|
Name |
Accession |
Description |
Interval |
E-value |
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
586-847 |
1.75e-152 |
|
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350760 [Multi-domain] Cd Length: 229 Bit Score: 462.74 E-value: 1.75e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNINPKRVMFfstwiisfdpwavrqicickracnvvrfqtlsdMDAGFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18002 81 YWGNPKDRKVLRKFWDRKNLYT---------------------------------RDAPFHVVITSYQLVVQDEKYFQRV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGIENHAEHG 825
Cdd:cd18002 128 KWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENK 207
|
250 260
....*....|....*....|..
gi 334186052 826 GTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18002 208 TGLNEHQLKRLHMILKPFMLRR 229
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
579-925 |
2.49e-88 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 303.30 E-value: 2.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 579 PELFKGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIwGPFLVVAPASVLNNWADEISRFC 658
Cdd:COG0553 235 PAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 659 PDLKTLPYWGGLQERTIlrkninpkrvmffstwiisFDPWavrqicickracnvvrfqtlsdmdAGFHILITSYQLLVTD 738
Cdd:COG0553 314 PGLRVLVLDGTRERAKG-------------------ANPF------------------------EDADLVITSYGLLRRD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 739 EKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGI 818
Cdd:COG0553 351 IELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 819 ENHaehggtlNEHQLNRLHAILKPFMLRRVKKDVVSELTTKTEVTVHCKLSSRQQAFYQAIknkisLAELFDSNRGQFTD 898
Cdd:COG0553 431 EKG-------DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV-----LEYLRRELEGAEGI 498
|
330 340
....*....|....*....|....*..
gi 334186052 899 KKVLNLMNIVIQLRKVCNHPELFERNE 925
Cdd:COG0553 499 RRRGLILAALTRLRQICSHPALLLEEG 525
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
589-921 |
1.06e-81 |
|
SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.
Pssm-ID: 425504 [Multi-domain] Cd Length: 289 Bit Score: 270.32 E-value: 1.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 589 YQMKGLQWLVNCYEQ-GLNGILADEMGLGKTIQAMAFLAHLAEEKNIWG-PFLVVAPASVLNNWADEISRFC--PDLKTL 664
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 665 PYWGGLQERTILRKNINpkrvmffstwiisfdpwavrqicickracnvvrfqtlsdMDAGFHILITSYQLLVTDEKYFRR 744
Cdd:pfam00176 81 VLHGNKRPQERWKNDPN---------------------------------------FLADFDVVITTYETLRKHKELLKK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 745 VKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGIENHAEH 824
Cdd:pfam00176 122 VHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 825 GGtlnehqLNRLHAILKPFMLRRVKKDVVSELTTKTEVTVHCKLSSRQQAFYQAIKNKISLAELFDSNRGqftDKKVLNL 904
Cdd:pfam00176 202 KG------VSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGG---REIKASL 272
|
330
....*....|....*..
gi 334186052 905 MNIVIQLRKVCNHPELF 921
Cdd:pfam00176 273 LNILMRLRKICNHPGLI 289
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
419-925 |
5.53e-81 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 290.16 E-value: 5.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 419 RYDKQMAEERKKQEKEAAEAFKREQEQR----ESKRQQQRLNFLIKQTELYSHFMQnktdsnpsealpigdenpidevlp 494
Cdd:PLN03142 59 KREKARLKELKKQKKQEIQKILEQQNAAidadMNNKGKGRLKYLLQQTEIFAHFAK------------------------ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 495 etsaaepseveDPEEAELKEKVLRAAQdavsKQKQITDAFDTEYMKlrqtSEMEGplndisVSGSSNIDLhnpstmpvts 574
Cdd:PLN03142 115 -----------GDQSASAKKAKGRGRH----ASKLTEEEEDEEYLK----EEEDG------LGGSGGTRL---------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 575 TVQtPELFKGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEI 654
Cdd:PLN03142 160 LVQ-PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 655 SRFCPDLKTLPYWGGLQERTILRKNInpkrvmffstwiisfdpwavrqicickracnvvrfqtlsdMDAG-FHILITSYQ 733
Cdd:PLN03142 239 RRFCPVLRAVKFHGNPEERAHQREEL----------------------------------------LVAGkFDVCVTSFE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 734 LLVTDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEW 813
Cdd:PLN03142 279 MAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEW 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 814 FSKGIENHaehggtlNEHQLNRLHAILKPFMLRRVKKDVVSELTTKTEVTVHCKLSSRQQAFYQAIKNKislaELFDSNR 893
Cdd:PLN03142 359 FQISGEND-------QQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK----DLDVVNA 427
|
490 500 510
....*....|....*....|....*....|..
gi 334186052 894 GqfTDKKvlNLMNIVIQLRKVCNHPELFERNE 925
Cdd:PLN03142 428 G--GERK--RLLNIAMQLRKCCNHPYLFQGAE 455
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1231-1363 |
5.10e-64 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 213.49 E-value: 5.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1231 PAKLLTD-SGKLQTLDILLKRLRAGNHRVLLFAQMTKMLNILEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFQHRSDIFV 1309
Cdd:cd18793 2 PPKIEEVvSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 334186052 1310 FLLSTRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAHRLGQTKDVTVYRLI 1363
Cdd:cd18793 82 FLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DBINO |
pfam13892 |
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ... |
345-476 |
4.58e-59 |
|
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator SNF2L1 proteins and chromatin re-modelling proteins.
Pssm-ID: 464024 [Multi-domain] Cd Length: 134 Bit Score: 199.30 E-value: 4.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 345 DKIRKAWINIVRRDIAKHHRIFTTFHRKLSIDAKRFADGCQREVRMKVGRSYKIPRTAPIRTRKISRDMLLFWKRYDKQM 424
Cdd:pfam13892 3 EKRRKIWKNIAKKDIPKVYRAKQQNHQARLANCKKVAQLCAREARRKASRTQKTMKDPQLRAKRLMREMLLFWKKNEKEE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 334186052 425 AEERKKQEKEAAEAFKREQEQRESKRQQQRLNFLIKQTELYSHFMQNKTDSN 476
Cdd:pfam13892 83 RELRKRAEKEALEQAKKEEELREAKRQQRKLNFLITQTELYSHFMGKKLKTD 134
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1234-1492 |
1.72e-53 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 205.03 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1234 LLTDSGKLQTLDILLKRLRAGNHRVLLFAQMTKMLNILEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFQHR-SDIFVFLL 1312
Cdd:PLN03142 466 LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1313 STRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAHRLGQTKDVTVYRLICKETVEEKILHRASQKNTVQQLVMTGGH- 1391
Cdd:PLN03142 546 STRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRl 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1392 -----VQGDDFL-----GAADVVS---LLMDDAEAAQLEQKFRELPLQVKDRQKKKT-KRIRIDAEGDATLEELEDVDRQ 1457
Cdd:PLN03142 626 aeqktVNKDELLqmvryGAEMVFSskdSTITDEDIDRIIAKGEEATAELDAKMKKFTeDAIKFKMDDTAELYDFDDEDDK 705
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 334186052 1458 DNGQEPLEE------PEKPKSSNKKR-----------RAASNPKARAPQKAK 1492
Cdd:PLN03142 706 DENKLDFKKivsdnwIDPPKRERKRNyseseyfkqamRQGAPAKPKEPRIPR 757
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
1208-1379 |
1.60e-52 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 197.76 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1208 VVQPALQLtHRIFGSCPPMQSFDPAKLLTDSGKLQTLDILLKRLRAGNHRVLLFAQMTKMLNILEDYMNYRKYKYLRLDG 1287
Cdd:COG0553 503 LILAALTR-LRQICSHPALLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHG 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1288 SSTIMDRRDMVRDFQHRSDIFVFLLSTRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAHRLGQTKDVTVYRLICKET 1367
Cdd:COG0553 582 GTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGT 661
|
170
....*....|..
