEDKEQMQLRLAEE-AEGFQKTLEAERQrql 2525
Cdd:pfam05667 195 TAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYR--KRKRTKLLKRIAEQlRSAALAGTEATSG--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2526 eitanAERLKVQVTELsLAQAKAEEEAKRFKKQAEQI--SQKLHQT---ELATQEKMTLVQTLEIQRQQSDSDAEKLRKA 2600
Cdd:pfam05667 270 -----ASRSAQDLAEL-LSSFSGSSTTDTGLTKGSRFthTEKLQFTneaPAATSSPPTKVETEEELQQQREEELEELQEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2601 IADLEQEKEKLKREAELLQQKSEEMqTAQKEQLRQETQMLQQTFRSEK---DVLLQkerfVEEEKAKLEKLFQEEVNKAQ 2677
Cdd:pfam05667 344 LEDLESSIQELEKEIKKLESSIKQV-EEELEELKEQNEELEKQYKVKKktlDLLPD----AEENIAKLQALVDASAQRLV 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2678 GLKAEQErqqkqmeqeKKQLTTVLEEARKKQAEAEenvrqkqeelQRLEKQRQKqekllaEENQKLREKLEQLQEEQKTA 2757
Cdd:pfam05667 419 ELAGQWE---------KHRVPLIEEYRALKEAKSN----------KEDESQRKL------EEIKELREKIKEVAEEAKQK 473
|
330
....*....|....*...
gi 2069539781 2758 LAQTREIMIQTDDLPQEV 2775
Cdd:pfam05667 474 EELYKQLVAEYERLPKDV 491
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1596-2179 |
2.39e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1596 RRKVEEEIRMVRlQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQ 1675
Cdd:PRK01156 151 RKKILDEILEIN-SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1676 AAREKQKALEDLQKLRLQAEEAERrmkqaelekerqvqlaHEAAQKSAEADLQSrrlsfaektaqlelslqqEHITITHL 1755
Cdd:PRK01156 230 AMDDYNNLKSALNELSSLEDMKNR----------------YESEIKTAESDLSM------------------ELEKNNYY 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1756 QEEAERLKKLQLEAE-QSREEAD------KEVEKWRQKAnEALRLRLQAEEVAHKKAlaqeeAEKQKEDAEREARKRSKA 1828
Cdd:PRK01156 276 KELEERHMKIINDPVyKNRNYINdyfkykNDIENKKQIL-SNIDAEINKYHAIIKKL-----SVLQKDYNDYIKKKSRYD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1829 EESALRQkELAEQELEKQRKLAEGTAQQKFLAE--QELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQkrkELEEEL 1906
Cdd:PRK01156 350 DLNNQIL-ELEGYEMDYNSYLKSIESLKKKIEEysKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ---DISSKV 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1907 AKLRAEMELLLQSKAKTEEESRSTSEKSK------QILEAEASKLRE-LAEEAARLRALSEEAKRQRQLAEEEATHQRAE 1979
Cdd:PRK01156 426 SSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSNHIINhYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1980 AERILKEKL-VAINEASRLKA-----------EAEIALKEKEAE--NERLRRLAEDEAYQRR--LLEEQAAQHKQDIE-- 2041
Cdd:PRK01156 506 KEYLESEEInKSINEYNKIESaradledikikINELKDKHDKYEeiKNRYKSLKLEDLDSKRtsWLNALAVISLIDIEtn 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2042 -----EKIAQLKKSS------ESELERQKSLVDDTVRQrrlVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRS 2110
Cdd:PRK01156 586 rsrsnEIKKQLNDLEsrlqeiEIGFPDDKSYIDKSIRE---IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEI 662
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2111 KEQAEREAeELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEK 2179
Cdd:PRK01156 663 DSIIPDLK-EITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKK 730
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
2134-2292 |
2.40e-05 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 47.94 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2134 EAEAKVKKISAAEQEAARQCKAALEEverlkaKAEEARRQKE--LAEKEserQI--QLAQEAAQ-KRIVAEEKAHLAAVQ 2208
Cdd:pfam05335 16 EAKAANDAQAAAAEAAARQVKNQLAD------KALQAAKAAEaaLAGKQ---QIveQLEQELREaEAVVQEESASLQQSQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2209 QKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAermKQRAEEEAQTKAKAQEDAEKLR 2288
Cdd:pfam05335 87 ANANAAQRAAQQAQQQLEALTAALKAAQANLENAEQVAAGAQQELAEKTQLLEAA---KKRVERLQRQLAEARADLEKTK 163
|
....
gi 2069539781 2289 KEAE 2292
Cdd:pfam05335 164 KAAY 167
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2307-2498 |
2.44e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2307 KQKQLADAEMAKHKKFAEQT--LRQKAQVEQELTKV--KLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKV 2382
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEQERLKQleKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2383 KVQMEELIKLKTRIEEENKmliTKDKDNMQKFLAEEAEKmkQVAEEAARLSVEA--QEAARLRELAEQDLAQQRSLAEKi 2460
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAK---KKAEAEAAKKAAAEAKK--KAEAEAAAKAAAEakKKAEAEAKKKAAAEAKKKAAAEA- 223
|
170 180 190
....*....|....*....|....*....|....*...
gi 2069539781 2461 lkeKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQED 2498
Cdd:PRK09510 224 ---KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1756-1972 |
2.52e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 50.34 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1756 QEEAERLKKLQLE-AEQSREEADKEvekwRQKANEALRLRLQAEEvahkkalaqEEAEKQKEDAEREARKRSKAEESALR 1834
Cdd:pfam15709 357 QEEQRRLQQEQLErAEKMREELELE----QQRRFEEIRLRKQRLE---------EERQRQEEEERKQRLQLQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1835 QKElaeqelEKQRKLAEGTAQQKflaEQELIRLKAEvengeqqrllleeelfrlknevneaVQKRKELEEELA---KLRA 1911
Cdd:pfam15709 424 QQE------EFRRKLQELQRKKQ---QEEAERAEAE-------------------------KQRQKELEMQLAeeqKRLM 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 1912 EMelllQSKAKTEEESRSTSEKSKQILEAEASKLRElaEEAARLraLSEEAKRQRQLAEEE 1972
Cdd:pfam15709 470 EM----AEEERLEYQRQKQEAEEKARLEAEERRQKE--EEAARL--ALEEAMKQAQEQARQ 522
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
179-304 |
2.56e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 47.36 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 179 QKKTFTKWVNKHLLKHWRAeaqRHV-------NDLYEDLRDGHNLISLLEVLSGDTLPrERDVIRNLRLPrekgrmrFHK 251
Cdd:cd21325 25 EKYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTID-ERAINKKKLTP-------FII 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 252 LQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 304
Cdd:cd21325 94 QENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1720-1872 |
2.59e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1720 QKSAEADLQSRRLSFAEKTAQlelSLQQEHItithlqEEAERLKKLqleaEQSREEADKEVEKWRQKANEALRLRLQAEE 1799
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAE---ELQQKQA------AEQERLKQL----EKERLAAQEQKKQAEEAAKQAALKQKQAEE 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 1800 VAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQElirLKAEVE 1872
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK---KKAEAE 206
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1752-2127 |
2.62e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.07 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1752 ITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEvahkkalAQEEAEKQKEDAEREARKRSKAEE- 1830
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEELVARLAKLEAALREAEAAKEe 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1831 --SALRQKELAEQELEKQRKlAEGTAQQKFLAEQELIRLKAEVengeqqrllLEEELFRLKNEVNEAVQKRKELEEELAK 1908
Cdd:pfam19220 109 lrIELRDKTAQAEALERQLA-AETEQNRALEEENKALREEAQA---------AEKALQRAEGELATARERLALLEQENRR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1909 LRAEMElllQSKAKTEEESRSTSEKSKQiLEAEASKLRELAEEAArlralSEEAKRQRQLAEEEATHQRAEAERI-LKEK 1987
Cdd:pfam19220 179 LQALSE---EQAAELAELTRRLAELETQ-LDATRARLRALEGQLA-----AEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1988 LVAINE----ASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKkssesELERQKSLVD 2063
Cdd:pfam19220 250 LEALTAraaaTEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-----EMQRARAELE 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2064 D---------TVRQRRLVEEEIRILKLNfEKASHGKTDLELELTRIKQSAEEIqRSKEQAEREAEELRQLALE 2127
Cdd:pfam19220 325 EraemltkalAAKDAALERAEERIASLS-DRIAELTKRFEVERAALEQANRRL-KEELQRERAERALAQGALE 395
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2595-2777 |
2.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2595 EKLRKAIADLE----QEKEKLKREAELLQQKSEEMQtAQKEQLRQETQMLQQTfRSEKDVLLQKERFVEEEKAKLEKLFQ 2670
Cdd:COG4717 49 ERLEKEADELFkpqgRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEEL-EEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2671 -----EEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLRE 2745
Cdd:COG4717 127 llplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|..
gi 2069539781 2746 KLEQLQEEQKTALAQTREIMIQTDDLPQEVVA 2777
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1339-1714 |
2.72e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1339 AILAQIDLRQRELDqlgRQLRYYRESYDWLIQWIREARQRQEHLQA-VPVTNsksvreqLLQEKKL---LEECDRNREKV 1414
Cdd:COG3096 836 AELAALRQRRSELE---RELAQHRAQEQQLRQQLDQLKEQLQLLNKlLPQAN-------LLADETLadrLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1415 EECQCFAKQYIDAIkdyelqlvtykAQVEPVAS-----PAKKPKVQSASDSVIQEYVDLRTRYSELTTLTSQYLKFiteT 1489
Cdd:COG3096 906 QEAQAFIQQHGKAL-----------AQLEPLVAvlqsdPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHF---S 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1490 LRRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEaharakaQAEKEALELQRRMEEEVSRRQLvavdAEQQKQTIQQ 1569
Cdd:COG3096 972 YEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLR-------QAQAQYSQYNQVLASLKSSRDA----KQQTLQELEQ 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1570 ELSQM--KLSSDAQIQAKLKlieevefsRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAE- 1646
Cdd:COG3096 1041 ELEELgvQADAEAEERARIR--------RDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVq 1112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1647 ------RLRKQVKDESQKKREAEDELKHKVQAEQQAAREK-----QKALEDLQKLR--LQAEEAERRmkqaeleKERQVQ 1713
Cdd:COG3096 1113 akagwcAVLRLARDNDVERRLHRRELAYLSADELRSMSDKalgalRLAVADNEHLRdaLRLSEDPRR-------PERKVQ 1185
|
.
gi 2069539781 1714 L 1714
Cdd:COG3096 1186 F 1186
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1556-1739 |
2.88e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1556 VAVD---AEQQKQTIQQelsQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEirmvrlqleaTERQRAGAEDELQALRDRaE 1632
Cdd:PRK09510 53 VMVDpgaVVEQYNRQQQ---QQKSAKRAEEQRKKKEQQQAEELQQKQAAE----------QERLKQLEKERLAAQEQK-K 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1633 EAERQKRLAQEEAERLRKQVKDESQK-KREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAE-----EAERRMKQAEL 1706
Cdd:PRK09510 119 QAEEAAKQAALKQKQAEEAAAKAAAAaKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEakkkaEAEAAAKAAAE 198
|
170 180 190
....*....|....*....|....*....|...
gi 2069539781 1707 EKERQVQLAHEAAQKSAEADLQSRRLSFAEKTA 1739
Cdd:PRK09510 199 AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAA 231
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1586-1728 |
2.89e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1586 LKLIEEVEFSRRKVEEEI-RMVRLQLEATERQRAGAED----ELQALRDRAEEAERQKRLAQEEAERLRKQVKDEsQKKR 1660
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAeRETEIAIAQANREAEEAELeqerEIETARIAEAEAELAKKKAEERREAETARAEAE-AAYE 269
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1661 EAEDELKHKVQAE-QQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAhEAAQKSAEADLQ 1728
Cdd:COG2268 270 IAEANAEREVQRQlEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA-EAEAEAIRAKGL 337
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4296-4324 |
2.93e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 2.93e-05
10 20
....*....|....*....|....*....
gi 2069539781 4296 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4324
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1549-1705 |
2.99e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.87 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1549 EVSRRQLVAVdAEQQKQTIQQELSQMKLSSDAQIQAKLKlIEEVEFSRRKVEEEIRMVRLQLEAtERQRAGAEdelQALR 1628
Cdd:COG2268 196 EIIRDARIAE-AEAERETEIAIAQANREAEEAELEQERE-IETARIAEAEAELAKKKAEERREA-ETARAEAE---AAYE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1629 DRAEEAERQKRLAQEEAERLRK---QVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAE-EAERRMKQA 1704
Cdd:COG2268 270 IAEANAEREVQRQLEIAEREREielQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEaEGKRALAEA 349
|
.
gi 2069539781 1705 E 1705
Cdd:COG2268 350 W 350
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2169-2511 |
3.11e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 49.65 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2169 EARRQKELAEKESERQIQLAQEAAQKRivaEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEfARIK 2248
Cdd:pfam15558 14 LARHKEEQRMRELQQQAALAWEELRRR---DQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRR-EKQV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2249 AEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALkQKQLADAEMAKHKKFAEQTLR 2328
Cdd:pfam15558 90 IEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQL-QERLEEACHKRQLKEREEQKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2329 QKAQVEQELTKVKLQLEETDHQkSILEEEQQRLkdevteAMKQKVQVEEELFKvKVQMEELIKLKTRIEEENKMLitkdk 2408
Cdd:pfam15558 169 VQENNLSELLNHQARKVLVDCQ-AKAEELLRRL------SLEQSLQRSQENYE-QLVEERHRELREKAQKEEEQF----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2409 dnmqkflaeeaEKMKQVAEEAARLSVEAQEAarLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQK--- 2485
Cdd:pfam15558 236 -----------QRAKWRAEEKEEERQEHKEA--LAELADRKIQQARQVAHKTVQDKAQRARELNLEREKNHHILKLKvek 302
|
330 340
....*....|....*....|....*...
gi 2069539781 2486 --DLAQEQAKKLQEDKEQMQLRLAEEAE 2511
Cdd:pfam15558 303 eeKCHREGIKEAIKKKEQRSEQISREKE 330
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1755-2150 |
3.16e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1755 LQEEAERLKKLqlEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQ-----EEAEKQKEDAEREARKRSKAE 1829
Cdd:pfam07888 40 LQERAELLQAQ--EAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQsrekhEELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1830 ESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVEngeqqrllleeelfrlknevnEAVQKRKELEEELAKL 1909
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK---------------------KAGAQRKEEEAERKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1910 RAEMElllqskaKTEEESRSTS---EKSKQILEAEASKLRELAEEAARLRALSEEAkrQRQLAEEEATHQRAeaeRILKE 1986
Cdd:pfam07888 177 QAKLQ-------QTEEELRSLSkefQELRNSLAQRDTQVLQLQDTITTLTQKLTTA--HRKEAENEALLEEL---RSLQE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1987 KLvainEASRLKAEaeiALKEKEAENERLRRLAEDEAYQRRL----LEEQAAQHKQDIEEKIAQ-------LKKSSESEL 2055
Cdd:pfam07888 245 RL----NASERKVE---GLGEELSSMAAQRDRTQAELHQARLqaaqLTLQLADASLALREGRARwaqeretLQQSAEADK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2056 ERQKSLVDDTVR-QRRLVEEEIRILKLNFEKASHGKTDL------ELELTRIKQSAEEIQRSKEQAEREAEELRQlalee 2128
Cdd:pfam07888 318 DRIEKLSAELQRlEERLQEERMEREKLEVELGREKDCNRvqlsesRRELQELKASLRVAQKEKEQLQAEKQELLE----- 392
|
410 420
....*....|....*....|..
gi 2069539781 2129 enHRREAEAKVKKISAAEQEAA 2150
Cdd:pfam07888 393 --YIRQLEQRLETVADAKWSEA 412
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1587-2122 |
3.18e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1587 KLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAE---DELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAE 1663
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1664 DELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELE-KERQVQLAHEAAQKSAE--ADLQSRRLSFAEKTAQ 1740
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQlNQLKSEISDLNNQKEQDwnKELKSELKNQEKKLEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1741 LELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEkwrqkanealrlrlqaeevahkkalaqeEAEKQKEDAER 1820
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE----------------------------EKQNEIEKLKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1821 EARKRSKAEESALRQKELAEQELEKQRKLA-------EGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVN 1893
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNqqkdeqiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1894 EAVQKRKELEEELAKLRAEMelllqskakteEESRSTSEKSKQILEAEASKLRELAEEaarlralseeakrQRQLAEEEA 1973
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSI-----------NKIKQNLEQKQKELKSKEKELKKLNEE-------------KKELEEKVK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1974 THQRAEAERILKEKlvaineasrlKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQaaqhKQDIEEKIAQLK---KS 2050
Cdd:TIGR04523 514 DLTKKISSLKEKIE----------KLESEKKEKESKISDLEDELNKDDFELKKENLEKE----IDEKNKEIEELKqtqKS 579
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2051 SESELERQKSLVDDTVRQR-----RLVEEEIRILKLN--FEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELR 2122
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKkdlikEIEEKEKKISSLEkeLEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2595-2751 |
3.27e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 49.11 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2595 EKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQtfrsekdvllQKERFVEEEKAKLEKLfqeevn 2674
Cdd:cd16269 149 EDREKLVEKYRQVPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEK----------EKEIEAERAKAEAAEQ------ 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2675 KAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQ--RLEKQRQKQEKLLAEENQKLREKLEQLQ 2751
Cdd:cd16269 213 ERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALesKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2366-2514 |
3.64e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 49.11 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2366 TEAMKQKVQVEEELFKVKVQMEELIK--LKTRIEEENKMLITkDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEaarlR 2443
Cdd:cd16269 148 LEDREKLVEKYRQVPRKGVKAEEVLQefLQSKEAEAEAILQA-DQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----R 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2444 ELAEQDLAQQRSLAEKI--LKEKMQavQEATRLKAEAEVLQKQKDlaQEQAKKLQEDKEQMQLRLAEEAEGFQ 2514
Cdd:cd16269 223 ELEQKLEDQERSYEEHLrqLKEKME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1761-1957 |
3.65e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1761 RLKKLQLEAEQSREEADKEVEkwrqkanEAlrlRLQAEEVAHKKAL-AQEEAEKQKEDAEREARKrskaeesalRQKELa 1839
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE-------EA---KKEAEAIKKEALLeAKEEIHKLRNEFEKELRE---------RRNEL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1840 eQELEKQRKLAEGTAQQKflaEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAE--MELLL 1917
Cdd:PRK12704 85 -QKLEKRLLQKEENLDRK---LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2069539781 1918 QskaKTEEESRstSEKSKQILEAEasklrELAEEAARLRA 1957
Cdd:PRK12704 161 E---KVEEEAR--HEAAVLIKEIE-----EEAKEEADKKA 190
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2092-2289 |
3.78e-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: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2092 DLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQckaaleeVERLKAKAEEAR 2171
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2172 RQKELaekeseRQIQLAQEAAQKRIVAEEKahlaavqqKEQELLQTRQQEQSILDKLREEAERAKkaaedAEFARIKAEQ 2251
Cdd:COG1579 87 NNKEY------EALQKEIESLKRRISDLED--------EILELMERIEELEEELAELEAELAELE-----AELEEKKAEL 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 2069539781 2252 EAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRK 2289
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKIPPELLALYERIRK 185
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1600-1977 |
3.84e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1600 EEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKR-----------LAQEEAERLRKQVKDESQKKREAEDElkh 1668
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpqanlLADETLADRLEELREELDAAQEAQAF--- 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1669 kVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAElEKERQVQlaheaAQKSAEADLQSRR--LSFAEKTAQLELSlq 1746
Cdd:COG3096 912 -IQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAK-EQQRRLK-----QQIFALSEVVQRRphFSYEDAVGLLGEN-- 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1747 qehitithlQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRlRLQAEEVAHKkALAQEEAEKQKEDAEREARKRS 1826
Cdd:COG3096 983 ---------SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ-VLASLKSSRD-AKQQTLQELEQELEELGVQADA 1051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1827 KAEESALRQKELAEQELEKQRklaegtaqqkflaeqelirlkaevengeqqrllleeelfrlknevneavQKRKELEEEL 1906
Cdd:COG3096 1052 EAEERARIRRDELHEELSQNR-------------------------------------------------SRRSQLEKQL 1082
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1907 AKLRAEMELLLQSKAKTEEESRSTSEkskQILEAEAS-----------------KLRELA-EEAARLRALSEEAKRQRQL 1968
Cdd:COG3096 1083 TRCEAEMDSLQKRLRKAERDYKQERE---QVVQAKAGwcavlrlardndverrlHRRELAyLSADELRSMSDKALGALRL 1159
|
....*....
gi 2069539781 1969 AEEEATHQR 1977
Cdd:COG3096 1160 AVADNEHLR 1168
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1660-1957 |
3.85e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.95 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1660 REAEDELKHKVQAEQQAAREKQKAleDLQKLRLQAEEAERRMKQAelEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTA 1739
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARF--EARQARLEREKAAREARHK--KAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1740 QLELSLQQEHITIThlQEEAERLKKLQLEAEQSREEADKEvekwRQKANEALRLRLQAeevahKKALAQEEAEKQKEDAE 1819
Cdd:PRK05035 508 IKAGARPDNSAVIA--AREARKAQARARQAEKQAAAAADP----KKAAVAAAIARAKA-----KKAAQQAANAEAEEEVD 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1820 REARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEvengeqqrllleEELFRLKNEVNEAVQKR 1899
Cdd:PRK05035 577 PKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAK------------KAEQQANAEPEEPVDPR 644
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 1900 KeleeelAKLRAEMElllQSKAKTEEESRSTSEKskqiLEAEASKLRELAEEAARLRA 1957
Cdd:PRK05035 645 K------AAVAAAIA---RAKARKAAQQQANAEP----EEAEDPKKAAVAAAIARAKA 689
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2113-2286 |
4.21e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2113 QAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQ-KELAEKESERQIQLAQEA 2191
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2192 -------------------------------------AQKRIVAEEKAHLAAVQQKEQELlqtrQQEQSILDKLREEAER 2234
Cdd:COG3883 93 ralyrsggsvsyldvllgsesfsdfldrlsalskiadADADLLEELKADKAELEAKKAEL----EAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2235 AKKAAEDAefariKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEK 2286
Cdd:COG3883 169 AKAELEAQ-----QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1249-1870 |
4.52e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1249 GAEDLIRKYEEQLKDVQAVPSDLKALEATKAELKRLRGQVEGHQPLFNTLEMDLAkasevnermvrghserdidldryRE 1328
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL-----------------------EA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1329 RVQQLLERWQAILAQIDLRQRELDQLGRQLRYYRESYDwliqwiREARQRQEHLQAvpvtnsksvreQLLQEKKLLEECD 1408
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIR------GNGGDRLEQLER-----------EIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1409 RNREkveecqcfakQYIDAIKDYELQLVTYKAQVEPVASPAK--KPKVQSASDSVIQEYVDLRTRYSELttltsqylkfi 1486
Cdd:COG4913 359 RRRA----------RLEALLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDL----------- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1487 tetlrrleeeekaaeklkeeeRQRLAEVEAQLEKQRqlaeahaRAKAQAEKEALELQRRMEEEVSRRQ--------LVAV 1558
Cdd:COG4913 418 ---------------------RRELRELEAEIASLE-------RRKSNIPARLLALRDALAEALGLDEaelpfvgeLIEV 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1559 DAEQQK--QTIQQELSQMKLS---SDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQ----ALRD 1629
Cdd:COG4913 470 RPEEERwrGAIERVLGGFALTllvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDfkphPFRA 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1630 --RAEEAERQKRLAQEEAERLRK---------QVKDeSQKKREAEDelKHKVQAE---QQAAREKQKALE-DLQKLRLQA 1694
Cdd:COG4913 550 wlEAELGRRFDYVCVDSPEELRRhpraitragQVKG-NGTRHEKDD--RRRIRSRyvlGFDNRAKLAALEaELAELEEEL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1695 EEAERRMKQAELEKERQVQLAHEAAQ----KSAEADLQSRRLSFAEKTAQLElSLQQEHITITHLQEEAERLKKLQLEAE 1770
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRlaeySWDEIDVASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAELEELE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1771 QSREEADKEVEKWRQKANEALRLRLQAEEVahkkalAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQeLEKQRKLA 1850
Cdd:COG4913 706 EELDELKGEIGRLEKELEQAEEELDELQDR------LEAAEDLARLELRALLEERFAAALGDAVERELREN-LEERIDAL 778
|
650 660
....*....|....*....|
gi 2069539781 1851 EGTAQQkflAEQELIRLKAE 1870
Cdd:COG4913 779 RARLNR---AEEELERAMRA 795
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2603-2753 |
4.53e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 48.86 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2603 DLEQEKEKLKREAELLQQKSEEMQTaqkeqLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAE 2682
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNS-----IKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMI 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2683 QERQQKQMEQEKKQLTTVLEEARKKQAEAEenvrqkqEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEE 2753
Cdd:smart00787 223 KVKKLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSL 286
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
179-303 |
4.87e-05 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 46.58 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 179 QKKTFTKWVNKHL-----LKHWrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPrERDVIRNLRLPrekgrmrFHKLQ 253
Cdd:cd21323 25 EKVAFVNWINKALegdpdCKHV-VPMNPTDESLFKSLADGILLCKMINLSQPDTID-ERAINKKKLTP-------FTISE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2069539781 254 NVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 303
Cdd:cd21323 96 NLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1565-1779 |
5.05e-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: 48.60 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1565 QTIQQELSQMKLSSDAQIQAKLKLIEEV-EFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRD-----RAEEAERQK 1638
Cdd:pfam09787 3 ESAKQELADYKQKAARILQSKEKLIASLkEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGqiqqlRTELQELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1639 RlAQEEAERLRKQVKD-------ESQKKREAEDELKhKVQAEQQAARekqkalEDLQKLRLQAEEAERRmKQAELEKERQ 1711
Cdd:pfam09787 83 Q-QQEEAESSREQLQEleeqlatERSARREAEAELE-RLQEELRYLE------EELRRSKATLQSRIKD-REAEIEKLRN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1712 vQLAHEAAQKSAEADLQSRrlsfaekTAQLELSLQQEHITITHLQEEAERLkKLQLE-AEQSREEADKE 1779
Cdd:pfam09787 154 -QLTSKSQSSSSQSELENR-------LHQLTETLIQKQTMLEALSTEKNSL-VLQLErMEQQIKELQGE 213
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1937-2169 |
5.05e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1937 ILEAEASKLR-ELAEEAARLRALSE-EAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENER 2014
Cdd:COG2268 185 YLDALGRRKIaEIIRDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2015 lrrlaeDEAYqrrllEEQAAQHKQDIEEKIAQLKKSSESELErqkslvddtvRQRRLVEEEirilklnfekashgktdlE 2094
Cdd:COG2268 265 ------EAAY-----EIAEANAEREVQRQLEIAEREREIELQ----------EKEAEREEA------------------E 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2095 LELTRIKQSAEEIQRSKEQAEREAEELRQLALeeenhrREAEAKVKKISAAEQ--EAARQCKAA--LEEVERLKAKAEE 2169
Cdd:COG2268 306 LEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL------AEAEGKRALAEAWNKlgDAAILLMLIekLPEIAEAAAKPLE 378
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1900-2184 |
5.15e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1900 KELEEELAKLRAEMELLLQSKAKTEEESRSTSEKskqiLEAEASKLRELAEEAARLRalseeaKRQRQLAEEEATHqRAE 1979
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEK----RDELNAQVKELREEAQELR------EKRDELNEKVKEL-KEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1980 AERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQrrlleeQAAQHKQDIEEKIAQLKKSSESELERQK 2059
Cdd:COG1340 80 RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ------QTEVLSPEEEKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2060 SLVDdtvRQRRLVEEEIRILKLNFEKASHGKtdleleltRIKQSAEEIQRSKEQ---AEREAEELRQLALEEENHRREAE 2136
Cdd:COG1340 154 KALE---KNEKLKELRAELKELRKEAEEIHK--------KIKELAEEAQELHEEmieLYKEADELRKEADELHKEIVEAQ 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2069539781 2137 AKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQ 2184
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2323-2511 |
5.15e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2323 AEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVqveeelfkVKVQMEELIKLKTRIEEENKM 2402
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV--------IQQLRAQLAELEAELAELSAR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2403 LiTKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQ 2482
Cdd:COG3206 286 Y-TPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAR 364
|
170 180 190
....*....|....*....|....*....|.
gi 2069539781 2483 KQKD--LAQEQAKKLQEDKEQMQLRLAEEAE 2511
Cdd:COG3206 365 ELYEslLQRLEEARLAEALTVGNVRVIDPAV 395
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1592-1715 |
5.44e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.63 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1592 VEFSRRKVEEEIRMVRLQLEaterQRAGAEDELQALRDRAE-EAERQKRL---AQEEAERLRKQVKDESQKKREAedeLK 1667
Cdd:PTZ00491 657 IEITTKSQEAAARHQAELLE----QEARGRLERQKMHDKAKaEEQRTKLLelqAESAAVESSGQSRAEALAEAEA---RL 729
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 1668 HKVQAEQQAAREKQKALE-----DLQKLRLQAE-EAERRMKQAELEKERQVQLA 1715
Cdd:PTZ00491 730 IEAEAEVEQAELRAKALRieaeaELEKLRKRQElELEYEQAQNELEIAKAKELA 783
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3844-3880 |
5.55e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 5.55e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2069539781 3844 KYLYGSGCIAGIYIPSSKQKLNVYQALKRGLITPEVA 3880
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3511-3549 |
5.61e-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: 5.61e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 3511 YLQGSDCIAGVYVEETKEKLSIYEAMRRNLLLPSTATIL 3549
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2578-2739 |
5.76e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2578 TLVQTLEIQRQQSDS--DAEKLRKAIAD--LEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQtfrSEKDVLLQ 2653
Cdd:PRK09510 59 AVVEQYNRQQQQQKSakRAEEQRKKKEQqqAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA---ALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2654 KERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQlttvLEEARKKQAEAEENVRQKQEELQRLEKQRQKQE 2733
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKK----AAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKA 211
|
....*.
