|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
206-430 |
1.29e-82 |
|
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: 269.07 E-value: 1.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSILVVCPAILRYSWAEELEHWLPFCLPADIHLVFGh 285
Cdd:cd18010 1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 286 eNNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVARKVKRIVLLSGTPSLSR 365
Cdd:cd18010 80 -SKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYL----KNSKAKRTKAALPLLKRAKRVILLSGTPALSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1366038577 366 PFDIFHQIDMLWPGLLGRDKFkFGETYCDAKyvrgvQGKVFQDFSKGTRLEELNMLLTRTVMIRR 430
Cdd:cd18010 155 PIELFTQLDALDPKLFGRFHD-FGRRYCAAK-----QGGFGWDYSGSSNLEELHLLLLATIMIRR 213
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
182-646 |
2.42e-76 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 267.48 E-value: 2.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 182 RPEHLLDDKVDELIGKLPKRLLDSLLPFQLEGVRF--GLQR-GGRCLIADEMGLGKTLQAIAIACCFMSEGS---ILVVC 255
Cdd:COG0553 218 AVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWllFLRRlGLGGLLADDMGLGKTIQALALLLELKERGLarpVLIVA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 256 PAILRYSWAEELEHWLPfCLPADIHlvFGHENNPANLKKWPR--VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctk 333
Cdd:COG0553 298 PTSLVGNWQRELAKFAP-GLRVLVL--DGTRERAKGANPFEDadLVITSYGLLRRDIELLAAVDWDLVILDEAQHI---- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 334 KKSEPREIKAVLDVarKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLLGrDKFKFGETYCDAKYVRGVQgkvfqdfskgt 413
Cdd:COG0553 371 KNPATKRAKAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPGLLG-SLKAFRERFARPIEKGDEE----------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 414 RLEELNMLLtRTVMIRRLKEHVLSQLPPKRRQIIQVVLKKsdivsAKAAIRvgkshdEDVSSEHLDELNDSMGcciskqL 493
Cdd:COG0553 437 ALERLRRLL-RPFLLRRTKEDVLKDLPEKTEETLYVELTP-----EQRALY------EAVLEYLRRELEGAEG------I 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 494 SHQELGIAKLAGFREwLSIHPVIAEADGV------AKL--------ESDSSSHKMLIFAHHHKVLDGVQEFIIHKEIDFV 559
Cdd:COG0553 499 RRRGLILAALTRLRQ-ICSHPALLLEEGAelsgrsAKLeallelleELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYA 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 560 RIDGNTLATDRQLAVRKFQLSSEVKIAIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYFFS 639
Cdd:COG0553 578 YLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLV 657
|
....*..
gi 1366038577 640 GKDTIDE 646
Cdd:COG0553 658 AEGTIEE 664
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
529-638 |
9.78e-36 |
|
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: 132.22 E-value: 9.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 529 SSSHKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQLSSEVKIAIVGITAGGVGLDFSSATHVVFL 608
Cdd:cd18793 25 EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILY 104
|
90 100 110
....*....|....*....|....*....|
gi 1366038577 609 ELPQSPSLMLQAEDRAHRRGQTNAVNIYFF 638
Cdd:cd18793 105 DPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
210-449 |
5.25e-25 |
|
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: 106.61 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 210 QLEGVRF------GLQRGgrCLIADEMGLGKTLQAIAI-----ACCFMSEGSILVVCPAILRYSWAEELEHWL-PFCLPA 277
Cdd:pfam00176 2 QIEGVNWmlslenNLGRG--GILADEMGLGKTLQTISLllylkHVDKNWGGPTLIVVPLSLLHNWMNEFERWVsPPALRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 278 DIHlvFGHENNPANLKKWPR------VVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKSepreIKAVLDVarKV 351
Cdd:pfam00176 80 VVL--HGNKRPQERWKNDPNfladfdVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKL----SKALKSL--KT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 352 KRIVLLSGTPSLSRPFDIFHQIDMLWPGLLG-----RDKF--KFGETYCDAKYVRgvqgkvfqdfskgtrleeLNMLLTR 424
Cdd:pfam00176 152 RNRWILTGTPLQNNLEELWALLNFLRPGPFGslstfRNWFdrPIERGGGKKGVSR------------------LHKLLKP 213
|
250 260
....*....|....*....|....*
gi 1366038577 425 TvMIRRLKEHVLSQLPPKRRQIIQV 449
Cdd:pfam00176 214 F-LLRRTKKDVEKSLPPKVEYILFC 237
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
198-362 |
9.87e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.56 E-value: 9.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 198 LPKRLLDSLLPFQLEGVRFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGS---ILVVCP-AILRYSWAEELEHWLPF 273
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggrVLVLVPtRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 274 cLPADIHLVFGHENNPANLKKW----PRVVVISY-TMLHHLQKSMLD-REWALLIVDESHHvrcTKKKSEPREIKAVLDV 347
Cdd:smart00487 81 -LGLKVVGLYGGDSKREQLRKLesgkTDILVTTPgRLLDLLENDKLSlSNVDLVILDEAHR---LLDGGFGDQLEKLLKL 156
|
170
....*....|....*
gi 1366038577 348 ARKVKRIVLLSGTPS 362
Cdd:smart00487 157 LPKNVQLLLLSATPP 171
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
225-646 |
9.66e-22 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 102.57 E-value: 9.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 225 LIADEMGLGKTLQAIAIACcFMSE-----GSILVVCPAILRYSWAEELEHWLPFCLPADIHlvfGHENNPANLKKWP--- 296
Cdd:PLN03142 192 ILADEMGLGKTLQTISLLG-YLHEyrgitGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFH---GNPEERAHQREELlva 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 297 ---RVVVISYTMLHHlQKSMLDR-EWALLIVDESHHVrctkkKSEPREIKAVLDVARKVKRIvLLSGTPSLSRPFDIFHQ 372
Cdd:PLN03142 268 gkfDVCVTSFEMAIK-EKTALKRfSWRYIIIDEAHRI-----KNENSLLSKTMRLFSTNYRL-LITGTPLQNNLHELWAL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 373 IDMLWPGLLGrDKFKFGETYCDAKyvRGVQGKVFQDFSKgtrleelnmlLTRTVMIRRLKEHVLSQLPPKRRQIIQVVLK 452
Cdd:PLN03142 341 LNFLLPEIFS-SAETFDEWFQISG--ENDQQEVVQQLHK----------VLRPFLLRRLKSDVEKGLPPKKETILKVGMS 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 453 KSDIVSAKAAIRvgksHDEDV---SSEHLDELNDSM---GCCiskqlSHQELGIAKLAGFREWLSIHPViaEADG----- 521