gi 334186052 1368 VEEKILHRASQK 1379
Cdd:COG0553 662 IEEKILELLEEK 673
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
578-808 |
6.50e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 6.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 578 TPELFKGTLKEYQMKGLQWLVNCYEqglNGILADEMGLGKTIQAMAFLAHLAEEKNiWGPFLVVAPASVL-NNWADEISR 656
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELaEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 657 FCPD--LKTLPYWGGLQERTILRKNINPKrvmffstwiisfdpwavrqicickracnvvrfqtlsdmdagFHILITSYQL 734
Cdd:smart00487 77 LGPSlgLKVVGLYGGDSKREQLRKLESGK-----------------------------------------TDILVTTPGR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 735 LVTD--EKYFRRVKWQYMVLDEAQAIKSSSSIR-WKTLLSF--NCRNRLLLTGTP---IQNNMAELWALLHFIMPMLFDN 806
Cdd:smart00487 116 LLDLleNDKLSLSNVDLVILDEAHRLLDGGFGDqLEKLLKLlpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPL 195
|
..
gi 334186052 807 HD 808
Cdd:smart00487 196 EP 197
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1239-1352 |
2.10e-25 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 101.90 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1239 GKLQTLDILLKRLRagNHRVLLFAQMTKMLNIlEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFqhRSDIFVFLLSTRAGG 1318
Cdd:pfam00271 1 EKLEALLELLKKER--GGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDF--RKGKIDVLVATDVAE 75
|
90 100 110
....*....|....*....|....*....|....
gi 334186052 1319 LGINLTAADTVIFYESDWNPTLDLQAMDRAHRLG 1352
Cdd:pfam00271 76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1270-1352 |
7.36e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.12 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1270 ILEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFqhRSDIFVFLLSTRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAH 1349
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKF--NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79
|
...
gi 334186052 1350 RLG 1352
Cdd:smart00490 80 RAG 82
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1411-1513 |
4.03e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.50 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1411 AEAAQLEQKFRELPLQVKDRQKKKTKRiRIDAEGDATLEELEDVDRQDNGQEPLEEPEKPKS-SNKKRRAASNPKARAPQ 1489
Cdd:PRK07735 103 AKAAALAKQKREGTEEVTEEEKAAAKA-KAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEkAKAKAAAAAKAKAAALA 181
|
90 100
....*....|....*....|....
gi 334186052 1490 KAKEEANGEDTPQRTKRVKRQTKS 1513
Cdd:PRK07735 182 KQKAAEAGEGTEEVTEEEKAKAKA 205
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
385-506 |
7.18e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 40.60 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 385 QREVRMKVGRSYKiprtapiRTRKISRDMLLF--WK--RYDKQMAEERK--KQEKEAAEAFKRE--QEQRESKRQQQRLN 456
Cdd:PRK00247 293 QYREKQKEKKAFL-------WTLRRNRLRMIItpWRapELHAENAEIKKtrTAEKNEAKARKKEiaQKRRAAEREINREA 365
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 334186052 457 FLIKQTELYSHFMQNKTDSNPSEALPIGDENPIDEVLPETSAAEPSEVED 506
Cdd:PRK00247 366 RQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQVEA 415
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
586-847 |
1.75e-152 |
|
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350760 [Multi-domain] Cd Length: 229 Bit Score: 462.74 E-value: 1.75e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNINPKRVMFfstwiisfdpwavrqicickracnvvrfqtlsdMDAGFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18002 81 YWGNPKDRKVLRKFWDRKNLYT---------------------------------RDAPFHVVITSYQLVVQDEKYFQRV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGIENHAEHG 825
Cdd:cd18002 128 KWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENK 207
|
250 260
....*....|....*....|..
gi 334186052 826 GTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18002 208 TGLNEHQLKRLHMILKPFMLRR 229
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
586-847 |
2.93e-96 |
|
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350761 [Multi-domain] Cd Length: 223 Bit Score: 308.90 E-value: 2.93e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNinpkrvmffstwiisfdpWavrqicickracnvvrfqtlSDMDAgFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18003 81 YYGSAKERKLKRQG------------------W--------------------MKPNS-FHVCITSYQLVVQDHQVFKRK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGIENHAEHG 825
Cdd:cd18003 122 KWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTAMSEGS 201
|
250 260
....*....|....*....|..
gi 334186052 826 GTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18003 202 QEENEELVRRLHKVLRPFLLRR 223
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
579-925 |
2.49e-88 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 303.30 E-value: 2.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 579 PELFKGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIwGPFLVVAPASVLNNWADEISRFC 658
Cdd:COG0553 235 PAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 659 PDLKTLPYWGGLQERTIlrkninpkrvmffstwiisFDPWavrqicickracnvvrfqtlsdmdAGFHILITSYQLLVTD 738
Cdd:COG0553 314 PGLRVLVLDGTRERAKG-------------------ANPF------------------------EDADLVITSYGLLRRD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 739 EKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGI 818
Cdd:COG0553 351 IELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 819 ENHaehggtlNEHQLNRLHAILKPFMLRRVKKDVVSELTTKTEVTVHCKLSSRQQAFYQAIknkisLAELFDSNRGQFTD 898
Cdd:COG0553 431 EKG-------DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV-----LEYLRRELEGAEGI 498
|
330 340
....*....|....*....|....*..
gi 334186052 899 KKVLNLMNIVIQLRKVCNHPELFERNE 925
Cdd:COG0553 499 RRRGLILAALTRLRQICSHPALLLEEG 525
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
583-849 |
4.80e-82 |
|
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350767 [Multi-domain] Cd Length: 236 Bit Score: 269.26 E-value: 4.80e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 583 KGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKnIWGPFLVVAPASVLNNWADEISRFCPDLK 662
Cdd:cd18009 1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERG-VWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 663 TLPYWGGLQERTILRKNINPkrvmffstwiisfdpwavrqicickracnvvrFQTLSDMdagFHILITSYQLLVTDEKYF 742
Cdd:cd18009 80 VLLYHGTKEERERLRKKIMK--------------------------------REGTLQD---FPVVVTSYEIAMRDRKAL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 743 RRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWF-----SKG 817
Cdd:cd18009 125 QHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFdfsslSDN 204
|
250 260 270
....*....|....*....|....*....|..
gi 334186052 818 IENHAEHGGTLNEHQLNRLHAILKPFMLRRVK 849
Cdd:cd18009 205 AADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
589-921 |
1.06e-81 |
|
SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.