gi 2069539781 2734 KLLAEE 2739
Cdd:PRK09510 212 AAEAKK 217
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
2629-2761 |
5.79e-05 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 46.02 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2629 QKEQLRQETQMLQQTFRSEKDVLlqkERFVEEEKAKLEKLF-QEEVNKAQGLKAEQERQ----QKQMEQEKKQLTTvlEE 2703
Cdd:pfam12474 8 QKDRFEQERQQLKKRYEKELEQL---ERQQKQQIEKLEQRQtQELRRLPKRIRAEQKKRlkmfRESLKQEKKELKQ--EV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2704 ARKKQAEAEENVRQKQEELQRLEKQRQKQEklLAEENQKLREKLEQLQEEQKTALAQT 2761
Cdd:pfam12474 83 EKLPKFQRKEAKRQRKEELELEQKHEELEF--LQAQSEALERELQQLQNEKRKELAEH 138
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2537-2769 |
5.81e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.76 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2537 QVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAE 2616
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2617 LLQQKSEEMQtAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQ---GLKAEQERQQKQMEQE 2693
Cdd:pfam13868 107 VERIQEEDQA-EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEreeEREAEREEIEEEKERE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2694 KKQLTTVLEEARKKQAEAEE-NVRQKQEELQRLEKQRQKQEkllAEENQKLREKLEQLQEEQKTALAQTREIMIQTD 2769
Cdd:pfam13868 186 IARLRAQQEKAQDEKAERDElRAKLYQEEQERKERQKEREE---AEKKARQRQELQQAREEQIELKERRLAEEAERE 259
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1980-2173 |
5.83e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 47.20 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1980 AERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRL-----------AEDEAYQRRLLeeqaAQHKQDIEEKIAQLK 2048
Cdd:pfam15619 2 TQRVLSARLHKIKELQNELAELQSKLEELRKENRLLKRLqkrqekalgkyEGTESELPQLI----ARHNEEVRVLRERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2049 KSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEReaeelrQLALEE 2128
Cdd:pfam15619 78 RLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQDLER------KLELEN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2069539781 2129 ENHRREAEAKVKKISAAEQEaarqCKAALEEVERLKAKAEEARRQ 2173
Cdd:pfam15619 152 KSFRRQLAAEKKKHKEAQEE----VKILQEEIERLQQKLKEKERE 192
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2549-2769 |
6.03e-05 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 48.91 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2549 EEEAKRFKKQAEQISQKLHQtelatQEKMTLVQTLEIQRQQSdsdaeKLRkaiadlEQEKEKLKREAELLQQKS-EEMQT 2627
Cdd:pfam15742 54 QEENIKIKAELKQAQQKLLD-----STKMCSSLTAEWKHCQQ-----KIR------ELELEVLKQAQSIKSQNSlQEKLA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2628 AQKEQLRQETQM---LQQTFRSEKDVLLQKERFVEeeKAKLEKLFQEEVNKAQGLKAE-QERQQKQ--MEQEKKQLTTVL 2701
Cdd:pfam15742 118 QEKSRVADAEEKileLQQKLEHAHKVCLTDTCILE--KKQLEERIKEASENEAKLKQQyQEEQQKRklLDQNVNELQQQV 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2702 EEARKKQAEAEENVRQKQEELQRLEKQRQKQ--EKLLAEE----NQKLREKLEQLQEEQKTALAQTREIMIQTD 2769
Cdd:pfam15742 196 RSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLenEKRKSDEhlksNQELSEKLSSLQQEKEALQEELQQVLKQLD 269
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1943-2233 |
6.20e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1943 SKLRELAEEAARLRALSEEAKRQRQLAEEEAthqraeaeRILKEKLVAINEASR-LKAEAEIALKEKEAENERLRRLAEd 2021
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEEL--------KELAEKRDELNAQVKeLREEAQELREKRDELNEKVKELKE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2022 eayQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKslvddtvrqrrlVEEEIRILKLNFEKASHGKtDLELEL-TRI 2100
Cdd:COG1340 79 ---ERDELNEKLNELREELDELRKELAELNKAGGSIDK------------LRKEIERLEWRQQTEVLSP-EEEKELvEKI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2101 KQSAEEIQRSKEQAE--REAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQ----K 2174
Cdd:COG1340 143 KELEKELEKAKKALEknEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEiveaQ 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2175 ELAEKESERQIQLAQEAAQKRIVAEEkahlaavqQKEQELLQTRQQEQSILDKLREEAE 2233
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKK--------LRKKQRALKREKEKEELEEKAEEIF 273
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2100-2275 |
6.37e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2100 IKQSAEEIQRSKEQAEREAEELRQ----LALEEEnhrreAEAKVKKISAAEQEaarqckaaleeVERLKAKAEEARRQKE 2175
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQknglVDLSEE-----AKLLLQQLSELESQ-----------LAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2176 LAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQT-----------RQQEQSILDKLREEAERAKKAAEdAEF 2244
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdvialRAQIAALRAQLQQEAQRILASLE-AEL 322
|
170 180 190
....*....|....*....|....*....|.
gi 2069539781 2245 ARIKAeQEAALSRQLVEEAERMKQRAEEEAQ 2275
Cdd:COG3206 323 EALQA-REASLQAQLAQLEARLAELPELEAE 352
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2593-2774 |
6.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2593 DAEKLRKAIADL---EQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQM-LQQTFRsekdvLLQKERFVEEEKAKLEKL 2668
Cdd:COG4913 226 AADALVEHFDDLeraHEALEDAREQIELLEPIRELAERYAAARERLAELEyLRAALR-----LWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2669 fQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEA---RKKQAEAEenVRQKQEELQRLEKQRQKQEKLLA-------- 2737
Cdd:COG4913 301 -RAELARLEAELERLEARLDALREELDELEAQIRGNggdRLEQLERE--IERLERELEERERRRARLEALLAalglplpa 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2738 -----EENQK--------LREKLEQLQEEQKTALAQTREIMIQTDDLPQE 2774
Cdd:COG4913 378 saeefAALRAeaaalleaLEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1541-1905 |
6.40e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1541 ELQRRMEEEVSRRQLVAVDAEQQKQTIQQELSQMKlSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGA 1620
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELD-KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1621 EDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERR 1700
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1701 MKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEV 1780
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1781 EKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLA 1860
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2069539781 1861 EQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEE 1905
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
179-303 |
6.51e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 46.16 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 179 QKKTFTKWVNKHLLKHWRAeaqRHV-------NDLYEDLRDGHNLISLLEVLSGDTLPrERDVIRNLRLPrekgrmrFHK 251
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTID-ERTINKKKLTP-------FTI 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 252 LQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 303
Cdd:cd21324 94 QENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1508-1711 |
6.87e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRR---MEEEVSRRQLVAVDAEQQKQTIQQELSQMKLSSDAQIQA 1584
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1585 KLKL----IEEVEFSRRKVEEEIRMVRLQLEATERQRagaeDELQALRDRAEEAERQKrlAQEEAER--LRKQVKDESQK 1658
Cdd:COG4942 113 LYRLgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARR----EQAEELRADLAELAALR--AELEAERaeLEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 1659 KREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQ 1711
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2201-2471 |
6.95e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2201 KAHLAAVQQKEQELLQTRQQEQSILDKlreEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAErmkqrAEEEAQTKAKA 2280
Cdd:TIGR02794 39 QAVLVDPGAVAQQANRIQQQKKPAAKK---EQERQKKLEQQAEEAEKQRAAEQARQKELEQRAA-----AEKAAKQAEQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2281 QEDAEKLRKEAEleaarraqaeqaALKQKQLADAEmAKHKKFAEQTLRQKAQVEQELTKVKlqleetdhqksileeeqqr 2360
Cdd:TIGR02794 111 AKQAEEKQKQAE------------EAKAKQAAEAK-AKAEAEAERKAKEEAAKQAEEEAKA------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2361 lkdEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEenkmliTKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAA 2440
Cdd:TIGR02794 159 ---KAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEE------AKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKA 229
|
250 260 270
....*....|....*....|....*....|.
gi 2069539781 2441 RLRELAEQDLAQQRSLAEKILKEKMQAVQEA 2471
Cdd:TIGR02794 230 DEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2593-2767 |
7.39e-05 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 48.03 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2593 DAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTfrSEKDVLLQKERFVEEEKAKLEKLFQEe 2672
Cdd:pfam09728 2 AARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQ--KEKDQLQSELSKAILAKSKLEKLCRE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2673 vnkaqglkaeQERQQKQMEQEKKQLTTVLEEARKkqaEAEENVRQKQEELQ-RLEKQRQKQEKLlAEENQKLREKLE--- 2748
Cdd:pfam09728 79 ----------LQKQNKKLKEESKKLAKEEEEKRK---ELSEKFQSTLKDIQdKMEEKSEKNNKL-REENEELREKLKsli 144
|
170 180
....*....|....*....|..
gi 2069539781 2749 ---QLQEEQKTALAQTREIMIQ 2767
Cdd:pfam09728 145 eqyELRELHFEKLLKTKELEVQ 166
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2385-2577 |
7.63e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2385 QMEELIKLKTRIEEenkmlITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKiLKEK 2464
Cdd:COG1579 8 ALLDLQELDSELDR-----LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2465 MQAVQEATRLKAeaevLQKQKdlaqEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQrqlEITANAERLKVQVTELSLA 2544
Cdd:COG1579 82 LGNVRNNKEYEA----LQKEI----ESLKRRISDLEDEILELMERIEELEEELAELEA---ELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|...
gi 2069539781 2545 QAKAEEEAKRFKKQAEQISQKLHQTELATQEKM 2577
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIPPELLALYERI 183
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1625-2086 |
7.73e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1625 QALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQA 1704
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1705 E---LEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSlqqehitithlQEEAERLKKLQLEAEQSREEADKEVE 1781
Cdd:COG3064 83 EkaaAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEA-----------KRKAEEEAKRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1782 KWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAE 1861
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1862 QELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAE 1941
Cdd:COG3064 232 AALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1942 ASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAED 2021
Cdd:COG3064 312 AAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGI 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2022 EAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKA 2086
Cdd:COG3064 392 LAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALT 456
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2220-2497 |
8.04e-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: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2220 QEQSILDklreeAERAKKAAE---DAEFARIKAEQEAALSrqlVEEAERMKQRAEEEAQ----TKAKAQEDAEKLRKEAE 2292
Cdd:COG2268 181 DENNYLD-----ALGRRKIAEiirDARIAEAEAERETEIA---IAQANREAEEAELEQEreieTARIAEAEAELAKKKAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2293 LEAarraQAEQAALKQKQLADAEMAKhkkfAEQTLRQKAQVEQELTKVKLQleetdhQKSILEEEQQRLKDEV--TEAMK 2370
Cdd:COG2268 253 ERR----EAETARAEAEAAYEIAEAN----AEREVQRQLEIAEREREIELQ------EKEAEREEAELEADVRkpAEAEK 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2371 QKVQVEEELfKVKVQMEELIKLKTRIEEENKMLITKDKDNMQKFLaeeAEKMKQVAEEAARlSVEAQEAARLRELAEQDL 2450
Cdd:COG2268 319 QAAEAEAEA-EAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLML---IEKLPEIAEAAAK-PLEKIDKITIIDGGNGGN 393
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2069539781 2451 AQQRSLAEKILKeKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQE 2497
Cdd:COG2268 394 GAGSAVAEALAP-LLESLLEETGLDLPGLLKGLTGAGAAAPAGEPAE 439
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1705-2393 |
8.05e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1705 ELEKERQVQlAHEAAQKSAEADlqsrrlsfAEKTAQLELslQQEHITITHLQEE--AERLKKLQLEAEQSREEADKEVEK 1782
Cdd:pfam10174 40 ELKKERALR-KEEAARISVLKE--------QYRVTQEEN--QHLQLTIQALQDElrAQRDLNQLLQQDFTTSPVDGEDKF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1783 WRQKANEALRLRLQAEEVAHKKAL-----------AQEEAEKQKEDAEREA-RKRSKAEESALRQKELAEQELEKQRKLA 1850
Cdd:pfam10174 109 STPELTEENFRRLQSEHERQAKELfllrktleemeLRIETQKQTLGARDESiKKLLEMLQSKGLPKKSGEEDWERTRRIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1851 EGTAQqkfLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQK---------------RKELEEELAKLRAEMEL 1915
Cdd:pfam10174 189 EAEMQ---LGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTviemkdtkisslernIRDLEDEVQMLKTNGLL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1916 LL---QSKAKTEEESRSTSE----KSKQILEAEASKLRELAEEAARLRALSEEAKRQRQLAEeeathqraeaerILKEKL 1988
Cdd:pfam10174 266 HTedrEEEIKQMEVYKSHSKfmknKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIE------------VLKESL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1989 VAINE-ASRLKAEAEiALKEKEAENERLrrLAEDEAYQRRLLEEQAAQ-----HKQDI----EEKIAQLKKSSESELERQ 2058
Cdd:pfam10174 334 TAKEQrAAILQTEVD-ALRLRLEEKESF--LNKKTKQLQDLTEEKSTLageirDLKDMldvkERKINVLQKKIENLQEQL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2059 KslvdDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTrikQSAEEIQRSKEQAEREAEELRQlalEEENHRREAEAK 2138
Cdd:pfam10174 411 R----DKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALS---EKERIIERLKEQREREDRERLE---ELESLKKENKDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2139 VKKISAAEQEAARQCKAALEEVERLKAKAEEARRqKELAEKESERQIQLAQEAAQKRIVAEEKAHLAA--VQQKEQELLQ 2216
Cdd:pfam10174 481 KEKVSALQPELTEKESSLIDLKEHASSLASSGLK-KDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEeaVRTNPEINDR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2217 TRQQEQSILDKlREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAE-----RMKQRAEEEAQTKAKAQEDAEKLRKEA 2291
Cdd:pfam10174 560 IRLLEQEVARY-KEESGKAQAEVERLLGILREVENEKNDKDKKIAELEsltlrQMKEQNKKVANIKHGQQEMKKKGAQLL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2292 ELEAARRAQAEQAAlKQKQLAD--AEMAKHKKFAEQTLRQKAQVEQELTK-----VKLQLEETDHQKSILEEEQQRLKDE 2364
Cdd:pfam10174 639 EEARRREDNLADNS-QQLQLEElmGALEKTRQELDATKARLSSTQQSLAEkdghlTNLRAERRKQLEEILEMKQEALLAA 717
|
730 740
....*....|....*....|....*....
gi 2069539781 2365 VTEAMKQKVQVEEELFKVKVQMEELIKLK 2393
Cdd:pfam10174 718 ISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2195-2406 |
8.12e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2195 RIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEdaefaRIKAEQEaalsrqlvEEAERMKqraEEEA 2274
Cdd:PRK00409 502 NIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE-----KLKEELE--------EKKEKLQ---EEED 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2275 QTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEmakhkkfaeqtlrqkAQVEQELTKVKLQLEETDHQKSIL 2354
Cdd:PRK00409 566 KLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKA---------------HELIEARKRLNKANEKKEKKKKKQ 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2355 EEEQQRLK--DEV-TEAMKQK-----------VQVEEELFKVKVQMEELIKLKTRIEEENKMLITK 2406
Cdd:PRK00409 631 KEKQEELKvgDEVkYLSLGQKgevlsipddkeAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTV 696
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1600-2079 |
8.18e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.09 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1600 EEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEE--------------AERLRKQVKDESQKKREAEDE 1665
Cdd:COG3899 740 EEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRhgnppasarayanlGLLLLGDYEEAYEFGELALAL 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1666 LKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSL 1745
Cdd:COG3899 820 AERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1746 QQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKR 1825
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAA 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1826 SKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLkAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEE 1905
Cdd:COG3899 980 AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLA-AALAALAAAAAAAALLAAAAALALLAALAAAAAAAAA 1058
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1906 LAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASklreLAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILK 1985
Cdd:COG3899 1059 AAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAA----LAAAAAAALALAAALAALALAAALAALALAAAARAAAA 1134
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1986 EKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDT 2065
Cdd:COG3899 1135 LLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALAL 1214
|
490
....*....|....
gi 2069539781 2066 VRQRRLVEEEIRIL 2079
Cdd:COG3899 1215 LALEAAALLLLLLL 1228
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2367-2561 |
8.32e-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: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2367 EAMKQKVQ--VEEELFKVKVqmeELIKLK-TRIEEENKMLitkdkDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLR 2443
Cdd:COG2268 150 EKFAEKVQevAGTDLAKNGL---ELESVAiTDLEDENNYL-----DALGRRKIAEIIRDARIAEAEAERETEIAIAQANR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2444 ELAEQDLAQQRSLAEKILKEKMQAVQEAtrlKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQR 2523
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2524 QLE----------ITANAERLKVQVTEL-----SLAQAKAEEEAKRFKKQAEQ 2561
Cdd:COG2268 299 AEReeaeleadvrKPAEAEKQAAEAEAEaeaeaIRAKGLAEAEGKRALAEAWN 351
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2118-2562 |
8.35e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2118 AEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIV 2197
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2198 AEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTK 2277
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2278 AKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEE 2357
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2358 QQRLKDEVTEAMKQKVQVEE--ELFKVKVQMEELIKLKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVE 2435
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGaaLAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2436 AQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQK 2515
Cdd:COG3064 322 AAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLL 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2069539781 2516 TLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQI 2562
Cdd:COG3064 402 GLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGL 448
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2467-2780 |
9.01e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.98 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2467 AVQEATRLKAEA-EVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLE------------ITANAER 2533
Cdd:pfam09731 71 VVSAVTGESKEPkEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEevlkeaiskaesATAVAKE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2534 LKVQVTELSLAQAKAEEEA-KRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQqSDSDAEKLRKAIADLEQEKEKLK 2612
Cdd:pfam09731 151 AKDDAIQAVKAHTDSLKEAsDTAEISREKATDSALQKAEALAEKLKEVINLAKQSE-EEAAPPLLDAAPETPPKLPEHLD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2613 REAELLQQKSEEMQTAQK------EQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQglkaeqERQ 2686
Cdd:pfam09731 230 NVEEKVEKAQSLAKLVDQykelvaSERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQLS------KKL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2687 QKQMEQEKKQLTTVLEEARKKQAEAEEnvrqkqEELQRLEKQRQKQEKLLAEENQKLREKL-EQLQEEQKTALAQTREIM 2765
Cdd:pfam09731 304 AELKKREEKHIERALEKQKEELDKLAE------ELSARLEEVRAADEAQLRLEFEREREEIrESYEEKLRTELERQAEAH 377
|
330
....*....|....*
gi 2069539781 2766 iqTDDLPQEVVAPSQ 2780
Cdd:pfam09731 378 --EEHLKDVLVEQEI 390
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
174-299 |
9.46e-05 |
|
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: 44.98 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 174 ERDRVQKKTFTKWVNKhllkhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSgdtLPRERDVIRNLRLPREKGRMRfhKLQ 253
Cdd:cd21330 9 EGETREERTFRNWMNS-------LGVNPRVNHLYSDLSDALVIFQLYEKIK---VPVDWNRVNKPPYPKLGENMK--KLE 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2069539781 254 NVQIALDYLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 299
Cdd:cd21330 77 NCNYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1825-2023 |
9.49e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1825 RSKAEESALRQKELAEQELEKQRKLAEGTAQQKFL-AEQELIRLKAEVENgeqqrllleeelfrlknevnEAVQKRKELE 1903
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEK--------------------ELRERRNELQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1904 EELAKLRAEMELLLQSKAKTEEESRSTsEKSKQILEAEASKLRELAEEAARLRalseeaKRQRQLAEEEATHQRAEAERI 1983
Cdd:PRK12704 86 KLEKRLLQKEENLDRKLELLEKREEEL-EKKEKELEQKQQELEKKEEELEELI------EEQLQELERISGLTAEEAKEI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2069539781 1984 LKEKLVAineasrlKAEAEIALKEKEAENErlrrlAEDEA 2023
Cdd:PRK12704 159 LLEKVEE-------EARHEAAVLIKEIEEE-----AKEEA 186
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1717-1862 |
9.50e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.46 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1717 EAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKanealrlrLQ 1796
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK--------QQ 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 1797 AEEVAHKKALAQEE------AEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQ 1862
Cdd:pfam05262 256 EAKNLPKPADTSSPkedkqvAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQ 327
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2158-2497 |
9.82e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.99 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2158 EEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVA-----EEKAHLAAVQQKEQELLQTRQQEQSILDKLREEA 2232
Cdd:pfam13868 6 DELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDemmeeERERALEEEEEKEEERKEERKRYRQELEEQIEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2233 ERAKKAAEDaEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKA------KAQEDAEKLRKEAELEAARRAQAEQAAL 2306
Cdd:pfam13868 86 EQKRQEEYE-EKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREeidefnEEQAEWKELEKEEEREEDERILEYLKEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2307 KQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQM 2386
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2387 EELIKLKTRIEEEnkmlitKDKDNMQKFLAEEAEKMKQVAEEAARlsveaqEAARLRELAEQDLAQQRSLAEKILKEKMQ 2466
Cdd:pfam13868 245 IELKERRLAEEAE------REEEEFERMLRKQAEDEEIEQEEAEK------RRMKRLEHRRELEKQIEEREEQRAAEREE 312
|
330 340 350
....*....|....*....|....*....|.
gi 2069539781 2467 AVQEATRLKAEAEvlQKQKDLAQEQAKKLQE 2497
Cdd:pfam13868 313 ELEEGERLREEEA--ERRERIEEERQKKLKE 341
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2392-2563 |
9.87e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2392 LKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEA 2471
Cdd:PRK00409 499 LPENIIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQA 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2472 TRlKAEAEVLQKQKDLAQEQAKKLQEDKEQ----MQLRLAEEAEGFQKTLEAERQRQ--------------------LEI 2527
Cdd:PRK00409 579 IK-EAKKEADEIIKELRQLQKGGYASVKAHelieARKRLNKANEKKEKKKKKQKEKQeelkvgdevkylslgqkgevLSI 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2069539781 2528 TANAE--------RLKVQVTELSLAQAKAEEEAKRFKKQAEQIS 2563
Cdd:PRK00409 658 PDDKEaivqagimKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3509-3546 |
1.03e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.03e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2069539781 3509 KKYLQGSDCIAGVYVEETKEKLSIYEAMRRNLLLPSTA 3546
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1581-1727 |
1.03e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1581 QIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQ---VKD--- 1654
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnVRNnke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1655 --------ESQKKR-----EAEDELKHKVQAEQQAAREKQKALEDLQKlRLQAEEAERRMKQAELEKER-QVQLAHEAAQ 1720
Cdd:COG1579 91 yealqkeiESLKRRisdleDEILELMERIEELEEELAELEAELAELEA-ELEEKKAELDEELAELEAELeELEAEREELA 169
|
....*..
gi 2069539781 1721 KSAEADL 1727
Cdd:COG1579 170 AKIPPEL 176
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4435-4468 |
1.04e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.04e-04
10 20 30
....*....|....*....|....*....|....
gi 2069539781 4435 EETGPVAGILDTDTLEKVSITEAMRRNLVDNITG 4468
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1644-2116 |
1.06e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1644 EAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMK--QAELEKERQVQLAHEAAQK 1721
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAelRQQLNNERDEPRSVPPNMS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1722 SAEadLQSRRLSFAEKTAQLELSLQQEHitiTHLQEEAERLKKL-QLEAEQSREEAdkEVEKWRQKA-------NEALRL 1793
Cdd:PRK10929 104 TDA--LEQEILQVSSQLLEKSRQAQQEQ---DRAREISDSLSQLpQQQTEARRQLN--EIERRLQTLgtpntplAQAQLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1794 RLQAEEVAHKKALaqeeaekqkedaerearkrskaeesalrqkelaeQELEkqrkLAEGTAQQKflaeQELIRLKAEVen 1873
Cdd:PRK10929 177 ALQAESAALKALV----------------------------------DELE----LAQLSANNR----QELARLRSEL-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1874 geqqrllleeelfrlknevneaVQKRKE-LEEELAKLRAEMELLLQSKAKteeesrSTSEKSKQILEAEASKLRELAEEA 1952
Cdd:PRK10929 213 ----------------------AKKRSQqLDAYLQALRNQLNSQRQREAE------RALESTELLAEQSGDLPKSIVAQF 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1953 ARLRALSEEAKRQRQLAEEEATHQRAEAERIL--KEKLVAINEASRLkaeaeiaLKEKEAENERLR----RLAEDEAYQR 2026
Cdd:PRK10929 265 KINRELSQALNQQAQRMDLIASQQRQAASQTLqvRQALNTLREQSQW-------LGVSNALGEALRaqvaRLPEMPKPQQ 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2027 rlLEEQAAQ------HKQDIEEKIAQLKKSseseleRQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRI 2100
Cdd:PRK10929 338 --LDTEMAQlrvqrlRYEDLLNKQPQLRQI------RQADGQPLTAEQNRILDAQLRTQRELLNSLLSGGDTLILELTKL 409
|
490 500
....*....|....*....|
gi 2069539781 2101 K----QSAEEIQRSKEQAER 2116
Cdd:PRK10929 410 KvansQLEDALKEVNEATHR 429
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
2200-2619 |
1.09e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 48.52 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2200 EKAHLAAVQQKEQELLQTR-QQEQSILDKLREEAERAKKAAEDAEfarikaEQEAALSRQLVEEAERMKQRAEEEAQTKA 2278
Cdd:pfam15070 12 ERDQYAENLKEEGAVWQQKmQQLSEQVRTLREEKERSVSQVQELE------TSLAELKNQAAVPPAEEEQPPAGPSEEEQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2279 KAQEDAEKLRKEAELEAARRaqaeqaalkQKQLADAEmakhkkfaeQTLRQKAQVEQELTKVKLQLEETDHQ----KSIL 2354
Cdd:pfam15070 86 RLQEEAEQLQKELEALAGQL---------QAQVQDNE---------QLSRLNQEQEQRLLELERAAERWGEQaedrKQIL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2355 EEEQQRlKDEVTEAMKQKVQVEEelfkvkvQMEELIKLKTRIEEENkMLITKDKDNMQKFLAEEAEKMKQVAEEAARL-- 2432
Cdd:pfam15070 148 EDMQSD-RATISRALSQNRELKE-------QLAELQNGFVKLTNEN-MELTSALQSEQHVKKELAKKLGQLQEELGELke 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2433 --SVEAQEAARLRELAEQDLA--QQRSLA--------EKILKEKMQAVQEATRL-------KAEAEVLQKQKDLAQEQAK 2493
Cdd:pfam15070 219 tlELKSQEAQSLQEQRDQYLAhlQQYVAAyqqlasekEELHKQYLLQTQLMDRLqheevqgKVAAEMARQELQETQERLE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2494 KLQEDKEQMQLRL---AEEAEG----FQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQisQKL 2566
Cdd:pfam15070 299 ALTQQNQQLQAQLsllANPGEGdgleSEEEEEEAPRPSLSIPEDFESREAMVAFFNSALAQAEEERAELRRQLKE--QKR 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2567 HQTELATQEKMTLVQTLEIQRQQSDSD--------------AEKLRKAIADLEQEKEKLKREAELLQ 2619
Cdd:pfam15070 377 RCRRLAQQAAPAQEEPEHEAHAPGTGGdsvpvevhqalqvaMEKLQSRFTELMQEKADLKERVEELE 443
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1645-1846 |
1.09e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 48.53 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1645 AERLRKQVKDESQKKREAEDELKHKVQAEQQAAREK---QKALEDLQKLRLQAEEaerrmkQAELEKERQVqLAH----- 1716
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEELRADEAERARELdllRFQLEELEAAALQPGE------EEELEEERRR-LSNaeklr 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1717 EAAQKSAEAdLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAeqsrEEADKEVEKWRQKAN------EA 1790
Cdd:COG0497 226 EALQEALEA-LSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIEL----EEAASELRRYLDSLEfdperlEE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1791 LRLRLQA------------EEV-AHKKALAQE------------EAEKQKEDAEREARKrsKAEE-SALRQKelAEQELE 1844
Cdd:COG0497 301 VEERLALlrrlarkygvtvEELlAYAEELRAElaelensderleELEAELAEAEAELLE--AAEKlSAARKK--AAKKLE 376
|
..
gi 2069539781 1845 KQ 1846
Cdd:COG0497 377 KA 378
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2248-2441 |
1.10e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2248 KAEQEAalsRQLVEEAERMKQRAEEEAQTKAKaqEDAEKLRKEAEleaarraqaeqaalKQKQLADAEMAKhkkfAEQTL 2327
Cdd:PRK12704 35 EAEEEA---KRILEEAKKEAEAIKKEALLEAK--EEIHKLRNEFE--------------KELRERRNELQK----LEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2328 RQKaqvEQELTKvklQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTriEEENKMLItkd 2407
Cdd:PRK12704 92 LQK---EENLDR---KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA--EEAKEILL--- 160
|
170 180 190
....*....|....*....|....*....|....
gi 2069539781 2408 kDNMQKFLAEEAEKMKQVAEEAARLsvEAQEAAR 2441
Cdd:PRK12704 161 -EKVEEEARHEAAVLIKEIEEEAKE--EADKKAK 191
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1624-1721 |
1.10e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1624 LQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAARE--KQKALEDLQKLRLQAEEAERRM 1701
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKeaKKEADEIIKELRQLQKGGYASV 604
|
90 100
....*....|....*....|.
gi 2069539781 1702 KQAEL-EKERQVQLAHEAAQK 1721
Cdd:PRK00409 605 KAHELiEARKRLNKANEKKEK 625
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4126-4160 |
1.10e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|....*
gi 2069539781 4126 LLEAQAATGYVVDPIKGLKLTVEEAVRMGIVGPEF 4160
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1537-1854 |
1.11e-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: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1537 KEALELQRRMEEEVSRRQLVAVDAEQ---QKQTIQQELSQMKLssdaqiqaKLKLIEEVEFSRRKVEEeiRMVRlQLEAT 1613
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKlllENKELTQEASDMTL--------ELKKHQEDIINCKKQEE--RMLK-QIENL 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1614 ERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQklrlQ 1693
Cdd:pfam05483 540 EEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH----Q 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1694 AEEAERRMKQAElekERQVQlAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSR 1773
Cdd:pfam05483 616 ENKALKKKGSAE---NKQLN-AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQ 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1774 EEADKEVEkwrQKANEALRLrLQAEEVAHKKALAQEEAE----KQKEDAEREARKRSKAEESALR--------QKELAEQ 1841
Cdd:pfam05483 692 KEIDKRCQ---HKIAEMVAL-MEKHKHQYDKIIEERDSElglyKNKEQEQSSAKAALEIELSNIKaellslkkQLEIEKE 767
|
330
....*....|....
gi 2069539781 1842 ELEK-QRKLAEGTA 1854
Cdd:pfam05483 768 EKEKlKMEAKENTA 781
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2474-2761 |
1.11e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.75 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2474 LKAEAEVLQKQKDLAQEQaKKLQEDKEQMQLRLA------EEAEGFQKTLEAERQRQLEITANAERLKvqvtelslaQAK 2547
Cdd:PRK11281 41 VQAQLDALNKQKLLEAED-KLVQQDLEQTLALLDkidrqkEETEQLKQQLAQAPAKLRQAQAELEALK---------DDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2548 AEEEAKRFKKQA-EQISQKLHQTELATQEkmtlvqtleIQRQQSDSDAEklrkAIAdleqekeklkreaelLQQKSEEMQ 2626
Cdd:PRK11281 111 DEETRETLSTLSlRQLESRLAQTLDQLQN---------AQNDLAEYNSQ----LVS---------------LQTQPERAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2627 TAqkeqLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEklfqeevnkaqglkAEQERQQKQMEQEKKQLT--TVLEEA 2704
Cdd:PRK11281 163 AA----LYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQ--------------AEQALLNAQNDLQRKSLEgnTQLQDL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2705 RKKQAEaeenvrQKQEELQRLEKQRQKQEKLLAEENQKLREK-LEQLQEEQKTALAQT 2761
Cdd:PRK11281 225 LQKQRD------YLTARIQRLEHQLQLLQEAINSKRLTLSEKtVQEAQSQDEAARIQA 276
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
2112-2260 |
1.12e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 48.33 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2112 EQAEREAEELRQLALEeenhrreaeakVKKISAAEQEAARQCKAALEEVERLKAKAEE--ARRQKELAEKESERQIQLAQ 2189
Cdd:PRK12472 193 ETLAREAEDAARAADE-----------AKTAAAAAAREAAPLKASLRKLERAKARADAelKRADKALAAAKTDEAKARAE 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2190 EAAQKrivAEEKAHLAAVQqkeqelLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLV 2260
Cdd:PRK12472 262 ERQQK---AAQQAAEAATQ------LDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDAKLALEPV 323
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1512-1925 |
1.15e-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: 48.35 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1512 AEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEE-EVSRRQLvavdaEQQKQTIQQELSQmklsSDAQIQAKLKLIE 1590
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQwERQRREL-----ESRVAELKEELRQ----SREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1591 EVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAErqkrlaqEEAERLRKQVKDESQKKREAEDELKHKV 1670
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-------TELERMKERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1671 QAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQksaeadlqsrrlsfaeKTAQLELSLQQehi 1750
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR----------------KEAENEALLEE--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1751 tithLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKAlaqeeaekQKEDAEREARKRSKAEE 1830
Cdd:pfam07888 239 ----LRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLA--------DASLALREGRARWAQER 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1831 SALRQKelAEQELEKQRKL-AEGTAQQKFLAEQELIRLKAEVENGeQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKL 1909
Cdd:pfam07888 307 ETLQQS--AEADKDRIEKLsAELQRLEERLQEERMEREKLEVELG-REKDCNRVQLSESRRELQELKASLRVAQKEKEQL 383
|
410
....*....|....*.