Cdd:PLN03142 408 QMQKQYYKALLQ----KDLDVvnaGGERKRLLNIAMqlrKCC-----NHPYLFQGAEPGPPYTTGEHLV--ENSGkmvll 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 522 ---VAKLESDSSshKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKF-QLSSEVKIAIVGITAGGVGL 597
Cdd:PLN03142 477 dklLPKLKERDS--RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFnKPGSEKFVFLLSTRAGGLGI 554
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1366038577 598 DFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYFFSGKDTIDE 646
Cdd:PLN03142 555 NLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEE 603
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
522-628 |
1.09e-17 |
|
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: 79.95 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 522 VAKLESDSSSHKMLIFAHHHKVLDgVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVGLDFSS 601
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFR-KGKIDV-LVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 1366038577 602 ATHVVFLELPQSPSLMLQAEDRAHRRG 628
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
547-628 |
2.41e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.16 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 547 VQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHR 626
Cdd:smart00490 3 LAELLKELGIKVARLHGGLSQEEREEILDKFN-NGKIKV-LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1366038577 627 RG 628
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
205-627 |
5.55e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 76.60 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 205 SLLPFQLEGV----RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSILVVCPAI-LRYSWAEELEHWLPfclpaDI 279
Cdd:COG1061 80 ELRPYQQEALeallAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRReLLEQWAEELRRFLG-----DP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 280 HLVFGHENNPAnlkkwpRVVVISY-TMLHHLQKSMLDREWALLIVDESHHVRctkkksePREIKAVLDvARKVKRIVLLS 358
Cdd:COG1061 155 LAGGGKKDSDA------PITVATYqSLARRAHLDELGDRFGLVIIDEAHHAG-------APSYRRILE-AFPAAYRLGLT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 359 GTP--SLSRPFDIFHQIdmlwpgllgrdkfkfgetycdakyvrgvqGKVFqdfskGTRLEELnmlltrtvmirrLKEHVL 436
Cdd:COG1061 221 ATPfrSDGREILLFLFD-----------------------------GIVY-----EYSLKEA------------IEDGYL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 437 SqlpPKRRQIIQVVLKKsdivsakaairvgKSHDEDVSSEHLDelndsmgccisKQLSHQElgIAKLAGFREWLSIHPvi 516
Cdd:COG1061 255 A---PPEYYGIRVDLTD-------------ERAEYDALSERLR-----------EALAADA--ERKDKILRELLREHP-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 517 aeadgvaklesdsSSHKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVG 596
Cdd:COG1061 304 -------------DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR-DGELRI-LVTVDVLNEG 368
|
410 420 430
....*....|....*....|....*....|.
gi 1366038577 597 LDFSSATHVVFLELPQSPSLMLQAEDRAHRR 627
Cdd:COG1061 369 VDVPRLDVAILLRPTGSPREFIQRLGRGLRP 399
|
|
| DpdE |
NF041062 |
protein DpdE; |
223-366 |
2.42e-09 |
|
protein DpdE;
Pssm-ID: 468989 [Multi-domain] Cd Length: 1048 Bit Score: 61.91 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 223 RCLIADEMGLGKTLQA-IAIACCFM--SEGSILVVCPAILRYSWAEELE---HWLPFcLPADIHLVfGHEnNPANLKKWP 296
Cdd:NF041062 172 RYLLADEVGLGKTIEAgLVIRQHLLdnPDARVLVLVPDALVRQWRRELRdkfFLDDF-PGARVRVL-SHE-EPERWEPLL 248
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1366038577 297 RVVvisytmlhhlqksmldrewALLIVDESHHVRCTKKKSEPREI---KAVLDVARKVKRIVLLSGTPSLSRP 366
Cdd:NF041062 249 DAP-------------------DLLVVDEAHQLARLAWSGDPPERaryRELAALAHAAPRLLLLSATPVLGNE 302
|
|
| PRK04914 |
PRK04914 |
RNA polymerase-associated protein RapA; |
205-361 |
1.38e-06 |
|
RNA polymerase-associated protein RapA;
Pssm-ID: 235319 [Multi-domain] Cd Length: 956 Bit Score: 52.92 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 205 SLLPFQL----E-GVRFGlqrgGRCLIADEMGLGKTLQAiaiaccfmseGSI-------------LVVCPAILRYSWAEE 266
Cdd:PRK04914 152 SLIPHQLyiahEvGRRHA----PRVLLADEVGLGKTIEA----------GMIihqqlltgraervLILVPETLQHQWLVE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 267 L--EHWLPFCL-----PADIhlvFGHENNP---ANLkkwprvVVISYTML---HHLQKSMLDREWALLIVDESHHVRCTK 333
Cdd:PRK04914 218 MlrRFNLRFSLfdeerYAEA---QHDADNPfetEQL------VICSLDFLrrnKQRLEQALAAEWDLLVVDEAHHLVWSE 288
|
170 180
....*....|....*....|....*...
gi 1366038577 334 KKSEpREIKAVLDVARKVKRIVLLSGTP 361
Cdd:PRK04914 289 EAPS-REYQVVEQLAEVIPGVLLLTATP 315
|
|
| McrA |
COG1403 |
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms]; |
1131-1163 |
5.59e-03 |
|
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
Pssm-ID: 441013 [Multi-domain] Cd Length: 64 Bit Score: 36.50 E-value: 5.59e-03
10 20 30
....*....|....*....|....*....|...
gi 1366038577 1131 GNAWHADHLVPVYLGGGEcRLENMRTLCVACHS 1163
Cdd:COG1403 31 GDALEVDHIIPRSRGGTD-TWENLVLLCRRCNR 62
|
|
| rad25 |
TIGR00603 |
DNA repair helicase rad25; All proteins in this family for which functions are known are ... |
206-329 |
6.54e-03 |
|
DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273168 [Multi-domain] Cd Length: 732 Bit Score: 40.94 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVR--FGLQRGGRCLIADEMGLGKTLQAIAIACCFmsEGSILVVC-PAILRYSWAEELEHWlpfCLPADIHL- 281
Cdd:TIGR00603 256 IRPYQEKSLSkmFGNGRARSGIIVLPCGAGKSLVGVTAACTV--KKSCLVLCtSAVSVEQWKQQFKMW---STIDDSQIc 330
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1366038577 282 VFGHENnpanlKKWPR----VVVISYTMLHHLQKS----------MLDREWALLIVDESHHV 329
Cdd:TIGR00603 331 RFTSDA-----KERFHgeagVVVSTYSMVAHTGKRsyesekvmewLTNREWGLILLDEVHVV 387
|
|
| HNHc |
cd00085 |
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ... |
1126-1166 |
7.24e-03 |
|
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.