Pssm-ID: 425504 [Multi-domain] Cd Length: 289 Bit Score: 270.32 E-value: 1.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 589 YQMKGLQWLVNCYEQ-GLNGILADEMGLGKTIQAMAFLAHLAEEKNIWG-PFLVVAPASVLNNWADEISRFC--PDLKTL 664
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 665 PYWGGLQERTILRKNINpkrvmffstwiisfdpwavrqicickracnvvrfqtlsdMDAGFHILITSYQLLVTDEKYFRR 744
Cdd:pfam00176 81 VLHGNKRPQERWKNDPN---------------------------------------FLADFDVVITTYETLRKHKELLKK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 745 VKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGIENHAEH 824
Cdd:pfam00176 122 VHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 825 GGtlnehqLNRLHAILKPFMLRRVKKDVVSELTTKTEVTVHCKLSSRQQAFYQAIKNKISLAELFDSNRGqftDKKVLNL 904
Cdd:pfam00176 202 KG------VSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEGG---REIKASL 272
|
330
....*....|....*..
gi 334186052 905 MNIVIQLRKVCNHPELF 921
Cdd:pfam00176 273 LNILMRLRKICNHPGLI 289
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
419-925 |
5.53e-81 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 290.16 E-value: 5.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 419 RYDKQMAEERKKQEKEAAEAFKREQEQR----ESKRQQQRLNFLIKQTELYSHFMQnktdsnpsealpigdenpidevlp 494
Cdd:PLN03142 59 KREKARLKELKKQKKQEIQKILEQQNAAidadMNNKGKGRLKYLLQQTEIFAHFAK------------------------ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 495 etsaaepseveDPEEAELKEKVLRAAQdavsKQKQITDAFDTEYMKlrqtSEMEGplndisVSGSSNIDLhnpstmpvts 574
Cdd:PLN03142 115 -----------GDQSASAKKAKGRGRH----ASKLTEEEEDEEYLK----EEEDG------LGGSGGTRL---------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 575 TVQtPELFKGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEI 654
Cdd:PLN03142 160 LVQ-PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 655 SRFCPDLKTLPYWGGLQERTILRKNInpkrvmffstwiisfdpwavrqicickracnvvrfqtlsdMDAG-FHILITSYQ 733
Cdd:PLN03142 239 RRFCPVLRAVKFHGNPEERAHQREEL----------------------------------------LVAGkFDVCVTSFE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 734 LLVTDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEW 813
Cdd:PLN03142 279 MAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEW 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 814 FSKGIENHaehggtlNEHQLNRLHAILKPFMLRRVKKDVVSELTTKTEVTVHCKLSSRQQAFYQAIKNKislaELFDSNR 893
Cdd:PLN03142 359 FQISGEND-------QQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK----DLDVVNA 427
|
490 500 510
....*....|....*....|....*....|..
gi 334186052 894 GqfTDKKvlNLMNIVIQLRKVCNHPELFERNE 925
Cdd:PLN03142 428 G--GERK--RLLNIAMQLRKCCNHPYLFQGAE 455
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
586-801 |
6.30e-77 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 252.49 E-value: 6.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNINPKRvmffstwiisfdpwavrqicickracnvvrfqtlsdmdagFHILITSYQLLVTDEKYFRRV 745
Cdd:cd17919 81 YHGSQRERAQIRAKEKLDK----------------------------------------FDVVLTTYETLRRDKASLRKF 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMP 801
Cdd:cd17919 121 RWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDP 176
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
583-849 |
2.36e-76 |
|
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350755 [Multi-domain] Cd Length: 222 Bit Score: 252.24 E-value: 2.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 583 KGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLK 662
Cdd:cd17997 1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 663 TLPYWGGLQER-TILRKNINPKRvmffstwiisfdpwavrqicickracnvvrfqtlsdmdagFHILITSYQLLVTDEKY 741
Cdd:cd17997 81 VVVLIGDKEERaDIIRDVLLPGK----------------------------------------FDVCITSYEMVIKEKTV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 742 FRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSkgienh 821
Cdd:cd17997 121 LKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN------ 194
|
250 260
....*....|....*....|....*...
gi 334186052 822 AEHGGTLNEHQLNRLHAILKPFMLRRVK 849
Cdd:cd17997 195 VNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
584-849 |
2.85e-74 |
|
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350754 [Multi-domain] Cd Length: 233 Bit Score: 246.90 E-value: 2.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 584 GTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKT 663
Cdd:cd17996 2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 664 LPYWGGLQERTILRKNInpkrvmffstwiisfdpwavrqicickRACNvvrfqtlsdmdagFHILITSYQLLVTDEKYFR 743
Cdd:cd17996 82 IVYKGTPDVRKKLQSQI---------------------------RAGK-------------FNVLLTTYEYIIKDKPLLS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 744 RVKWQYMVLDEAQAIKSSSSIRWKTLLSFNC-RNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGIENHA 822
Cdd:cd17996 122 KIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHaRYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTG 201
|
250 260 270
....*....|....*....|....*....|..
gi 334186052 823 E-HGGTLNEHQ----LNRLHAILKPFMLRRVK 849
Cdd:cd17996 202 EqVKIELNEEEtlliIRRLHKVLRPFLLRRLK 233
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
582-849 |
2.99e-71 |
|
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350770 [Multi-domain] Cd Length: 218 Bit Score: 237.46 E-value: 2.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 582 FKGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIwGPFLVVAPASVLNNWADEISRFCPDL 661
Cdd:cd18012 1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRK-GPSLVVAPTSLIYNWEEEAAKFAPEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 662 KTLPYWGGLQERTILRKninpkrvmffstwiisfdpwavrqicickracnvvrfqtLSDMDagfhILITSYQLLVTDEKY 741
Cdd:cd18012 80 KVLVIHGTKRKREKLRA---------------------------------------LEDYD----LVITSYGLLRRDIEL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 742 FRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGIENH 821
Cdd:cd18012 117 LKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKD 196
|
250 260
....*....|....*....|....*...
gi 334186052 822 AehggtlNEHQLNRLHAILKPFMLRRVK 849
Cdd:cd18012 197 G------DEEALEELKKLISPFILRRLK 218
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
585-847 |
2.81e-66 |
|
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350751 [Multi-domain] Cd Length: 218 Bit Score: 223.39 E-value: 2.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 585 TLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTL 664
Cdd:cd17993 1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 665 PYWGGLQERTILRKninpkrvmffstwiisfdpwavrqicickracnvVRFQTLSDMDAGFHILITSYQLLVTDEKYFRR 744
Cdd:cd17993 81 VYLGDIKSRDTIRE----------------------------------YEFYFSQTKKLKFNVLLTTYEIILKDKAFLGS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 745 VKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGienhaeh 824
Cdd:cd17993 127 IKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEE------- 199
|
250 260
....*....|....*....|...
gi 334186052 825 ggtlNEHQLNRLHAILKPFMLRR 847
Cdd:cd17993 200 ----QEKGIADLHKELEPFILRR 218
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
586-847 |
4.76e-66 |
|
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350753 [Multi-domain] Cd Length: 223 Bit Score: 222.89 E-value: 4.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCpDLKTLP 665
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRkninpKRVMFFstwiisfdPWAVRqicicKRACNVVRfqtlsdmdagFHILITSYQLLVTDEKYFRRV 745
Cdd:cd17995 80 YHGSGESRQIIQ-----QYEMYF--------KDAQG-----RKKKGVYK----------FDVLITTYEMVIADAEELRKI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEwfskgienhaEHG 825
Cdd:cd17995 132 PWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLE----------EFG 201
|
250 260
....*....|....*....|..
gi 334186052 826 GTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd17995 202 DLKTAEQVEKLQALLKPYMLRR 223
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
586-847 |
2.62e-64 |
|
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350764 [Multi-domain] Cd Length: 216 Bit Score: 217.69 E-value: 2.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNINpkrvmffstwiiSFDPWavrqicickracnvvrfqtlsdmdagfHILITSYQLLVTDEKYFRRV 745
Cdd:cd18006 81 YMGDKEKRLDLQQDIK------------STNRF---------------------------HVLLTTYEICLKDASFLKSF 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLF--DNHDQFNEWFSKgIENHAE 823
Cdd:cd18006 122 PWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYSE-TDDESE 200
|
250 260
....*....|....*....|....
gi 334186052 824 hggTLNEhqlnrLHAILKPFMLRR 847
Cdd:cd18006 201 ---TVEE-----LHLLLQPFLLRR 216
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1231-1363 |
5.10e-64 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 213.49 E-value: 5.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1231 PAKLLTD-SGKLQTLDILLKRLRAGNHRVLLFAQMTKMLNILEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFQHRSDIFV 1309
Cdd:cd18793 2 PPKIEEVvSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 334186052 1310 FLLSTRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAHRLGQTKDVTVYRLI 1363
Cdd:cd18793 82 FLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
586-804 |
2.10e-61 |
|
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350756 [Multi-domain] Cd Length: 187 Bit Score: 208.01 E-value: 2.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLaEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYL-KEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNINPKRVmffstwiisfdpwavrqicickracnvvrfqtlsdmdaGFHILITSYQLLVT---DEKYF 742
Cdd:cd17998 80 YYGSQEERKHLRYDILKGLE--------------------------------------DFDVIVTTYNLATSnpdDRSFF 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186052 743 RRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLF 804
Cdd:cd17998 122 KRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
|
|
| DBINO |
pfam13892 |
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator ... |
345-476 |
4.58e-59 |
|
DNA-binding domain; DBINO is a DNA-binding domain found on global transcription activator SNF2L1 proteins and chromatin re-modelling proteins.