gi 2069539781 1910 RAEMELLLQSKAKTEE 1925
Cdd:pfam07888 384 QAEKQELLEYIRQLEQ 399
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1568-1926 |
1.17e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1568 QQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAER 1647
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1648 LRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADL 1727
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1728 QSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALA 1807
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1808 QEEAEKQkeDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFR 1887
Cdd:COG4372 252 LEEVILK--EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350
....*....|....*....|....*....|....*....
gi 2069539781 1888 LKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEE 1926
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1272-2024 |
1.18e-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: 48.80 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1272 KALEATKAELKRLRGQVEGHQPLFNTLEMDLAKASEVNERMVRG--HSERdidLDRYRERVQQL---LERWQAILAQIDL 1346
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAlrQQEK---IERYQEDLEELterLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1347 R-----------QRELDQLGRQLRYYRESYDWL----IQWiREARQRQEHLQAV---PVTNSKSVREQLLQEKKLLEECD 1408
Cdd:COG3096 376 QlaeaearleaaEEEVDSLKSQLADYQQALDVQqtraIQY-QQAVQALEKARALcglPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1409 RN----REKVEECQCFAKQYIDAikdYELqlvtykaqVEPVASPAKKPKVQSASDSVIQEYVDLRTRYSELTTLTSQY-- 1482
Cdd:COG3096 455 EEvlelEQKLSVADAARRQFEKA---YEL--------VCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLae 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1483 LKFITETLRRLEEEEKAAEKLKEEERQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEE------EVSRRQLV 1556
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQlrarikELAARAPA 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1557 AVDAEQQKQTIQQELSQMKLSS---DAQIQAKLKLIEEVEFSRRKVEEeiRMVRLQLEATE-RQRAGAED-ELQALRDRA 1631
Cdd:COG3096 604 WLAAQDALERLREQSGEALADSqevTAAMQQLLEREREATVERDELAA--RKQALESQIERlSQPGGAEDpRLLALAERL 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1632 EE---AERQKRLAQEEA-------------------ERLRKQVK-------------------DESQKKREaEDELKHKV 1670
Cdd:COG3096 682 GGvllSEIYDDVTLEDApyfsalygparhaivvpdlSAVKEQLAgledcpedlyliegdpdsfDDSVFDAE-ELEDAVVV 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1671 QAEQ---------------QAAREKQkaledLQKLRLQAEEAERRMKQAELEKERQVQLAHE-----------AAQKSAE 1724
Cdd:COG3096 761 KLSDrqwrysrfpevplfgRAAREKR-----LEELRAERDELAEQYAKASFDVQKLQRLHQAfsqfvgghlavAFAPDPE 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1725 ADLQ--SRRLSFAEKT-AQLELSLQQEHITITHLQEEAERLKKLQLEA--------EQSREEADKEVEKWRQKAN----- 1788
Cdd:COG3096 836 AELAalRQRRSELERElAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladetlADRLEELREELDAAQEAQAfiqqh 915
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1789 -EALR--------LR---LQAEEVA--HKKALAQEEAEKQKEDAEREARKRSKA---EES------------ALRQK-EL 1838
Cdd:COG3096 916 gKALAqleplvavLQsdpEQFEQLQadYLQAKEQQRRLKQQIFALSEVVQRRPHfsyEDAvgllgensdlneKLRARlEQ 995
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1839 AEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFR-----LKNEVNEAVQKRKELEEELAKLRAEM 1913
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqaDAEAEERARIRRDELHEELSQNRSRR 1075
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1914 ELLLQSKAKTEEESRSTSEKSKQiLEAEASKLRELAEEA----ARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKlv 1989
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRK-AERDYKQEREQVVQAkagwCAVLRLARDNDVERRLHRRELAYLSADELRSMSDK-- 1152
|
890 900 910
....*....|....*....|....*....|....*...
gi 2069539781 1990 aineasRLKaeaeiALKEKEAENERLR---RLAEDEAY 2024
Cdd:COG3096 1153 ------ALG-----ALRLAVADNEHLRdalRLSEDPRR 1179
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2050-2258 |
1.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2050 SSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELT----RIKQSAEEIQRSKEQAEREAEELRQLA 2125
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqaEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2126 ---------------------LEEENHRREAeakVKKISAAEQEAARQCKAALEEVERLKAKAEEARR-----QKELAEK 2179
Cdd:COG3883 93 ralyrsggsvsyldvllgsesFSDFLDRLSA---LSKIADADADLLEELKADKAELEAKKAELEAKLAelealKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2180 ESERQIQLAQeaaQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQ 2258
Cdd:COG3883 170 KAELEAQQAE---QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1889-2190 |
1.23e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1889 KNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESrstsEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQL 1968
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1969 AEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLK 2048
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2049 KSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEE 2128
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2129 ENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQE 2190
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3881-3917 |
1.23e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.23e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2069539781 3881 RPLLEAQAATGFIVDPIKNEMLTVDEAVRKAVVGPEM 3917
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2435-2764 |
1.26e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 47.72 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2435 EAQEAARLRELAEQDLAQQRSLAEKI----LKEKMQAVQEATRLKaEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEA 2510
Cdd:pfam15558 19 EEQRMRELQQQAALAWEELRRRDQKRqetlERERRLLLQQSQEQW-QAEKEQRKARLGREERRRADRREKQVIEKESRWR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2511 EGFQKTlEAERQRQLEITANAERLKVQVTELSLaqaKAEEEAKRfkKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQS 2590
Cdd:pfam15558 98 EQAEDQ-ENQRQEKLERARQEAEQRKQCQEQRL---KEKEEELQ--ALREQNSLQLQERLEEACHKRQLKEREEQKKVQE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2591 DSDAEKLRKAIadLEQEKEKLKREAELLQQKSEEmQTAQKEQLRQETQMLQqtfrsekdvllqKERFVEEEKAKLEKLFQ 2670
Cdd:pfam15558 172 NNLSELLNHQA--RKVLVDCQAKAEELLRRLSLE-QSLQRSQENYEQLVEE------------RHRELREKAQKEEEQFQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2671 eevnKAQGLKAEQERQQkqmeQEKKQLTTVLEEARKKQAE--AEENVRQKQEELQ--RLEKQR-QKQEKLLAEENQKLR- 2744
Cdd:pfam15558 237 ----RAKWRAEEKEEER----QEHKEALAELADRKIQQARqvAHKTVQDKAQRARelNLEREKnHHILKLKVEKEEKCHr 308
|
330 340 350
....*....|....*....|....*....|.
gi 2069539781 2745 -----------EKLEQLQEEQKTALAQTREI 2764
Cdd:pfam15558 309 egikeaikkkeQRSEQISREKEATLEEARKT 339
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1901-2180 |
1.26e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 48.31 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1901 ELEEELAKLRAEMELLLQSKAK-TEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEE---AKRQRQLA------- 1969
Cdd:PLN03229 433 ELEGEVEKLKEQILKAKESSSKpSELALNEMIEKLKKEIDLEYTEAVIAMGLQERLENLREEfskANSQDQLMhpvlmek 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1970 ----EEEATHQ--RAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAedEAYQRRLLEEQAaqhkQDIEEK 2043
Cdd:PLN03229 513 ieklKDEFNKRlsRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFK--EVMDRPEIKEKM----EALKAE 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2044 IAQLKKSSESELErqKSLVDDTVRQRRLVEEEI-RILK---LNFEKASHGKTDLELELT------RIKQSAEEIQRSKEQ 2113
Cdd:PLN03229 587 VASSGASSGDELD--DDLKEKVEKMKKEIELELaGVLKsmgLEVIGVTKKNKDTAEQTPppnlqeKIESLNEEINKKIER 664
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2114 AEREAE-----ELRQLALEEENHRREAEAKvKKISAAEQEAARQCKAALEEVErLKAKAEEARrqKELAEKE 2180
Cdd:PLN03229 665 VIRSSDlkskiELLKLEVAKASKTPDVTEK-EKIEALEQQIKQKIAEALNSSE-LKEKFEELE--AELAAAR 732
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1656-1869 |
1.31e-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: 48.68 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1656 SQKKREAEDELKHKVQ--AEQQAAREKQKALEDLQKLrlqaeeaerrmkqaelEKERQVQLAHEAaqkSAEADLQSRRLS 1733
Cdd:NF012221 1538 SESSQQADAVSKHAKQddAAQNALADKERAEADRQRL----------------EQEKQQQLAAIS---GSQSQLESTDQN 1598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1734 FAEKTAQLEL-SLQQEHITITH-LQEEAERLKKLQLEAEQSREEADkeveKWR----------------------QKANE 1789
Cdd:NF012221 1599 ALETNGQAQRdAILEESRAVTKeLTTLAQGLDALDSQATYAGESGD----QWRnpfagglldrvqeqlddakkisGKQLA 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1790 ALRLRLQAEEVAHKKALAQEE------------AEKQKEDAEREARKRskaEESALRQKELAEQElEKQRKLAEGTAQQK 1857
Cdd:NF012221 1675 DAKQRHVDNQQKVKDAVAKSEagvaqgeqnqanAEQDIDDAKADAEKR---KDDALAKQNEAQQA-ESDANAAANDAQSR 1750
|
250
....*....|..
gi 2069539781 1858 FLAEQELIRLKA 1869
Cdd:NF012221 1751 GEQDASAAENKA 1762
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2456-2825 |
1.34e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2456 LAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQ---LRLAEEAEGFQKTLEAERQRQLEITANAE 2532
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2533 RLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELAtqekmtlVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLK 2612
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE-------RQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2613 REAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQ 2692
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2693 EKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLP 2772
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2773 QEVVAPSQVPQMKAVPNGRDMIDGISQNGEAELAFDGIRQKVSAKKLAEAGIL 2825
Cdd:COG4372 317 LLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2890-2923 |
1.37e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.37e-04
10 20 30
....*....|....*....|....*....|....
gi 2069539781 2890 LLEAQAASGFVIDPVRNRTLSVSEAVKEGVVGPE 2923
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YydB |
COG5293 |
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]; |
2034-2264 |
1.40e-04 |
|
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown];
Pssm-ID: 444096 [Multi-domain] Cd Length: 572 Bit Score: 48.02 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2034 AQHKQDIEEKIAQLKKSSES-ELERQKSLVDDT--VRQRRLVEEEiRILKLNFEKAshgKTDLELELTRIKQSAEEIQRS 2110
Cdd:COG5293 183 AAEKYELKEEIKELKKLRKAlKDELIGSVVKSIseLRAEILELEE-EIEKLEKDLE---KFDVAENYEELEKELDELKRE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2111 KEQAEREAEEL-RQLALEEENHRREAEAKVKKISAAEQEAAR----QCKAALEEVERLKAK----------AEEARRQKE 2175
Cdd:COG5293 259 INELRNERYSLeRRLKKIERSLEEEIDIDPDELEKLYEEAGVffpdQVKKRFEEVEAFHKSivenrreyleEEIAELEAE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2176 LAEKESERQIQLAQEAAQKRIVAEEKA--HLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEA 2253
Cdd:COG5293 339 LEELEAELAELGKERAELLSLLDSKGAldKYKELQEELAELEAELEELESRLEKLQELEDEIRELKEERAELKEEIESDI 418
|
250
....*....|.
gi 2069539781 2254 ALSRQLVEEAE 2264
Cdd:COG5293 419 EERKELLDEIN 429
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
2109-2292 |
1.45e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 48.50 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2109 RSKEQAEREAEELRQLALEEENHRREAeakvkkisaAEQEAARQCKAALEEVErlKAKAEEARRQKELAEKESERQ---I 2185
Cdd:PRK10811 620 RRDTRDNRTRREGRENREENRRNRRQA---------QQQTAETRESQQAEVTE--KARTQDEQQQAPRRERQRRRNdekR 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2186 QLAQEAaqKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLR-EEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAe 2264
Cdd:PRK10811 689 QAQQEA--KALNVEEQSVQETEQEERVQQVQPRRKQRQLNQKVRiEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELV- 765
|
170 180
....*....|....*....|....*...
gi 2069539781 2265 rmKQRAEEEAQTKAKAQEDAEKLRKEAE 2292
Cdd:PRK10811 766 --KVPLPVVAQTAPEQDEENNAENRDNN 791
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2579-2744 |
1.49e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2579 LVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLqqtfRSEKDVLLQKERFV 2658
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEA----KKEADEIIKELRQL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2659 EEE-----KAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKK-----------QLTTVLEEARKKQAEAEE---NVRQKQ 2719
Cdd:PRK00409 597 QKGgyasvKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKvgdevkylslgQKGEVLSIPDDKEAIVQAgimKMKVPL 676
|
170 180
....*....|....*....|....*
gi 2069539781 2720 EELQRLEKQRQKQEKLLAEENQKLR 2744
Cdd:PRK00409 677 SDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1576-1808 |
1.49e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1576 LSSDAQIQAKLKLIEEvefsRRKVEEEIRMVRLQLEATERQRAGAED---ELQALRDRAEEAERQKRLAQEEAERLRKQV 1652
Cdd:PRK11281 35 LPTEADVQAQLDALNK----QKLLEAEDKLVQQDLEQTLALLDKIDRqkeETEQLKQQLAQAPAKLRQAQAELEALKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1653 KDESQKKREAE--DELKHKVQAEQQAAREKQKALEDLQKL---------RLQAE--EAERRMKQ------------AELE 1707
Cdd:PRK11281 111 DEETRETLSTLslRQLESRLAQTLDQLQNAQNDLAEYNSQlvslqtqpeRAQAAlyANSQRLQQirnllkggkvggKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1708 KERQVQLahEAAQKSAEADLQSRRLSFAEKTA-QLELSLQQEHIT--ITHLQEEAERL------KKLQLeAEQSREEADK 1778
Cdd:PRK11281 191 PSQRVLL--QAEQALLNAQNDLQRKSLEGNTQlQDLLQKQRDYLTarIQRLEHQLQLLqeainsKRLTL-SEKTVQEAQS 267
|
250 260 270
....*....|....*....|....*....|
gi 2069539781 1779 evekwRQKANEALRLRLQAEEVAHKKALAQ 1808
Cdd:PRK11281 268 -----QDEAARIQANPLVAQELEINLQLSQ 292
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1557-1837 |
1.51e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.77 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1557 AVDAEQQKQTIQQElsqmklssdaqIQAKLKlieevefsrrkveeeirMVRLQleatERQRAGAEDELQALRDRAEEAER 1636
Cdd:PRK11637 42 ASDNRDQLKSIQQD-----------IAAKEK-----------------SVRQQ----QQQRASLLAQLKKQEEAISQASR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1637 QKRLAQEEAERLRKQVK--DESQKKREAEDELKHKVQAEQQAAREKQKALEDLQkLRLQAEEAERRmkqaelekERqvQL 1714
Cdd:PRK11637 90 KLRETQNTLNQLNKQIDelNASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQ-LILSGEESQRG--------ER--IL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1715 AH-----EAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHItithLQEEAERLKKLQlEAEQSREEADKEVEKWRQKANE 1789
Cdd:PRK11637 159 AYfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTL----LYEQQAQQQKLE-QARNERKKTLTGLESSLQKDQQ 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2069539781 1790 ALrLRLQAEEVAHKKALAQEEAEKqKEDAEREARkrskaEESALRQKE 1837
Cdd:PRK11637 234 QL-SELRANESRLRDSIARAEREA-KARAEREAR-----EAARVRDKQ 274
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2224-2387 |
1.52e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.08 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2224 ILDKLREEAER-AKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAE 2302
Cdd:pfam05262 182 VVEALREDNEKgVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLP 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2303 QAALKQKQLADAEMAKH-KKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSilEEEQQRLKDEVTEAMKQKVQVEEELFK 2381
Cdd:pfam05262 262 KPADTSSPKEDKQVAENqKREIEKAQIEIKKNDEEALKAKDHKAFDLKQES--KASEKEAEDKELEAQKKREPVAEDLQK 339
|
....*.
gi 2069539781 2382 VKVQME 2387
Cdd:pfam05262 340 TKPQVE 345
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2314-2705 |
1.58e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.98 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2314 AEMAKHKKFAEQTLRQKAQVEQEL----TKVKLQLE----ETDHQKSILEEE---QQRLKDEVTEAMKQKVQVEEELFKV 2382
Cdd:pfam15964 324 AEAQQRESSAYEQVKQAVQMTEEAnfekTKALIQCEqlksELERQKERLEKElasQQEKRAQEKEALRKEMKKEREELGA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2383 KV-----QMEELIKLKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEaarlRELAEQDLAQQRSLA 2457
Cdd:pfam15964 404 TMlalsqNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMK----KDEAEKEHREYRTKT 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2458 EKILKEKMQAVQ----EATRLKAEAEVLQKQKDLAQEQAKKLQE--DKEQMQLRLA-EEAEGFQKTLEAErqrqleitAN 2530
Cdd:pfam15964 480 GRQLEIKDQEIEklglELSESKQRLEQAQQDAARAREECLKLTEllGESEHQLHLTrLEKESIQQSFSNE--------AK 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2531 AERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELAT---QEKMTLVQTLEiqrqqsdSDAEKLRKAIADLEQE 2607
Cdd:pfam15964 552 AQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAklkEECCTLAKKLE-------EITQKSRSEVEQLSQE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2608 KEKLKREAELLQQKSEEMQtaqkeqlrqetqmlqqtfrsekDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLkAEQERQQ 2687
Cdd:pfam15964 625 KEYLQDRLEKLQKRNEELE----------------------EQCVQHGRMHERMKQRLRQLDKHCQATAQQL-VQLLSKQ 681
|
410
....*....|....*...
gi 2069539781 2688 KQMEQEKKQLTTVLEEAR 2705
Cdd:pfam15964 682 NQLFKERQNLTEEVQSLR 699
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1515-1684 |
1.68e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1515 EAQLEKQRQLAEAHARAKA-------QAEKEALELQRRMEEEV-SRRQLVavdAEQQKQTIQQElsqmklssdAQIQAKL 1586
Cdd:PRK12704 35 EAEEEAKRILEEAKKEAEAikkeallEAKEEIHKLRNEFEKELrERRNEL---QKLEKRLLQKE---------ENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1587 KLIEevefsrrKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEA-ERQKRLAQEEA-ERLRKQVKDESQKK----- 1659
Cdd:PRK12704 103 ELLE-------KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElERISGLTAEEAkEILLEKVEEEARHEaavli 175
|
170 180
....*....|....*....|....*
gi 2069539781 1660 REAEDElkhkvqAEQQAAREKQKAL 1684
Cdd:PRK12704 176 KEIEEE------AKEEADKKAKEIL 194
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2545-2736 |
1.69e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2545 QAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAE-KLRKAIADLEQEKEKLKREAELLQQKSE 2623
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEeAAKQAALKQKQAEEAAAKAAAAAKAKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2624 EMQTAQKEQLRQETQMLQQTFRSEkdvllQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQK-QMEQEKKQLTTVLE 2702
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAE-----AAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKaAAEAKKKAAAEAKA 225
|
170 180 190
....*....|....*....|....*....|....
gi 2069539781 2703 EARKKQAEAEENVRQKQEELQRLEKQRQKQEKLL 2736
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1960-2242 |
1.69e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 47.67 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1960 EEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQD 2039
Cdd:PRK07735 13 EAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2040 IEEKIAQLKKSSESELERQKslvddtvrqrrlveeeirilklnfEKASHGKTDLELELTRIKQSAEEIQRSKEQAeREAE 2119
Cdd:PRK07735 93 AKAKAAAAAKAKAAALAKQK------------------------REGTEEVTEEEKAAAKAKAAAAAKAKAAALA-KQKR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2120 ELRQLALEEENHRREAEAKVKKISAAEQEAarqckAALEeverlKAKAEEARRQKELAEKEserqiqlAQEAAQKRIVAE 2199
Cdd:PRK07735 148 EGTEEVTEEEEETDKEKAKAKAAAAAKAKA-----AALA-----KQKAAEAGEGTEEVTEE-------EKAKAKAKAAAA 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2069539781 2200 EKAHLAAVQQkeQELLQTRQQEQSILDKLREEAERAKKAAEDA 2242
Cdd:PRK07735 211 AKAKAAALAK--QKASQGNGDSGDEDAKAKAIAAAKAKAAAAA 251
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2585-2760 |
1.74e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2585 IQRQQSDS-DAEKLRKAIAdleqekeklKREAELLQQKSEEMQTAQKEQLRQETQMLQQtfrsekdvllQKErfvEEEKA 2663
Cdd:PRK09510 67 QQQQQKSAkRAEEQRKKKE---------QQQAEELQQKQAAEQERLKQLEKERLAAQEQ----------KKQ---AEEAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2664 KLEKLFQEEVNKAQglKAEQERQQKQMEQEKKQLttvleEARKKQAEAEENVRQKQEELQRLEKQRQKqeKLLAEENQKL 2743
Cdd:PRK09510 125 KQAALKQKQAEEAA--AKAAAAAKAKAEAEAKRA-----AAAAKKAAAEAKKKAEAEAAKKAAAEAKK--KAEAEAAAKA 195
|
170
....*....|....*..
gi 2069539781 2744 REKLEQLQEEQKTALAQ 2760
Cdd:PRK09510 196 AAEAKKKAEAEAKKKAA 212
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1606-1856 |
1.77e-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: 48.29 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1606 VRLQLEATERQRAGAEDELQALRDRAE-EAERQkRLAQEEAERLRKQVKdeSQKKREAEDElkHKVQAEQQAAREkqkal 1684
Cdd:NF012221 1540 SSQQADAVSKHAKQDDAAQNALADKERaEADRQ-RLEQEKQQQLAAISG--SQSQLESTDQ--NALETNGQAQRD----- 1609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1685 edlqklrlqAEEAERRMKQAEL-EKERQVQLAHEAAQKSAEADlQSRRLSFAEKTaqleLSLQQEHItithlqEEAERLK 1763
Cdd:NF012221 1610 ---------AILEESRAVTKELtTLAQGLDALDSQATYAGESG-DQWRNPFAGGL----LDRVQEQL------DDAKKIS 1669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1764 KLQLEAEQSREEA-----DKEVEKWRQKANEALRLRLQAEEVAHKkalAQEEAEKQKEDAEREARKRSKAEESALRQKEL 1838
Cdd:NF012221 1670 GKQLADAKQRHVDnqqkvKDAVAKSEAGVAQGEQNQANAEQDIDD---AKADAEKRKDDALAKQNEAQQAESDANAAAND 1746
|
250
....*....|....*...
gi 2069539781 1839 AEQELEKQRKLAEGTAQQ 1856
Cdd:NF012221 1747 AQSRGEQDASAAENKANQ 1764
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3549-3582 |
1.84e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.84e-04
10 20 30
....*....|....*....|....*....|....
gi 2069539781 3549 LLEAQAATGFMVDPVRNQRLPVHEAVKAGFVGPE 3582
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1507-1683 |
1.86e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1507 ERQRLAEveaqlEKQRQLAEahARAKAQAEKEALELQRRMEEEVSRRQLvAVDAEQQKQTIQQELSQMKLSsdaqiqakl 1586
Cdd:pfam17380 436 EVRRLEE-----ERAREMER--VRLEEQERQQQVERLRQQEEERKRKKL-ELEKEKRDRKRAEEQRRKILE--------- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1587 kliEEVEFSRRK-VEEEIRMVRLQLEATERQRAGAEDElqalRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDE 1665
Cdd:pfam17380 499 ---KELEERKQAmIEEERKRKLLEKEMEERQKAIYEEE----RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM 571
|
170
....*....|....*...
gi 2069539781 1666 LKHKVQAEQQAAREKQKA 1683
Cdd:pfam17380 572 EREREMMRQIVESEKARA 589
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2215-2570 |
1.94e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 47.72 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2215 LQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEE-------------------------AERMKQR 2269
Cdd:pfam05701 34 VERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElklnleraqteeaqakqdselaklrVEEMEQG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2270 AEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQ---LADAEMAKHKkfAEQTLRQKAQVEQ-------ELTK 2339
Cdd:pfam05701 114 IADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYaslVSERDIAIKR--AEEAVSASKEIEKtveeltiELIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2340 VKLQLEETdhQKSILEEEQQRL------KDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKDKD---N 2410
Cdd:pfam05701 192 TKESLESA--HAAHLEAEEHRIgaalarEQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLKAElaaY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2411 MQKFLAEEAEKMKQvAEEAARLSVEAQEAARlRELAEQDLAQQRSLAE-KILKEKMQAVQ-EATRLKAEAEVLQKQKDLA 2488
Cdd:pfam05701 270 MESKLKEEADGEGN-EKKTSTSIQAALASAK-KELEEVKANIEKAKDEvNCLRVAAASLRsELEKEKAELASLRQREGMA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2489 QEQAKKLQE--DKEQMQLRLAEEAEGFQKTLEAERQRQLEITAN-AERLKvqvtelSLAQAkAEEEAKRFKKQAEQISQK 2565
Cdd:pfam05701 348 SIAVSSLEAelNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQeAEEAK------SLAQA-AREELRKAKEEAEQAKAA 420
|
....*
gi 2069539781 2566 LHQTE 2570
Cdd:pfam05701 421 ASTVE 425
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1725-2224 |
2.01e-04 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 47.52 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1725 ADLQSRRLSF---AEKTAQLELSLQQEHITI-THLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEV 1800
Cdd:pfam15450 23 ADLQAEVVSLrghKERCEHATLSLLRELLQVrAHVQLQDSELKQLRQEVQQAARAPEKEALEFPGPQNQNQMQALDKRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1801 AHKKALAQEEAEKQKEDAEREARKrskaEESALRQKELA---EQElEKQRKLAEGTAQQK-----FLAEQELIRLKAEVe 1872
Cdd:pfam15450 103 EVREALTQIRRKQALQDSERKGAE----QEANLRLTKLTgklKQE-EQGREAACSALQKSqeeasQKVDHEVARMQAQV- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1873 ngeqqrllleeelFRLKNEVNEAVQKRkelEEELAKLRAEMELLLQSKAKTEEESRSTSEKS-KQILEAEASKLRELAEE 1951
Cdd:pfam15450 177 -------------TKLGEEMSLRFLKR---EAKLCSFLQKSFLALEKRMKASESTRLKAESSlREELEGRWQKLQELTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1952 aaRLRALseeaKRQRqlaEEEATHQRAEAeRILKEKLVAINEASRLKAEA--EIALKEKEAENERlrrlaedEAYQRRLL 2029
Cdd:pfam15450 241 --RLRAL----QGQR---EQEEGHLLEQC-RGLDAAVVQLTKFVRQNQVSlnRVLLAEQKARDAK-------GQLEESQA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2030 EEQAAQHKQDIEE-----KIAQLKKSSESELERQKSLV-DDTVRQrrlVEEEIRILKLNFEKASHgKTDLELELTRIKQS 2103
Cdd:pfam15450 304 GELASYVQENLEAvqlagELAQQETQGALELLQEKSQVlEGSVAE---LVRQVKDLSDHFLALSW-RLDLQEQTLGLKLS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2104 aeEIQRSKEQAEREA-EELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVErLKAKAEEARRQKELAEKESE 2182
Cdd:pfam15450 380 --EAKKEWEGAERKSlEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSD-LKISAEGKAREFEVEAMRQE 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2069539781 2183 -----RQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSI 2224
Cdd:pfam15450 457 laallSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQDNKTI 503
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1508-1710 |
2.22e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAVDAEQQKQtiQQELSQMKlssDAQIQAKLK 1587
Cdd:TIGR02794 69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA--KQAAEAKA---KAEAEAERK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEvefSRRKVEEEirmvRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEE----AERLRKQVKDESQKKREAE 1663
Cdd:TIGR02794 144 AKEE---AAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAKAAAEAAAKAEAE 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2069539781 1664 DELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKER 1710
Cdd:TIGR02794 217 AAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
179-293 |
2.38e-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: 44.58 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 179 QKKTFTKWVNKHL-----LKHWrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTLPrERDVIRnlrlpreKGRMRFHKLQ 253
Cdd:cd21292 25 EKVAFVNWINKNLgddpdCKHL-LPMDPNTDDLFEKVKDGILLCKMINLSVPDTID-ERAINK-------KKLTVFTIHE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2069539781 254 NVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 293
Cdd:cd21292 96 NLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2591-2769 |
2.45e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.30 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2591 DSDAEKLRKAIADLEQEKEK---LKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEK 2667
Cdd:pfam05262 173 DTDSISDKKVVEALREDNEKgvnFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2668 LFQEEVNKAQGLKAEQERQQKQMEQEKKQlttvleEARKKQAEAEenvrQKQEELQRLEKQrqkqekllAEENQKLREKL 2747
Cdd:pfam05262 253 KQQEAKNLPKPADTSSPKEDKQVAENQKR------EIEKAQIEIK----KNDEEALKAKDH--------KAFDLKQESKA 314
|
170 180
....*....|....*....|..
gi 2069539781 2748 EQLQEEQKTALAQTREIMIQTD 2769
Cdd:pfam05262 315 SEKEAEDKELEAQKKREPVAED 336
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2423-2646 |
2.46e-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: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2423 KQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEkiLKEKMQAVQEATRLKAEAEVLQKQkdLAQEQAKKLQEDKEQM 2502
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELLEP--IRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2503 QLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQ-AKAEEEAKRFKKQAEQISQKLHQTElatqekmTLVQ 2581
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLE-------ALLA 369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2582 TLEIQRQQSDSDAEKLRKAIADLeqeKEKLKREAELLQQKSEEmQTAQKEQLRQETQMLQQTFRS 2646
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAE-AEAALRDLRRELRELEAEIAS 430
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1508-1707 |
2.49e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQ------------------AEKEALELQRRMEEEVSRRQLVAVDAEQQKQ-TIQ 1568
Cdd:PRK05035 472 RHKKAAEARAAKDKDAVAAALARVKAKkaaatqpivikagarpdnSAVIAAREARKAQARARQAEKQAAAAADPKKaAVA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1569 QELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRmvRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAerl 1648
Cdd:PRK05035 552 AAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIA--RAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKA--- 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1649 RKQVKDESQKKREAEDELKHKVQA----------EQQAAREKQKALEDLQKLRLQAEEAERRMKQAELE 1707
Cdd:PRK05035 627 KKAEQQANAEPEEPVDPRKAAVAAaiarakarkaAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1614-1782 |
2.49e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1614 ERQRAGAEDELQALRDRAE-EAERQKRL----AQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQ 1688
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKkEAEAIKKEalleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1689 KlRLQAEEAERRMKQAELEKERQvqlahEAAQKSAEADLQSRRLSfaektaqlelSLQQE---HITITHLQEEA--ERLK 1763
Cdd:PRK12704 110 E-ELEKKEKELEQKQQELEKKEE-----ELEELIEEQLQELERIS----------GLTAEeakEILLEKVEEEArhEAAV 173
|
170
....*....|....*....