Pssm-ID: 238038 [Multi-domain] Cd Length: 57 Bit Score: 35.91 E-value: 7.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1366038577 1126 KDPTEGNAWHADHLVPVYlGGGECRLENMRTLCVACHSDVT 1166
Cdd:cd00085 18 GKPGGTEGLEVDHIIPLS-DGGNNDLDNLVLLCRKCHRKKH 57
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
206-430 |
1.29e-82 |
|
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: 269.07 E-value: 1.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSILVVCPAILRYSWAEELEHWLPFCLPADIHLVFGh 285
Cdd:cd18010 1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 286 eNNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVARKVKRIVLLSGTPSLSR 365
Cdd:cd18010 80 -SKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYL----KNSKAKRTKAALPLLKRAKRVILLSGTPALSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1366038577 366 PFDIFHQIDMLWPGLLGRDKFkFGETYCDAKyvrgvQGKVFQDFSKGTRLEELNMLLTRTVMIRR 430
Cdd:cd18010 155 PIELFTQLDALDPKLFGRFHD-FGRRYCAAK-----QGGFGWDYSGSSNLEELHLLLLATIMIRR 213
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
182-646 |
2.42e-76 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 267.48 E-value: 2.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 182 RPEHLLDDKVDELIGKLPKRLLDSLLPFQLEGVRF--GLQR-GGRCLIADEMGLGKTLQAIAIACCFMSEGS---ILVVC 255
Cdd:COG0553 218 AVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWllFLRRlGLGGLLADDMGLGKTIQALALLLELKERGLarpVLIVA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 256 PAILRYSWAEELEHWLPfCLPADIHlvFGHENNPANLKKWPR--VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctk 333
Cdd:COG0553 298 PTSLVGNWQRELAKFAP-GLRVLVL--DGTRERAKGANPFEDadLVITSYGLLRRDIELLAAVDWDLVILDEAQHI---- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 334 KKSEPREIKAVLDVarKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLLGrDKFKFGETYCDAKYVRGVQgkvfqdfskgt 413
Cdd:COG0553 371 KNPATKRAKAVRAL--KARHRLALTGTPVENRLEELWSLLDFLNPGLLG-SLKAFRERFARPIEKGDEE----------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 414 RLEELNMLLtRTVMIRRLKEHVLSQLPPKRRQIIQVVLKKsdivsAKAAIRvgkshdEDVSSEHLDELNDSMGcciskqL 493
Cdd:COG0553 437 ALERLRRLL-RPFLLRRTKEDVLKDLPEKTEETLYVELTP-----EQRALY------EAVLEYLRRELEGAEG------I 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 494 SHQELGIAKLAGFREwLSIHPVIAEADGV------AKL--------ESDSSSHKMLIFAHHHKVLDGVQEFIIHKEIDFV 559
Cdd:COG0553 499 RRRGLILAALTRLRQ-ICSHPALLLEEGAelsgrsAKLeallelleELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYA 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 560 RIDGNTLATDRQLAVRKFQLSSEVKIAIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYFFS 639
Cdd:COG0553 578 YLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLV 657
|
....*..
gi 1366038577 640 GKDTIDE 646
Cdd:COG0553 658 AEGTIEE 664
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
529-638 |
9.78e-36 |
|
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: 132.22 E-value: 9.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 529 SSSHKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQLSSEVKIAIVGITAGGVGLDFSSATHVVFL 608
Cdd:cd18793 25 EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAGGVGLNLTAANRVILY 104
|
90 100 110
....*....|....*....|....*....|
gi 1366038577 609 ELPQSPSLMLQAEDRAHRRGQTNAVNIYFF 638
Cdd:cd18793 105 DPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
206-378 |
2.90e-35 |
|
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: 132.69 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQR---GGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLPFCLPAD 278
Cdd:cd17919 1 LRPYQLEGLNFLLELyenGPGGILADEMGLGKTLQAIAFLAYLLKEgkerGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 279 IHLVFGHENNPANLKKWPR--VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVARkvKRIVL 356
Cdd:cd17919 81 YHGSQRERAQIRAKEKLDKfdVVLTTYETLRRDKASLRKFRWDLVVVDEAHRL----KNPKSQLSKALKALRA--KRRLL 154
|
170 180
....*....|....*....|..
gi 1366038577 357 LSGTPSLSRPFDIFHQIDMLWP 378
Cdd:cd17919 155 LTGTPLQNNLEELWALLDFLDP 176
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
206-385 |
8.45e-34 |
|
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: 129.33 E-value: 8.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQRG-GRCLIADEMGLGKTLQAIAIACCFMSEG---SILVVCPAILRYSWAEELEH--WLPF--CLPA 277
Cdd:cd18011 1 PLPHQIDAVLRALRKPpVRLLLADEVGLGKTIEAGLIIKELLLRGdakRVLILCPASLVEQWQDELQDkfGLPFliLDRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 278 DIHLVFGHENNPANLkkwPRVVVISYTMLH---HLQKSMLDREWALLIVDESHHVRCTKKKSEPREIKAVLDVARKVKRI 354
Cdd:cd18011 81 TAAQLRRLIGNPFEE---FPIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLGRLLAKRARHV 157
|
170 180 190
....*....|....*....|....*....|.