Pssm-ID: 464024 [Multi-domain] Cd Length: 134 Bit Score: 199.30 E-value: 4.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 345 DKIRKAWINIVRRDIAKHHRIFTTFHRKLSIDAKRFADGCQREVRMKVGRSYKIPRTAPIRTRKISRDMLLFWKRYDKQM 424
Cdd:pfam13892 3 EKRRKIWKNIAKKDIPKVYRAKQQNHQARLANCKKVAQLCAREARRKASRTQKTMKDPQLRAKRLMREMLLFWKKNEKEE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 334186052 425 AEERKKQEKEAAEAFKREQEQRESKRQQQRLNFLIKQTELYSHFMQNKTDSN 476
Cdd:pfam13892 83 RELRKRAEKEALEQAKKEEELREAKRQQRKLNFLITQTELYSHFMGKKLKTD 134
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
584-859 |
3.05e-55 |
|
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350822 [Multi-domain] Cd Length: 244 Bit Score: 192.96 E-value: 3.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 584 GTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKT 663
Cdd:cd18064 14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 664 LPYWGGLQERTILRKNinpkrVMFFSTWiisfdpwavrQICIckracnvvrfqtlsdmdagfhiliTSYQLLVTDEKYFR 743
Cdd:cd18064 94 VCLIGDKDQRAAFVRD-----VLLPGEW----------DVCV------------------------TSYEMLIKEKSVFK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 744 RVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFskgienhaE 823
Cdd:cd18064 135 KFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF--------D 206
|
250 260 270
....*....|....*....|....*....|....*..
gi 334186052 824 HGGTLNEHQL-NRLHAILKPFMLRRVKKDVVSELTTK 859
Cdd:cd18064 207 TNNCLGDQKLvERLHMVLRPFLLRRIKADVEKSLPPK 243
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
586-847 |
4.97e-55 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350812 [Multi-domain] Cd Length: 237 Bit Score: 191.76 E-value: 4.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18054 21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKninpkrvmffstwiisFDpWAVRQiciCKRAcnvvrfqtlsdmdaGFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18054 101 YIGDLMSRNTIRE----------------YE-WIHSQ---TKRL--------------KFNALITTYEILLKDKTVLGSI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGIENHAEhg 825
Cdd:cd18054 147 NWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQ-- 224
|
250 260
....*....|....*....|..
gi 334186052 826 gtlnehqlnRLHAILKPFMLRR 847
Cdd:cd18054 225 ---------SLHKVLEPFLLRR 237
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
577-849 |
5.08e-55 |
|
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350823 [Multi-domain] Cd Length: 233 Bit Score: 191.77 E-value: 5.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 577 QTPELFKG-TLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEIS 655
Cdd:cd18065 6 ESPSYVKGgTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 656 RFCPDLKTLPYWGGLQERTILRKNinpkrVMFFSTWiisfdpwavrQICIckracnvvrfqtlsdmdagfhiliTSYQLL 735
Cdd:cd18065 86 RWVPSLRAVCLIGDKDARAAFIRD-----VMMPGEW----------DVCV------------------------TSYEMV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 736 VTDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFs 815
Cdd:cd18065 127 IKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF- 205
|
250 260 270
....*....|....*....|....*....|....*
gi 334186052 816 kgienhaEHGGTLNEHQL-NRLHAILKPFMLRRVK 849
Cdd:cd18065 206 -------DTKNCLGDQKLvERLHAVLKPFLLRRIK 233
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1234-1492 |
1.72e-53 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 205.03 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1234 LLTDSGKLQTLDILLKRLRAGNHRVLLFAQMTKMLNILEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFQHR-SDIFVFLL 1312
Cdd:PLN03142 466 LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1313 STRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAHRLGQTKDVTVYRLICKETVEEKILHRASQKNTVQQLVMTGGH- 1391
Cdd:PLN03142 546 STRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRl 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1392 -----VQGDDFL-----GAADVVS---LLMDDAEAAQLEQKFRELPLQVKDRQKKKT-KRIRIDAEGDATLEELEDVDRQ 1457
Cdd:PLN03142 626 aeqktVNKDELLqmvryGAEMVFSskdSTITDEDIDRIIAKGEEATAELDAKMKKFTeDAIKFKMDDTAELYDFDDEDDK 705
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 334186052 1458 DNGQEPLEE------PEKPKSSNKKR-----------RAASNPKARAPQKAK 1492
Cdd:PLN03142 706 DENKLDFKKivsdnwIDPPKRERKRNyseseyfkqamRQGAPAKPKEPRIPR 757
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
1208-1379 |
1.60e-52 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 197.76 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1208 VVQPALQLtHRIFGSCPPMQSFDPAKLLTDSGKLQTLDILLKRLRAGNHRVLLFAQMTKMLNILEDYMNYRKYKYLRLDG 1287
Cdd:COG0553 503 LILAALTR-LRQICSHPALLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHG 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1288 SSTIMDRRDMVRDFQHRSDIFVFLLSTRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAHRLGQTKDVTVYRLICKET 1367
Cdd:COG0553 582 GTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGT 661
|
170
....*....|..
gi 334186052 1368 VEEKILHRASQK 1379
Cdd:COG0553 662 IEEKILELLEEK 673
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
577-849 |
7.95e-50 |
|
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350820 [Multi-domain] Cd Length: 251 Bit Score: 177.54 E-value: 7.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 577 QTPELFKGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISR 656
Cdd:cd18062 15 QSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 657 FCPDLKTLPYWGglqertilrkninpkrvmffstwiisfDPWAVRQICICKRAcnvvrfqtlsdmdAGFHILITSYQLLV 736
Cdd:cd18062 95 WAPSVVKVSYKG---------------------------SPAARRAFVPQLRS-------------GKFNVLLTTYEYII 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 737 TDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLS-FNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFS 815
Cdd:cd18062 135 KDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 334186052 816 KGIENHAEHgGTLNEHQ----LNRLHAILKPFMLRRVK 849
Cdd:cd18062 215 APFAMTGEK-VDLNEEEtiliIRRLHKVLRPFLLRRLK 251
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
577-849 |
1.36e-49 |
|
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350821 [Multi-domain] Cd Length: 251 Bit Score: 176.79 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 577 QTPELFKGTLKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEisr 656
Cdd:cd18063 15 QSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYE--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 657 fcpdlktlpywgglqertilrkninpkrvmffstwiisFDPWAVRQICICKRACNVVRFQTLSDMDAG-FHILITSYQLL 735
Cdd:cd18063 92 --------------------------------------FDKWAPSVVKISYKGTPAMRRSLVPQLRSGkFNVLLTTYEYI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 736 VTDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLS-FNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWF 814
Cdd:cd18063 134 IKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWF 213
|
250 260 270
....*....|....*....|....*....|....*....