gi 2069539781 1764 KLQLEAEQSREEADKEVEK 1782
Cdd:PRK12704 174 LIKEIEEEAKEEADKKAKE 192
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1759-2065 |
2.50e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1759 AERLKKLQLEAEQSREEADKEVEKWRQ---KANEALRLRLQAEEVAHKKALAQE---EAEKQKEDAEREARKRSKAEESA 1832
Cdd:COG5022 768 LKRIKKIQVIQHGFRLRRLVDYELKWRlfiKLQPLLSLLGSRKEYRSYLACIIKlqkTIKREKKLRETEEVEFSLKAEVL 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1833 LRQKELAEQELEKQRKL-----AEGTAQQKFLAEQELIRLKAEVEngeqqrllleeelfrlknEVNEAVQKRKELEEELA 1907
Cdd:COG5022 848 IQKFGRSLKAKKRFSLLkketiYLQSAQRVELAERQLQELKIDVK------------------SISSLKLVNLELESEII 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1908 KLRAEME--LLLQSKAKTEEESR-----------------STSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQL 1968
Cdd:COG5022 910 ELKKSLSsdLIENLEFKTELIARlkkllnnidleegpsieYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNK 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1969 AEEEATHQRAEAERILKEKLVAINEASRLKaEAEIALKEKEAEnerLRRLAEDEAYQRRLLEEQaaQHKQDIEEKIAQLK 2048
Cdd:COG5022 990 ANSELKNFKKELAELSKQYGALQESTKQLK-ELPVEVAELQSA---SKIISSESTELSILKPLQ--KLKGLLLLENNQLQ 1063
|
330
....*....|....*...
gi 2069539781 2049 KSSES-ELERQKSLVDDT 2065
Cdd:COG5022 1064 ARYKAlKLRRENSLLDDK 1081
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1609-1912 |
2.52e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1609 QLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKRE--AEDELKHKVQAEQQAAREKQKALED 1686
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAelAAEAAKKLAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1687 LQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRlSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQ 1766
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEER-KAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1767 LEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQ 1846
Cdd:COG3064 176 AGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLA 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1847 RKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAE 1912
Cdd:COG3064 256 AVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1561-1715 |
2.55e-04 |
|
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: 46.52 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1561 EQQKQTIQQELSQMklSSDAQIQA----KLKLIEEVEFSRRKVEEEIRMVrlqLEATERQRAgAEdelqalrdraEEAER 1636
Cdd:cd03406 131 ENLKDALQADLNKM--APGLEIIAvrvtKPKIPEAIRRNYEAMEAEKTKL---LIAEQHQKV-VE----------KEAET 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1637 QKRLAQEEAERLRKQVKDESQKK-REAEDELK-HKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQL 1714
Cdd:cd03406 195 ERKRAVIEAEKDAEVAKIQMQQKiMEKEAEKKiSEIEDEMHLAREKARADAEYYRALREAEANKLKLTPEYLELKKYQAI 274
|
.
gi 2069539781 1715 A 1715
Cdd:cd03406 275 A 275
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1593-1711 |
2.55e-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: 44.65 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1593 EFSRRKVEEEIRMVRLQLEATERQRagaedELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKhkvQA 1672
Cdd:pfam05672 10 EEAARILAEKRRQAREQREREEQER-----LEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQR---KA 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 2069539781 1673 EQQAAREKQKALEDLQKLRLQAEEAERRMkQAELEKERQ 1711
Cdd:pfam05672 82 EEEAEEREQREQEEQERLQKQKEEAEAKA-REEAERQRQ 119
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1508-1712 |
2.69e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQR-QLAEAHARAKA-QAEKEALELQRRMEEEVSRRqlvaVDAEQQKQTIQQELSQMKlSSDAQIQAK 1585
Cdd:COG3206 174 RKALEFLEEQLPELRkELEEAEAALEEfRQKNGLVDLSEEAKLLLQQL----SELESQLAEARAELAEAE-ARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1586 LKLIEEVEfSRRKVEEEIRMVRLQLEATERQRAGAED-------ELQALRDRAEEAERQKrlaQEEAERLRKQVKDESQK 1658
Cdd:COG3206 249 LGSGPDAL-PELLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQL---QQEAQRILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 1659 KREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAER-------RMKQAELEKERQV 1712
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARElyesllqRLEEARLAEALTV 385
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2306-2635 |
2.74e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2306 LKQKQLADAEMAKHKKFAEQTLR---QKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKV------QVE 2376
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2377 EELFKVKVQMEELIKlktRIEEENKMLITKDK--DNMQKFLAEEAEKMKQ---------VAEEAARLSVEAQEAARLREL 2445
Cdd:PRK11281 128 SRLAQTLDQLQNAQN---DLAEYNSQLVSLQTqpERAQAALYANSQRLQQirnllkggkVGGKALRPSQRVLLQAEQALL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2446 AEQDLAQQRSLAEkilKEKMQAVQEATR--LKAEAEVLQKQKDLAQE--QAKKLQEDKEQmqlrlAEEAEGFQKTLEAER 2521
Cdd:PRK11281 205 NAQNDLQRKSLEG---NTQLQDLLQKQRdyLTARIQRLEHQLQLLQEaiNSKRLTLSEKT-----VQEAQSQDEAARIQA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2522 ----QRQLEI-TANAERLKVQVTEL-SLAQakaeeEAKRFKKQAEqisqKLHQTELATQE-----KMTLVQTLEIQRQQ- 2589
Cdd:PRK11281 277 nplvAQELEInLQLSQRLLKATEKLnTLTQ-----QNLRVKNWLD----RLTQSERNIKEqisvlKGSLLLSRILYQQQq 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2590 ---SDSDAEKLRKAIADLE-------QEKEKLKREAE----LLQQKSEEMQTAQKEQLRQ 2635
Cdd:PRK11281 348 alpSADLIEGLADRIADLRleqfeinQQRDALFQPDAyidkLEAGHKSEVTDEVRDALLQ 407
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2486-2795 |
2.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2486 DLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQK 2565
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2566 LHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQT------AQKEQLRQETQM 2639
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSeiaereEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2640 LQQTFRSEKDVLLQKERfvEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQ 2719
Cdd:COG4372 162 LQEELAALEQELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2720 EELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREIMIQTDDLPQEVVAPSQVPQMKAVPNGRDMID 2795
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2537-2760 |
2.83e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2537 QVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKmtlvqtleIQRQQSDSDAEKLRKAIADLEQEKEKLKREAE 2616
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQAR--------QKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2617 LLQQKSEEMQTAQKEQLRqETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAqglKAEQERQQKQMEQEKKQ 2696
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEA-ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA---KAEAEAKAKAEEAKAKA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2697 lttvlEEARKK-QAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQ 2760
Cdd:TIGR02794 199 -----EAAKAKaAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1635-1787 |
2.89e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1635 ERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKaLEDlQKLRLQAEEAERRMKQaelekERQVQL 1714
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEE-LEE-KKEKLQEEEDKLLEEA-----EKEAQQ 577
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 1715 AHEAAQKSAEADLQS-RRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADK-EVEKWRQKA 1787
Cdd:PRK00409 578 AIKEAKKEADEIIKElRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvKYLSLGQKG 652
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2097-2575 |
3.13e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.82 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2097 LTRIKQSAEEIQRSkEQAEREAEELRQLALEEENHRR------------EAEAKVKKISAAEQEAARQCKAALEEVERLK 2164
Cdd:COG5278 32 LNRLREASEWVEHT-YEVLRALEELLSALLDAETGQRgylltgdesflePYEEARAEIDELLAELRSLTADNPEQQARLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2165 AKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEE-KAHLAAVQQKEQELLQTRQQEQSI-LDKLREEAERAKKAAEDA 2242
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEgKALMDEIRARLLLLALALAALLLAaAALLLLLLALAALLALAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2243 EFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKF 2322
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2323 AEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKM 2402
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2403 LITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQ 2482
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2483 KQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQI 2562
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
490
....*....|...
gi 2069539781 2563 SQKLHQTELATQE 2575
Cdd:COG5278 511 AAAEAALAAALAA 523
|
|
| PDCD7 |
pfam16021 |
Programmed cell death protein 7; |
2579-2755 |
3.13e-04 |
|
Programmed cell death protein 7;
Pssm-ID: 464979 [Multi-domain] Cd Length: 305 Bit Score: 46.26 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2579 LVQTLEIQRQQsdsdaekLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFV 2658
Cdd:pfam16021 16 LVSRLETLCLE-------LRENVEDDSVWSESYSRAAELKHELQEKLLLLEDPELLESLKRKLERRQKKRLRRKRRKEER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2659 EEEKAKLEKLFQEEVNKAQG--LKAEQERQQKQMEQEKKQLTT-VLEEARKKQAEAEE--NVRQKQEELQRLEKQ--RQK 2731
Cdd:pfam16021 89 KEEKKEEQERRAEREAKIDKwrRKQIQEVEEKKRERELKLAADaVLSEVRKKQADAKRmlDILRSLEKLRKLRKEaaRRK 168
|
170 180
....*....|....*....|....
gi 2069539781 2732 QEKLLAEENQKLREKLEQLQEEQK 2755
Cdd:pfam16021 169 GIKPESECDEAFESHLEKLRSVWK 192
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2482-2757 |
3.18e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2482 QKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAE---RLKVQVTELSLAQAKAEEEAKRFKKQ 2558
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDdhnRASMQRDEAIAAIDNEQQTNSKDGEQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2559 AEQISQKLHQTELATQEKMTLVqtLEIQRQQSDSDAEKLRKaiadleqEKEKLKREAELLQQKSEE----MQTAQKEQLR 2634
Cdd:PLN02939 125 LSDFQLEDLVGMIQNAEKNILL--LNQARLQALEDLEKILT-------EKEALQGKINILEMRLSEtdarIKLAAQEKIH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2635 QETQMLQ-QTFRSEKDVLLQKERFVEEEKAK-LEKLFQEEV---NKAQGLKA------EQERQQKQMEQEKKQLTTVLEE 2703
Cdd:PLN02939 196 VEILEEQlEKLRNELLIRGATEGLCVHSLSKeLDVLKEENMllkDDIQFLKAelievaETEERVFKLEKERSLLDASLRE 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2704 ARKKQAEAEENVRQ-----------KQEELQRL---EKQRQKQEKLLAEENQKLREKLEQLQEEQKTA 2757
Cdd:PLN02939 276 LESKFIVAQEDVSKlsplqydcwweKVENLQDLldrATNQVEKAALVLDQNQDLRDKVDKLEASLKEA 343
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1962-2210 |
3.34e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1962 AKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAyqrrLLEEQAAQHKQDIE 2041
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----EAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2042 EKIAQLKKSSES-----ELERQKSLvDDTVRQRRLVEEEIRilklnfekashgkTDLELeLTRIKQSAEEIQRSKEQAER 2116
Cdd:COG3883 90 ERARALYRSGGSvsyldVLLGSESF-SDFLDRLSALSKIAD-------------ADADL-LEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2117 EAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRI 2196
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
250
....*....|....
gi 2069539781 2197 VAEEKAHLAAVQQK 2210
Cdd:COG3883 235 AAAAAAAAAASAAG 248
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2274-2466 |
3.36e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2274 AQTKAK-AQEDAEKLRKEAEleaarraqAEQAALKQKQLADAEmakhkkfaEQTLRQKAQVEQEltkVKLQLEETDHQKS 2352
Cdd:PRK12704 29 AEAKIKeAEEEAKRILEEAK--------KEAEAIKKEALLEAK--------EEIHKLRNEFEKE---LRERRNELQKLEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2353 ILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEenkmLITKDKDNMQK---FLAEEAEKM--KQVAE 2427
Cdd:PRK12704 90 RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE----LIEEQLQELERisgLTAEEAKEIllEKVEE 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 2069539781 2428 EAarlsvEAQEAARLRELAEQDLAQQRSLAEKILKEKMQ 2466
Cdd:PRK12704 166 EA-----RHEAAVLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2123-2268 |
3.37e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.93 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2123 QLALEEENHRREAEAKVKKiSAAEQEAarqcKAALEEvERL--KAKAEEARRQKELAEKESERQIQLAQEAAQKRivAEE 2200
Cdd:PTZ00491 654 QLAIEITTKSQEAAARHQA-ELLEQEA----RGRLER-QKMhdKAKAEEQRTKLLELQAESAAVESSGQSRAEAL--AEA 725
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2201 KAHLAAVqQKEQELLQTRQQEQSILDKLREEAERAKKAAEdAEFARIKAEQEAALSRQLVE-EAERMKQ 2268
Cdd:PTZ00491 726 EARLIEA-EAEVEQAELRAKALRIEAEAELEKLRKRQELE-LEYEQAQNELEIAKAKELADiEATKFER 792
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1668-2148 |
3.40e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 46.95 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1668 HKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLA-----------HEAAQKSAEADLQSRRLSFAE 1736
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIeelklnleraqTEEAQAKQDSELAKLRVEEME 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1737 K----------TAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEE-----VA 1801
Cdd:pfam05701 112 QgiadeasvaaKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEEltielIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1802 HKKAL-----AQEEAEKQKEDAEREARKRSKAEESALRQkelAEQELEKQRK--LAEGTAQQKF-LAEQELIRLKAE--- 1870
Cdd:pfam05701 192 TKESLesahaAHLEAEEHRIGAALAREQDKLNWEKELKQ---AEEELQRLNQqlLSAKDLKSKLeTASALLLDLKAElaa 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1871 -VENGEQQRLLLEEELFRLKNEVNEAV-QKRKELEEelakLRAEMElllqsKAKTEEES-RSTSEKSKQILEAEASKLRE 1947
Cdd:pfam05701 269 yMESKLKEEADGEGNEKKTSTSIQAALaSAKKELEE----VKANIE-----KAKDEVNClRVAAASLRSELEKEKAELAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1948 L--AEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKL-----VAINEASRLKAEAEIALKE-KEAENERLRRLA 2019
Cdd:pfam05701 340 LrqREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELpkqlqQAAQEAEEAKSLAQAAREElRKAKEEAEQAKA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2020 EDEAYQRRLLEEQAAQHKQDIEEKIA--QLKKSSESELERQKSLVDDTVRQRRLVEEEIRIL-KLNFEKASHGKTDLELE 2096
Cdd:pfam05701 420 AASTVESRLEAVLKEIEAAKASEKLAlaAIKALQESESSAESTNQEDSPRGVTLSLEEYYELsKRAHEAEELANKRVAEA 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2097 LTRIKQSAEEIQRSKE---QAEREAEELRQlALEEENHRREaEAKVKKIsAAEQE 2148
Cdd:pfam05701 500 VSQIEEAKESELRSLEkleEVNREMEERKE-ALKIALEKAE-KAKEGKL-AAEQE 551
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1860-2060 |
3.46e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1860 AEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILE 1939
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1940 A------EASKL------RELAEEAARLRALSEEAKRQRQL------AEEEATHQRAEAERILKEKLVAINEASRLKAEA 2001
Cdd:COG3883 94 AlyrsggSVSYLdvllgsESFSDFLDRLSALSKIADADADLleelkaDKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2002 EIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESELERQKS 2060
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2202-2441 |
3.47e-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: 46.30 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2202 AHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEfariKAEQEAALSRQLVEEAErmkQRAEEEAQTKAKAQ 2281
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALE---QELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2282 EDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRL 2361
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2362 KDEVTEAMKQKVQVEEElfkvKVQMEELIKLKTRIEEEnkmlITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAAR 2441
Cdd:COG4942 170 EAERAELEALLAELEEE----RAALEALKAERQKLLAR----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2482-2632 |
3.80e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2482 QKQKDLAQEQAKKLQEDKEQMQLRLAEEAEgfQKtlEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRF---KKQ 2558
Cdd:PRK09510 87 QQAEELQQKQAAEQERLKQLEKERLAAQEQ--KK--QAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAaaaAKK 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2559 AEQISQKLHQTELATQEKMTLVQTLEIQRQQSdSDAEKLRKAIADLEQ-----EKEKLKREAELLQQKSEEMQTAQKEQ 2632
Cdd:PRK09510 163 AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK-AAAEAKKKAEAEAKKkaaaeAKKKAAAEAKAAAAKAAAEAKAAAEK 240
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2852-2890 |
3.92e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.77 E-value: 3.92e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 2852 YLRGTSSIAGLLLKPSNEKMSIYSAMKQQLLSPGTALIL 2890
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2475-2746 |
4.09e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.96 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2475 KAEAEVLQKQKDLAQEQAKKLQEDKEQMQ--LRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELS----LAQAKA 2548
Cdd:pfam15905 66 QKNLKESKDQKELEKEIRALVQERGEQDKrlQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTrvneLLKAKF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2549 EEEA--KRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEqekEKLKreaELLQQKSEEmq 2626
Cdd:pfam15905 146 SEDGtqKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLE---EKLV---STEKEKIEE-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2627 TAQKEQLRQETQMLQQTfrSEKDVLLQKERFVEEEKakLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARK 2706
Cdd:pfam15905 218 KSETEKLLEYITELSCV--SEQVEKYKLDIAQLEEL--LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEE 293
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2069539781 2707 KQAEAEENVRQKQEELQRLEKQRQKQEkllaEENQKLREK 2746
Cdd:pfam15905 294 LLREYEEKEQTLNAELEELKEKLTLEE----QEHQKLQQK 329
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1702-1935 |
4.09e-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: 46.30 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1702 KQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEVE 1781
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1782 KWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAE 1861
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 1862 QELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSK 1935
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
2333-2745 |
4.13e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.39 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2333 VEQELTKVKlQLEETDHQKSILEEEQQRLKDEVTEAM----KQKVQVEEELFKVKvqmeeLIKLKTRIEEENKMLITKDK 2408
Cdd:pfam06160 27 VQEELSKVK-KLNLTGETQEKFEEWRKKWDDIVTKSLpdieELLFEAEELNDKYR-----FKKAKKALDEIEELLDDIEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2409 DnMQKFLAEEAEKMKQvaEEAARLSVEAQEAaRLRELAEQDLAQQRSL--AEKILKEKMQAV----QEATRLKAEAEVLQ 2482
Cdd:pfam06160 101 D-IKQILEELDELLES--EEKNREEVEELKD-KYRELRKTLLANRFSYgpAIDELEKQLAEIeeefSQFEELTESGDYLE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2483 kqkdlAQEQAKKLQEDKEQMQLRLaEEAEGFQKTLEAERQRQL-EITANAERLKVQvtELSLAQAKAEEEAKRFKKQAEQ 2561
Cdd:pfam06160 177 -----AREVLEKLEEETDALEELM-EDIPPLYEELKTELPDQLeELKEGYREMEEE--GYALEHLNVDKEIQQLEEQLEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2562 ISQKLHQTELATQEKmtLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKreaELLQQkseemQTAQKEQLRQETQMLQ 2641
Cdd:pfam06160 249 NLALLENLELDEAEE--ALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIE---DYLEH-----AEEQNKELKEELERVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2642 QTFRsekdvllqkerFVEEEKAKLEKlFQEEVNKaqgLKAEQERQQKQMEQEKK---QLTTVLEEARKKQAEAEENVRQK 2718
Cdd:pfam06160 319 QSYT-----------LNENELERVRG-LEKQLEE---LEKRYDEIVERLEEKEVaysELQEELEEILEQLEEIEEEQEEF 383
|
410 420
....*....|....*....|....*..
gi 2069539781 2719 QEELQRLEKQRQKQEKLLAEENQKLRE 2745
Cdd:pfam06160 384 KESLQSLRKDELEAREKLDEFKLELRE 410
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2421-2596 |
4.15e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.63 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2421 KMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAK-KLQEDK 2499
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKlDNLENQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2500 EQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQiSQKLHQTELATQekmTL 2579
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE-EADLEAERKAQN---IL 182
|
170
....*....|....*..
gi 2069539781 2580 VQTleIQRQQSDSDAEK 2596
Cdd:PRK12705 183 AQA--MQRIASETASDL 197
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2416-2635 |
4.15e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2416 AEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEA-TRLKAEAEVLQKQKDLAQEQAKK 2494
Cdd:TIGR02794 59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAeEKQKQAEEAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2495 LQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAErlkvqvtelslAQAKAEEEAKRfKKQAEQISQKLHQTElatq 2574
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAE-----------AEAKAKAEAEA-KAKAEEAKAKAEAAK---- 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2575 ekmtlvqtlEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQ 2635
Cdd:TIGR02794 203 ---------AKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2513-2849 |
4.69e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2513 FQKTLEAERQRQLEITANAERLKvQVTELSlAQAKAEEEAKRFKKQAEQIsqklhQTELATQEKMTLVQTLEIQRQQSDS 2592
Cdd:TIGR00618 154 FAQFLKAKSKEKKELLMNLFPLD-QYTQLA-LMEFAKKKSLHGKAELLTL-----RSQLLTLCTPCMPDTYHERKQVLEK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2593 DAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQ----QTFRSEKDVLLQKERFVEEEKAKLEKL 2668
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQeavlEETQERINRARKAAPLAAHIKAVTQIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2669 FQeevnkAQGLKAEQERQQKQMEQEKKQLTTVL-EEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKL 2747
Cdd:TIGR00618 307 QQ-----AQRIHTELQSKMRSRAKLLMKRAAHVkQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2748 EQLQeEQKTALAQTREIMIQTDDLPQEVVApSQVPQMKAVPNGRDMIDGISQNGEAELAFDGIRQKVSAKKLAEAGILSR 2827
Cdd:TIGR00618 382 HTLQ-QQKTTLTQKLQSLCKELDILQREQA-TIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
330 340
....*....|....*....|..
gi 2069539781 2828 ESMEKLAKGKATVQELSQRDDI 2849
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQI 481
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
2681-2762 |
4.73e-04 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 46.65 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2681 AEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAE--ENQKL-REKLEQLQEEQKTA 2757
Cdd:PTZ00266 435 AERARIEKENAHRKALEMKILEKKRIERLEREERERLERERMERIERERLERERLERErlERDRLeRDRLDRLERERVDR 514
|
....*
gi 2069539781 2758 LAQTR 2762
Cdd:PTZ00266 515 LERDR 519
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
1773-1848 |
4.86e-04 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 45.64 E-value: 4.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1773 REEADKEVEKWRQKANEALRLRLQAEEvahkkalaQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRK 1848
Cdd:pfam07946 255 RPEALKKAKKTREEEIEKIKKAAEEER--------AEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEKERKKEQR 322
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2188-2518 |
4.94e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2188 AQEAAQKRivaEEKAHLAAVQQKEQE--LLQTRQQEQSILDKLREEAERAKKAAEDAEfarikaEQEAALSRQLvEEAER 2265
Cdd:pfam02029 4 EEEAARER---RRRAREERRRQKEEEepSGQVTESVEPNEHNSYEEDSELKPSGQGGL------DEEEAFLDRT-AKREE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2266 MKQRAEEEAQTKAKAQEDA----------EKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQK-AQVE 2334
Cdd:pfam02029 74 RRQKRLQEALERQKEFDPTiadekesvaeRKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEvRQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2335 QELTKVKLQLEET------DHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKDK 2408
Cdd:pfam02029 154 EEGEEEEDKSEEAeevpteNFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2409 DNMQKFLAEEAEKMKQVAEEAARLS-VEAQEAARLRElAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDl 2487
Cdd:pfam02029 234 QEREEEAEVFLEAEQKLEELRRRRQeKESEEFEKLRQ-KQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLRE- 311
|
330 340 350
....*....|....*....|....*....|.
gi 2069539781 2488 aQEQAKKLqedKEQMQLRLAEEAEGFQKTLE 2518
Cdd:pfam02029 312 -EEEKRRM---KEEIERRRAEAAEKRQKLPE 338
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1559-1724 |
4.97e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1559 DAEQQ-KQTIQQELSQMK-LSSDAQIQAKlkliEEVEFSRRKVEEEIRMVRLQLEATERQragaedelqaLRDRAEEAER 1636
Cdd:PRK12704 35 EAEEEaKRILEEAKKEAEaIKKEALLEAK----EEIHKLRNEFEKELRERRNELQKLEKR----------LLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1637 QKRLAQEEAERLRKQVKDESQKKREAEdelkhKVQAEQQAAREKQkaLEDLQKL-RLQAEEAERRM-----KQAELEKER 1710
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELE-----KKEEELEELIEEQ--LQELERIsGLTAEEAKEILlekveEEARHEAAV 173
|
170
....*....|....
gi 2069539781 1711 QVQLAHEAAQKSAE 1724
Cdd:PRK12704 174 LIKEIEEEAKEEAD 187
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2049-2636 |
5.12e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2049 KSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAeREAEELRQLALEE 2128
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI-KTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2129 ENHRREAEAKVKKISAAEQEAARQckaalEEVERLKAKAEEARRQKELAEKESerQIQLAQEAAQKrivaeekahlAAVQ 2208
Cdd:PRK01156 272 NNYYKELEERHMKIINDPVYKNRN-----YINDYFKYKNDIENKKQILSNIDA--EINKYHAIIKK----------LSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2209 QKEQELLQTRQQEQSILDKLREEAerakKAAEDAEFARIKAEQEaaLSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLR 2288
Cdd:PRK01156 335 QKDYNDYIKKKSRYDDLNNQILEL----EGYEMDYNSYLKSIES--LKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2289 KEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEA 2368
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREI 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2369 MKQKVQVEEELFKVKVQMEELIKLKTR--IEEENKML-----ITKDKDNMQKfLAEEAEKMKQVAEEAARLSVEAQEAAR 2441
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINksINEYNKIEsaradLEDIKIKINE-LKDKHDKYEEIKNRYKSLKLEDLDSKR 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2442 ------LRELAEQDLAQQRSLAEKI---LKEKMQAVQEAT---------------RLKAEAEVLQKQKDLAQE---QAKK 2494
Cdd:PRK01156 568 tswlnaLAVISLIDIETNRSRSNEIkkqLNDLESRLQEIEigfpddksyidksirEIENEANNLNNKYNEIQEnkiLIEK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2495 LQEDKEQMQLRLAEEaEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTElATQ 2574
Cdd:PRK01156 648 LRGKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN-ETL 725
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2575 EKMtlvqtleiqrqqsdsdaEKLRKAIADLEQEKEKLKREA--ELLQQKSEEMQTAQKEQLRQE 2636
Cdd:PRK01156 726 ESM-----------------KKIKKAIGDLKRLREAFDKSGvpAMIRKSASQAMTSLTRKYLFE 772
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1741-1873 |
5.12e-04 |
|
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: 45.36 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1741 LELSLQQEHitiTHLQEEAERLKKLQLEAEQSREEadkevekwRQKANEALRLRLQAEEVAHKKALAQEEAE--KQKEDA 1818
Cdd:pfam12037 48 LELMKKQEQ---TRQAELQAKIKEYEAAQEQLKIE--------RQRVEYEERRKTLQEETKQKQQRAQYQDElaRKRYQD 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 1819 EREARKRSKA------EESALRQKELAEQELEKQrklaegTAQQKFLAEQELIRLKAEVEN 1873
Cdd:pfam12037 117 QLEAQRRRNEellrkqEESVAKQEAMRIQAQRRQ------TEEHEAELRRETERAKAEAEA 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1599-1928 |
5.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1599 VEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAR 1678
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1679 EKQKALEDLQKLRLQAEEAERRMKQ--AELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHIT-ITHL 1755
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQleAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQaLDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1756 QEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQ 1835
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1836 KELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMEL 1915
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330
....*....|...
gi 2069539781 1916 LLQSKAKTEEESR 1928
Cdd:COG4372 349 GLLDNDVLELLSK 361
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2580-2763 |
5.30e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.61 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2580 VQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLK--REAELLQQKSEEMQTAQKEQLRQETQmlqqtfrsEKDVLLQKERF 2657
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEkqRAAEQARQKELEQRAAAEKAAKQAEQ--------AAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2658 VEEEKAKLEKlfqeevnkAQGLKAEQERQQKQMEQEKKQ-----LTTVLEEARKKQAEAEEnvRQKQEELQRLEKQRQKQ 2732
Cdd:TIGR02794 121 AEEAKAKQAA--------EAKAKAEAEAERKAKEEAAKQaeeeaKAKAAAEAKKKAEEAKK--KAEAEAKAKAEAEAKAK 190
|
170 180 190
....*....|....*....|....*....|.
gi 2069539781 2733 EKLLAEENQKLREKLEQLQEEQKTALAQTRE 2763
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2309-2745 |
5.34e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2309 KQLADAEmAKHKkfaeQTLRQKAQVEQELTKV---KLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQ 2385
Cdd:PRK01156 204 KQIADDE-KSHS----ITLKEIERLSIEYNNAmddYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2386 MEEL------------------IKLKTRIEEENKML------ITKDKDNMQKflAEEAEKMKQVAEEAARlsvEAQEAAR 2441
Cdd:PRK01156 279 EERHmkiindpvyknrnyindyFKYKNDIENKKQILsnidaeINKYHAIIKK--LSVLQKDYNDYIKKKS---RYDDLNN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2442 LRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAE---EAEGFQKTLE 2518
Cdd:PRK01156 354 QILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIR 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2519 AERQRQLEITANAERLKVQ----VTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELAT----QEKMTLVQTL------E 2584
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVkdidEKIVDLKKRKeyleseE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2585 IQR-QQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQ--ETQMLQQTFRSEKDVLLQKERFVEEE 2661
Cdd:PRK01156 514 INKsINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSkrTSWLNALAVISLIDIETNRSRSNEIK 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2662 KA--KLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEEnVRQKQEELQRLEKQRQKQEKLLAEE 2739
Cdd:PRK01156 594 KQlnDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEK-LRGKIDNYKKQIAEIDSIIPDLKEI 672
|
....*.
gi 2069539781 2740 NQKLRE 2745
Cdd:PRK01156 673 TSRIND 678
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3586-3622 |
5.37e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.37e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2069539781 3586 KLLSAEKAVTGYKDPYSGNTISLFEAMKKGLILREHA 3622
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2100-2214 |
5.45e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 43.62 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2100 IKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKI-----SAAEQEAARQCKAALEEVERLKAKAE-EARRQ 2173
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIiaearKEAEAIAEEAKAEAEAEAERIIAQAEaEIEQE 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2069539781 2174 KELAEKESERQI-QLAQEAAQKRIVAE--EKAHLAAVQQKEQEL 2214
Cdd:COG0711 109 RAKALAELRAEVaDLAVAIAEKILGKEldAAAQAALVDRFIAEL 152
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1573-1849 |
5.53e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1573 QMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLrkqv 1652
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1653 KDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRL 1732
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1733 SFAEKTAQLELSLQQE-------HITITHLQEEAERLKKLQLE----AEQSREEADKEVEKWRQKANEALRLRLQAEEVA 1801
Cdd:COG1340 157 EKNEKLKELRAELKELrkeaeeiHKKIKELAEEAQELHEEMIElykeADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2069539781 1802 HKKALAQEEAEKQKEdaEREARKRSKAEESALRQKELAEQELEKQRKL 1849
Cdd:COG1340 237 KELRELRKELKKLRK--KQRALKREKEKEELEEKAEEIFEKLKKGEKL 282
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2413-2760 |
5.72e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 46.44 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2413 KFLAEEAEKMKQ----VAEEAARLSVEAQEAARLRELAEQDLAQQR-SLAEKILKEKMQAVQEATRLKAEAEVLQKQKDL 2487
Cdd:pfam15964 131 KFCKEELSEMKQrvqvVVLENEKLQQELKSQTQEETLREQTLLDSSgNMQNSWCTPEDSRVHQTSKRPASHNLAERLKSA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2488 AQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTEL-SLAQAKAEEEAKRFKKQAEQISQKL 2566
Cdd:pfam15964 211 TTGEDEKWRLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHKeSLVAASTSSRVGGLCLKCAQHEAVL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2567 HQT---------ELATQEK-------MTLVQTLEIQRQQSDSDAEKLRKAI-----ADLEQEK-----EKLKREAELLQQ 2620
Cdd:pfam15964 291 AQThtnvhmqtiERLTKERddlmsalVSVRSSLAEAQQRESSAYEQVKQAVqmteeANFEKTKaliqcEQLKSELERQKE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2621 KSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTV 2700
Cdd:pfam15964 371 RLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKV 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2701 -------LEEARKKQAEAEENVRQKQEELQR-LEKQRQKQEKLLAEENQKlREKLEqlQEEQKTALAQ 2760
Cdd:pfam15964 451 cgemryqLNQTKMKKDEAEKEHREYRTKTGRqLEIKDQEIEKLGLELSES-KQRLE--QAQQDAARAR 515
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1509-1686 |
5.80e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.95 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1509 QRLAEVEAQL--EKQRQLAEAHARAKAQAEKEAlelqrrmEEEVSRRQLVAVDAEQQKQTIQQELSQMKLSSDAQIQAkl 1586
Cdd:PRK09510 117 KKQAEEAAKQaaLKQKQAEEAAAKAAAAAKAKA-------EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1587 klieevefsrrkveeeirmvrlqlEATERQRAGAEDELQAlrdRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDEL 1666
Cdd:PRK09510 188 ------------------------EAEAAAKAAAEAKKKA---EAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEK 240
|
170 180
....*....|....*....|
gi 2069539781 1667 KHKVQAEQQAAREKQKALED 1686
Cdd:PRK09510 241 AAAAKAAEKAAAAKAAAEVD 260
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2549-2739 |
5.87e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.15 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2549 EEEAKRFKKQAEQISQKLHQTELATQEKmtlvqtlEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTA 2628
Cdd:pfam05262 188 EDNEKGVNFRRDMTDLKERESQEDAKRA-------QQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2629 QKEQLRQETQmlqqtfrsekdvllQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTtvlEEARKKQ 2708
Cdd:pfam05262 261 PKPADTSSPK--------------EDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASE---KEAEDKE 323
|
170 180 190
....*....|....*....|....*....|.