gi 1366038577 355 VLLSGTPSLSRPFDIFHQIDMLWPGLLGRDK 385
Cdd:cd18011 158 LLLTATPHNGKEEDFRALLSLLDPGRFAVLG 188
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
210-449 |
5.25e-25 |
|
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: 106.61 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 210 QLEGVRF------GLQRGgrCLIADEMGLGKTLQAIAI-----ACCFMSEGSILVVCPAILRYSWAEELEHWL-PFCLPA 277
Cdd:pfam00176 2 QIEGVNWmlslenNLGRG--GILADEMGLGKTLQTISLllylkHVDKNWGGPTLIVVPLSLLHNWMNEFERWVsPPALRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 278 DIHlvFGHENNPANLKKWPR------VVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKSepreIKAVLDVarKV 351
Cdd:pfam00176 80 VVL--HGNKRPQERWKNDPNfladfdVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKL----SKALKSL--KT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 352 KRIVLLSGTPSLSRPFDIFHQIDMLWPGLLG-----RDKF--KFGETYCDAKYVRgvqgkvfqdfskgtrleeLNMLLTR 424
Cdd:pfam00176 152 RNRWILTGTPLQNNLEELWALLNFLRPGPFGslstfRNWFdrPIERGGGKKGVSR------------------LHKLLKP 213
|
250 260
....*....|....*....|....*
gi 1366038577 425 TvMIRRLKEHVLSQLPPKRRQIIQV 449
Cdd:pfam00176 214 F-LLRRTKKDVEKSLPPKVEYILFC 237
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
206-418 |
3.64e-24 |
|
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: 102.75 E-value: 3.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRF----------GLQRGGRCLIADEMGLGKTLQAI----AIACCFMSEGSILVVCPAILRYSWAEELEHWL 271
Cdd:cd18007 1 LKPHQVEGVRFlwsnlvgtdvGSDEGGGCILAHTMGLGKTLQVItflhTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 272 PFCLPAD---IHLVFGH--ENNPANLKKW---PRVVVISYTML-------------HHLQ-KSMLDREWALLIVDESHHV 329
Cdd:cd18007 81 PPDLRPLlvlVSLSASKraDARLRKINKWhkeGGVLLIGYELFrnlasnattdprlKQEFiAALLDPGPDLLVLDEGHRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 330 RCTKKKsepreikaVLDVARKVK--RIVLLSGTPsLSRPFDIFHQ-IDMLWPGLLGR-DKFKfgetycdAKYVRGVQGKV 405
Cdd:cd18007 161 KNEKSQ--------LSKALSKVKtkRRILLTGTP-LQNNLKEYWTmVDFARPKYLGTlKEFK-------KKFVKPIEAGQ 224
|
250
....*....|...
gi 1366038577 406 FQDFSKGTRLEEL 418
Cdd:cd18007 225 CVDSTEEDVRLML 237
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
206-432 |
5.65e-24 |
|
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: 101.49 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFgLQR------GGrCLiADEMGLGKTLQAIAIACCFMSEGSI---LVVCPAILRYSWAEELEHWLPfclp 276
Cdd:cd18012 5 LRPYQKEGFNW-LSFlrhyglGG-IL-ADDMGLGKTLQTLALLLSRKEEGRKgpsLVVAPTSLIYNWEEEAAKFAP---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 277 aDIHLVFGHENNPANLKKWPR----VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVarKVK 352
Cdd:cd18012 78 -ELKVLVIHGTKRKREKLRALedydLVITSYGLLRRDIELLKEVKFHYLVLDEAQNI----KNPQTKTAKAVKAL--KAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 353 RIVLLSGTP---SLSRPFDIFhqiDMLWPGLLG-RDKFKfgetycdAKYVRGVqgkvfQDFSKGTRLEELnMLLTRTVMI 428
Cdd:cd18012 151 HRLALTGTPienHLGELWSIF---DFLNPGLLGsYKRFK-------KRFAKPI-----EKDGDEEALEEL-KKLISPFIL 214
|
....
gi 1366038577 429 RRLK 432
Cdd:cd18012 215 RRLK 218
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
198-362 |
9.87e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.56 E-value: 9.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 198 LPKRLLDSLLPFQLEGVRFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGS---ILVVCP-AILRYSWAEELEHWLPF 273
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAALLPALEALKRGKggrVLVLVPtRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 274 cLPADIHLVFGHENNPANLKKW----PRVVVISY-TMLHHLQKSMLD-REWALLIVDESHHvrcTKKKSEPREIKAVLDV 347
Cdd:smart00487 81 -LGLKVVGLYGGDSKREQLRKLesgkTDILVTTPgRLLDLLENDKLSlSNVDLVILDEAHR---LLDGGFGDQLEKLLKL 156
|
170
....*....|....*
gi 1366038577 348 ARKVKRIVLLSGTPS 362
Cdd:smart00487 157 LPKNVQLLLLSATPP 171
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
225-646 |
9.66e-22 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 102.57 E-value: 9.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 225 LIADEMGLGKTLQAIAIACcFMSE-----GSILVVCPAILRYSWAEELEHWLPFCLPADIHlvfGHENNPANLKKWP--- 296
Cdd:PLN03142 192 ILADEMGLGKTLQTISLLG-YLHEyrgitGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFH---GNPEERAHQREELlva 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 297 ---RVVVISYTMLHHlQKSMLDR-EWALLIVDESHHVrctkkKSEPREIKAVLDVARKVKRIvLLSGTPSLSRPFDIFHQ 372
Cdd:PLN03142 268 gkfDVCVTSFEMAIK-EKTALKRfSWRYIIIDEAHRI-----KNENSLLSKTMRLFSTNYRL-LITGTPLQNNLHELWAL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 373 IDMLWPGLLGrDKFKFGETYCDAKyvRGVQGKVFQDFSKgtrleelnmlLTRTVMIRRLKEHVLSQLPPKRRQIIQVVLK 452
Cdd:PLN03142 341 LNFLLPEIFS-SAETFDEWFQISG--ENDQQEVVQQLHK----------VLRPFLLRRLKSDVEKGLPPKKETILKVGMS 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 453 KSDIVSAKAAIRvgksHDEDV---SSEHLDELNDSM---GCCiskqlSHQELGIAKLAGFREWLSIHPViaEADG----- 521
Cdd:PLN03142 408 QMQKQYYKALLQ----KDLDVvnaGGERKRLLNIAMqlrKCC-----NHPYLFQGAEPGPPYTTGEHLV--ENSGkmvll 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 522 ---VAKLESDSSshKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKF-QLSSEVKIAIVGITAGGVGL 597
Cdd:PLN03142 477 dklLPKLKERDS--RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFnKPGSEKFVFLLSTRAGGLGI 554
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1366038577 598 DFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYFFSGKDTIDE 646
Cdd:PLN03142 555 NLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEE 603
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
206-392 |
1.08e-19 |
|
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: 89.33 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGV-------RFGLQRggrcLIADEMGLGKTLQAIAI--ACCFMSEGSI-------LVVCPAILRYSWAEELEH 269
Cdd:cd17999 1 LRPYQQEGInwlaflnKYNLHG----ILCDDMGLGKTLQTLCIlaSDHHKRANSFnsenlpsLVVCPPTLVGHWVAEIKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 270 WLPFCLPADIHLVfGHENNPANLKKWP---RVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKSepreIKAVLD 346
Cdd:cd17999 77 YFPNAFLKPLAYV-GPPQERRRLREQGekhNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL----SKAVKQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1366038577 347 VARKvKRIVlLSGTPSLSRPFDIFHQIDMLWPGLLGRDKfKFGETY 392
Cdd:cd17999 152 LKAN-HRLI-LSGTPIQNNVLELWSLFDFLMPGYLGTEK-QFQRRF 194
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
206-430 |
2.55e-19 |
|
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: 88.50 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQR--------GGRCLIADEMGLGKTLQAIAIACCFMSEG--------SILVVCPAILRYSWAEELEH 269
Cdd:cd18004 1 LRPHQREGVQFLYDCltgrrgygGGGAILADEMGLGKTLQAIALVWTLLKQGpygkptakKALIVCPSSLVGNWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 270 WLPFCLPADIHLVFGHENNPANLKK------WPrVVVISY-TMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIK 342
Cdd:cd18004 81 WLGLRRIKVVTADGNAKDVKASLDFfssastYP-VLIISYeTLRRHAEKLSKKISIDLLICDEGHRL----KNSESKTTK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 343 AVLdvARKVKRIVLLSGTPsLSRPFDIFHQ-IDMLWPGLLG-RDKFKfgeTYCDAKYVRGVQ-GKVFQDFSKGT-RLEEL 418
Cdd:cd18004 156 ALN--SLPCRRRLLLTGTP-IQNDLDEFFAlVDFVNPGILGsLASFR---KVFEEPILRSRDpDASEEDKELGAeRSQEL 229
|
250
....*....|..