gi 334186052 815 SKGIENHAEHgGTLNEHQ----LNRLHAILKPFMLRRVK 849
Cdd:cd18063 214 NAPFAMTGER-VDLNEEEtiliIRRLHKVLRPFLLRRLK 251
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
586-847 |
5.07e-49 |
|
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350757 [Multi-domain] Cd Length: 232 Bit Score: 174.46 E-value: 5.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLA----HLAEEKNIWG-PFLVVAPASVLNNWADEISRFCPD 660
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILAsdhhKRANSFNSENlPSLVVCPPTLVGHWVAEIKKYFPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 661 --LKTLPYWGGLQERTILRKNINpkrvmffstwiisfdpwavrqicickrACNVVrfqtlsdmdagfhilITSYQLLVTD 738
Cdd:cd17999 81 afLKPLAYVGPPQERRRLREQGE---------------------------KHNVI---------------VASYDVLRND 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 739 EKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGI 818
Cdd:cd17999 119 IEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPI 198
|
250 260 270
....*....|....*....|....*....|....*..
gi 334186052 819 --------ENHAEHGGTLnehQLNRLHAILKPFMLRR 847
Cdd:cd17999 199 lasrdskaSAKEQEAGAL---ALEALHKQVLPFLLRR 232
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
586-847 |
2.21e-47 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350811 [Multi-domain] Cd Length: 237 Bit Score: 169.85 E-value: 2.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18053 21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNinpkrvmffstwiisfdPWAVRQICICKracnvvrfqtlsdmdagFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18053 101 YLGDINSRNMIRTH-----------------EWMHPQTKRLK-----------------FNILLTTYEILLKDKSFLGGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKGienhaehg 825
Cdd:cd18053 147 NWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKG-------- 218
|
250 260
....*....|....*....|..
gi 334186052 826 gtlNEHQLNRLHAILKPFMLRR 847
Cdd:cd18053 219 ---REYGYASLHKELEPFLLRR 237
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
586-847 |
1.09e-46 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350813 [Multi-domain] Cd Length: 232 Bit Score: 167.88 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNinpkrvmffstwIISFDPWAVRQiciCKRAcnvvrFQTLSDMDAGFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18055 81 YTGDKDSRAIIREN------------EFSFDDNAVKG---GKKA-----FKMKREAQVKFHVLLTSYELVTIDQAALGSI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKgienhaehg 825
Cdd:cd18055 141 RWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD--------- 211
|
250 260
....*....|....*....|..
gi 334186052 826 gTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18055 212 -ISKEDQIKKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
586-847 |
2.05e-46 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350752 [Multi-domain] Cd Length: 196 Bit Score: 165.69 E-value: 2.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YwgglqertilrkninpkrvmffstwiisfdpwavrqicickracnvvrfqtlsdmdAGFHILITSYQLLVTDEKYFRRV 745
Cdd:cd17994 81 Y--------------------------------------------------------VGDHVLLTSYELISIDQAILGSI 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKgienhaehg 825
Cdd:cd17994 105 DWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFAD--------- 175
|
250 260
....*....|....*....|..
gi 334186052 826 gTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd17994 176 -ISKEDQIKKLHDLLGPHMLRR 196
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
586-847 |
9.63e-46 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350815 [Multi-domain] Cd Length: 232 Bit Score: 165.24 E-value: 9.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNinpkrvmffstwIISFDPWAVRQiciCKRAcnvvrFQTLSDMDAGFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18057 81 YTGDKESRSVIREN------------EFSFEDNAIRS---GKKV-----FRMKKEAQIKFHVLLTSYELITIDQAILGSI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKgienhaehg 825
Cdd:cd18057 141 EWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD--------- 211
|
250 260
....*....|....*....|..
gi 334186052 826 gTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18057 212 -ISKEDQIKKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
586-847 |
4.17e-45 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350814 [Multi-domain] Cd Length: 232 Bit Score: 163.31 E-value: 4.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKNinpkrvmffstwIISFDPWAVRQiciCKRACNVVRfqtlsDMDAGFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18056 81 YVGDKDSRAIIREN------------EFSFEDNAIRG---GKKASRMKK-----EASVKFHVLLTSYELITIDMAILGSI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFSKgienhaehg 825
Cdd:cd18056 141 DWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFAD--------- 211
|
250 260
....*....|....*....|..
gi 334186052 826 gTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18056 212 -IAKEDQIKKLHDMLGPHMLRR 232
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
586-847 |
1.07e-42 |
|
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350759 [Multi-domain] Cd Length: 232 Bit Score: 156.38 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIwGPFLVVAPASVLNNWADEISRFCPDLKTLP 665
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLI-KSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGlqERTILRKNINPkrvmffstwiisfdpwavrqiciCKRacnvvrfqtlsdmdaGFHILITSYQLLVTDEKYF--- 742
Cdd:cd18001 80 FHGT--SKKERERNLER-----------------------IQR---------------GGGVLLTTYGMVLSNTEQLsad 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 743 --RRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMP-MLFDNHDQFNEWFSKGIE 819
Cdd:cd18001 120 dhDEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPIT 199
|
250 260 270
....*....|....*....|....*....|...
gi 334186052 820 NHAEHGGTLNEHQLNR-----LHAILKPFMLRR 847
Cdd:cd18001 200 RGRDKDATQGEKALGSevaenLRQIIKPYFLRR 232
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
586-847 |
8.47e-42 |
|
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350763 [Multi-domain] Cd Length: 245 Bit Score: 154.07 E-value: 8.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHL-------AEEKNI-------------WGPFLVVAPAS 645
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrRDRENNrprfkkkppassaKKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 646 VLNNWADEISRfcpdlktlpyWGglqertilrkninpkrvmFFSTWII-SFDPWAVRQICICKRACNVVrfqtlsdmdag 724
Cdd:cd18005 81 VLYNWKDELDT----------WG------------------HFEVGVYhGSRKDDELEGRLKAGRLEVV----------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 725 fhilITSYQLLVTDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLF 804
Cdd:cd18005 122 ----VTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGAL 197
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 334186052 805 DNHDQFNEWFSKGIENHAEHGGTLNEHQLNR-----LHAILKPFMLRR 847
Cdd:cd18005 198 GSRSQFKKHFSEPIKRGQRHTATARELRLGRkrkqeLAVKLSKFFLRR 245
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
586-801 |
1.92e-41 |
|
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350758 [Multi-domain] Cd Length: 193 Bit Score: 151.32 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIWGPFLVVAPASVLNNWADEISRFCPDLKTlp 665
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 ywgglqertilrkninpkrVMFFSTWIISFDPWAVRQIcickracnVVRFQTLSDMDAGFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18000 79 -------------------VVLHSSGSGTGSEEKLGSI--------ERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNH 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 334186052 746 KWQYMVLDEAQAIK---SSSSIRWKtllSFNCRNRLLLTGTPIQNNMAELWALLHFIMP 801
Cdd:cd18000 132 NWQYVILDEGHKIRnpdAEITLACK---QLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
586-847 |
5.83e-40 |
|
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350766 [Multi-domain] Cd Length: 241 Bit Score: 148.59 E-value: 5.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCyeqGlnGILADEMGLGKTIQAMAF-LAHLAEEKNI----------------WGPFLVVAPASVLN 648
Cdd:cd18008 1 LLPYQKQGLAWMLPR---G--GILADEMGLGKTIQALALiLATRPQDPKIpeeleenssdpkklylSKTTLIVVPLSLLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 649 NWADEISRFC--PDLKTLPYWGGlqertilRKNINPKrvmffstwiisfdpwavrqicickracnvvrfqTLSDMDagfh 726
Cdd:cd18008 76 QWKDEIEKHTkpGSLKVYVYHGS-------KRIKSIE---------------------------------ELSDYD---- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 727 ILITSYQLLVTDEKYF----------------RRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMA 790
Cdd:cd18008 112 IVITTYGTLASEFPKNkkgggrdskekeasplHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLD 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 334186052 791 ELWALLHFIMPMLFDNHDQFNEWFSKGIENHaehggtlNEHQLNRLHAILKPFMLRR 847
Cdd:cd18008 192 DLYSLLRFLRVEPFGDYPWFNSDISKPFSKN-------DRKALERLQALLKPILLRR 241
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
586-847 |
1.84e-38 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350818 [Multi-domain] Cd Length: 222 Bit Score: 143.66 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEeKNIWGPFLVVAPASVLNNWADEISRFCpDLKTLP 665
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYN-VGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKninpkRVMFFSTWIISFDPWAVRqicickracnvvrfqtlsdmdagFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18060 79 YHGSLASRQMIQQ-----YEMYCKDSRGRLIPGAYK-----------------------FDALITTFEMILSDCPELREI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFskgienhaehG 825
Cdd:cd18060 131 EWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF----------G 200
|
250 260
....*....|....*....|..