gi 2069539781 2709 AEAEENVRQKQEELQRLEKQRQKQEKLLAEE 2739
Cdd:pfam05262 324 LEAQKKREPVAEDLQKTKPQVEAQPTSLNED 354
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2193-2648 |
5.87e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.16 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2193 QKRIVAEEKAHLAAVQQKEQELLQTRQQEQS--ILDKLRE-------EAERAKKAAEDAEFARIKAEQEAALSRQLVEEA 2263
Cdd:NF033838 56 QKEHAKEVESHLEKILSEIQKSLDKRKHTQNvaLNKKLSDikteylyELNVLKEKSEAELTSKTKKELDAAFEQFKKDTL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2264 ERMKQRAE-----EEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQlADAEMAKHKKFA---EQTLRQ-KAQVE 2334
Cdd:NF033838 136 EPGKKVAEatkkvEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKK-AELELVKEEAKEprdEEKIKQaKAKVE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2335 QELTKVKlQLEETDHQKSILEEEQQRLKD-EVTEAMKQKVQV-EEELFKVKVQMEELIKLKTRIEEENKMLiTKDKDNMQ 2412
Cdd:NF033838 215 SKKAEAT-RLEKIKTDREKAEEEAKRRADaKLKEAVEKNVATsEQDKPKRRAKRGVLGEPATPDKKENDAK-SSDSSVGE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2413 KFLAEEAEKMKQVAEEAARLSVEAQEAARlrelaEQDLAQQRSLAEKILKE-KMQAVQEATRLKaEAEVlqkqkDLAQEQ 2491
Cdd:NF033838 293 ETLPSPSLKPEKKVAEAEKKVEEAKKKAK-----DQKEEDRRNYPTNTYKTlELEIAESDVKVK-EAEL-----ELVKEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2492 AKKLQEDKEQMQLRLAEEAegfqKTLEAERqrqleitanAERLKVQvtelslaQAKAEEEAKRfkKQAEQISQKLHQTEl 2571
Cdd:NF033838 362 AKEPRNEEKIKQAKAKVES----KKAEATR---------LEKIKTD-------RKKAEEEAKR--KAAEEDKVKEKPAE- 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2572 atqekmtlvqtleiqrQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQmlQQTFRSEK 2648
Cdd:NF033838 419 ----------------QPQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQAEEDYARRSEEEYNRLTQ--QQPPKTEK 477
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3218-3251 |
5.92e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.92e-04
10 20 30
....*....|....*....|....*....|....
gi 2069539781 3218 LLEAQAATGYMVDPVRNEQLPVDDAVRSGMVGPE 3251
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3293-3328 |
6.04e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.04e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2069539781 3293 RLLDAQLATGGIIDPANSHRLPLDVACKRGYFSEEM 3328
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3180-3218 |
6.23e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.00 E-value: 6.23e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2069539781 3180 YLKGTSAIAGILVESTGQRLLLDDALKKNFLKPEIALTL 3218
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2362-2642 |
6.27e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.57 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2362 KDEVTEAMKQKVQVEEELFKVKVQMEELIKLKtRIEEENKMLITK--DKDNMQKFLAEEAEKMKQ-----VAEEAARLSV 2434
Cdd:pfam15905 45 KDASTPATARKVKSLELKKKSQKNLKESKDQK-ELEKEIRALVQErgEQDKRLQALEEELEKVEAklnaaVREKTSLSAS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2435 EAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQ-EATRLKAEAEVLQKQKDLAQEQ-AKKLQEDKEQMQLRLAEEAEG 2512
Cdd:pfam15905 124 VASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSmELMKLRNKLEAKMKEVMAKQEGmEGKLQVTQKNLEHSKGKVAQL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2513 FQKTLEAERQRQLEiTANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKlhqtelaTQEKMTLVQTLEIQRQQSDS 2592
Cdd:pfam15905 204 EEKLVSTEKEKIEE-KSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEK-------NDEIESLKQSLEEKEQELSK 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2593 DAEKLRKAIADLEQEKEKLKREAELLQQK-SEEMQTAQKE--QLRQETQMLQQ 2642
Cdd:pfam15905 276 QIKDLNEKCKLLESEKEELLREYEEKEQTlNAELEELKEKltLEEQEHQKLQQ 328
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1757-1846 |
6.28e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 43.24 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1757 EEAERLKKlqlEAEQSREEADKEVEKWRQKAnealrlrlqAEEVAHKKALAQEEAEKQKEDAEREA-RKRSKAEESALRQ 1835
Cdd:COG0711 41 AEAERAKE---EAEAALAEYEEKLAEARAEA---------AEIIAEARKEAEAIAEEAKAEAEAEAeRIIAQAEAEIEQE 108
|
90
....*....|.
gi 2069539781 1836 KELAEQELEKQ 1846
Cdd:COG0711 109 RAKALAELRAE 119
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2417-2581 |
6.46e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.71 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2417 EEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEaevlQKQKDLAQEQAKKLQ 2496
Cdd:pfam15709 366 EQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQE----EFRRKLQELQRKKQQ 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2497 EDKEQmqlrlAEEAEGFQKTLE---AERQRQLEITANAERLKVQvtelslaQAKAEEEAKRFKKQAEQISQKLHQTELAT 2573
Cdd:pfam15709 442 EEAER-----AEAEKQRQKELEmqlAEEQKRLMEMAEEERLEYQ-------RQKQEAEEKARLEAEERRQKEEEAARLAL 509
|
....*...
gi 2069539781 2574 QEKMTLVQ 2581
Cdd:pfam15709 510 EEAMKQAQ 517
|
|
| BAR_Gvp36 |
cd07600 |
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ... |
1527-1689 |
6.60e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 kDa and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Proteomic analysis shows that Golgi vesicle protein of 36 kDa (Gvp36) may be involved in vesicular trafficking and nutritional adaptation. A Saccharomyces cerevisiae strain deficient in Gvp36 shows defects in growth, in actin cytoskeleton polarization, in endocytosis, in vacuolar biogenesis, and in the cell cycle. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153284 [Multi-domain] Cd Length: 242 Bit Score: 44.65 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1527 AHARAKAqAEKEALELQRRMEEEVSRrqlvAVDAEQQKQTIQQELSQMKLSSDAQIQAKL--KLIEEVEFS-------RR 1597
Cdd:cd07600 80 NHALSRA-ALASSLELKSLEPEDEDP----LSKALGKYSDAEEKIAEARLEQDQLIQKEFnaKLRETLNTSfqkahkaRK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1598 KVEEEirmvRLQLEA--TERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESqkkrEAEDELKHKVQAeqQ 1675
Cdd:cd07600 155 KVEDK----RLQLDTarAELKSAEPAEKQEAARVEVETAEDEFVSATEEAVELMKEVLDNP----EPLQLLKELVKA--Q 224
|
170
....*....|....*.
gi 2069539781 1676 AAREKQKA--LEDLQK 1689
Cdd:cd07600 225 LAYHKTAAelLEELLS 240
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1537-1791 |
6.80e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 46.00 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1537 KEALElqrRMEEEVSRRQlvaVDAEQQKQTIQQELSQMKLSSDAQIQAKlklieeVEFSRRKVEEEIRMVRLQLEATERQ 1616
Cdd:pfam09726 394 PDALV---RLEQDIKKLK---AELQASRQTEQELRSQISSLTSLERSLK------SELGQLRQENDLLQTKLHNAVSAKQ 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1617 RagaedelqalrDRAEEAERQKRLAQEEAER--LRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALE--------D 1686
Cdd:pfam09726 462 K-----------DKQTVQQLEKRLKAEQEARasAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKqrkrelesE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1687 LQKLRLQAEEAERRMKQAELEKERQVQlaHEAAQKSAEAdLQSRRLSFAEKTAQLELSLQQEhitithlqeeaERLK--- 1763
Cdd:pfam09726 531 IKKLTHDIKLKEEQIRELEIKVQELRK--YKESEKDTEV-LMSALSAMQDKNQHLENSLSAE-----------TRIKldl 596
|
250 260 270
....*....|....*....|....*....|....*.
gi 2069539781 1764 -------KLQLE-AEQSREEADKEVEKWRQKANEAL 1791
Cdd:pfam09726 597 fsalgdaKRQLEiAQGQIYQKDQEIKDLKQKIAEVM 632
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2040-2401 |
6.89e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2040 IEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAE 2119
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2120 ELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKriVAE 2199
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ--LES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2200 EKAHLAAVQQKEQELLQTRQQEQsiLDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKqRAEEEAQTKAK 2279
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQA--LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL-EAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2280 AQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQ 2359
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2069539781 2360 RLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENK 2401
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2161-2603 |
7.02e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2161 ERLKAKAEEARRQKELAEKESERQI-QLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAA 2239
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAaAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2240 E----------DAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQK 2309
Cdd:COG3064 83 EkaaaeaekkaAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2310 QLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEEL 2389
Cdd:COG3064 163 AAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2390 IKLKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQ 2469
Cdd:COG3064 243 AALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2470 EATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAE 2549
Cdd:COG3064 323 AAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLG 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 2550 EEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIAD 2603
Cdd:COG3064 403 LRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALT 456
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2321-2520 |
7.07e-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: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2321 KFAEQTLrqkAQVEQELTKVKLQLE-----ETDHQKSILEEEQQRLKDEVTEamKQKVQVEEelfkvkVQMEELIKLKTR 2395
Cdd:COG2268 151 KFAEKVQ---EVAGTDLAKNGLELEsvaitDLEDENNYLDALGRRKIAEIIR--DARIAEAE------AERETEIAIAQA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2396 IEEENKMLITKDKDNMQKFLAEeAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLA---EKILKEKMQAVQEAT 2472
Cdd:COG2268 220 NREAEEAELEQEREIETARIAE-AEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQrqlEIAEREREIELQEKE 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2473 RLKAEAEVL--QKQKDLAQEQAKKLQEDKEQ--MQLRLAEEAEGFQKTLEAE 2520
Cdd:COG2268 299 AEREEAELEadVRKPAEAEKQAAEAEAEAEAeaIRAKGLAEAEGKRALAEAW 350
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1678-2050 |
7.07e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.41 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1678 REKQKALEDLQKLRLQAEEAERR--MKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEktaqlelslqqehitithl 1755
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELRRRdqKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREE------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1756 QEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEdAEREARKRSKAEESALRQ 1835
Cdd:pfam15558 79 RRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQAL-REQNSLQLQERLEEACHK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1836 KELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKlraEMEL 1915
Cdd:pfam15558 158 RQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQK---EEEQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1916 LLQSKAKTEEESRSTSEkSKQILEAEASKLRELAEEAARLRALsEEAKRQRQLAEEEATHQRAEAERILKE---KLVAIN 1992
Cdd:pfam15558 235 FQRAKWRAEEKEEERQE-HKEALAELADRKIQQARQVAHKTVQ-DKAQRARELNLEREKNHHILKLKVEKEekcHREGIK 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 1993 EASRLKAE-AEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKS 2050
Cdd:pfam15558 313 EAIKKKEQrSEQISREKEATLEEARKTARASFHMREKVREETNNRTFDKMALEAQLHAS 371
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2671-2760 |
7.08e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2671 EEVNKAQGLKAEQERQQkqmEQEKKQLTTVLEEARKKQAEAEEnvRQKQEELQRLEKQRQKQEKllAEENQKLREKLEQL 2750
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAE---EQRKKKEQQQAEELQQKQAAEQE--RLKQLEKERLAAQEQKKQA--EEAAKQAALKQKQA 134
|
90
....*....|
gi 2069539781 2751 QEEQKTALAQ 2760
Cdd:PRK09510 135 EEAAAKAAAA 144
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1809-2169 |
7.45e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1809 EEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRL 1888
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1889 KNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQRQ- 1967
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEe 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1968 ---LAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKI 2044
Cdd:COG4372 166 laaLEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2045 AQLKKSSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQL 2124
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2069539781 2125 ALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEE 2169
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2092-2285 |
7.48e-04 |
|
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: 44.29 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2092 DLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAeakvkkISAAEQEAARqckAALEEVERLkakaeear 2171
Cdd:pfam04012 33 DMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA------LTKGNEELAR---EALAEKKSL-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2172 rQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKeQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQ 2251
Cdd:pfam04012 96 -EKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK-KNLLKARLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKI 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2069539781 2252 E-----AALSRQLVEEAERMKQRAEEEAQTKAKAQEDAE 2285
Cdd:pfam04012 174 EerearADAAAELASAVDLDAKLEQAGIQMEVSEDVLAR 212
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1605-1717 |
7.70e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1605 MVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLA-QEEAERLRkqvkDESQKKREAEDELKHKVQAEQQAAREKQKA 1683
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELR----DELAELEEELEALKARWEAEKELIEEIQEL 476
|
90 100 110
....*....|....*....|....*....|....
gi 2069539781 1684 LEDLQKLRLQAEEAERRMKQAELEKERQVQLAHE 1717
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
2603-2753 |
8.13e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 44.62 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2603 DLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKdvlLQKERFVEEEKAKLEKLFQEEVNkaqgLKAE 2682
Cdd:PRK06669 28 KVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVE---AAEEEAKEELLKKTDEASSIIEK----LQMQ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2683 QERQQKQMEQEKKQLttvLEEARKKQAEAEENVrQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEE 2753
Cdd:PRK06669 101 IEREQEEWEEELERL---IEEAKAEGYEEGYEK-GREEGLEEVRELIEQLNKIIEKLIKKREEILESSEEE 167
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
179-293 |
8.16e-04 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 42.13 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 179 QKKTFTKWVNKHL-----LKHWrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTL-PRERDVIRNLRlPREKgrmrfhkL 252
Cdd:cd21293 2 EKGSYVDHINRYLgddpfLKQF-LPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIdERAINTKKVLN-PWER-------N 72
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2069539781 253 QNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 293
Cdd:cd21293 73 ENHTLCLNSAKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2112-2281 |
8.38e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.05 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2112 EQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQ--KELAEKESERQIQLAQ 2189
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgrEDLAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2190 EAAQkrivaeEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEA-ERMKQ 2268
Cdd:COG1842 99 QAEA------LEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSAlERMEE 172
|
170
....*....|....
gi 2069539781 2269 RAEE-EAQTKAKAQ 2281
Cdd:COG1842 173 KIEEmEARAEAAAE 186
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1519-2123 |
8.75e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1519 EKQRQLAEAHARAkaqAEKEALELQRRME-----EEVSRRQLVAVDAEQQK--QTIqqelsqmklssdaqIQAKLKLIEE 1591
Cdd:pfam10174 182 ERTRRIAEAEMQL---GHLEVLLDQKEKEnihlrEELHRRNQLQPDPAKTKalQTV--------------IEMKDTKISS 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1592 VEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAE-----EAERQKRLAQEEAERLRKQVKDESQKKREAEDEL 1666
Cdd:pfam10174 245 LERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKfmknkIDQLKQELSKKESELLALQTKLETLTNQNSDCKQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1667 KHKVQAEQQAAREKQKAL--EDLQKLRLQAEEAERRMKqaelEKERQVQlaheaaqksaeaDLQSRRLSFAEKTAQLELS 1744
Cdd:pfam10174 325 HIEVLKESLTAKEQRAAIlqTEVDALRLRLEEKESFLN----KKTKQLQ------------DLTEEKSTLAGEIRDLKDM 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1745 LQQEHITITHLQEEAERLKklqleaEQSREEaDKEVEKWRQKANEalrlrLQAEEVAHKKALAQ-EEAEKQKE------D 1817
Cdd:pfam10174 389 LDVKERKINVLQKKIENLQ------EQLRDK-DKQLAGLKERVKS-----LQTDSSNTDTALTTlEEALSEKEriierlK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1818 AEREARKRSKAEESALRQKELaeQELEKQRKLAEGTAQQKflaEQELIRLKAEVENGEQQRLLLEeelfrlknevneavQ 1897
Cdd:pfam10174 457 EQREREDRERLEELESLKKEN--KDLKEKVSALQPELTEK---ESSLIDLKEHASSLASSGLKKD--------------S 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1898 KRKELEEELAKLRAEMeLLLQSKAKTEEESRSTSEKSKQIleaeASKLRELAEEAARLRalSEEAKRQRQLAEEEATHQR 1977
Cdd:pfam10174 518 KLKSLEIAVEQKKEEC-SKLENQLKKAHNAEEAVRTNPEI----NDRIRLLEQEVARYK--EESGKAQAEVERLLGILRE 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1978 AEAERILKEKLVAINEASRL---KAEAEIALKEKEAENE-RLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKK---- 2049
Cdd:pfam10174 591 VENEKNDKDKKIAELESLTLrqmKEQNKKVANIKHGQQEmKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKtrqe 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2050 ---------SSESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTD-----LELELTRIKQSAEEIQRSKEQAE 2115
Cdd:pfam10174 671 ldatkarlsSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAISEKDanialLELSSSKKKKTQEEVMALKREKD 750
|
....*...
gi 2069539781 2116 REAEELRQ 2123
Cdd:pfam10174 751 RLVHQLKQ 758
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
1517-1864 |
8.76e-04 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 45.41 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1517 QLEKQRQLAEAHARAKAQAEKEALELQRR--MEEEVSRRQ-------LVAVDAEQQKQTIQQELSQMKLSSDAQIQAKLK 1587
Cdd:pfam01271 113 QVEKEFKTDHSDDYETQQWEEEKLKHMRFplRYEENSEEKhseregeLSEVFENPRSQATLKKVFEEVSRLDTPSKQKRE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEVEFSRRKVEEEIRmvRLQLEATERQRAGAEDELQA--LRDRAEEAERQKRLAQEEAERLRKQVK--------DESQ 1657
Cdd:pfam01271 193 KSDEREKSSQESGEDTY--RQENIPQEDQVGPEDQEPSEegEEDATQEEVKRSRPRTHHGRSLPDESSrggqlgleEEAS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1658 KKREAEDELKHKVQAEQQAARE---------KQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQKSAEADLQ 1728
Cdd:pfam01271 271 EEEEEYGEESRGLSAVQTYLLRlvnargrgrSEKRAERERSEESEEEELKRASPYEELEITANLQIPPSEEERMLKKAGR 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1729 SRRLSfAEKTAQLELSLQQEHItithlqeeaerlKKLQLEAEQSREEADKEVEKWRQKA-NEALRLRLQAEEVAHKKALA 1807
Cdd:pfam01271 351 SPRGR-VDEAGALEALEALEEK------------RKLDLDHSRVFESSEDGAPRAPQGAwVEALRNYLSYGEEGMEGKWN 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 1808 QEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLAEQEL 1864
Cdd:pfam01271 418 QQGPYFPNEENREEARFRLPQYLGELSNPWEDPKQWKPSDFERKELTADKFLEGEEE 474
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2366-2561 |
8.86e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2366 TEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKDKDNMQKFLAEEAEKM-----KQVAEEAARLSVEAQ--- 2437
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKAKQAAEAKaka 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2438 EAARLRELAEQdlAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKtl 2517
Cdd:TIGR02794 137 EAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAK-- 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2069539781 2518 eAERQRQLEITANAERlKVQVTELSLAQAKAEEEAKRFKKQAEQ 2561
Cdd:TIGR02794 213 -AEAEAAAAAAAEAER-KADEAELGDIFGLASGSNAEKQGGARG 254
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1892-2151 |
9.17e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1892 VNEAVQKRKELeeeLAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALSEE---AKRQRQ- 1967
Cdd:PRK11637 63 VRQQQQQRASL---LAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQldaAFRQGEh 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1968 ------LAEEEAthQRAEaeRILKeKLVAINEAsRLKAEAEialkekeaenerLRRLAEDEAYQRRLLEEQAAQHKQDIE 2041
Cdd:PRK11637 140 tglqliLSGEES--QRGE--RILA-YFGYLNQA-RQETIAE------------LKQTREELAAQKAELEEKQSQQKTLLY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2042 EKIAQLKKSSESELERQKSLVDdtvrqrrlveeeiriLKLNFEKASHGKTDLELELTRIKQSAEEIQR-SKEQAEREAEE 2120
Cdd:PRK11637 202 EQQAQQQKLEQARNERKKTLTG---------------LESSLQKDQQQLSELRANESRLRDSIARAEReAKARAEREARE 266
|
250 260 270
....*....|....*....|....*....|.
gi 2069539781 2121 LRQLaleeenHRREAEAKVKKISAAEQEAAR 2151
Cdd:PRK11637 267 AARV------RDKQKQAKRKGSTYKPTESER 291
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3920-3956 |
9.97e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 9.97e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2069539781 3920 RLLSAERAVTGYRDPYSEQKVSLFQAMKKDLIPSEEA 3956
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2682-2781 |
1.01e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2682 EQERQQKQMEQEKKQLTTVLEEARKKQAEA-EENVRQKQEELQRLeKQRQKQEKLLAEENQKLREKLEQLQE---EQKTA 2757
Cdd:COG0542 415 ELERRLEQLEIEKEALKKEQDEASFERLAElRDELAELEEELEAL-KARWEAEKELIEEIQELKEELEQRYGkipELEKE 493
|
90 100
....*....|....*....|....
gi 2069539781 2758 LAQTREIMIQTDDLPQEVVAPSQV 2781
Cdd:COG0542 494 LAELEEELAELAPLLREEVTEEDI 517
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2147-2553 |
1.04e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2147 QEAARQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIV-AEEKAHLAAVQQKEQELLQTRQQEQSIL 2225
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRqAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2226 DKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAA 2305
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2306 LKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQ 2385
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2386 MEELIKLKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKM 2465
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2466 QAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQ 2545
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
....*...
gi 2069539781 2546 AKAEEEAK 2553
Cdd:COG3064 401 LGLRLDLG 408
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1703-1948 |
1.04e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 44.43 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1703 QAELEkERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEhiTITHLQEEAERLKKLQLEAEQSREEADKEVEK 1782
Cdd:pfam17045 5 EAELQ-ELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELLSARN--TLERKHKEIGLLRQQLEELEKGKQELVAKYEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1783 WRQKANEALRLRLQAEEVAHKKAL--AQEEAEKQKEDAEREARKRSKAEESALRQKELAEQELEKQRKLAEGTAQQKFLA 1860
Cdd:pfam17045 82 QLQKLQEELSKLKRSYEKLQRKQLkeAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1861 EQ-ELIRLKAEVENGEQQRLLLEEELFR-----LKNEVNEAVQKRKELEEELAKLRAE-----MELLLQSKAKTEEESRS 1929
Cdd:pfam17045 162 EQsSLIQSAAYQVQLEGRKQCLEASQSEiqrlrSKLERAQDSLCAQELELERLRMRVSelgdsNRKLLEEQQRLLEELRM 241
|
250
....*....|....*....
gi 2069539781 1930 tSEKSKQILEAEASKLREL 1948
Cdd:pfam17045 242 -SQRQLQVLQNELMELKAT 259
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1617-1978 |
1.05e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1617 RAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQK---------KREAEDELKHKVQAEQQAAREKQKALEDL 1687
Cdd:PRK04863 781 RAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFigshlavafEADPEAELRQLNRRRVELERALADHESQE 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1688 QKLRLQAEEAERRMKQ-AELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKtaqlelSLQQEHITITHLQEEAERLKKLQ 1766
Cdd:PRK04863 861 QQQRSQLEQAKEGLSAlNRLLPRLNLLADETLADRVEEIREQLDEAEEAKR------FVQQHGNALAQLEPIVSVLQSDP 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1767 LEAEQSREEADKEVEKWRQKANealRLRLQAEEVAHKKALAQEEAEKQKEDaerearkrSKAEESALRQK-ELAEQELEK 1845
Cdd:PRK04863 935 EQFEQLKQDYQQAQQTQRDAKQ---QAFALTEVVQRRAHFSYEDAAEMLAK--------NSDLNEKLRQRlEQAEQERTR 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1846 QRKLAEGTAQQ-----KFLA---------EQELIRLKAEVEN-GEQQRLLLEEELFRLKNEVNEAV----QKRKELEEEL 1906
Cdd:PRK04863 1004 AREQLRQAQAQlaqynQVLAslkssydakRQMLQELKQELQDlGVPADSGAEERARARRDELHARLsanrSRRNQLEKQL 1083
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 1907 AKLRAEMELLLQSKAKTEEESRSTSEkskQILEAEAS--KLRELAEEAARLRALSeeakrQRQLAEEEATHQRA 1978
Cdd:PRK04863 1084 TFCEAEMDNLTKKLRKLERDYHEMRE---QVVNAKAGwcAVLRLVKDNGVERRLH-----RRELAYLSADELRS 1149
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2447-2753 |
1.07e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 44.56 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2447 EQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKqkdLAQEQAKKLQEDKEQMQLRLAEEaegfqktleaeRQRQLE 2526
Cdd:pfam09728 38 QKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEK---LCRELQKQNKKLKEESKKLAKEE-----------EEKRKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2527 ITanaERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKL----HQTELATQEKMTLVQTLEIQRQQSDSdaeKLRKAIA 2602
Cdd:pfam09728 104 LS---EKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLksliEQYELRELHFEKLLKTKELEVQLAEA---KLQQATE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2603 dleqEKEKLKREAELLqqKSEEMQTAQKEQLRQETQMLQQtfrsekdVLLQKERF--VEEEKAKLEKLFQeevnkaqGLK 2680
Cdd:pfam09728 178 ----EEEKKAQEKEVA--KARELKAQVQTLSETEKELREQ-------LNLYVEKFeeFQDTLNKSNEVFT-------TFK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 2681 AEQER---QQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQrqkqekllaeeNQKLREKLEQLQEE 2753
Cdd:pfam09728 238 KEMEKmskKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKK-----------LEKLENLCRALQAE 302
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
2600-2745 |
1.14e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 45.23 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2600 AIADLEQEKEKLKREAELLQQKSEEM-----------QTAQKE--QLRQETQMLQ-------QTFRSEKDVLLQKERFVE 2659
Cdd:pfam09726 396 ALVRLEQDIKKLKAELQASRQTEQELrsqissltsleRSLKSElgQLRQENDLLQtklhnavSAKQKDKQTVQQLEKRLK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2660 EEK---AKLEKLFQEevnkaqglkaeqERQQKQMEQEK-KQLTTVLEEARKKQAEAEENVRQKQE-ELQRLEKQ---RQK 2731
Cdd:pfam09726 476 AEQearASAEKQLAE------------EKKRKKEEEATaARAVALAAASRGECTESLKQRKRELEsEIKKLTHDiklKEE 543
|
170
....*....|....
gi 2069539781 2732 QEKLLAEENQKLRE 2745
Cdd:pfam09726 544 QIRELEIKVQELRK 557
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2339-2659 |
1.16e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.23 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2339 KVKLQLEETDHQKSI-LEEEQQRLKDEVTEAMKQKVQVEEELFKvkvqmEELIKLKTRIEEEnkmlITKDKDNM---QKF 2414
Cdd:PLN03229 418 KVNMKKREAVKTPVReLEGEVEKLKEQILKAKESSSKPSELALN-----EMIEKLKKEIDLE----YTEAVIAMglqERL 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2415 LAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAqqRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKK 2494
Cdd:PLN03229 489 ENLREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLS--RAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKK 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2495 LQEDKEQMQLRLAEEAegfqktLEAERQRQlEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQ 2574
Cdd:PLN03229 567 FKEVMDRPEIKEKMEA------LKAEVASS-GASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTA 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2575 EKMT---LVQTLEIQRQQSDSDAEKLRKAiADLEQEKEKLKREaelLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVL 2651
Cdd:PLN03229 640 EQTPppnLQEKIESLNEEINKKIERVIRS-SDLKSKIELLKLE---VAKASKTPDVTEKEKIEALEQQIKQKIAEALNSS 715
|
....*...
gi 2069539781 2652 LQKERFVE 2659
Cdd:PLN03229 716 ELKEKFEE 723
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2595-2698 |
1.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2595 EKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQkerfVEEEKAKLEKLFQEEVN 2674
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEE----IQELKEELEQRYGKIPE 489
|
90 100
....*....|....*....|....
gi 2069539781 2675 KAQGLKAEQERQQKQMEQEKKQLT 2698
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEVT 513
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1676-1831 |
1.19e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1676 AAREKQKALEDLQKLRLQAEEAERRMK---------QAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLE-LSL 1745
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKelpaelaelEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1746 QQEHIT----ITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEAL-RLRLQAEEVAHKKALAQEEAEKQKEDAER 1820
Cdd:COG1579 81 QLGNVRnnkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEaELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|.
gi 2069539781 1821 EARKRSKAEES 1831
Cdd:COG1579 161 LEAEREELAAK 171
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2564-2777 |
1.24e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.83 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2564 QKLHQTELATQEKMTLVQTLEI------QRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQET 2637
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQalslldKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLSLEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2638 qmLQQTFRSEKDVLLQkerfVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLT------TVLEEARKKQAEA 2711
Cdd:pfam12795 83 --LEQRLLQTSAQLQE----LQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNgpappgEPLSEAQRWALQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2712 EENVRQKQEELQRLEKQR--------QKQEKLLAEENQKLREKLEQLQEEQKTA-LAQTREIMIQTDDLPQEVVA 2777
Cdd:pfam12795 157 ELAALKAQIDMLEQELLSnnnrqdllKARRDLLTLRIQRLEQQLQALQELLNEKrLQEAEQAVAQTEQLAEEAAG 231
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1889-2159 |
1.28e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.07 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1889 KNEVNEAVQKRKELEEELAKLRAEMELLLQskaktEEEsrstsEKSKQILEAEASKLR-----ELAEE------AARLRA 1957
Cdd:COG0497 157 LEEYREAYRAWRALKKELEELRADEAERAR-----ELD-----LLRFQLEELEAAALQpgeeeELEEErrrlsnAEKLRE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1958 LSEEAkrQRQLAEEE--ATHQRAEAERILkEKLVAINE-----ASRLkAEAEIALKEKEAEnerLRRLAED-EAYQRRLl 2029
Cdd:COG0497 227 ALQEA--LEALSGGEggALDLLGQALRAL-ERLAEYDPslaelAERL-ESALIELEEAASE---LRRYLDSlEFDPERL- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2030 eeqaaqhkQDIEEKIAQLKKsseseLERqkslvddtvRQRRLVEEEIRILKlnfekashgktDLELELTRIKQSAEEIQR 2109
Cdd:COG0497 299 --------EEVEERLALLRR-----LAR---------KYGVTVEELLAYAE-----------ELRAELAELENSDERLEE 345
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2110 SKEQAEREAEELRQLAleeenhrreaeakvKKISAAEQEAARQCKAALEE 2159
Cdd:COG0497 346 LEAELAEAEAELLEAA--------------EKLSAARKKAAKKLEKAVTA 381
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1600-1859 |
1.28e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.59 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1600 EEEIRMVRLQLEATERQRAGAEDELQAlRDRAEEAE-RQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAR 1678
Cdd:PRK07735 2 DPEKDLEDLKKEAARRAKEEARKRLVA-KHGAEISKlEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1679 EKQKALEDLQKLRLQAEEAERRMKQAELEKERQvqlahEAAQKSAEADLQSRRLSFAE--KTAQLELSLQQEHITITHLQ 1756
Cdd:PRK07735 81 GTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKR-----EGTEEVTEEEKAAAKAKAAAaaKAKAAALAKQKREGTEEVTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1757 EEAERLKKLQLE-------------AEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREAR 1823
Cdd:PRK07735 156 EEEETDKEKAKAkaaaaakakaaalAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2069539781 1824 K-------RSKAEESALRQKELAEQELEKQRKLAEGTAQQKFL 1859
Cdd:PRK07735 236 KakaiaaaKAKAAAAARAKTKGAEGKKEEEPKQEEPSVNQPYL 278
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1925-2212 |
1.29e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.45 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1925 EESRSTSEKSKQILEAEASKLRELAEEAARLRALSEEAKRQ--------RQLAEEEATHQRAEAERILKEKlvaineaSR 1996
Cdd:TIGR02794 25 HSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKeqerqkklEQQAEEAEKQRAAEQARQKELE-------QR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1997 LKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSEselerqkslvddtvrqrrlveeei 2076
Cdd:TIGR02794 98 AAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE------------------------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2077 rilklnfekashgktdleleltrikqsAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAA 2156
Cdd:TIGR02794 154 ---------------------------EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAA 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2157 LE-----EVERLKAKAEEARRQKELAEK------ESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQ 2212
Cdd:TIGR02794 207 AEaaakaEAEAAAAAAAEAERKADEAELgdifglASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2681-2763 |
1.31e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.33 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2681 AEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEkllaEENQKLREKLEQLQEEQKTALAQ 2760
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELE----EKQQELEAQLEQLQEKAAETSQE 213
|
...