gi 1366038577 419 NmLLTRTVMIRR 430
Cdd:cd18004 230 S-ELTSRFILRR 240
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
522-628 |
1.09e-17 |
|
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: 79.95 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 522 VAKLESDSSSHKMLIFAHHHKVLDgVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVGLDFSS 601
Cdd:pfam00271 6 LLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFR-KGKIDV-LVATDVAERGLDLPD 82
|
90 100
....*....|....*....|....*..
gi 1366038577 602 ATHVVFLELPQSPSLMLQAEDRAHRRG 628
Cdd:pfam00271 83 VDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
206-387 |
2.82e-17 |
|
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: 82.90 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRF------GLQRGGR--CLIADEMGLGKTLQAIAIACCFMSEGSI--------LVVCPAILRYSWAEELEH 269
Cdd:cd18067 1 LRPHQREGVKFlyrcvtGRRIRGShgCIMADEMGLGKTLQCITLMWTLLRQSPQckpeidkaIVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 270 WLP---FCLPADihlvfG--HENNPANLKKWPR---------VVVISYTMLH----HLQKSmldrEWALLIVDESHHVrc 331
Cdd:cd18067 81 WLGgrlQPLAID-----GgsKKEIDRKLVQWASqqgrrvstpVLIISYETFRlhveVLQKG----EVGLVICDEGHRL-- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 332 tkKKSEPREIKAVLDVarKVKRIVLLSGTP---SLSRPFDIFHQIDmlwPGLLG-RDKFK 387
Cdd:cd18067 150 --KNSDNQTYQALDSL--NTQRRVLLSGTPiqnDLSEYFSLVNFVN---PGILGtAAEFK 202
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
206-430 |
1.01e-16 |
|
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: 81.27 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRF---GLQRGGRCLIADEMGLGKTLQAIA-----------------IACCFMSEGS-------ILVVCPAI 258
Cdd:cd18005 1 LRDYQREGVEFmydLYKNGRGGILGDDMGLGKTVQVIAflaavlgktgtrrdrenNRPRFKKKPPassakkpVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 259 LRYSWAEELEHWLPFCLpADIHLVfGHENNPANLKKWPR--VVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKS 336
Cdd:cd18005 81 VLYNWKDELDTWGHFEV-GVYHGS-RKDDELEGRLKAGRleVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 337 EpreiKAVLDVarKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLLG-RDKFKfgETYCDAKYVRGVQGKVFQDFSKGTRL 415
Cdd:cd18005 159 T----QAMKEL--KCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGsRSQFK--KHFSEPIKRGQRHTATARELRLGRKR 230
|
250
....*....|....*
gi 1366038577 416 EELNMLLTRTVMIRR 430
Cdd:cd18005 231 KQELAVKLSKFFLRR 245
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
206-361 |
1.84e-16 |
|
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: 78.90 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQRGGRC---LIADEMGLGKTLQAIA----IACCFMSEGSILVVCPAILRYSWAEELEHWLPFCLPAD 278
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRvggILGDEMGLGKTIQIIAflaaLHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 279 IH-------------LVFGHENNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKksepreikavl 345
Cdd:cd18000 81 LHssgsgtgseeklgSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDA----------- 149
|
170 180
....*....|....*....|.
gi 1366038577 346 DVARKVKRI-----VLLSGTP 361
Cdd:cd18000 150 EITLACKQLrtphrLILSGTP 170
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
206-430 |
2.93e-16 |
|
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: 78.64 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGV---RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLPfclpaD 278
Cdd:cd17994 1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEghskGPFLVSAPLSTIINWEREFEMWAP-----D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 279 IHLVFGHENNpanlkkwprVVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKKKSEPREIKAVLDVARKvkriVLLS 358
Cdd:cd17994 76 FYVVTYVGDH---------VLLTSYELISIDQAILGSIDWAVLVVDEAH--RLKNNQSKFFRILNSYKIGYK----LLLT 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1366038577 359 GTPSLSRPFDIFHQIDMLWPgllgrDKFKFGETYCDAkyvrgvqgkvFQDFSKGTRLEELNMLLTRTvMIRR 430
Cdd:cd17994 141 GTPLQNNLEELFHLLNFLTP-----ERFNNLQGFLEE----------FADISKEDQIKKLHDLLGPH-MLRR 196
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
206-430 |
5.88e-16 |
|
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: 78.87 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQRGGrcLIADEMGLGKTLQAIAIACCFMSEGSI---------------------LVVCPAILRYSWA 264
Cdd:cd18008 1 LLPYQKQGLAWMLPRGG--ILADEMGLGKTIQALALILATRPQDPKipeeleenssdpkklylskttLIVVPLSLLSQWK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 265 EELE-HWLPFCLPADIHLVFGHENNPANLKKwPRVVVISYTML----------------HHLQKSMLDREWALLIVDESH 327
Cdd:cd18008 79 DEIEkHTKPGSLKVYVYHGSKRIKSIEELSD-YDIVITTYGTLasefpknkkgggrdskEKEASPLHRIRWYRVILDEAH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 328 HVRCTK-KKSepreiKAVLDVarKVKRIVLLSGTPSLSRpfdifhqIDMLWPgllgrdKFKFG--ETYCDAKYVRGVQGK 404
Cdd:cd18008 158 NIKNRStKTS-----RAVCAL--KAERRWCLTGTPIQNS-------LDDLYS------LLRFLrvEPFGDYPWFNSDISK 217
|
250 260
....*....|....*....|....*.