gi 334186052 826 GTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18060 201 DLKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
586-847 |
2.86e-37 |
|
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350762 [Multi-domain] Cd Length: 240 Bit Score: 140.88 E-value: 2.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCY--EQGLNG---ILADEMGLGKTIQAMAFLAHLAEEKNIWGP----FLVVAPASVLNNWADEISR 656
Cdd:cd18004 1 LRPHQREGVQFLYDCLtgRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 657 fcpdlktlpyWGGLQERTILRKNINPKRVMFFSTWIISFDPWavrqicickracnvvrfqtlsdmdagfHILITSYQLLV 736
Cdd:cd18004 81 ----------WLGLRRIKVVTADGNAKDVKASLDFFSSASTY---------------------------PVLIISYETLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 737 T-DEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFS 815
Cdd:cd18004 124 RhAEKLSKKISIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFE 203
|
250 260 270
....*....|....*....|....*....|....*..
gi 334186052 816 KGIENHAEHGGTLNEHQLNRLHA-----ILKPFMLRR 847
Cdd:cd18004 204 EPILRSRDPDASEEDKELGAERSqelseLTSRFILRR 240
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
586-847 |
7.85e-36 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350816 [Multi-domain] Cd Length: 222 Bit Score: 136.33 E-value: 7.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEeKNIWGPFLVVAPASVLNNWADEIsRFCPDLKTLP 665
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFL-MGIRGPFLIIAPLSTITNWEREF-RTWTEMNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKninpkRVMFFSTWIISFDPWAVRqicickracnvvrfqtlsdmdagFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18058 79 YHGSQISRQMIQQ-----YEMYYRDEQGNPLSGIFK-----------------------FQVVITTFEMILADCPELKKI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEwfskgienhaEHG 825
Cdd:cd18058 131 NWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLE----------EFG 200
|
250 260
....*....|....*....|..
gi 334186052 826 GTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18058 201 DLKTEEQVKKLQSILKPMMLRR 222
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
586-847 |
8.96e-36 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350817 [Multi-domain] Cd Length: 222 Bit Score: 135.93 E-value: 8.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEeKNIWGPFLVVAPASVLNNWADEIsRFCPDLKTLP 665
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYL-KGIHGPFLVIAPLSTIPNWEREF-RTWTELNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKninpkRVMFFStwiisfDPwavrQICICKRACNvvrfqtlsdmdagFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18059 79 YHGSQASRRTIQL-----YEMYFK------DP----QGRVIKGSYK-------------FHAIITTFEMILTDCPELRNI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEwfskgienhaEHG 825
Cdd:cd18059 131 PWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQ----------EFG 200
|
250 260
....*....|....*....|..
gi 334186052 826 GTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18059 201 DLKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
586-847 |
3.96e-33 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350819 [Multi-domain] Cd Length: 222 Bit Score: 128.20 E-value: 3.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEeKNIWGPFLVVAPASVLNNWADEIsRFCPDLKTLP 665
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILL-TGIRGPFLIIAPLSTIANWEREF-RTWTDLNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 YWGGLQERTILRKninpkRVMFFSTwiisfdpwavRQICICKRAcnvVRFQTLsdmdagfhilITSYQLLVTDEKYFRRV 745
Cdd:cd18061 79 YHGSLISRQMIQQ-----YEMYFRD----------SQGRIIRGA---YRFQAI----------ITTFEMILGGCPELNAI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEwfskgienhaEHG 825
Cdd:cd18061 131 DWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQ----------EFG 200
|
250 260
....*....|....*....|..
gi 334186052 826 GTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18061 201 DLKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
586-847 |
5.67e-31 |
|
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350768 [Multi-domain] Cd Length: 213 Bit Score: 121.93 E-value: 5.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVncyEQGLNGILADEMGLGKTIQAMAFLAHLAEEkniWgPFLVVAPASVLNNWADEISRFCPDLKtlp 665
Cdd:cd18010 1 LLPFQREGVCFAL---RRGGRVLIADEMGLGKTVQAIAIAAYYREE---W-PLLIVCPSSLRLTWADEIERWLPSLP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 666 ywgglqertilrkninpkrvmffstwiisfdpwaVRQIcickracNVVRFQTLSDMDAGFHILITSYQLLVTDEKYFRRV 745
Cdd:cd18010 71 ----------------------------------PDDI-------QVIVKSKDGLRDGDAKVVIVSYDLLRRLEKQLLAR 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 746 KWQYMVLDEAQAIKSSSSIRWKTLLSF--NCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNE----------- 812
Cdd:cd18010 110 KFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRrycaakqggfg 189
|
250 260 270
....*....|....*....|....*....|....*.
gi 334186052 813 WFSKGIENHAEhggtlnehqlnrLHAIL-KPFMLRR 847
Cdd:cd18010 190 WDYSGSSNLEE------------LHLLLlATIMIRR 213
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
586-820 |
1.50e-29 |
|
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350765 [Multi-domain] Cd Length: 239 Bit Score: 118.55 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWL-VNCYEQGLNG------ILADEMGLGKTIQAMAFL-AHLAEEKNIWGPfLVVAPASVLNNWADEisrf 657
Cdd:cd18007 1 LKPHQVEGVRFLwSNLVGTDVGSdegggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 658 cpdlktlpywgglqertilrkninpkrvmfFSTWIISF-DPWAVrqiCICKRACNVVRfQTLSDMDAGFH---ILITSYQ 733
Cdd:cd18007 76 ------------------------------FKKWLPPDlRPLLV---LVSLSASKRAD-ARLRKINKWHKeggVLLIGYE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 734 LLV-------TDEKYFRRV-KWQYM------VLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFI 799
Cdd:cd18007 122 LFRnlasnatTDPRLKQEFiAALLDpgpdllVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFA 201
|
250 260
....*....|....*....|.