gi 2069539781 2761 TRE 2763
Cdd:PRK11448 214 RKQ 216
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
2024-2292 |
1.39e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.31 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2024 YQRRLLEEQAAQHKQDIEEKIaQLKKSSEsELERQKSLVDdtVRQRRLVEEEIRILKLNFE------KASHGKTDLELEL 2097
Cdd:PLN03188 947 HEHKLLKEKYENHPEVLRTKI-ELKRVQD-ELEHYRNFYD--MGEREVLLEEIQDLRSQLQyyidssLPSARKRNSLLKL 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2098 T------------RIKQSAEEIQRSKEQAER----EAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVE 2161
Cdd:PLN03188 1023 TyscepsqapplnTIPESTDESPEKKLEQERlrwtEAESKWISLAEELRTELDASRALAEKQKHELDTEKRCAEELKEAM 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2162 RLkAKAEEARRQKELAEKEsERQIQL-------------AQEAAQKRIV--AEEK------AHLAAVQ-QKEQELLQTRQ 2219
Cdd:PLN03188 1103 QM-AMEGHARMLEQYADLE-EKHIQLlarhrriqegiddVKKAAARAGVrgAESKfinalaAEISALKvEREKERRYLRD 1180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2220 QEQSILDKLREEAERAKKAAEdaEFARIKAEQEAalsrqlVEEAERMKQRAEEEAqtkAKAQEDAEKLRKEAE 2292
Cdd:PLN03188 1181 ENKSLQAQLRDTAEAVQAAGE--LLVRLKEAEEA------LTVAQKRAMDAEQEA---AEAYKQIDKLKRKHE 1242
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1508-1728 |
1.50e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.44 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEeevsrrqlvavDAEQQKQTIQQELSQMKLSSDAQIQAKLK 1587
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEAAPKEILA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEVEFSRRKVEEEIRMVRLQleateRQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELK 1667
Cdd:pfam12795 77 SLSLEELEQRLLQTSAQLQELQ-----NQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 1668 HKVQAEQQAAREKQKALE-----------------DLQKLRLQAEEAERRMKQAELEKERQVQlaHEAAQKSAEADLQ 1728
Cdd:pfam12795 152 WALQAELAALKAQIDMLEqellsnnnrqdllkarrDLLTLRIQRLEQQLQALQELLNEKRLQE--AEQAVAQTEQLAE 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1839-2054 |
1.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1839 AEQELEKQRKLAEGTAQQKFLAEQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQ 1918
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1919 SKAKTEE---------ESRSTSE------KSKQILEAEASKLRELAEEAARLralsEEAKRQRQLAEEEATHQRAEAERI 1983
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDfldrlsALSKIADADADLLEELKADKAEL----EAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 1984 LKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESE 2054
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2036-2195 |
1.60e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2036 HKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRL-VEEEIRILKLNFEKashgktDLELELTRIKQSAEEIQRSKEQA 2114
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2115 EREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKA-KAEEARRQ-KELAEKESERQI------- 2185
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGlTAEEAKEIlLEKVEEEARHEAavlikei 178
|
170
....*....|.
gi 2069539781 2186 -QLAQEAAQKR 2195
Cdd:PRK12704 179 eEEAKEEADKK 189
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2415-2748 |
1.65e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2415 LAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKK 2494
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2495 LQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEE-EAKRFKKQAEQISQKLHQTELAT 2573
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAlEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2574 QEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQEtqmLQQTFRSEKDVLLQ 2653
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV---ILKEIEELELAILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2654 KERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQE 2733
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
330
....*....|....*
gi 2069539781 2734 KLLAEENQKLREKLE 2748
Cdd:COG4372 350 LLDNDVLELLSKGAE 364
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2542-2771 |
1.66e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2542 SLAQAKAEEEaKRFKKQAEQISQKLHQteLATQEKMTLVQTLEIQRQQS-----DSDAEKLRKAIADLEQEKEKlkREAE 2616
Cdd:PRK11637 51 SIQQDIAAKE-KSVRQQQQQRASLLAQ--LKKQEEAISQASRKLRETQNtlnqlNKQIDELNASIAKLEQQQAA--QERL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2617 LLQQ-----------------KSEEMQTAQK--------EQLRQET-QMLQQTfrsEKDVLLQKerfveeekakleKLFQ 2670
Cdd:PRK11637 126 LAAQldaafrqgehtglqlilSGEESQRGERilayfgylNQARQETiAELKQT---REELAAQK------------AELE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2671 EEVNKAQGLKAEQERQQKQMEQ----EKKQLTTV---LEEARKKQAEAEEN---VRQKQEELQRLEKQRQKQEkllAEEN 2740
Cdd:PRK11637 191 EKQSQQKTLLYEQQAQQQKLEQarneRKKTLTGLessLQKDQQQLSELRANesrLRDSIARAEREAKARAERE---AREA 267
|
250 260 270
....*....|....*....|....*....|...
gi 2069539781 2741 QKLREKLEQLQEEQKT--ALAQTREIMIQTDDL 2771
Cdd:PRK11637 268 ARVRDKQKQAKRKGSTykPTESERSLMSRTGGL 300
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
2313-2523 |
1.66e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.67 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2313 DAEMAKHKKFAEQTL--RQKAqvEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEE--------LFKV 2382
Cdd:pfam05911 2 DDLVKQHAKVAEEAVsgWEKA--EAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEqeqkihdvVLKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2383 KVQMEeliklKTRIEEENKMlitkdkDNMQKFLAEeaekmkqVAEEAARLSVEAQEAARLRElaeqDLAQQRSLAE---K 2459
Cdd:pfam05911 80 TKEWE-----KIKAELEAKL------VETEQELLR-------AAAENDALSRSLQERENLLM----KLSEEKSQAEaeiE 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2460 ILKEKMQAVQ-EATRLKAEAEVLQKQKDLAQEQakklqedKEqMQLRLAEEA-----EGFQK--TLEAERQR 2523
Cdd:pfam05911 138 ALKSRLESCEkEINSLKYELHVLSKELEIRNEE-------KN-MSRRSADAAhkqhlESVKKiaKLEAECQR 201
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2084-2189 |
1.70e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2084 EKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAA-EQEAARQCKAALEEVER 2162
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQlEQLQEKAAETSQERKQK 217
|
90 100
....*....|....*....|....*....
gi 2069539781 2163 LKAKAEEARRQKELAEKESERQI--QLAQ 2189
Cdd:PRK11448 218 RKEITDQAAKRLELSEEETRILIdqQLRK 246
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2003-2291 |
1.87e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.83 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2003 IALKEKEAENERLRR-LAEDEAYQRRLLE-EQAAQHKQDIE-EKIAQLK--KSSESELER--QKSLVDDTVRQRRLVEEE 2075
Cdd:NF012221 1535 VATSESSQQADAVSKhAKQDDAAQNALADkERAEADRQRLEqEKQQQLAaiSGSQSQLEStdQNALETNGQAQRDAILEE 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2076 IRilklnfekashgktDLELELTRIKQSAEEIQRSKEQAEREAEELR-QLALEEENHRREAEAKVKKISAAEQEAARQC- 2153
Cdd:NF012221 1615 SR--------------AVTKELTTLAQGLDALDSQATYAGESGDQWRnPFAGGLLDRVQEQLDDAKKISGKQLADAKQRh 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2154 KAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRivaeekahlaavqqkEQELLQTRQqeqsildklreeae 2233
Cdd:NF012221 1681 VDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR---------------KDDALAKQN-------------- 1731
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2234 RAKKAAEDAEFArikaeqeaalsrqlVEEAERMKQRAEEEAQTKA-KAQEDAEKLRKEA 2291
Cdd:NF012221 1732 EAQQAESDANAA--------------ANDAQSRGEQDASAAENKAnQAQADAKGAKQDE 1776
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2359-2745 |
1.89e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2359 QRLKDEVTEAMkqkvqveEELfkVKVQMEELIK---LKTR----------IEEENKMLITKDKDNMQKF--LAEEAEKMK 2423
Cdd:PLN03229 372 QQIKIAINENM-------DEL--GKMDTEELLKhrmLKFRkiggfqegvpVDPERKVNMKKREAVKTPVreLEGEVEKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2424 QVAEEAARLSVEAQEAArlrelaeqdlaqqrsLAEKILKEKMQAVQEATRlKAEAEVLQKQKDLAQEQAKKLQEDKEQMQ 2503
Cdd:PLN03229 443 EQILKAKESSSKPSELA---------------LNEMIEKLKKEIDLEYTE-AVIAMGLQERLENLREEFSKANSQDQLMH 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2504 LRLAEEAEgfqkTLEAERQRQLEITANAERLKVQV---TELSLAQAKAEEEAKRFKKQAEqISQKLHQT--ELATQEKMt 2578
Cdd:PLN03229 507 PVLMEKIE----KLKDEFNKRLSRAPNYLSLKYKLdmlNEFSRAKALSEKKSKAEKLKAE-INKKFKEVmdRPEIKEKM- 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2579 lvQTLEIQRQQSD-SDAEKLRKaiaDLEQEKEKLKRE-----AELLQQKSEEMQTAQKEQLRQETQMLQQTFRSekdvll 2652
Cdd:PLN03229 581 --EALKAEVASSGaSSGDELDD---DLKEKVEKMKKEielelAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQE------ 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2653 QKERFVEEEKAKLEKLFQ--EEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQ 2730
Cdd:PLN03229 650 KIESLNEEINKKIERVIRssDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELA 729
|
410
....*....|....*
gi 2069539781 2731 KQEKLLAEENQKLRE 2745
Cdd:PLN03229 730 AARETAAESNGSLKN 744
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1772-2022 |
1.91e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1772 SREEADKEVEKWR--QKANEALRLRLQAEEVAHKKALAQEEAEKQK----------EDAEREARKRSKAEESALRQK--- 1836
Cdd:PRK07735 1 MDPEKDLEDLKKEaaRRAKEEARKRLVAKHGAEISKLEEENREKEKalpknddmtiEEAKRRAAAAAKAKAAALAKQkre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1837 ---ELAEQELEKQRKLA--EGTAQQKFLAEQ---------ELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKEL 1902
Cdd:PRK07735 81 gteEVTEEEKAKAKAKAaaAAKAKAAALAKQkregteevtEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1903 EEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEAEASKLRELAEEAARLRALS---EEAKRQRQLAEEEATHQRAE 1979
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAAlakQKASQGNGDSGDEDAKAKAI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2069539781 1980 AerilkeklvaineASRLKAEAEIALKEKEAENERLRRLAEDE 2022
Cdd:PRK07735 241 A-------------AAKAKAAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
671-765 |
1.94e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.78 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 671 LRYLQDLLAWVEENQRRIGAAEWGVDLPTVESQLGSHRGLHQSIEEFRAKIERARADETQL---SPGPRSAYRDCLSKLD 747
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 2069539781 748 LQYAKLLTSSKARLRHLE 765
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2190-2509 |
1.95e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 44.33 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2190 EAAQKRIVAEEKAH---LAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQlveEAERM 2266
Cdd:pfam03528 4 EDLQQRVAELEKENaefYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARA---EMENI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2267 KQRAEEEAQTKAKAQEDAEKLRKE--AELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTK----- 2339
Cdd:pfam03528 81 KAVATVSENTKQEAIDEVKSQWQEevASLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRRRLSEgqeee 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2340 -----VKLQLEETDHQKSI---LEEEQQRLKDEVTEAMKQKVQVEEELFK-VKVQMEELIKLKTRIEEENKMLITKdkdn 2410
Cdd:pfam03528 161 nledeMKKAQEDAEKLRSVvmpMEKEIAALKAKLTEAEDKIKELEASKMKeLNHYLEAEKSCRTDLEMYVAVLNTQ---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2411 mQKFLAEEAEKMKQVAEEAAR-LSVEAQEAARLR----ELAEQDLAQQRSLAEKIlkEKMQAVQEATRLKAEAEVlqKQK 2485
Cdd:pfam03528 237 -KSVLQEDAEKLRKELHEVCHlLEQERQQHNQLKhtwqKANDQFLESQRLLMRDM--QRMESVLTSEQLRQVEEI--KKK 311
|
330 340
....*....|....*....|....
gi 2069539781 2486 DLAQEQAKKLQEDKEQMQLRLAEE 2509
Cdd:pfam03528 312 DQEEHKRARTHKEKETLKSDREHT 335
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1632-1732 |
2.06e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1632 EEAERQKRLAQEEAERLRKQVKDESQKKREAEDEL----KHKVQAEQQAA--REKQKALE-DLQKLRLQAEEAERRmkqa 1704
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAeaqqQELVALEGLAAelEEKQQELEaQLEQLQEKAAETSQE---- 213
|
90 100
....*....|....*....|....*...
gi 2069539781 1705 elEKERQVQLAHEAAQKSAEADLQSRRL 1732
Cdd:PRK11448 214 --RKQKRKEITDQAAKRLELSEEETRIL 239
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2514-2684 |
2.17e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2514 QKTLEAERQRQlEITANAERLKVQVTELSLAQAKaeEEAKRFKKQAEQ-ISQKlhQTELATQEKmtlvqTLEIQRQQSDS 2592
Cdd:PRK12704 31 AKIKEAEEEAK-RILEEAKKEAEAIKKEALLEAK--EEIHKLRNEFEKeLRER--RNELQKLEK-----RLLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2593 DAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKerfVEEE-KAKLEKLFQE 2671
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEK---VEEEaRHEAAVLIKE 177
|
170
....*....|...
gi 2069539781 2672 EVNKAQgLKAEQE 2684
Cdd:PRK12704 178 IEEEAK-EEADKK 189
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1537-1759 |
2.19e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1537 KEALELQRRMEEEVSRRQLVAvdaEQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQ 1616
Cdd:pfam05262 138 KENAGLARRYDQWPGKTQIVI---PLKKNILSGNVSDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1617 RAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAED-------ELKHKVQAEQQAAREK-----QKAL 1684
Cdd:pfam05262 215 AQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKpadtsspKEDKQVAENQKREIEKaqieiKKND 294
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1685 EDLQKLRLQ-AEEAERRMKQAElekerqvqlaHEAAQKSAEAdlQSRRLSFAEKTAQLelsLQQEHITITHLQEEA 1759
Cdd:pfam05262 295 EEALKAKDHkAFDLKQESKASE----------KEAEDKELEA--QKKREPVAEDLQKT---KPQVEAQPTSLNEDA 355
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2679-2760 |
2.22e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 41.41 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2679 LKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQ-RQKQEKLLAEENQKLREKLEQLQEEQKTA 2757
Cdd:pfam03938 24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQElQQLQQKAQQELQKKQQELLQPIQDKINKA 103
|
...
gi 2069539781 2758 LAQ 2760
Cdd:pfam03938 104 IKE 106
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2850-2887 |
2.23e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.23e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2069539781 2850 RRYLRGTSSIAGLLLKPSNEKMSIYSAMKQQLLSPGTA 2887
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1588-1709 |
2.23e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 LIEEVEFSRRKVEEEIRmvrlqleaterqragaedELQALRdraEEAERQKRLAQEEAERLRKQvkdESQKKREAEDELK 1667
Cdd:PRK00409 521 LIASLEELERELEQKAE------------------EAEALL---KEAEKLKEELEEKKEKLQEE---EDKLLEEAEKEAQ 576
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2069539781 1668 HKVQAEQQAAREKQKALEDLQKLRL------QAEEAERRMKQAELEKE 1709
Cdd:PRK00409 577 QAIKEAKKEADEIIKELRQLQKGGYasvkahELIEARKRLNKANEKKE 624
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1620-1689 |
2.25e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 41.27 E-value: 2.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1620 AEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQK-----KREAEDELKH-KVQAEQQAAREKQKALEDLQK 1689
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKikeeiLAEAKEEAERiLEQAKAEIEQEKEKALAELRK 117
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2333-2745 |
2.25e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2333 VEQELTKVKlQLEETDHQKSILEEEQQRLKDEVTEAM----KQKVQVEEEL-----FKVKVQMEELIKLKTRIEEEnkml 2403
Cdd:PRK04778 46 VNDELEKVK-KLNLTGQSEEKFEEWRQKWDEIVTNSLpdieEQLFEAEELNdkfrfRKAKHEINEIESLLDLIEED---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2404 ITKDKDNMQKFLAEEAEKMKQVAEeaARlsveaqeaARLRELAEQDLAQQRSL--AEKILKEKMQAV----QEATRLKAE 2477
Cdd:PRK04778 121 IEQILEELQELLESEEKNREEVEQ--LK--------DLYRELRKSLLANRFSFgpALDELEKQLENLeeefSQFVELTES 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2478 AEVLQkqkdlAQEQAKKLQEDKEQMQlRLAEEAEGFQKTLEAERQRQL-EITANAERLKVQ---VTELSLaqakaEEEAK 2553
Cdd:PRK04778 191 GDYVE-----AREILDQLEEELAALE-QIMEEIPELLKELQTELPDQLqELKAGYRELVEEgyhLDHLDI-----EKEIQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2554 RFKKQAEQISQKLHQTEL-ATQEKMTLVQTlEIqrqqsDSDAEKLRKAIA---DLEQEKEKLKreaellqqKSEEMQTAQ 2629
Cdd:PRK04778 260 DLKEQIDENLALLEELDLdEAEEKNEEIQE-RI-----DQLYDILEREVKarkYVEKNSDTLP--------DFLEHAKEQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2630 KEQLRQETQMLQQTFR-SEKDVLLQKErfVEEEKAKLEKLFQEEVNK-AQGLKAEQERQQKQMEQEKKqlttvLEEARKK 2707
Cdd:PRK04778 326 NKELKEEIDRVKQSYTlNESELESVRQ--LEKQLESLEKQYDEITERiAEQEIAYSELQEELEEILKQ-----LEEIEKE 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 2069539781 2708 QAEAeenvrqkQEELQRLEKQRQKQEKLLAEENQKLRE 2745
Cdd:PRK04778 399 QEKL-------SEMLQGLRKDELEAREKLERYRNKLHE 429
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1973-2174 |
2.28e-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: 42.99 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1973 ATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSe 2052
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2053 selERQKSLvdDTVRQRRLVEEEIRILKLNfekashgKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQlalEEENHR 2132
Cdd:COG1579 80 ---EQLGNV--RNNKEYEALQKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2069539781 2133 REAEAKVKKISAAEQEAARQCKAALEEV-ERLKAKAEEARRQK 2174
Cdd:COG1579 145 AELDEELAELEAELEELEAEREELAAKIpPELLALYERIRKRK 187
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2416-2597 |
2.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2416 AEEAEKM-KQVAEEAARlsvEAQEAARLREL-AEQDLAQQRSLAEKILKEKMQAVQEA-TRLKAEAEVLQKQKDLAQEQA 2492
Cdd:PRK12704 33 IKEAEEEaKRILEEAKK---EAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLeKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2493 KKLQEDKEQM--QLRLAEEAEGFQKTLEAERQRQLEITAN--AERLKVQVteLSLAQAKAEEEAKRFKKQAEQISQklhq 2568
Cdd:PRK12704 110 EELEKKEKELeqKQQELEKKEEELEELIEEQLQELERISGltAEEAKEIL--LEKVEEEARHEAAVLIKEIEEEAK---- 183
|
170 180 190
....*....|....*....|....*....|
gi 2069539781 2569 tELATQE-KMTLVQTleIQRQQSDSDAEKL 2597
Cdd:PRK12704 184 -EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2308-2499 |
2.35e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2308 QKQLADAEMAKHKKFAEqtlRQKAQVEQELTKvkLQLEETDHQKSILEEEQQ--RLKDEVTEAMKQKVQVEEEL------ 2379
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIE---EQRKKNGENIAR--KQNKYDELVEEAKTIKAEieELTDELLNLVMDIEDPSAALnklnta 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2380 -FKVKVQMEELIKL-------------KTRIEEENKML--ITKDKDNMQKFLAEEAEKMKQVAE---EAARLSVEAQEAA 2440
Cdd:PHA02562 264 aAKIKSKIEQFQKVikmyekggvcptcTQQISEGPDRItkIKDKLKELQHSLEKLDTAIDELEEimdEFNEQSKKLLELK 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2441 RLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDK 2499
Cdd:PHA02562 344 NKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2684-2763 |
2.39e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2684 ERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTRE 2763
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKK 584
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
2154-2293 |
2.40e-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: 43.57 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2154 KAALE--EVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSIlDKLREE 2231
Cdd:pfam00529 57 QAALDsaEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR-RVLAPI 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2232 AERAKKAAEDAEFARIKAEQE-----AALSRQLVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAEL 2293
Cdd:pfam00529 136 GGISRESLVTAGALVAQAQANllatvAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1508-1665 |
2.41e-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: 42.99 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQAEKEALELQRrmeeEVSRRQLVAVDAEQQKQTIQQELSQMKlsSDAQIQAKLK 1587
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 1588 LIEEVEFSRRKVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDE 1665
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2606-2768 |
2.43e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2606 QEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSekdvllQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQER 2685
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERN------QQRQEARREREELQREEERLVQKEEQLDARAEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2686 qqkqMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEK--LLAEENQKLREKLEQL--QEEQKTALAQT 2761
Cdd:PRK12705 100 ----LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARklLLKLLDAELEEEKAQRvkKIEEEADLEAE 175
|
170
....*....|
gi 2069539781 2762 RE---IMIQT 2768
Cdd:PRK12705 176 RKaqnILAQA 185
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2253-2574 |
2.64e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.44 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2253 AALSRQLVEEAERMKQ-RAEEEA-QTKAKAQEDAEKLRKEaeleaarraqaeqaalKQKQLAdaEMAKHKKFAEQT---- 2326
Cdd:NF012221 1538 SESSQQADAVSKHAKQdDAAQNAlADKERAEADRQRLEQE----------------KQQQLA--AISGSQSQLESTdqna 1599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2327 LRQKAQVEQ------------ELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQmEELIKLKT 2394
Cdd:NF012221 1600 LETNGQAQRdaileesravtkELTTLAQGLDALDSQATYAGESGDQWRNPFAGGLLDRVQEQLDDAKKISG-KQLADAKQ 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2395 RIEeenkmlitkdkDNMQkflaeeaekmkQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRL 2474
Cdd:NF012221 1679 RHV-----------DNQQ-----------KVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQA 1736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2475 KAEAEVLQKQKDLAQEQAKKLQEDK-EQMQlrlaEEAEGFQKTL--EAERQRQLEITANAERLKVQVTELSLAQAKAEEE 2551
Cdd:NF012221 1737 ESDANAAANDAQSRGEQDASAAENKaNQAQ----ADAKGAKQDEsdKPNRQGAAGSGLSGKAYSVEGVAEPGSHINPDSP 1812
|
330 340
....*....|....*....|....
gi 2069539781 2552 AKRFKKQAEQIS-QKLHQTELATQ 2574
Cdd:NF012221 1813 AAADGRFSEGLTeQEQEALEGATN 1836
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
2111-2196 |
2.64e-03 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 40.50 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2111 KEQAEREAEelrqLALEEENHRREAEAKVkkiSAAEQEAARQCKAALEEVERLKAK-----AEEARRQKELAEKESERQI 2185
Cdd:pfam16999 8 SELAEREAA----LDQQIEAARKEAEREV---EAAEAEAARILREAEAKAKALQAEyrqelAAETARIREEARARAEAEA 80
|
90
....*....|.
gi 2069539781 2186 QLAQEAAQKRI 2196
Cdd:pfam16999 81 QAVRTRAEGRL 91
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2354-2624 |
2.70e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2354 LEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKdKDNMQKFLAEEAEKMKQVAEEAARLS 2433
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREK-RDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2434 VEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLR-LAEEAEG 2512
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKeLRAELKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2513 FQKTLEAERQRQLEITANAERLKVQVTELSlaqakaeEEAKRFKKQAEQisqkLHQTELATQEKMTLVQTLEIQRQQSDS 2592
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELY-------KEADELRKEADE----LHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270
....*....|....*....|....*....|..
gi 2069539781 2593 DAEKLRKAIADlEQEKEKLKREAELLQQKSEE 2624
Cdd:COG1340 241 ELRKELKKLRK-KQRALKREKEKEELEEKAEE 271
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
2658-2751 |
2.73e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.56 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2658 VEEEKAKLEKLfQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAE-AEENVRQKQEELQRLEKQRQKQEKLL 2736
Cdd:TIGR04320 263 LATAQADLAAA-QTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQtAQNNLATAQAALANAEARLAKAKEAL 341
|
90
....*....|....*
gi 2069539781 2737 AEENQKLREKLEQLQ 2751
Cdd:TIGR04320 342 ANLNADLAKKQAALD 356
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2442-2631 |
2.81e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2442 LRELAEQDLAQQRSLAEKILKEKmqavqeatrlKAEAEVLQKQKDL-AQEQAKKLQEDKE-----------QMQLRLAEE 2509
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEA----------KKEAEAIKKEALLeAKEEIHKLRNEFEkelrerrnelqKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2510 AEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQklhqtelatqekMTlvqtleiqrqq 2589
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG------------LT----------- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2069539781 2590 sdsdAEKLRKAIadLEQEKEKLKREAELLQQKSEE--MQTAQKE 2631
Cdd:PRK12704 152 ----AEEAKEIL--LEKVEEEARHEAAVLIKEIEEeaKEEADKK 189
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2158-2262 |
2.89e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2158 EEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEEKahlaaVQQKEQELLQTRQQEQSildKLREEAERAKK 2237
Cdd:PRK11448 149 QEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEK-----QQELEAQLEQLQEKAAE---TSQERKQKRKE 220
|
90 100
....*....|....*....|....*
gi 2069539781 2238 AAEDAEfARIKAEQEaaLSRQLVEE 2262
Cdd:PRK11448 221 ITDQAA-KRLELSEE--ETRILIDQ 242
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2089-2372 |
2.93e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2089 GKTDLELELTRIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAE 2168
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2169 EARRQ-KELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQSILDK---LREEAERAKKAAEDAEF 2244
Cdd:COG1340 82 ELNEKlNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKikeLEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2245 ARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKAKAQE---DAEKLRKEAEleaarraQAEQAALKQKQLADAEmakHKK 2321
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIElykEADELRKEAD-------ELHKEIVEAQEKADEL---HEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2322 FaEQTLRQKAQVEQELTKVKLQLEETdhQKSILEEEQQRLKDEVTEAMKQK 2372
Cdd:COG1340 232 I-IELQKELRELRKELKKLRKKQRAL--KREKEKEELEEKAEEIFEKLKKG 279
|
|
| TTKRSYEDQ |
pfam10212 |
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a ... |
2572-2756 |
2.94e-03 |
|
Predicted coiled-coil domain-containing protein; This is the C-terminal 500 amino acids of a family of proteins with a predicted coiled-coil domain conserved from nematodes to humans. It carries a characteriztic TTKRSYEDQ sequence-motif. The function is not known.