gi 1366038577 405 VFQDFSKGtRLEELNMLLtRTVMIRR 430
Cdd:cd18008 218 PFSKNDRK-ALERLQALL-KPILLRR 241
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
206-361 |
2.59e-15 |
|
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: 76.66 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGL---QRGGRCLIADEMGLGKTLQAIAIACCfMSE----GSILVVCPAILRYSWAEELEHWLPfCLPAD 278
Cdd:cd18009 4 MRPYQLEGMEWLRmlwENGINGILADEMGLGKTIQTIALLAH-LRErgvwGPFLVIAPLSTLPNWVNEFARFTP-SVPVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 279 IH---------LVFGHENNPANLKKWPrVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVAR 349
Cdd:cd18009 82 LYhgtkeererLRKKIMKREGTLQDFP-VVVTSYEIAMRDRKALQHYAWKYLIVDEGHRL----KNLNCRLIQELKTFNS 156
|
170
....*....|..
gi 1366038577 350 KVKriVLLSGTP 361
Cdd:cd18009 157 DNR--LLLTGTP 166
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
208-394 |
9.74e-15 |
|
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: 74.69 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 208 PFQLEGVRFGLQRGGRCLIADeMGLGKTLQAI-AIACCFMSE--GSILVVCPA-ILRYSWAEELEHW-LPFCLPADIHLV 282
Cdd:cd18013 3 PYQKVAINFIIEHPYCGLFLD-MGLGKTVTTLtALSDLQLDDftRRVLVIAPLrVARSTWPDEVEKWnHLRNLTVSVAVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 283 FGHENNPAnLKKWPRVVVISYTMLHHLQKSMLDR-EWALLIVDESHhvrcTKKKSEPREIKAVLDVARKVKRIVLLSGTP 361
Cdd:cd18013 82 TERQRSKA-ANTPADLYVINRENLKWLVNKSGDPwPFDMVVIDELS----SFKSPRSKRFKALRKVRPVIKRLIGLTGTP 156
|
170 180 190
....*....|....*....|....*....|....
gi 1366038577 362 SLSRPFDIFHQIDMLWPG-LLGRDKFKFGETYCD 394
Cdd:cd18013 157 SPNGLMDLWAQIALLDQGeRLGRSITAYRERWFD 190
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
206-396 |
1.98e-14 |
|
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: 73.82 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGL-----QRGgrCLIADEMGLGKTLQAIAIACCFMSEGSI----LVVCPAILRYSWAEELEHWlpfclp 276
Cdd:cd17995 1 LRDYQLEGVNWLLfnwynRRN--CILADEMGLGKTIQSIAFLEHLYQVEGIrgpfLVIAPLSTIPNWQREFETW------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 277 ADIHLVFGHEN-------------NPANLKKWPR------VVVISYTMLhhlqksMLDRE------WALLIVDESHHVRC 331
Cdd:cd17995 73 TDMNVVVYHGSgesrqiiqqyemyFKDAQGRKKKgvykfdVLITTYEMV------IADAEelrkipWRVVVVDEAHRLKN 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1366038577 332 TKKKsepreikaVLDVARKVK--RIVLLSGTPslsrpfdIFHQIDMLWPGL--LGRDKF----KFGETYCDAK 396
Cdd:cd17995 147 RNSK--------LLQGLKKLTleHKLLLTGTP-------LQNNTEELWSLLnfLEPEKFpsseEFLEEFGDLK 204
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
206-382 |
2.38e-14 |
|
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: 74.11 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRF------GLQRGGR--CLIADEMGLGKTLQAIAIACCFMSEG---------SILVVCPAILRYSWAEELE 268
Cdd:cd18066 1 LRPHQREGIEFlyecvmGMRVNERfgAILADEMGLGKTLQCISLIWTLLRQGpyggkpvikRALIVTPGSLVKNWKKEFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 269 HWLP------FCLPADiHLVFGHENNPANlkkwpRVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKSepreiK 342
Cdd:cd18066 81 KWLGserikvFTVDQD-HKVEEFIASPLY-----SVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKT-----T 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1366038577 343 AVLDVARKVKRIVlLSGTPSLSRPFDIFHQIDMLWPGLLG 382
Cdd:cd18066 150 TALTSLSCERRII-LTGTPIQNDLQEFFALIDFVNPGILG 188
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
547-628 |
2.41e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.16 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 547 VQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHR 626
Cdd:smart00490 3 LAELLKELGIKVARLHGGLSQEEREEILDKFN-NGKIKV-LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1366038577 627 RG 628
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
205-627 |
5.55e-14 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 76.60 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 205 SLLPFQLEGV----RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSILVVCPAI-LRYSWAEELEHWLPfclpaDI 279
Cdd:COG1061 80 ELRPYQQEALeallAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRReLLEQWAEELRRFLG-----DP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 280 HLVFGHENNPAnlkkwpRVVVISY-TMLHHLQKSMLDREWALLIVDESHHVRctkkksePREIKAVLDvARKVKRIVLLS 358
Cdd:COG1061 155 LAGGGKKDSDA------PITVATYqSLARRAHLDELGDRFGLVIIDEAHHAG-------APSYRRILE-AFPAAYRLGLT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 359 GTP--SLSRPFDIFHQIdmlwpgllgrdkfkfgetycdakyvrgvqGKVFqdfskGTRLEELnmlltrtvmirrLKEHVL 436
Cdd:COG1061 221 ATPfrSDGREILLFLFD-----------------------------GIVY-----EYSLKEA------------IEDGYL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 437 SqlpPKRRQIIQVVLKKsdivsakaairvgKSHDEDVSSEHLDelndsmgccisKQLSHQElgIAKLAGFREWLSIHPvi 516
Cdd:COG1061 255 A---PPEYYGIRVDLTD-------------ERAEYDALSERLR-----------EALAADA--ERKDKILRELLREHP-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 517 aeadgvaklesdsSSHKMLIFAHHHKVLDGVQEFIIHKEIDFVRIDGNTLATDRQLAVRKFQlSSEVKIaIVGITAGGVG 596
Cdd:COG1061 304 -------------DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR-DGELRI-LVTVDVLNEG 368
|
410 420 430
....*....|....*....|....*....|.