gi 334186052 800 MPMLFDNHDQFNEWFSKGIEN 820
Cdd:cd18007 202 RPKYLGTLKEFKKKFVKPIEA 222
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
578-808 |
6.50e-26 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 106.81 E-value: 6.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 578 TPELFKGTLKEYQMKGLQWLVNCYEqglNGILADEMGLGKTIQAMAFLAHLAEEKNiWGPFLVVAPASVL-NNWADEISR 656
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELaEQWAEELKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 657 FCPD--LKTLPYWGGLQERTILRKNINPKrvmffstwiisfdpwavrqicickracnvvrfqtlsdmdagFHILITSYQL 734
Cdd:smart00487 77 LGPSlgLKVVGLYGGDSKREQLRKLESGK-----------------------------------------TDILVTTPGR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 735 LVTD--EKYFRRVKWQYMVLDEAQAIKSSSSIR-WKTLLSF--NCRNRLLLTGTP---IQNNMAELWALLHFIMPMLFDN 806
Cdd:smart00487 116 LLDLleNDKLSLSNVDLVILDEAHRLLDGGFGDqLEKLLKLlpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPL 195
|
..
gi 334186052 807 HD 808
Cdd:smart00487 196 EP 197
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1239-1352 |
2.10e-25 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 101.90 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1239 GKLQTLDILLKRLRagNHRVLLFAQMTKMLNIlEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFqhRSDIFVFLLSTRAGG 1318
Cdd:pfam00271 1 EKLEALLELLKKER--GGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDF--RKGKIDVLVATDVAE 75
|
90 100 110
....*....|....*....|....*....|....
gi 334186052 1319 LGINLTAADTVIFYESDWNPTLDLQAMDRAHRLG 1352
Cdd:pfam00271 76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
586-847 |
3.92e-25 |
|
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350825 [Multi-domain] Cd Length: 243 Bit Score: 106.01 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCYE----QGLNG-ILADEMGLGKTIQAMAFLAHLAEEKNIWGPFL----VVAPASVLNNWADEISR 656
Cdd:cd18067 1 LRPHQREGVKFLYRCVTgrriRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 657 FC-PDLKTLPYWGGLQERTILrkninpkrvmffstwiisfdpwavrqicickracNVVRFQTLSDMDAGFHILITSYQLL 735
Cdd:cd18067 81 WLgGRLQPLAIDGGSKKEIDR----------------------------------KLVQWASQQGRRVSTPVLIISYETF 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 736 VTDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFS 815
Cdd:cd18067 127 RLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFE 206
|
250 260 270
....*....|....*....|....*....|....*..
gi 334186052 816 KGI-----ENHAEHGGTLNEHQLNRLHAILKPFMLRR 847
Cdd:cd18067 207 LPIlkgrdADASEKERQLGEEKLQELISIVNRCIIRR 243
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
602-847 |
1.37e-22 |
|
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350829 [Multi-domain] Cd Length: 239 Bit Score: 98.31 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 602 EQGLNGILADEMGLGKTIQAMAFLAHlaeekniwGPFLVVAPASVLNNWADEISRFCPD--LKTLPYWGGlqertilRKN 679
Cdd:cd18071 46 ELVRGGILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHGG-------ERN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 680 INPKRVMffstwiisfdpwavrqicickracnvvrfqtlsdmdaGFHILITSYQLLVTDEKY-----FRRVKWQYMVLDE 754
Cdd:cd18071 111 RDPKLLS-------------------------------------KYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 755 AQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNhdqfNEWFSKGIENHAEHGgtlNEHQLN 834
Cdd:cd18071 154 GHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSN----PEYWRRLIQRPLTMG---DPTGLK 226
|
250
....*....|...
gi 334186052 835 RLHAILKPFMLRR 847
Cdd:cd18071 227 RLQVLMKQITLRR 239
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1270-1352 |
7.36e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.12 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1270 ILEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFqhRSDIFVFLLSTRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAH 1349
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKF--NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79
|
...
gi 334186052 1350 RLG 1352
Cdd:smart00490 80 RAG 82
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
586-846 |
7.15e-21 |
|
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350828 [Multi-domain] Cd Length: 257 Bit Score: 93.95 E-value: 7.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNcyeqgLNGILADEMGLGKTIQAMAF-LAH----LAEEKNIW--------------------GPFLV 640
Cdd:cd18070 1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLALiLLHprpdNDLDAADDdsdemvccpdclvaetpvssKATLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 641 VAPASVLNNWADEISRFCPD-LKTLPYWGglqertiLRKNinpkrvmffsTWIISFDPW--AVRQICICkrACNVVRFQT 717
Cdd:cd18070 76 VCPSAILAQWLDEINRHVPSsLKVLTYQG-------VKKD----------GALASPAPEilAEYDIVVT--TYDVLRTEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 718 LSDMDAGFHILITSYQLLVTDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLH 797
Cdd:cd18070 137 HYAEANRSNRRRRRQKRYEAPPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLS 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 334186052 798 FIMpmlFDNHDQFNEWFSKGIENHAEHGGTLnehqlnRLHAILKPFMLR 846
Cdd:cd18070 217 FLG---VEPFCDSDWWARVLIRPQGRNKARE------PLAALLKELLWR 256
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
608-847 |
1.45e-19 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350769 [Multi-domain] Cd Length: 207 Bit Score: 88.89 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 608 ILADEMGLGKTIQA-MAFLAHLAEekNIWGPFLVVAPASVLNNWADEISRFcpdlktlpywGGLQERTILRKNINPKRVM 686
Cdd:cd18011 21 LLADEVGLGKTIEAgLIIKELLLR--GDAKRVLILCPASLVEQWQDELQDK----------FGLPFLILDRETAAQLRRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 687 FFSTWiisfdpwavrqicickracnvvrfqtlsdmdAGFHILITSYQLLVTDEKY---FRRVKWQYMVLDEAQAIKSSSS 763
Cdd:cd18011 89 IGNPF-------------------------------EEFPIVIVSLDLLKRSEERrglLLSEEWDLVVVDEAHKLRNSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 764 IRWKTLLSF------NCRNRLLLTGTPIQNNMAELWALLHFIMPmlfdnhDQFNEWFSkgienhaehggtlnEHQLNRLH 837
Cdd:cd18011 138 GKETKRYKLgrllakRARHVLLLTATPHNGKEEDFRALLSLLDP------GRFAVLGR--------------FLRLDGLR 197
|
250
....*....|
gi 334186052 838 AILKPFMLRR 847
Cdd:cd18011 198 EVLAKVLLRR 207
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
591-847 |
2.03e-19 |
|
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350830 [Multi-domain] Cd Length: 241 Bit Score: 89.08 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 591 MKGLQWLVNCYEQGlnGILADEMGLGKTIQAMAF----------------------LAHLAEEKNIWGPFLVVAPASVLN 648
Cdd:cd18072 9 LAWLLWRERQKPRG--GILADDMGLGKTLTMIALilaqkntqnrkeeekekaltewESKKDSTLVPSAGTLVVCPASLVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 649 NWADEISRfcpdlktlpywgglqertilRKNINPKRVMFFStwiisfdpwAVRQICICKracnvvrfqTLSDMDagfhIL 728
Cdd:cd18072 87 QWKNEVES--------------------RVASNKLRVCLYH---------GPNRERIGE---------VLRDYD----IV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 729 ITSYQLLVTDEKYFR---------RVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFI 799
Cdd:cd18072 125 ITTYSLVAKEIPTYKeesrssplfRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 334186052 800 MPMLFdnhDQFNEWfSKGIENHAEHGGtlnehqlNRLHAILKPFMLRR 847
Cdd:cd18072 205 RCSPF---DDLKVW-KKQVDNKSRKGG-------ERLNILTKSLLLRR 241
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
586-847 |
6.07e-19 |
|
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350824 [Multi-domain] Cd Length: 235 Bit Score: 87.59 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNC-----YEQGLNGILADEMGLGKTIQAMAFLAHLAEE-----KNIWGPFLVVAPASVLNNWADEIS 655
Cdd:cd18066 1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQgpyggKPVIKRALIVTPGSLVKNWKKEFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 656 RfcpdlktlpyWGGLQERTILRKNINPKRVMFFSTWIISfdpwavrqicickracnvvrfqtlsdmdagfhILITSYQLL 735
Cdd:cd18066 81 K----------WLGSERIKVFTVDQDHKVEEFIASPLYS--------------------------------VLIISYEML 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 736 VTDEKYFRRVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFNEWFS 815
Cdd:cd18066 119 LRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYE 198
|
250 260 270
....*....|....*....|....*....|....*..