Pssm-ID: 463001 Cd Length: 523 Bit Score: 43.66 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2572 ATQEKMTLVQtleiQRQQSdsdAEKLRKaiadLEQEKEKLKREAELLQQKSE-EMQTA---QKEQLRQETQMLQQTFRSE 2647
Cdd:pfam10212 300 STESREGLAQ----QVQQS---QEKIAK----LEQEKEHWMLEAQLLKIKLEkENQRIadlEKQLLKGSTSGQLPELVQS 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2648 KDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQ------------LTTVLEEARKKQAEAEENV 2715
Cdd:pfam10212 369 KATLPLTAKQGSEASSISEKEPTPSTSLIGMLTVTTDSEESSDEESREQlikshymariaeLTSQLQLADSKAVHFHAEC 448
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2069539781 2716 RQKQEELQRLEKQRQKqeklLAEENQKLREKLEQLQEEQKT 2756
Cdd:pfam10212 449 RALAKRLALAEKSKES----LTEELKLANQNISRLQDELTT 485
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2125-2755 |
3.00e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 44.17 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2125 ALEEENHRREAEAKVKKisaaeqeaarQCKAALEEVERLKAKAEEARRQKELAEKESERQIQLAQEAAQKRIVAEE---- 2200
Cdd:pfam15818 12 ALEELRMRREAETQYEE----------QIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEeekg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2201 KAHLAA-VQQKE----QELLQTRQQEQSILDKLREEAERAKK----AAEDAEFARIKAEQ-EAALSRQ--LVEEA-ERMK 2267
Cdd:pfam15818 82 KYQLATeIKEKEieglKETLKALQVSKYSLQKKVSEMEQKLQlhllAKEDHHKQLNEIEKyYATITGQfgLVKENhGKLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2268 QRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMA--------KHKKFAEqtLRQKAQVEQELTK 2339
Cdd:pfam15818 162 QNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQYKMGeeninltiKEQKFQE--LQERLNMELELNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2340 vKLQlEETDHqksILEEEQQRLKD--EVTEAMKQKVQVEEELfkvKVQMEELIKLKTRIEEENKMLITKDKDNMQKF--L 2415
Cdd:pfam15818 240 -KIN-EEITH---IQEEKQDIIISfqHMQQLLQQQTQANTEM---EAELKALKENNQTLERDNELQREKVKENEEKFlnL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2416 AEEAEKM-----KQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKE---KMQAVQEATRLKAEaEVLQKQKDL 2487
Cdd:pfam15818 312 QNEHEKAlgtwkKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEedkKFQNVPEVNNENSE-MSTEKSENL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2488 AQEQAKKLQEDKEQMQLRLAEEAEgFQKTLEAERQRQLEITANaerlKVQVTElslaqakaeeeaKRFKKQAE-QISQKL 2566
Cdd:pfam15818 391 IIQKYNSEQEIREENTKSFCSDTE-YRETEKKKGPPVEEIIIE----DLQVLE------------KSFKNEIDtSVPQDK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2567 HQTELATQEkmTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKS-EEMQTAQKEQLRQETQMLQQTFR 2645
Cdd:pfam15818 454 NQSEISLSK--TLCTDKDLISQGQTLNVTDFRKSVTTEIKDKLCLEKDNGCSEFKSpNNLFLVADQSIETEKIHLESTEG 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2646 SE---KDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEA---------EE 2713
Cdd:pfam15818 532 LGlhhADIHLETESNRSSFNGTLNEMAHNTNHNKDVSENEPFKQQFRLLLCTQENATEKRITNSDQTKAgldssldvkKN 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2069539781 2714 NVRQKQEELQ-----RLEKQRQKQEKLLAEENQKLREKLEQLQEEQK 2755
Cdd:pfam15818 612 PVQCQKYSLQdssnvSLDDKQCKIEQLLNKKSECSTLPLKQTSSFQQ 658
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1643-2048 |
3.03e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1643 EEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQK- 1721
Cdd:pfam15709 174 ELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNLEVAAELSGPd 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1722 ---SAEADLQSRRLSFAEKTAQLELSL------QQEHITIThlqeeaERLKKLQLEAEQSREEADKEVekwrqkanealr 1792
Cdd:pfam15709 254 vinSKETEDASERGAFSSDSVVEDPWLsskydaEESQVSID------GRSSPTQTFVVTGNMESEEER------------ 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1793 lrlqAEEVAHKKALAQEEAEKqkedaerEARKRSKAEESALRQkelaeqeLEKQRKLAEGTAQQKFLAEQElirlkaeve 1872
Cdd:pfam15709 316 ----SEEDPSKALLEKREQEK-------ASRDRLRAERAEMRR-------LEVERKRREQEEQRRLQQEQL--------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1873 ngeqqrllleeelfrlknevNEAVQKRKELEEELAKLRAEMELLLQSkaKTEEESRSTSEKSKQILEAEASKLRELAEEA 1952
Cdd:pfam15709 369 --------------------ERAEKMREELELEQQRRFEEIRLRKQR--LEEERQRQEEEERKQRLQLQAAQERARQQQE 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1953 ARLRALSEeakRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQRRLLEEQ 2032
Cdd:pfam15709 427 EFRRKLQE---LQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEE 503
|
410
....*....|....*.
gi 2069539781 2033 AAQHKQDIEEKIAQLK 2048
Cdd:pfam15709 504 AARLALEEAMKQAQEQ 519
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2605-2746 |
3.15e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.38 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2605 EQEKEKLKREAellqQKSEEMQTAQKEQLRQETQMLQQTFRsekdvllQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQE 2684
Cdd:pfam13904 43 KLEGLKLERQP----LEAYENWLAAKQRQRQKELQAQKEER-------EKEEQEAELRKRLAKEKYQEWLQRKARQQTKK 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2685 RQQKQMEQEKKQLTT--------VLEEARKKQAEAEENVRQKQEELQRLEKQR-QKQEKLLAEENQKLREK 2746
Cdd:pfam13904 112 REESHKQKAAESASKslakperkVSQEEAKEVLQEWERKKLEQQQRKREEEQReQLKKEEEEQERKQLAEK 182
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2212-2291 |
3.24e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 41.30 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2212 QELLQTRQQeqsildKLREEAERAKKAAEDAEFARIKAEQEAALSR----QLVEEAERMKQRAEEEAqtKAKAQEDAEKL 2287
Cdd:PRK05759 30 MKALEERQK------KIADGLAAAERAKKELELAQAKYEAQLAEARaeaaEIIEQAKKRAAQIIEEA--KAEAEAEAARI 101
|
....
gi 2069539781 2288 RKEA 2291
Cdd:PRK05759 102 KAQA 105
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2592-2775 |
3.28e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2592 SDAEKLRKAIADLEQEKEKLKREAELLQQKseemqtaqKEQLRQETQmlqqTFRSEKDVLLQKERFVEEEKAKLEKLFQE 2671
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEK--------RDELNEELK----ELAEKRDELNAQVKELREEAQELREKRDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2672 EVNKAQGLKAEQERQQKQMEQEKKQLTTvLEEARKKQAEAEENVRQKQEELQRLEKQRQ------KQEKLLAEENQKLRE 2745
Cdd:COG1340 69 LNEKVKELKEERDELNEKLNELREELDE-LRKELAELNKAGGSIDKLRKEIERLEWRQQtevlspEEEKELVEKIKELEK 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 2069539781 2746 KLEQLQ------EEQKTALAQTREIMIQTDDLPQEV 2775
Cdd:COG1340 148 ELEKAKkaleknEKLKELRAELKELRKEAEEIHKKI 183
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2171-2577 |
3.30e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2171 RRQKELAEKEsERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQTRQQEQS--ILDKLREEAERAKKAAEDAEFarIK 2248
Cdd:PRK04778 26 RNYKRIDELE-ERKQELENLPVNDELEKVKKLNLTGQSEEKFEEWRQKWDEIVtnSLPDIEEQLFEAEELNDKFRF--RK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2249 AEQEAALSRQLVEEAERMKQRAEEEAQtkaKAQEDAEKLRKEAEleaarRAQAEQAALKQKQLADAEmakhkKF--AEQT 2326
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQ---ELLESEEKNREEVE-----QLKDLYRELRKSLLANRF-----SFgpALDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2327 LRQK-AQVEQELTKVKLQLEETDHQKSilEEEQQRLKDEvTEAMKQKVQVEEELFK-----VKVQMEELIKLKTRIEEEN 2400
Cdd:PRK04778 170 LEKQlENLEEEFSQFVELTESGDYVEA--REILDQLEEE-LAALEQIMEEIPELLKelqteLPDQLQELKAGYRELVEEG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2401 KMLitkDKDNMQKFLAEEAEKMKQVAEEAARLSVEAqeaarlrelAEQDLAQqrsLAEKIlkEKMQAVQEaTRLKAEAEV 2480
Cdd:PRK04778 247 YHL---DHLDIEKEIQDLKEQIDENLALLEELDLDE---------AEEKNEE---IQERI--DQLYDILE-REVKARKYV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2481 LQKQKDL------AQEQAKKLQEDKEQMQL------RLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKA 2548
Cdd:PRK04778 309 EKNSDTLpdflehAKEQNKELKEEIDRVKQsytlneSELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEI 388
|
410 420 430
....*....|....*....|....*....|..
gi 2069539781 2549 EEEAKRFKKQAEQIS---QKLHQTELATQEKM 2577
Cdd:PRK04778 389 LKQLEEIEKEQEKLSemlQGLRKDELEAREKL 420
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2680-2776 |
3.38e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2680 KAEQERQQKQMEQEKKQLTTVLE---EARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKT 2756
Cdd:PRK12705 34 EAERILQEAQKEAEEKLEAALLEakeLLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKA 113
|
90 100
....*....|....*....|
gi 2069539781 2757 ALAQTREIMIQTDDLPQEVV 2776
Cdd:PRK12705 114 LSARELELEELEKQLDNELY 133
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1633-1730 |
3.41e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1633 EAERQKRLAQEEAERLRKqvkdESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERRMKQAELEKERQV 1712
Cdd:pfam05672 28 EREEQERLEKEEEERLRK----EELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQK 103
|
90
....*....|....*...
gi 2069539781 1713 QLAHEAAQKSAEADLQSR 1730
Cdd:pfam05672 104 EEAEAKAREEAERQRQER 121
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2393-2566 |
3.47e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.45 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2393 KTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEaarlsvEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEAT 2472
Cdd:pfam05262 185 ALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKE------ELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2473 RLKAEAEVLQKQKDlaqeqaKKLQEDKEQMQLRLAEEAEgfQKTLEAERQRQleitANAERLKVQVTELSLAQAKAEEEA 2552
Cdd:pfam05262 259 NLPKPADTSSPKED------KQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEA 326
|
170
....*....|....
gi 2069539781 2553 KRFKKQAEQISQKL 2566
Cdd:pfam05262 327 QKKREPVAEDLQKT 340
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2549-2718 |
3.51e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.48 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2549 EEEAKRFKKQAEQISQKLhqTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIAD-LEQEKEKLKREAELLQQKSEEMQT 2627
Cdd:pfam01442 3 EDSLDELSTYAEELQEQL--GPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPyLEELQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2628 AQKEQLRQETQMLQQTFRSEKDVLLQK-ERFVEEEKAKLEKLFQEEVNK-AQGLKAEQERQQKQMEQEKKQLTTVLEEAR 2705
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERlEQNVDALRARLAPYAEELRQKlAERLEELKESLAPYAEEVQAQLSQRLQELR 160
|
170
....*....|...
gi 2069539781 2706 KKQAEAEENVRQK 2718
Cdd:pfam01442 161 EKLEPQAEDLREK 173
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
2092-2174 |
3.56e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 40.61 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2092 DLELELTRIKQSAEEIQRSKEQAEREAEELRqlaleeENHRREAEAKVKKisaAEQEAARQCKAALEEVERLKAKAEEAR 2171
Cdd:COG3599 52 ELEEELEEYRELEETLQKTLVVAQETAEEVK------ENAEKEAELIIKE---AELEAEKIIEEAQEKARKIVREIEELK 122
|
...
gi 2069539781 2172 RQK 2174
Cdd:COG3599 123 RQR 125
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2214-2484 |
3.58e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2214 LLQTRQQEQSILDKLREEAERAKKAAEDAEF--ARI---KAEQEAALSRQLVEEAERMKQrAEEEAQTKAKAQEDAEKLR 2288
Cdd:PRK05035 427 LVQYYRQAKAEIRAIEQEKKKAEEAKARFEArqARLereKAAREARHKKAAEARAAKDKD-AVAAALARVKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2289 KEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEA 2368
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2369 M-----KQKVQVEEELFKVKVQMEELIKlKTRIEEENKMLITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEAARLR 2443
Cdd:PRK05035 586 IarakaKKAAQQAASAEPEEQVAEVDPK-KAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQ 664
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2069539781 2444 ELAEQDLAqqrslaekiLKEKMQAVQEATRlKAEAEVLQKQ 2484
Cdd:PRK05035 665 ANAEPEEA---------EDPKKAAVAAAIA-RAKAKKAAQQ 695
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
2395-2758 |
3.59e-03 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 43.42 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2395 RIEEENKMLITKDKDNMQKFLAEEAEKM----KQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAvqE 2470
Cdd:pfam14643 21 SLSNEVEPLIAEAGELLLQKLAESDEEInalfKKLEDDDALEDYTIQQLEELWDIVAQHSLLRKSWIKELDETLEKL--E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2471 ATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMqlrLAEEAEGFQKTLEAERQrqleitANAErLKVQVTElslaQAKAEE 2550
Cdd:pfam14643 99 KERADKLKSVLKKYVEILEDIAHLLPPDVYRL---IDKEAMEINQALLENRR------AYAK-LFANLME----AELKQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2551 EAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSdsdaeklrkaiadLEQEKEKLKREAELLQQKSEEM----- 2625
Cdd:pfam14643 165 LSFRLRWQDRVDRWKALKTEHLIQEFKEFIASEEIQNPPE-------------RKKELEEMLKEQKKLQQKRLELlqkis 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2626 -------QTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEK-----AKLEKLfQEEVNKAQGLKAEQERQ------- 2686
Cdd:pfam14643 232 dllppaySKSKVEEWWASLEALNEQLDQYHDQCMTKLRAEYEEVwqeclARVQKL-KQELLDYKVCSEEEAEAlvneefl 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2687 ------QKQMEQEKKQLTTVLEEARKKQA-----------------EAEENVRQKQE-ELQ-RLEKQRQKQEkllaEENQ 2741
Cdd:pfam14643 311 plvgklQRDAEDELEKLDKFLEELAKQTEaqsedlfkffreaaqlwDVHQTELAKQElELEkKLEQCRQKHD----QENQ 386
|
410
....*....|....*..
gi 2069539781 2742 KLREKLEQLQEEQKTAL 2758
Cdd:pfam14643 387 AKEAALDKKLDQLRQAS 403
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4425-4471 |
3.66e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.08 E-value: 3.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2069539781 4425 AQLASwsdpteetgpvAGILDTDTLEKVSITEAMRRNLVDNITGQRL 4471
Cdd:pfam00681 4 AQAAT-----------GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
2685-2761 |
3.66e-03 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 41.32 E-value: 3.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2069539781 2685 RQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKlEQLQEEQKTALAQT 2761
Cdd:pfam15236 50 KRQKALEHQNAIKKQLEEKERQKKLEEERRRQEEQEEEERLRREREEEQKQFEEERRKQKEK-EEAMTRKTQALLQA 125
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1957-2204 |
3.68e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1957 ALSEEAKRQRQlaeEEATHQRAEAERILKEKLVAINEASRLKAEAEialKEKEAENERLRrlAEDEAYQRRLLEEQAAQH 2036
Cdd:PRK09510 59 AVVEQYNRQQQ---QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQE---RLKQLEKERLA--AQEQKKQAEEAAKQAALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2037 KQDIEEKIAQLKKSSESELERQKslvddtvrqrrlveeeirilklnfekashgktdleleltriKQSAEEIQRSKEQAE- 2115
Cdd:PRK09510 131 QKQAEEAAAKAAAAAKAKAEAEA-----------------------------------------KRAAAAAKKAAAEAKk 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2116 REAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAE-EARRQKELAEKESERQIQLAQEAAQK 2194
Cdd:PRK09510 170 KAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
250
....*....|
gi 2069539781 2195 RIVAEEKAHL 2204
Cdd:PRK09510 250 AAAAKAAAEV 259
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2661-2850 |
3.77e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2661 EKAKleKLFQEEVNKAQGLKAEQERQQKQMEQEkkqlttvLEEARKKQAEAEenvRQKQEELQRLEKQRQKQEKLLAEEN 2740
Cdd:PRK00409 505 EEAK--KLIGEDKEKLNELIASLEELERELEQK-------AEEAEALLKEAE---KLKEELEEKKEKLQEEEDKLLEEAE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2741 QKLREKLEQLQEEQKTALAQTREIMIQTD---------------DLPQEVVAPSQVPQMKAVP-------------NGRD 2792
Cdd:PRK00409 573 KEAQQAIKEAKKEADEIIKELRQLQKGGYasvkaheliearkrlNKANEKKEKKKKKQKEKQEelkvgdevkylslGQKG 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2793 MIDGISQNGEAELAFDGIRQKVSAKKLAEAGILSRESMEKLAKGKATVQELSQRDDIR 2850
Cdd:PRK00409 653 EVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTVSLELDLR 710
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2426-2655 |
3.85e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2426 AEEAARLSVEAQEAARLRELAEQ-DLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQL 2504
Cdd:PRK11281 29 AASNGDLPTEADVQAQLDALNKQkLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2505 RLAEEAegfQKTLEAERQRQLE-----------------ITANAErLKVQVTELSLAQAKAEEEAKRfkkqAEQISQKLH 2567
Cdd:PRK11281 109 DNDEET---RETLSTLSLRQLEsrlaqtldqlqnaqndlAEYNSQ-LVSLQTQPERAQAALYANSQR----LQQIRNLLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2568 -------------QTELATQEKMtLVQTLEIQRQ--QSDSDAEKLRKAIADLEQEK-EKLKREAELLQQKSEEMQTAQKE 2631
Cdd:PRK11281 181 ggkvggkalrpsqRVLLQAEQAL-LNAQNDLQRKslEGNTQLQDLLQKQRDYLTARiQRLEHQLQLLQEAINSKRLTLSE 259
|
250 260
....*....|....*....|....
gi 2069539781 2632 QLRQETQMLQQTFRSEKDVLLQKE 2655
Cdd:PRK11281 260 KTVQEAQSQDEAARIQANPLVAQE 283
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2442-2771 |
3.96e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2442 LRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAER 2521
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2522 QRQLEItanaERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAI 2601
Cdd:COG4372 98 QAQEEL----ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2602 ADLEQEK--EKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGL 2679
Cdd:COG4372 174 QALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2680 KAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALA 2759
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
330
....*....|..
gi 2069539781 2760 QTREIMIQTDDL 2771
Cdd:COG4372 334 ILLAELADLLQL 345
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
2677-2759 |
4.03e-03 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 40.35 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2677 QGLKAEQERQQKQMEQEKKQlttvlEEARKKQAEaEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKT 2756
Cdd:pfam04696 23 KEESKQKEKEERRAEIEKRL-----EEKAKQEKE-ELEERKREEREELFEERRAEQIELRALEEKLELKELMETWHENLK 96
|
...
gi 2069539781 2757 ALA 2759
Cdd:pfam04696 97 ALA 99
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2550-2697 |
4.07e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2550 EEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQK---SEEMQ 2626
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKqkeEEQMM 234
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2627 TAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFqeevnkaqgLKAEQERQQKQMEQEKKQL 2697
Cdd:pfam02841 235 EAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEEL---------LKEGFKTEAESLQKEIQDL 296
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2604-2763 |
4.20e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.40 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2604 LEQEKEKLKREAELLQQKSEEMqTAQKEQLRQETQmlqQTFRSEKDVLLQKERF---VEEEKAKLEKLFQEEVNKAQG-L 2679
Cdd:pfam06008 45 LEKELSSLAQETEELQKKATQT-LAKAQQVNAESE---RTLGHAKELAEAIKNLidnIKEINEKVATLGENDFALPSSdL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2680 KAEQERQQKQMEQEK-KQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTAL 2758
Cdd:pfam06008 121 SRMLAEAQRMLGEIRsRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAA 200
|
....*
gi 2069539781 2759 AQTRE 2763
Cdd:pfam06008 201 AKTRD 205
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2279-2618 |
4.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2279 KAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQ 2358
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2359 QRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLitkdKDNMQKFLAEEAEKMKQVAEEAARLSVEAQE 2438
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL----EAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2439 AARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQMQLRLAEEAEGFQKTLE 2518
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2519 AERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLR 2598
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|
gi 2069539781 2599 KAIADLEQEKEKLKREAELL 2618
Cdd:COG4372 326 KKLELALAILLAELADLLQL 345
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1581-1733 |
4.26e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1581 QIQAKLKLIEEVEFSRRKVEEEIRMVR--LQLEATERQRAGAEDELQALRDRAEEAERQ-KRLAQEEAERLRKQVKDESQ 1657
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLeaALLEAKELLLRERNQQRQEARREREELQREeERLVQKEEQLDARAEKLDNL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2069539781 1658 KKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAeRRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLS 1733
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQA-RKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKA 178
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1939-2202 |
4.27e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1939 EAEASKLRELAEEAARlrALSEEAKRQRQLAEEEATHQRAEAERILKEKlvaineaSRLKAEAEIALKEKEAENERLRRL 2018
Cdd:TIGR02794 49 AQQANRIQQQKKPAAK--KEQERQKKLEQQAEEAEKQRAAEQARQKELE-------QRAAAEKAAKQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2019 AEDEAYQRRLLEEQAAQHKQDIEEKIAQLKKSSESElerqkslvddtvrqRRLVEEEIRILKLNFEKASHGKTDLELELT 2098
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEE--------------AKAKAAAEAKKKAEEAKKKAEAEAKAKAEA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2099 RIKQSAEEIQRSKEQAEREAEElrqlaleEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAE 2178
Cdd:TIGR02794 186 EAKAKAEEAKAKAEAAKAKAAA-------EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
250 260
....*....|....*....|....
gi 2069539781 2179 KESERQIQLAQEAAQKRIVAEEKA 2202
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQNLYDDPSF 282
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1932-2059 |
4.30e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1932 EKSKQILEAEASKLRELAEEAARlRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAE 2011
Cdd:PRK12705 36 ERILQEAQKEAEEKLEAALLEAK-ELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKAL 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2069539781 2012 NERLRRLAEDEAYQRRLLEEQAAQHKQDIEEKIAQLkksSESELERQK 2059
Cdd:PRK12705 115 SARELELEELEKQLDNELYRVAGLTPEQARKLLLKL---LDAELEEEK 159
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2618-2763 |
4.53e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2618 LQQKSEEMQTAQKEQLRQETQMLQQtFRSEKDVLLQKERFVEEEKAkleklfqeevnKAQGLKAEQERQQKQMEQEKKQl 2697
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEE-LQQKQAAEQERLKQLEKERL-----------AAQEQKKQAEEAAKQAALKQKQ- 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2698 ttvLEEARKKQAE-----AEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTRE 2763
Cdd:PRK09510 134 ---AEEAAAKAAAaakakAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKK 201
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2023-2186 |
4.64e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2023 AYQRRLLEEQAAQHKQDIEEKIAQLKKssESELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHGKTDLELEltrikq 2102
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLE--AALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAR------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2103 sAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESE 2182
Cdd:PRK12705 97 -AEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
....
gi 2069539781 2183 RQIQ 2186
Cdd:PRK12705 176 RKAQ 179
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1610-1689 |
4.66e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.93 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1610 LEATERQRAGAEDELQALRDRAE----EAERQKRLAQEEAERLRKQVKDESQKKRE-----AEDELKHKV-QAEQQAARE 1679
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEaalaEYEEKLAEARAEAAEIIAEARKEAEAIAEeakaeAEAEAERIIaQAEAEIEQE 108
|
90
....*....|
gi 2069539781 1680 KQKALEDLQK 1689
Cdd:COG0711 109 RAKALAELRA 118
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2042-2440 |
4.67e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2042 EKIAQLKKSSESELERQKSLVDDtvrQRRLVEEEIRILKLNFEKASHGKTDLELELTRIKQSAEEIQRSKEQAEREAEEL 2121
Cdd:COG5185 127 KSEIVALKDELIKVEKLDEIADI---EASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2122 RQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEVERLKAKAEEARRQKELAEKESE-RQIQLAQEAAQKRIVAEE 2200
Cdd:COG5185 204 VNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDlRLEKLGENAESSKRLNEN 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2201 KAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQLVEEAERMKQRAEEEAQTKA-- 2278
Cdd:COG5185 284 ANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEei 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2279 ----------KAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEqtlRQKAQVEQELTKVKLQLEETD 2348
Cdd:COG5185 364 enivgevelsKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD---RQIEELQRQIEQATSSNEEVS 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2349 HQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQ------MEELIKLKTRIeEENKMLITKDKDNMQKFLAEEAEKM 2422
Cdd:COG5185 441 KLLNELISELNKVMREADEESQSRLEEAYDEINRSVRskkedlNEELTQIESRV-STLKATLEKLRAKLERQLEGVRSKL 519
|
410
....*....|....*...
gi 2069539781 2423 KQVAEEAARLSVEAQEAA 2440
Cdd:COG5185 520 DQVAESLKDFMRARGYAH 537
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2032-2292 |
4.83e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 42.63 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2032 QAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIR---ILKLNFEKASHGKTDLElELTRikqsaeEIQ 2108
Cdd:pfam09728 8 QLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKekdQLQSELSKAILAKSKLE-KLCR------ELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2109 RskeQAEREAEELRQLALEEENHRREAEAK----VKKISAAEQEAARQCKAALEEVERLKAKAE------EAR------- 2171
Cdd:pfam09728 81 K---QNKKLKEESKKLAKEEEEKRKELSEKfqstLKDIQDKMEEKSEKNNKLREENEELREKLKslieqyELRelhfekl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2172 -RQKELAEKESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELLQT----RQQEQSILDKLREEAERAKKAAEdaEFAR 2246
Cdd:pfam09728 158 lKTKELEVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSETekelREQLNLYVEKFEEFQDTLNKSNE--VFTT 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2069539781 2247 IKAEQE--AALSRQLVEEAERMKQRAE-------EEAQTKAKAQEDAEKLRKEAE 2292
Cdd:pfam09728 236 FKKEMEkmSKKIKKLEKENLTWKRKWEksnkallEMAEERQKLKEELEKLQKKLE 290
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1766-2050 |
4.96e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1766 QLEAEQSREEADKEVEKWRQKANEALRL-----RLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQKELAE 1840
Cdd:PRK11281 44 QLDALNKQKLLEAEDKLVQQDLEQTLALldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1841 QELEKQrkLAEGTAQ----QKFLAE--QELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKEL-EEELAKLRAEM 1913
Cdd:PRK11281 124 RQLESR--LAQTLDQlqnaQNDLAEynSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALrPSQRVLLQAEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1914 ELL-LQSkakteEESRSTSEKSKQILEAEASKLRELAEEAARL---RALSEEAKRQRQLAEEEATHQRAEAerilKEKLV 1989
Cdd:PRK11281 202 ALLnAQN-----DLQRKSLEGNTQLQDLLQKQRDYLTARIQRLehqLQLLQEAINSKRLTLSEKTVQEAQS----QDEAA 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2069539781 1990 AINEASRLKAEAEIALKEKE---AENERLRRLAEDEAYQRRLLeEQAAQHKQDIEEKIAQLKKS 2050
Cdd:PRK11281 273 RIQANPLVAQELEINLQLSQrllKATEKLNTLTQQNLRVKNWL-DRLTQSERNIKEQISVLKGS 335
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2099-2292 |
4.96e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.93 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2099 RIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAeakvkkisaAEQEAARQCKAALeeverLKAKaEEARRQKELAE 2178
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKT---------AKRESKALKKELL-----LEAK-EEARKYREEIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2179 KE--SERQiqlaqEAAQKRIVAEEKAhlAAVQQKEQELLQTR----QQEQSILDKLREEAERakkaaedaefarikAEQE 2252
Cdd:PRK00106 90 QEfkSERQ-----ELKQIESRLTERA--TSLDRKDENLSSKEktleSKEQSLTDKSKHIDER--------------EEQV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2069539781 2253 AALSRQLVEEAERMKQRAEEEA------QTKAKAQEDAEKLRKEAE 2292
Cdd:PRK00106 149 EKLEEQKKAELERVAALSQAEAreiilaETENKLTHEIATRIREAE 194
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1949-2127 |
5.01e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.93 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1949 AEEAARLRALS--EEAKRQRQLAEEEATHQRAEAER----ILKEKLV-AINEASRLKAEAEIALKEKEAE--------NE 2013
Cdd:PRK00106 29 AKEAAELTLLNaeQEAVNLRGKAERDAEHIKKTAKReskaLKKELLLeAKEEARKYREEIEQEFKSERQElkqiesrlTE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2014 R---LRRLAEDEAYQRRLLE--EQA----AQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEEEIrilKLNFE 2084
Cdd:PRK00106 109 RatsLDRKDENLSSKEKTLEskEQSltdkSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETEN---KLTHE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2069539781 2085 KAshgktdlelelTRIKQSAEEIqrsKEQAEREAEELRQLALE 2127
Cdd:PRK00106 186 IA-----------TRIREAEREV---KDRSDKMAKDLLAQAMQ 214
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1620-1709 |
5.06e-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: 42.18 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1620 AEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAE-QQAAREKQKALEDLQKLRLQAEEAE 1698
Cdd:cd16269 196 KEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEErENLLKEQERALESKLKEQEALLEEG 275
|
90
....*....|.
gi 2069539781 1699 RRMKQAELEKE 1709
Cdd:cd16269 276 FKEQAELLQEE 286
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2154-2241 |
5.09e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2154 KAALEEVERLKAKAEEarrqkelAEKESERQIQLAQEAAQKRIvaeEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAE 2233
Cdd:cd06503 36 AESLEEAEKAKEEAEE-------LLAEYEEKLAEARAEAQEII---EEARKEAEKIKEEILAEAKEEAERILEQAKAEIE 105
|
....*...
gi 2069539781 2234 RAKKAAED 2241
Cdd:cd06503 106 QEKEKALA 113
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2031-2293 |
5.15e-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: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2031 EQAAQHKQDIEEKIAQLKKSSESELERQKSLVDDTVRQRRLVEE---EIRILKLNFEKASHGKTDLELELTRIKQSAEEI 2107
Cdd:pfam19220 44 PQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEElvaRLAKLEAALREAEAAKEELRIELRDKTAQAEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2108 QRskeQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAArqckaalEEVERLKAKAEEARRQKELAEKeserqiQL 2187
Cdd:pfam19220 124 ER---QLAAETEQNRALEEENKALREEAQAAEKALQRAEGELA-------TARERLALLEQENRRLQALSEE------QA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2188 AQEAAQKRIVAEEKAHLAAVQQkeqellQTRQQEQSILDklrEEAERAK-KAAEDAEFARIKAEQEAALSR-----QLVE 2261
Cdd:pfam19220 188 AELAELTRRLAELETQLDATRA------RLRALEGQLAA---EQAERERaEAQLEEAVEAHRAERASLRMKlealtARAA 258
|
250 260 270
....*....|....*....|....*....|..
gi 2069539781 2262 EAERMKQRAEEEAQTKAKAQEDAEKLRKEAEL 2293
Cdd:pfam19220 259 ATEQLLAEARNQLRDRDEAIRAAERRLKEASI 290
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1918-2063 |
5.16e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.08 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1918 QSKAKTEEESRSTSEKSKQIL--------EAEASKLRELAEEAARLR---------ALSEEAKRQ--RQLAEEEATHQ-- 1976
Cdd:PTZ00491 636 QSVEPVDERTRDSLQKSVQLAieittksqEAAARHQAELLEQEARGRlerqkmhdkAKAEEQRTKllELQAESAAVESsg 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1977 --RAEAErilkeklvAINEASRLKAEAEIALKEKEAENERLRRLAE-DEAYQRRLLEEQAAQHKQDIEekIAQLKKSSES 2053
Cdd:PTZ00491 716 qsRAEAL--------AEAEARLIEAEAEVEQAELRAKALRIEAEAElEKLRKRQELELEYEQAQNELE--IAKAKELADI 785
|
170
....*....|
gi 2069539781 2054 ELERQKSLVD 2063
Cdd:PTZ00491 786 EATKFERIVE 795
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2418-2531 |
5.20e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.08 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2418 EAEKMK-QVAEEAAR---LSVEAQEAARlrELAEQDLAQQRSLAEKILKEkMQAVQEATRLKAEAEVLQKQKDLAQEQAK 2493
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2069539781 2494 KLQEDKEQMQL---------RLAE-EAEGFQKTLEAERQRQLEITANA 2531
Cdd:PTZ00491 761 QELELEYEQAQneleiakakELADiEATKFERIVEALGRETLIAIARA 808
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1813-2043 |
5.25e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 43.28 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1813 KQKEDAEREARKRSKAEESALRQKELAEQ-----ELEKQRKLAEGTAQQKFLAEQELIRLKAeveNGEQQRLLLEEELFR 1887
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQSQLESTDQNALET---NGQAQRDAILEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1888 LKNEVNEAVQKRKELEEElAKLRAEM---------ELLLQSKAKTEEESRSTS----EKSKQILEAEASKLRELAEEAAR 1954
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQ-ATYAGESgdqwrnpfaGGLLDRVQEQLDDAKKISgkqlADAKQRHVDNQQKVKDAVAKSEA 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1955 LRALSEEAKRQRQLAEEEAthqRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAEDEAYQrrlLEEQAA 2034
Cdd:NF012221 1697 GVAQGEQNQANAEQDIDDA---KADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQ---AQADAK 1770
|
....*....