gi 1366038577 597 LDFSSATHVVFLELPQSPSLMLQAEDRAHRR 627
Cdd:COG1061 369 VDVPRLDVAILLRPTGSPREFIQRLGRGLRP 399
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
206-430 |
7.33e-14 |
|
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: 72.40 E-value: 7.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGV---RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLPfclpaD 278
Cdd:cd18057 1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEghskGPYLVSAPLSTIINWEREFEMWAP-----D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 279 IHLV----------------FGHENNPA-------NLKKWPR----VVVISYTMLHHLQKSMLDREWALLIVDESHHVRC 331
Cdd:cd18057 76 FYVVtytgdkesrsvireneFSFEDNAIrsgkkvfRMKKEAQikfhVLLTSYELITIDQAILGSIEWACLVVDEAHRLKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 332 TKKKsepreIKAVLDvARKVKRIVLLSGTPSLSRPFDIFHQIDMLWPgllgrDKFKFGETYCDAkyvrgvqgkvFQDFSK 411
Cdd:cd18057 156 NQSK-----FFRVLN-SYKIDYKLLLTGTPLQNNLEELFHLLNFLTP-----ERFNNLEGFLEE----------FADISK 214
|
250
....*....|....*....
gi 1366038577 412 GTRLEELNMLLTRTvMIRR 430
Cdd:cd18057 215 EDQIKKLHDLLGPH-MLRR 232
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
206-443 |
3.18e-13 |
|
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: 70.85 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGL---QRGGRCLIADEMGLGKTLQAIAIaCCFMSE-----GSILVVCPAILRYSWAEELEHWLP----F 273
Cdd:cd18064 16 LRDYQVRGLNWLIslyENGINGILADEMGLGKTLQTISL-LGYMKHyrnipGPHMVLVPKSTLHNWMAEFKRWVPtlraV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 274 CLPADIHLVFGHENNPANLKKWPrVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkkKSEPREIKAVLDVARKVKR 353
Cdd:cd18064 95 CLIGDKDQRAAFVRDVLLPGEWD-VCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRI-----KNEKSKLSEIVREFKTTNR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 354 IvLLSGTPSLSRPFDIFHQIDMLWPGLLGR-DKFkfgETYCDAKYVRGVQGKVfqdfskgtrlEELNMLLtRTVMIRRLK 432
Cdd:cd18064 169 L-LLTGTPLQNNLHELWALLNFLLPDVFNSaEDF---DSWFDTNNCLGDQKLV----------ERLHMVL-RPFLLRRIK 233
|
250
....*....|.
gi 1366038577 433 EHVLSQLPPKR 443
Cdd:cd18064 234 ADVEKSLPPKK 244
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
225-361 |
2.02e-12 |
|
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: 68.15 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 225 LIADEMGLGKTLQAIAI----ACCFMSEGSILVVCPAILRYSWAEELEHWLPfCLpaDIHLVFGhenNPANLKK----WP 296
Cdd:cd18003 23 ILADEMGLGKTIQTIALlahlACEKGNWGPHLIVVPTSVMLNWEMEFKRWCP-GF--KILTYYG---SAKERKLkrqgWM 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 297 R-----VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVarKVKRIVLLSGTP 361
Cdd:cd18003 97 KpnsfhVCITSYQLVVQDHQVFKRKKWKYLILDEAHNI----KNFKSQRWQTLLNF--NTQRRLLLTGTP 160
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
206-430 |
2.67e-12 |
|
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: 67.46 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQR---GGRCLIADEMGLGKTLQAIAI----ACCFMSEGSILVVCPAILRYSWAEELEHWLP------ 272
Cdd:cd18006 1 LRPYQLEGVNWLLQCraeQHGCILGDEMGLGKTCQTISLlwylAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPdlsvit 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 273 --------FCLPADIhlvfgHENNPANlkkwprVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkkKSEPREIKAV 344
Cdd:cd18006 81 ymgdkekrLDLQQDI-----KSTNRFH------VLLTTYEICLKDASFLKSFPWASLVVDEAHRL-----KNQNSLLHKT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 345 LDvARKVKRIVLLSGTP---SLSRPFDIFHQIDmlwPGLLGRDKFKfgetycdaKYVrgvqgKVFQDFSKGTRL-EELNM 420
Cdd:cd18006 145 LS-EFSVDFRLLLTGTPiqnSLQELYALLSFIE---PNVFPKDKLD--------DFI-----KAYSETDDESETvEELHL 207
|
250
....*....|
gi 1366038577 421 LLtRTVMIRR 430
Cdd:cd18006 208 LL-QPFLLRR 216
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
206-387 |
2.89e-12 |
|
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: 67.78 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRF--GL---QRGGrcLIADEMGLGKTLQAIA-IACCFMSE--GSILVVCPAILRYSWAEELEHWLPfclpa 277
Cdd:cd18001 1 LYPHQREGVAWlwSLhdgGKGG--ILADDMGLGKTVQICAfLSGMFDSGliKSVLVVMPTSLIPHWVKEFAKWTP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 278 DIHLVFGHENNPANLKKWPR-------VVVISYTML--HHLQKSMLDRE---WALLIVDESHHVRCTKKKSEpreiKAVL 345
Cdd:cd18001 74 GLRVKVFHGTSKKERERNLEriqrgggVLLTTYGMVlsNTEQLSADDHDefkWDYVILDEGHKIKNSKTKSA----KSLR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1366038577 346 DVARKVKriVLLSGTP---SLSRPFDIFhqiDMLWPG-LLG-RDKFK 387
Cdd:cd18001 150 EIPAKNR--IILTGTPiqnNLKELWALF---DFACNGsLLGtRKTFK 191
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
209-430 |
3.73e-11 |
|
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: 64.65 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 209 FQLEGV---RFGLQRGGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLPfclpaDIHL 281
Cdd:cd18055 4 YQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEghtkGPFLVSAPLSTIINWEREFQMWAP-----DFYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 282 V----------------FGHENNPANLKKWP-----------RVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKK 334
Cdd:cd18055 79 VtytgdkdsraiireneFSFDDNAVKGGKKAfkmkreaqvkfHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 335 KsepreIKAVLDvARKVKRIVLLSGTPSLSRPFDIFHQIDMLWPgllgrDKFKFGETYCDAkyvrgvqgkvFQDFSKGTR 414
Cdd:cd18055 159 K-----FFRVLN-GYKIDHKLLLTGTPLQNNLEELFHLLNFLTP-----ERFNNLEGFLEE----------FADISKEDQ 217
|
250
....*....|....*.