gi 334186052 816 KGIENHAEHGGTLNEHQLNRLHA-----ILKPFMLRR 847
Cdd:cd18066 199 EPIVRSREPTATPEEKKLGEARAaeltrLTGLFILRR 235
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
586-820 |
5.55e-16 |
|
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350827 [Multi-domain] Cd Length: 227 Bit Score: 78.70 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLV-NCYE--------QGLNGILADEMGLGKTIQAMAF----LAHLAEEKniwgpFLVVAPASVLNNWAD 652
Cdd:cd18069 1 LKPHQIGGIRFLYdNIIEslerykgsSGFGCILAHSMGLGKTLQVISFldvlLRHTGAKT-----VLAIVPVNTLQNWLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 653 EISRFCPDLKTLPywgglqertilrkNINPKrvmFFSTWIISFDPWAVRQicickracnvvRFQTLSDMDAGFHILITSY 732
Cdd:cd18069 76 EFNKWLPPPEALP-------------NVRPR---PFKVFILNDEHKTTAA-----------RAKVIEDWVKDGGVLLMGY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 733 QLlvtdekyFR-RVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIMPMLFDNHDQFN 811
Cdd:cd18069 129 EM-------FRlRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFS 201
|
....*....
gi 334186052 812 EWFSKGIEN 820
Cdd:cd18069 202 NMFERPILN 210
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
586-820 |
7.90e-15 |
|
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350826 [Multi-domain] Cd Length: 246 Bit Score: 76.08 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVNCY---------EQGLNGILADEMGLGKTIQAMAFLaH---LAEEKNIWGPFLVVAPASVLNNWADE 653
Cdd:cd18068 1 LKPHQVDGVQFMWDCCceslkktkkSPGSGCILAHCMGLGKTLQVVTFL-HtvlLCEKLENFSRVLVVCPLNTVLNWLNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 654 ISRFCPDLKTlpyWGGLQERTILRKNINPKRVMFFSTWiisfdpwavrqicickracnvvrFQTLSDMDAGFHIlitsYQ 733
Cdd:cd18068 80 FEKWQEGLKD---EEKIEVNELATYKRPQERSYKLQRW-----------------------QEEGGVMIIGYDM----YR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 734 LLVT--DEKYFRRVKWQYM-----------VLDEAQAIKSSSSIRWKTLLSFNCRNRLLLTGTPIQNNMAELWALLHFIM 800
Cdd:cd18068 130 ILAQerNVKSREKLKEIFNkalvdpgpdfvVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVK 209
|
250 260
....*....|....*....|
gi 334186052 801 PMLFDNHDQFNEWFSKGIEN 820
Cdd:cd18068 210 PNLLGTIKEFRNRFVNPIQN 229
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
586-799 |
6.59e-11 |
|
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350771 [Multi-domain] Cd Length: 218 Bit Score: 63.91 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 586 LKEYQMKGLQWLVncyEQGLNGILADeMGLGKTIQAMAFLAHLAEEKNIwGPFLVVAPASVL-NNWADEISRfcpdlktl 664
Cdd:cd18013 1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFT-RRVLVIAPLRVArSTWPDEVEK-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 665 pyWGGLQERTILRKNINPKRvmffstwiisfdpwavrqicickracnvvRFQTLsdmDAGFHILITSYQLLV-TDEKYFR 743
Cdd:cd18013 68 --WNHLRNLTVSVAVGTERQ-----------------------------RSKAA---NTPADLYVINRENLKwLVNKSGD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334186052 744 RVKWQYMVLDEAQAIKSSSSIRWKTLLSFNCR-NRLL-LTGTPIQNNMAELWALLHFI 799
Cdd:cd18013 114 PWPFDMVVIDELSSFKSPRSKRFKALRKVRPViKRLIgLTGTPSPNGLMDLWAQIALL 171
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
582-784 |
7.04e-06 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 50.79 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 582 FKGTLKEYQMKGL-QWLVNCYEQGLNGILADEMGLGKTIQAMAFLAHLAEEKNIwgpfLVVAPASVLNN-WADEISRFCP 659
Cdd:COG1061 77 TSFELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 660 DlktlPYWGGLQErtilrkninpkrvmffstwiisfdpwavrqicickracnvvrfqtlsdmDAGFHILITSYQLLVTDE 739
Cdd:COG1061 153 D----PLAGGGKK-------------------------------------------------DSDAPITVATYQSLARRA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 334186052 740 --KYFRRvKWQYMVLDEAQAIkSSSSIRwKTLLSFNCRNRLLLTGTP 784
Cdd:COG1061 180 hlDELGD-RFGLVIIDEAHHA-GAPSYR-RILEAFPAAYRLGLTATP 223
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
1305-1360 |
1.18e-05 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 44.62 E-value: 1.18e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 334186052 1305 SDIFVFLLSTRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAHRLGQTKDVTVY 1360
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
606-783 |
1.95e-03 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 40.46 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 606 NGILADEMGLGKTIQAMAFLAHLAEEKNiwGPFLVVAPASVL-NNWADEI-SRFCPDLKTLPYWGGlqertilrKNINPK 683
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALaLQTAERLrELFGPGIRVAVLVGG--------SSAEER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 684 RVMFFSTWiisfdpwavrqicickracnvvrfqtlsdmdagfHILITSYQLLVTD---EKYFRRVKWQYMVLDEAQAIKS 760
Cdd:cd00046 73 EKNKLGDA----------------------------------DIIIATPDMLLNLllrEDRLFLKDLKLIIVDEAHALLI 118
|
170 180 190
....*....|....*....|....*....|.
gi 334186052 761 SS--------SIRWktLLSFNCRnRLLLTGT 783
Cdd:cd00046 119 DSrgalildlAVRK--AGLKNAQ-VILLSAT 146
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1411-1513 |
4.03e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.50 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 1411 AEAAQLEQKFRELPLQVKDRQKKKTKRiRIDAEGDATLEELEDVDRQDNGQEPLEEPEKPKS-SNKKRRAASNPKARAPQ 1489
Cdd:PRK07735 103 AKAAALAKQKREGTEEVTEEEKAAAKA-KAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEkAKAKAAAAAKAKAAALA 181
|
90 100
....*....|....*....|....
gi 334186052 1490 KAKEEANGEDTPQRTKRVKRQTKS 1513
Cdd:PRK07735 182 KQKAAEAGEGTEEVTEEEKAKAKA 205
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
385-506 |
7.18e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 40.60 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186052 385 QREVRMKVGRSYKiprtapiRTRKISRDMLLF--WK--RYDKQMAEERK--KQEKEAAEAFKRE--QEQRESKRQQQRLN 456
Cdd:PRK00247 293 QYREKQKEKKAFL-------WTLRRNRLRMIItpWRapELHAENAEIKKtrTAEKNEAKARKKEiaQKRRAAEREINREA 365
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 334186052 457 FLIKQTELYSHFMQNKTDSNPSEALPIGDENPIDEVLPETSAAEPSEVED 506
Cdd:PRK00247 366 RQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQVEA 415
|
|
| |