gi 2069539781 2035 QHKQDIEEK 2043
Cdd:NF012221 1771 GAKQDESDK 1779
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1861-2123 |
5.32e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1861 EQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEa 1940
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1941 easKLRELAEEAARLRALSEEAKR-QRQLAEEEATHQRA----EAERILkeklvaINEASRLKAEAEIALKEKEAENERL 2015
Cdd:COG1340 93 ---ELDELRKELAELNKAGGSIDKlRKEIERLEWRQQTEvlspEEEKEL------VEKIKELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2016 RRLAEDEAyqrrlLEEQAAQHKQDIEEKIAQLKKSSES------ELERQKSLVDDTVRQRRLVEEEIRILKLNFEKASHG 2089
Cdd:COG1340 164 ELRAELKE-----LRKEAEEIHKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 2069539781 2090 KTDLELELTRIKQSAEEIQRSKEQAE--REAEELRQ 2123
Cdd:COG1340 239 LRELRKELKKLRKKQRALKREKEKEEleEKAEEIFE 274
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1508-1639 |
5.40e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRLAEVEAQLEKQRQLAEAHARAKAQA-EKEALELQRRMEEEVSRRqlvavdAEQQKQTiQQELsQMKLSSDAQIQAKL 1586
Cdd:pfam15709 400 RQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAER------AEAEKQR-QKEL-EMQLAEEQKRLMEM 471
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 1587 KLIEEVEFSRRKVEEEirmVRLQLEATERQRAGAEDELQALRDRAEEAERQKR 1639
Cdd:pfam15709 472 AEEERLEYQRQKQEAE---EKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2654-2754 |
5.43e-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: 40.79 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2654 KERFVEEEKAKLEKlfQEEVNKAQGLKAEQERQQKQMEQEKKQltTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQE 2733
Cdd:pfam05672 32 QERLEKEEEERLRK--EELRRRAEEERARREEEARRLEEERRR--EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAE 107
|
90 100
....*....|....*....|...
gi 2069539781 2734 KLLAEENQKLREKLEQL--QEEQ 2754
Cdd:pfam05672 108 AKAREEAERQRQEREKImqQEEQ 130
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1509-1694 |
5.44e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1509 QRLAEVE-AQLEKQRQLAEAhARAKAQAEKEALELQRRMEEEVSRrqlvavdAEQQKQTIQQELSQmklssdAQIQAKlk 1587
Cdd:COG1566 71 QVLARLDpTDLQAALAQAEA-QLAAAEAQLARLEAELGAEAEIAA-------AEAQLAAAQAQLDL------AQRELE-- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 lieevefsrrkveeeiRMVRLQleateRQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQkKREAEDELk 1667
Cdd:COG1566 135 ----------------RYQALY-----KKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV- 191
|
170 180
....*....|....*....|....*..
gi 2069539781 1668 hkvqaeQQAAREKQKALEDLQKLRLQA 1694
Cdd:COG1566 192 ------AQAEAALAQAELNLARTTIRA 212
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
2427-2545 |
5.45e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 41.08 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2427 EEAARLSVEAQEAARLRELAEQDLAQQRSlaekilkEKMQAVQEATRLKAEAEVLQKQkdLAQEQAKKLQEDKEqmqlRL 2506
Cdd:PRK14475 41 AYAAKIQAELDEAQRLREEAQALLADVKA-------EREEAERQAAAMLAAAKADARR--MEAEAKEKLEEQIK----RR 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 2069539781 2507 AEEAEgfQKTLEAERQRQLEITANAERLKVQVTELSLAQ 2545
Cdd:PRK14475 108 AEMAE--RKIAQAEAQAAADVKAAAVDLAAQAAETVLAA 144
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2423-2771 |
5.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2423 KQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQM 2502
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2503 QLRLAE---EAEGFQKTLEAERQRQLEITANAERLKVQVTELSLAQAKAEEEAKRFKKQAEQISQKLHQTELATQEKMTL 2579
Cdd:COG4372 86 NEQLQAaqaELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2580 VQTLEIQRQQSDSDA--EKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQKEQLRQETQMLQQTFRSEKDVLLQKERF 2657
Cdd:COG4372 166 LAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2658 VEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLA 2737
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|....
gi 2069539781 2738 EENQKLREKLEQLQEEQKTALAQTREIMIQTDDL 2771
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1598-1786 |
5.71e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1598 KVEEEIRMVRLQLEATERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKRE--AEDELKHKVQAEQQ 1675
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREdlAREALERKAELEAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1676 AAREKQ---KALEDLQKLRLQAEEAERRMKQAELEKErQVQLAHEAAQksAEADLQSRRLSFAEKTAQLELSLQQEHitI 1752
Cdd:COG1842 100 AEALEAqlaQLEEQVEKLKEALRQLESKLEELKAKKD-TLKARAKAAK--AQEKVNEALSGIDSDDATSALERMEEK--I 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2069539781 1753 THLQEEAERLKKL--------QLEAEQSREEADKEVEKWRQK 1786
Cdd:COG1842 175 EEMEARAEAAAELaagdslddELAELEADSEVEDELAALKAK 216
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1900-1984 |
5.72e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1900 KELEEELAKLRAEMELLLQSKAKTEEESRSTSEKS----KQILEAEAsKLRELAEEAARLRALSEEAKRQRQLAEEEATH 1975
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvaleGLAAELEE-KQQELEAQLEQLQEKAAETSQERKQKRKEITD 223
|
90
....*....|....*.
gi 2069539781 1976 QRA------EAE-RIL 1984
Cdd:PRK11448 224 QAAkrlelsEEEtRIL 239
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1992-2079 |
6.22e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1992 NEASRLKAEAEIALKEKEAENERLRRLAEDeayqRRLLEEQAAQH---KQDIEEKIAQLKKSSES----ELERQKSLVDD 2064
Cdd:PRK11448 149 QEVLTLKQQLELQAREKAQSQALAEAQQQE----LVALEGLAAELeekQQELEAQLEQLQEKAAEtsqeRKQKRKEITDQ 224
|
90
....*....|....*
gi 2069539781 2065 TVRQRRLVEEEIRIL 2079
Cdd:PRK11448 225 AAKRLELSEEETRIL 239
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
780-860 |
6.31e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.22 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 780 WLNEKEE----EEVNYDWTErnsnMVAKKESYSGLMRELEQRERKIKEIQSTGDRLLQEDHPAKQAVEAFQAALQTQWSW 855
Cdd:pfam00435 16 WIEEKEAllssEDYGKDLES----VQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQ 91
|
....*
gi 2069539781 856 MLQMC 860
Cdd:pfam00435 92 LLELA 96
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1508-1699 |
6.46e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1508 RQRlaevEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQlvAVDAEQQKQTiQQELSQMKLSSDAQIQAKLk 1587
Cdd:pfam15709 352 RKR----REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQ--RLEEERQRQE-EEERKQRLQLQAAQERARQ- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1588 liEEVEFsRRKVEEEIRmvrlQLEATERQRAGAEDELQAlRDRAEEAERQKRLAQ-EEAERLRKQvkdesQKKREAEDel 1666
Cdd:pfam15709 424 --QQEEF-RRKLQELQR----KKQQEEAERAEAEKQRQK-ELEMQLAEEQKRLMEmAEEERLEYQ-----RQKQEAEE-- 488
|
170 180 190
....*....|....*....|....*....|...
gi 2069539781 1667 KHKVQAEQQAAREKQKALEDLQKLRLQAEEAER 1699
Cdd:pfam15709 489 KARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1891-2110 |
6.46e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1891 EVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEEsrstsekskqiLEAEASKLRELAEEAarlralseeakrQRQLAE 1970
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQ-----------QQEEAESSREQLQEL------------EEQLAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1971 EEATHQRAEAE-RILKEKLVAI-NEASRLKAEAEIALKEKEAENERLRRlaedeayqrrlleeqaaqhkqdiEEKIAQLK 2048
Cdd:pfam09787 105 ERSARREAEAElERLQEELRYLeEELRRSKATLQSRIKDREAEIEKLRN-----------------------QLTSKSQS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2049 KSSESELE-RQKSLVDDTVRQRRLVEEeirilkLNFEKAShgktdLELELTRIKQSAEEIQRS 2110
Cdd:pfam09787 162 SSSQSELEnRLHQLTETLIQKQTMLEA------LSTEKNS-----LVLQLERMEQQIKELQGE 213
|
|
| Selenoprotein_S |
pfam06936 |
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ... |
1705-1825 |
6.47e-03 |
|
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.
Pssm-ID: 462043 [Multi-domain] Cd Length: 192 Bit Score: 40.98 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1705 ELEKERQVQLaheaaqkSAEADLQSRRLSFAEKTAQLELSLQQEHIT---------ITHLQEEAERLKKLQLEAEQSREE 1775
Cdd:pfam06936 2 ELEEEPGVQL-------PARPALENEGLRFLQVTVGSLLSSYGWYLLfgcvlvyllIQKLRKRRTALRQRSSDHSAATVD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1776 ADKEVEkwRQKANEALRLRLQAEEvahkKALAQEEAEKQKEdAEREARKR 1825
Cdd:pfam06936 75 PDLVVK--RQEALEASRLRMQEEL----DAQAEKFKEKQKQ-LEEEKRRQ 117
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2388-2554 |
6.53e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2388 ELIKLKTRIEEENKMLITKDKDNMQKfLAEEAEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILKEKMQA 2467
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDK-KQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2468 VQEATRLKAE------AEVLQKQKDLAQEQAKklQEDKEQmqlrlaeEAEGFQKTLEAERQRqLEITANAERLKVQVTel 2541
Cdd:pfam05262 278 NQKREIEKAQieikknDEEALKAKDHKAFDLK--QESKAS-------EKEAEDKELEAQKKR-EPVAEDLQKTKPQVE-- 345
|
170
....*....|...
gi 2069539781 2542 slAQAKAEEEAKR 2554
Cdd:pfam05262 346 --AQPTSLNEDAI 356
|
|
| PRK15362 |
PRK15362 |
type III secretion system translocon protein; |
2399-2651 |
6.55e-03 |
|
type III secretion system translocon protein;
Pssm-ID: 237952 Cd Length: 473 Bit Score: 42.49 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2399 ENKMLITKDKDNMQKfLAEEAEKMkQVAEEAARLSVEAQEAARlRELAEQDLAQQrslAEKILKEKM-QAVQEATRLKAE 2477
Cdd:PRK15362 204 ETAMLCGADHDKCQA-IIDVASKI-QLGCEIVAMALDVFQIGR-AFMATRGIAKA---AEKVLDSGAgEELVERMVGGSE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2478 AEVlqkqKDLAQEQAKKLQED-KEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQVTE-LSLAQAKAEEEAKRF 2555
Cdd:PRK15362 278 EAI----EELAEEFGKQVSEQvSKQVANELAEESAEFSRNVEKNMTRSLGKAFTKEAIEAMVTEaVEEALKKAVQEGVKF 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2556 --KKQAEQISQKLHQTELATQEKMTLVQTLEIQRQQ----SDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTAQ 2629
Cdd:PRK15362 354 llKEFTKQVVKEVFKKVIKALIRACSFKGLQAIRCTtegaNQINTGMINTEKAKLQKKIEQLILQQRFLDFIMEQYEKQK 433
|
250 260
....*....|....*....|..
gi 2069539781 2630 KEQLRQETQMLQQTFRSEKDVL 2651
Cdd:PRK15362 434 KIEQKRLEELYKGSGAALRDAL 455
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2176-2292 |
6.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2176 LAEKESERQIQLAQEAAqKRIVAEekAHLAAVQQKEQELLQTRQQEQsildKLREEAERAKKAAEDaEFARIK---AEQE 2252
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA-KRILEE--AKKEAEAIKKEALLEAKEEIH----KLRNEFEKELRERRN-ELQKLEkrlLQKE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2069539781 2253 AALSRQLvEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAE 2292
Cdd:PRK12704 96 ENLDRKL-ELLEKREEELEKKEKELEQKQQELEKKEEELE 134
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
176-292 |
6.61e-03 |
|
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: 39.56 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 176 DRVQKKTFTKWVNKHLLKhwrAEAQRHVNDLYEDLRDGHNLISLLEVLSGDTlprerdvIRNLR-LPREKGRMrfhkLQN 254
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEK-------IEDINgCPKNRSQM----IEN 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 2069539781 255 VQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTI 292
Cdd:cd21285 74 IDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1614-1730 |
6.67e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.71 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1614 ERQRAGAEDELQALRDRAEEA-----ERQKRL--AQEEAERLRKQVKDESQKKREAEDElkhkvQAEQQAAREKQKALED 1686
Cdd:PRK07352 49 EERREAILQALKEAEERLRQAaqalaEAQQKLaqAQQEAERIRADAKARAEAIRAEIEK-----QAIEDMARLKQTAAAD 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2069539781 1687 LQKlrlqaeEAERRMkqAELEKErqvqlAHEAAQKSAEADLQSR 1730
Cdd:PRK07352 124 LSA------EQERVI--AQLRRE-----AAELAIAKAESQLPGR 154
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2433-2626 |
6.78e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2433 SVEAQEAARLRELAEQDlaQQRSLAEKILKEKMQAVQEATRLKAEAEV----LQKQKDLAQEQAKKLQEDKEQMQLRLAE 2508
Cdd:PRK11637 51 SIQQDIAAKEKSVRQQQ--QQRASLLAQLKKQEEAISQASRKLRETQNtlnqLNKQIDELNASIAKLEQQQAAQERLLAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2509 ---------EAEGFQKTLEAER-QRQLEITA-----NAERLK----VQVTELSLAQAKAEEEAKRFKKQA-----EQISQ 2564
Cdd:PRK11637 129 qldaafrqgEHTGLQLILSGEEsQRGERILAyfgylNQARQEtiaeLKQTREELAAQKAELEEKQSQQKTllyeqQAQQQ 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2069539781 2565 KLHQTELATQEKMT-LVQTLEiQRQQSDSDAE----KLRKAIADLEQE----KEKLKREAELLQQKSEEMQ 2626
Cdd:PRK11637 209 KLEQARNERKKTLTgLESSLQ-KDQQQLSELRanesRLRDSIARAEREakarAEREAREAARVRDKQKQAK 278
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2549-2638 |
6.82e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2549 EEEAKRFKKQAEQISQKLHQTELATQEKmtlvQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKSEEMQTA 2628
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREK----AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE 213
|
90
....*....|
gi 2069539781 2629 QKEQLRQETQ 2638
Cdd:PRK11448 214 RKQKRKEITD 223
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2107-2237 |
6.88e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2107 IQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAAR------QCKAALEEVER-LKAKAEEARRQK-ELAE 2178
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKlkeeleEKKEKLQEEEDkLLEEAEKEAQQAiKEAK 583
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2179 KESERQIQLAQEAAQKRIVAeekahlaavqQKEQELLQTRQQeqsiLDKLREEAERAKK 2237
Cdd:PRK00409 584 KEADEIIKELRQLQKGGYAS----------VKAHELIEARKR----LNKANEKKEKKKK 628
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2553-2692 |
7.13e-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: 41.79 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2553 KRFKKQAEQISQKLHQT-------ELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQK---S 2622
Cdd:cd16269 145 QLYLEDREKLVEKYRQVprkgvkaEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQqreL 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2623 EEMQTAQKEQLRQETQMLQQTFRSEKDVLLQkerfvEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQMEQ 2692
Cdd:cd16269 225 EQKLEDQERSYEEHLRQLKEKMEEERENLLK-----EQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1622-2068 |
7.51e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1622 DELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKreaedELKHKVQAeqqaAREKQKALEDLQKLRLqaeeaerrM 1701
Cdd:TIGR01612 1365 DEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLE-----ECKSKIES----TLDDKDIDECIKKIKE--------L 1427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1702 KQAELEKERQVQLAHEAAQKSAE-ADLQSRRLSFAEKTAQLELSLQQEHIT------ITHLQEEAERLKKLQLEAEQSRE 1774
Cdd:TIGR01612 1428 KNHILSEESNIDTYFKNADENNEnVLLLFKNIEMADNKSQHILKIKKDNATndhdfnINELKEHIDKSKGCKDEADKNAK 1507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1775 EADKEVEKWRQKANEALRLRLQAEEVAHKKALAQeeaekQKEDAEREARKRSKAEESALRQKELAEQELEKQRKlaegta 1854
Cdd:TIGR01612 1508 AIEKNKELFEQYKKDVTELLNKYSALAIKNKFAK-----TKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKK------ 1576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1855 qqkflaeqELIRLKAEVENgeqqrllleeelfrlKNEVNEAVqkrKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKS 1934
Cdd:TIGR01612 1577 --------EKFRIEDDAAK---------------NDKSNKAA---IDIQLSLENFENKFLKISDIKKKINDCLKETESIE 1630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1935 KQI----LEAEASKLRELAEEAARLRALSEEAKRQRQLAEEEATHqraeaerilkeklvaineasrlkaeaeiaLKEKEA 2010
Cdd:TIGR01612 1631 KKIssfsIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKE-----------------------------LDELDS 1681
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 2011 ENERlrrlaedeayqrrlLEEQAAQHKQDIE----EKIAQLKKSSESELERQKSLVDDTVRQ 2068
Cdd:TIGR01612 1682 EIEK--------------IEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1523-1722 |
7.62e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.14 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1523 QLAEAH-----ARAKAQAEKEAlelqrrmEEEVSRrqlvavdAEQQKQTIQQELSQMK-----LSSDAQIQAKLKLIeev 1592
Cdd:COG3524 161 AESEELvnqlsERAREDAVRFA-------EEEVER-------AEERLRDAREALLAFRnrngiLDPEATAEALLQLI--- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1593 efsrrkveeeirmvrLQLEAterQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDelkhkvqa 1672
Cdd:COG3524 224 ---------------ATLEG---QLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASG-------- 277
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2069539781 1673 EQQAARekqkALEDLQKLRLQAEEAERRMKQA--ELEKERQvqlahEAAQKS 1722
Cdd:COG3524 278 GDSLAS----LLAEYERLELEREFAEKAYTSAlaALEQARI-----EAARQQ 320
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
2382-2731 |
7.68e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2382 VKVQMEELIKLKTRIEEENkmLITKDKDNMQKFLAEEAEKMKQVAeeAARLSVEAQEAARLRELAEQDLAqqrslaekIL 2461
Cdd:PTZ00108 944 EEEGIEKVFKLKSTISTTN--MVLFDENGKIKKYSDALDILKEFY--LVRLDLYKKRKEYLLGKLERELA--------RL 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2462 KEKMQAVQEATrlKAEAEVLQKQKDLAQEQAKKL------QEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAER-- 2533
Cdd:PTZ00108 1012 SNKVRFIKHVI--NGELVITNAKKKDLVKELKKLgyvrfkDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSyd 1089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2534 --LKVQVTELSLaqakaeEEAKRFKKQAEQISQKLHQTELATQEKMTLvqtleiqrqqsdSDAEKLRKAIADLEQEKEKL 2611
Cdd:PTZ00108 1090 ylLSMPIWSLTK------EKVEKLNAELEKKEKELEKLKNTTPKDMWL------------EDLDKFEEALEEQEEVEEKE 1151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2612 KREAELLQQKSEEMQ--TAQKEQLRQETQMLQQTFRSEKDVLLQKERFVEEEKAKLEKLFQEEVNKAQGLKAEQERQQKQ 2689
Cdd:PTZ00108 1152 IAKEQRLKSKTKGKAskLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQ 1231
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2069539781 2690 MEQEKKQLTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQK 2731
Cdd:PTZ00108 1232 KTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKN 1273
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1513-1841 |
7.71e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.44 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1513 EVEAQLEKQRQLAEAHARAKAQAEKEALELQRRMEEEVSRRQLVAVDAEQQKQTIQQELSqmklssdaqiqAKLKLIEEV 1592
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAES-----------ATAVAKEAK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1593 EFSRRKVEEEIRMVRLQLEATERQRAGAEDE-LQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQ 1671
Cdd:pfam09731 153 DDAIQAVKAHTDSLKEASDTAEISREKATDSaLQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1672 AEQQAAREKQKALEDLQKLrlqaEEAERRMKQAELEK----------------------------------ERQVQLAHE 1717
Cdd:pfam09731 233 EKVEKAQSLAKLVDQYKEL----VASERIVFQQELVSifpdiipvlkednllsnddlnsliahahreidqlSKKLAELKK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1718 AAQKSAEADLQSRRLSFaeKTAQLELSLQQEHititHLQEEAERLK-KLQLEAEQSREEADKEVEKWRQKANEALRLRLQ 1796
Cdd:pfam09731 309 REEKHIERALEKQKEEL--DKLAEELSARLEE----VRAADEAQLRlEFEREREEIRESYEEKLRTELERQAEAHEEHLK 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2069539781 1797 aEEVAHKKALAQEEAEKQKEDA---EREARKrSKAEESALRQKELAEQ 1841
Cdd:pfam09731 383 -DVLVEQEIELQREFLQDIKEKveeERAGRL-LKLNELLANLKGLEKA 428
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2463-2752 |
7.82e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2463 EKMQAVQEATRLKAEAEVLQKQKDLA----QEQAKKLQEDKEQMQLRLAEEAEGFQKTLEAERQRQLEITANAERLKVQV 2538
Cdd:PRK10246 201 EKLQAQASGVALLTPEQVQSLTASLQvltdEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQPQL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2539 TELSLAQAkAEEEAKRFKKQAEQiSQKLHQTELATQEKMTLVQTLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELL 2618
Cdd:PRK10246 281 AALSLAQP-ARQLRPHWERIQEQ-SAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRF 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2619 QQKSEEM---------QTAQKEQLRQETQMLQQTFRsekdvllqkerfveeekaKLEKLFQEEVNKAQGLKAEQERQQKQ 2689
Cdd:PRK10246 359 RQWNNELagwraqfsqQTSDREQLRQWQQQLTHAEQ------------------KLNALPAITLTLTADEVAAALAQHAE 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2690 MEQEKKQLTTVLEEARKKQaeaeENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQE 2752
Cdd:PRK10246 421 QRPLRQRLVALHGQIVPQQ----KRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD 479
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
2658-2755 |
7.87e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 41.07 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2658 VEEEKAKLEKLfqEEVNKAQGLK------------AEQERQQKQMEQEKKQlttvlEEARKKQAEAEENVRQKQEELQRL 2725
Cdd:pfam06391 63 VEETEKKIEQY--EKENKDLILKnkmklsqeeeelEELLELEKREKEERRK-----EEKQEEEEEKEKKEKAKQELIDEL 135
|
90 100 110
....*....|....*....|....*....|
gi 2069539781 2726 EKQRQKQEKLLAEENQKLREKLEQLQEEQK 2755
Cdd:pfam06391 136 MTSNKDAEEIIAQHKKTAKKRKSERRRKLE 165
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1593-1850 |
7.88e-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: 42.68 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1593 EFSRRKVEEEIRM------VRLQLEAT-ERQRAGAEDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDE 1665
Cdd:TIGR00927 615 QLSRRPVAKVMALgdlskgDVAEAEHTgERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1666 LKHKVQAEQQAAREKQKALEDLQKLRLQAE--------EAERRMKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAE- 1736
Cdd:TIGR00927 695 GEGEIEAKEADHKGETEAEEVEHEGETEAEgtedegeiETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEg 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1737 KTAQLELSLQQEHiTITHLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKE 1816
Cdd:TIGR00927 775 KEDEDEGEIQAGE-DGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVD 853
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2069539781 1817 --------DAEREARKRSKAEESALRQKELAEQELEKQRKLA 1850
Cdd:TIGR00927 854 ggggsdggDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLS 895
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2466-2573 |
7.94e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2466 QAVQEATRLKAEAEVLQKQKDLAQEQAKKLQEDKEQmQLRLAEEAEGFQKTLEAErqrqleitanAERLKVQvtelslAQ 2545
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVA-LEGLAAELEEKQQELEAQ----------LEQLQEK------AA 208
|
90 100
....*....|....*....|....*...
gi 2069539781 2546 AKAEEEAKRFKKQAEQISQKLHQTELAT 2573
Cdd:PRK11448 209 ETSQERKQKRKEITDQAAKRLELSEEET 236
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1753-1857 |
8.21e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1753 THLQEEAERLKKLQLEAEQSREEADKEVEKWRQKANEALRLRlqaEEVAHKKALAQEEAEKQKEDAEREARKRSKA--EE 1830
Cdd:PRK00409 509 KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQEEEDKLLEEAEKEAQQAIKEakKE 585
|
90 100
....*....|....*....|....*..
gi 2069539781 1831 SALRQKELAEQELEKQRKLAEGTAQQK 1857
Cdd:PRK00409 586 ADEIIKELRQLQKGGYASVKAHELIEA 612
|
|
| PRK09173 |
PRK09173 |
F0F1 ATP synthase subunit B; Validated |
2427-2567 |
8.35e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 169691 [Multi-domain] Cd Length: 159 Bit Score: 40.11 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2427 EEAARLSVEAQEAARLRELAEQDLAQ-QRSLAEkilkekmqAVQEATRLKAEAEvlqKQKDLAQEQAKKLQEDKEQMQLR 2505
Cdd:PRK09173 33 ARADRIKNELAEARRLREEAQQLLAEyQRKRKE--------AEKEAADIVAAAE---REAEALTAEAKRKTEEYVARRNK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2069539781 2506 LAEeaegfQKTLEAERQRQLEITANAERLKVQVTELSLAQ-AKAEEEAKRFKKQAEQISQKLH 2567
Cdd:PRK09173 102 LAE-----QKIAQAETDAINAVRSSAVDLAIAAAEKLLAEkVDAKAASELFKDALAQVKTRLN 159
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2086-2193 |
8.56e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2086 ASHGKTDLELEltriKQSAEEIQRSKEQAEreAEELRQLALEEENHRREAEAKVKKISAAEQEA-ARQCKAALE-EVERL 2163
Cdd:PTZ00491 668 ARHQAELLEQE----ARGRLERQKMHDKAK--AEEQRTKLLELQAESAAVESSGQSRAEALAEAeARLIEAEAEvEQAEL 741
|
90 100 110
....*....|....*....|....*....|
gi 2069539781 2164 KAKAEEARRQKELAEKESERQIQLAQEAAQ 2193
Cdd:PTZ00491 742 RAKALRIEAEAELEKLRKRQELELEYEQAQ 771
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1175-1353 |
8.70e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.89 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1175 QQQIHQELEGIKKNLGKVSAKTEQVLAqpEQASSAPTLHSELDITLQKMDQVYSLSSIYLEKLKTIHLVIRSTQGAEDLI 1254
Cdd:cd00176 42 HEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1255 RKYEEQLKDVQA--VPSDLKALEATKAELKRLRGQVEGHQPLFNTLEmdlakaSEVNERMVRGHSERDidlDRYRERVQQ 1332
Cdd:cd00176 120 QWLEEKEAALASedLGKDLESVEELLKKHKELEEELEAHEPRLKSLN------ELAEELLEEGHPDAD---EEIEEKLEE 190
|
170 180
....*....|....*....|.
gi 2069539781 1333 LLERWQAILAQIDLRQRELDQ 1353
Cdd:cd00176 191 LNERWEELLELAEERQKKLEE 211
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2310-2460 |
8.83e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2310 QLADAEMAKHKKFAEQTLRQKAQVEQELTKVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQME-- 2387
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2388 ----ELIKLKTRIEE-ENKML-ITKDKDNMQKFLAEEAEKMKQVAEEAARLSVEAQEA-ARLRELAEQDLAQQRSLAEKI 2460
Cdd:COG1579 93 alqkEIESLKRRISDlEDEILeLMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEAEREELAAKI 172
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4163-4194 |
8.86e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 8.86e-03
10 20 30
....*....|....*....|....*....|..
gi 2069539781 4163 KLLSAERAVTGYKDPYSGKLISLFQAMKKGLI 4194
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2165-2242 |
8.91e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 40.14 E-value: 8.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2069539781 2165 AKAEEARRQKELAEKESERQIQLAQEAAQKRIvaeEKAHLAAVQQKEQELLQTRQQEQSILDKLREEAERAKKAAEDA 2242
Cdd:PRK05759 45 AAAERAKKELELAQAKYEAQLAEARAEAAEII---EQAKKRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREE 119
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2099-2462 |
9.10e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.95 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2099 RIKQSAEEIQRSKEQAEREAEELRQLALEEENHRREAEAKVKKISAAEQEAARQCKAALEEverlkaKAEEARRQKELAE 2178
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK------KLAEAEKAAAEAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2179 KESERQIQLAQEAAQKRIVAEEKAHLAAVQQKEQELlqtRQQEQSILDKLREEAERAKKAAEDAEFARIKAEQEAALSRQ 2258
Cdd:COG3064 91 KKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAK---RKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2259 LVEEAERMKQRAEEEAQTKAKAQEDAEKLRKEAELEAARRAQAEQAALKQKQLADAEMAKHKKFAEQTLRQKAQVEQELT 2338
Cdd:COG3064 168 AAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2339 KVKLQLEETDHQKSILEEEQQRLKDEVTEAMKQKVQVEEELFKVKVQMEELIKLKTRIEEENKMLITKDKDNMQKFLAEE 2418
Cdd:COG3064 248 AEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGAL 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2069539781 2419 AEKMKQVAEEAARLSVEAQEAARLRELAEQDLAQQRSLAEKILK 2462
Cdd:COG3064 328 VVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2546-2775 |
9.28e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.24 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2546 AKAEEEAKRFKKQAEQISQKLHQTELATQEKMTLVQ---TLEIQRQQSDSDAEKLRKAIADLEQEKEKLKREAELLQQKS 2622
Cdd:pfam06008 19 YNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQeteELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2623 EEMqTAQKEQLRQETQMLQQTFRSEKdvLLQKERFVEEEKAKleKLFQEEVNKAQGLKAEQ---ERQQKQMEQEKKQLTT 2699
Cdd:pfam06008 99 KEI-NEKVATLGENDFALPSSDLSRM--LAEAQRMLGEIRSR--DFGTQLQNAEAELKAAQdllSRIQTWFQSPQEENKA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 2700 VLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLRE---KLEQLQEEQKTA---LAQTREIMIQTDDLPQ 2773
Cdd:pfam06008 174 LANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREfqrKKEEVSEQKNQLeetLKTARDSLDAANLLLQ 253
|
..
gi 2069539781 2774 EV 2775
Cdd:pfam06008 254 EI 255
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1610-1721 |
9.46e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 40.84 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1610 LEATERQRagaEDELQALRD----RAEEAERQKRLAQE-------EAERLRKQVKDESQKKREAEDELKHKVQAEQQAAR 1678
Cdd:pfam13904 61 LAAKQRQR---QKELQAQKEerekEEQEAELRKRLAKEkyqewlqRKARQQTKKREESHKQKAAESASKSLAKPERKVSQ 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2069539781 1679 EKQKA------LEDLQKLRLQAEEAERRMKQAELEKERQVQLAHEAAQK 1721
Cdd:pfam13904 138 EEAKEvlqeweRKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQK 186
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
2687-2764 |
9.50e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 40.64 E-value: 9.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2069539781 2687 QKQMEQEKKQ-LTTVLEEARKKQAEAEENVRQKQEELQRLEKQRQKQEKLLAEENQKLREKLEQLQEEQKTALAQTREI 2764
Cdd:pfam12072 44 KKEAETKKKEaLLEAKEEIHKLRAEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQL 122
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1541-2024 |
9.50e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.95 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1541 ELQRRMEEEVSRRQLVAvdAEQQKQTIQQELSQMKLSSDAQIQAKLKLIEEVEFSRRKVEEEIRMVRLQLEATERQRAGA 1620
Cdd:COG3064 4 ALEEKAAEAAAQERLEQ--AEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1621 EDELQALRDRAEEAERQKRLAQEEAERLRKQVKDESQKKREAEDELKHKVQAEQQAAREKQKALEDLQKLRLQAEEAERR 1700
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1701 MKQAELEKERQVQLAHEAAQKSAEADLQSRRLSFAEKTAQLELSLQQEHITITHLQEEAERLKKLQLEAEQSREEADKEV 1780
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1781 EKWRQKANEALRLRLQAEEVAHKKALAQEEAEKQKEDAEREARKRSKAEESALRQkELAEQELEKQRKLAEGTAQQKFLA 1860
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLV-LDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1861 EQELIRLKAEVENGEQQRLLLEEELFRLKNEVNEAVQKRKELEEELAKLRAEMELLLQSKAKTEEESRSTSEKSKQILEA 1940
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2069539781 1941 EASKLRELAEEAARLRALSEEAKRQRQLAEEEATHQRAEAERILKEKLVAINEASRLKAEAEIALKEKEAENERLRRLAE 2020
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
....
gi 2069539781 2021 DEAY 2024
Cdd:COG3064 481 LLLG 484
|
|
| |