gi 1366038577 415 LEELNMLLTRTvMIRR 430
Cdd:cd18055 218 IKKLHDLLGPH-MLRR 232
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
220-370 |
4.50e-11 |
|
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: 64.41 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 220 RGGrcLIADEMGLGKTLQAIA-IACCFMsegsiLVVCPAILRYSWAEEL-EHWLPFCLpaDIHLVFGHENN--PANLKKW 295
Cdd:cd18071 49 RGG--ILADDMGLGKTLTTISlILANFT-----LIVCPLSVLSNWETQFeEHVKPGQL--KVYTYHGGERNrdPKLLSKY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 296 PrVVVISYTMLHHLQKSMLDR-----EWALLIVDESHHVRCTKKKseprEIKAVLDVarKVKRIVLLSGTPSLSRPFDIF 370
Cdd:cd18071 120 D-IVLTTYNTLASDFGAKGDSplhtiNWLRVVLDEGHQIRNPNAQ----QTKAVLNL--SSERRWVLTGTPIQNSPKDLG 192
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
206-378 |
6.67e-11 |
|
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: 63.93 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGV---RFGLQRGGRCLIADEMGLGKTLQ-AIAIACCFM---SEGSILVVCPAILRYSWAEELEHWLPfclpaD 278
Cdd:cd18056 1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQtAVFLYSLYKeghSKGPFLVSAPLSTIINWEREFEMWAP-----D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 279 IHLV----------------FGHENN-------PANLKKWP----RVVVISYTMLHHLQKSMLDREWALLIVDESHHVRC 331
Cdd:cd18056 76 MYVVtyvgdkdsraiireneFSFEDNairggkkASRMKKEAsvkfHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1366038577 332 TKKKsepreIKAVLDvARKVKRIVLLSGTPSLSRPFDIFHQIDMLWP 378
Cdd:cd18056 156 NQSK-----FFRVLN-GYSLQHKLLLTGTPLQNNLEELFHLLNFLTP 196
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
225-361 |
7.84e-11 |
|
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: 63.49 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 225 LIADEMGLGKTLQAIAIaCCFMSE-----GSILVVCPAILRYSWAEELEHWLPFCLPADIHlvfGHENNPANL------- 292
Cdd:cd17997 26 ILADEMGLGKTLQTISL-LGYLKHykninGPHLIIVPKSTLDNWMREFKRWCPSLRVVVLI---GDKEERADIirdvllp 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 293 KKWPrVVVISYTMLHHlQKSMLDR-EWALLIVDESHhvRCTKKKSEPREIKAVLDVARKvkriVLLSGTP 361
Cdd:cd17997 102 GKFD-VCITSYEMVIK-EKTVLKKfNWRYIIIDEAH--RIKNEKSKLSQIVRLFNSRNR----LLLTGTP 163
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
225-361 |
1.10e-10 |
|
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: 63.16 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 225 LIADEMGLGKTLQAIAIACCFM----SEGSILVVCPAILRYSWAEELEHWLP------FCLPADIHLVFGHENNPANLKk 294
Cdd:cd17996 26 ILADEMGLGKTIQTISLITYLMekkkNNGPYLVIVPLSTLSNWVSEFEKWAPsvskivYKGTPDVRKKLQSQIRAGKFN- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1366038577 295 wprVVVISYTMLHHlQKSMLDR-EWALLIVDESHHVRCTKKKsepreIKAVLDVARKVKRIVLLSGTP 361
Cdd:cd17996 105 ---VLLTTYEYIIK-DKPLLSKiKWKYMIIDEGHRMKNAQSK-----LTQTLNTYYHARYRLLLTGTP 163
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
206-361 |
3.21e-10 |
|
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: 62.36 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQRGGrcLIADEMGLGKTLQAIA------------------------IACCFMSE-----GSILVVCP 256
Cdd:cd18070 1 LLPYQRRAVNWMLVPGG--ILADEMGLGKTVEVLAlillhprpdndldaadddsdemvcCPDCLVAEtpvssKATLIVCP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 257 AILRYSWAEELEHWLPFCLPADIHlvFGHENNPANLKKWPR------VVVISYTML----HH------------LQKSML 314
Cdd:cd18070 79 SAILAQWLDEINRHVPSSLKVLTY--QGVKKDGALASPAPEilaeydIVVTTYDVLrtelHYaeanrsnrrrrrQKRYEA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1366038577 315 DR------EWALLIVDESHHVRCTKKKSEpreikavlDVARKVKRIV--LLSGTP 361
Cdd:cd18070 157 PPsplvlvEWWRVCLDEAQMVESSTSKAA--------EMARRLPRVNrwCVSGTP 203
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
209-361 |
3.48e-10 |
|
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: 61.22 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 209 FQLEGVRFGLQ---RGGRCLIADEMGLGKTLQAIaiacCFMS--------EGSILVVCPAILRYSWAEELEHWLPfclpa 277
Cdd:cd17993 5 YQLTGLNWLAHswcKGNNGILADEMGLGKTVQTI----SFLSylfhsqqqYGPFLVVVPLSTMPAWQREFAKWAP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 278 DIHLV--FGHENNPANLKKWP-----------RVVVISYTMLhhLQ-KSMLDR-EWALLIVDESHHVrctkKKSEPREIK 342
Cdd:cd17993 76 DMNVIvyLGDIKSRDTIREYEfyfsqtkklkfNVLLTTYEII--LKdKAFLGSiKWQYLAVDEAHRL----KNDESLLYE 149
|
170
....*....|....*....
gi 1366038577 343 AVLDVarKVKRIVLLSGTP 361
Cdd:cd17993 150 ALKEF--KTNNRLLITGTP 166
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
225-361 |
7.24e-10 |
|
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: 60.60 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 225 LIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLP--FCLPadihlVFGHENNPANLKK-WPR 297
Cdd:cd18002 23 ILADEMGLGKTVQSIAVLAHLAEEhniwGPFLVIAPASTLHNWQQEISRFVPqfKVLP-----YWGNPKDRKVLRKfWDR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1366038577 298 -----------VVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLdvARKVKRIVLLSGTP 361
Cdd:cd18002 98 knlytrdapfhVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAI----KSSSSSRWKTLL--SFHCRNRLLLTGTP 166
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
206-386 |
2.00e-09 |
|
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: 59.44 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRF-------GLQR-----GGRCLIADEMGLGKTLQAIAIACCFM---SEGSILVVCPAILRYSWAEELEHW 270
Cdd:cd18069 1 LKPHQIGGIRFlydniieSLERykgssGFGCILAHSMGLGKTLQVISFLDVLLrhtGAKTVLAIVPVNTLQNWLSEFNKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 271 LP--------FCLPADIHLVF-GHENNPANLK---KWPR---VVVISYTMLHhlqksmLDREWALLIVDESHHVRCTKKk 335
Cdd:cd18069 81 LPppealpnvRPRPFKVFILNdEHKTTAARAKvieDWVKdggVLLMGYEMFR------LRPGPDVVICDEGHRIKNCHA- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1366038577 336 seprEIKAVLDVARKVKRIVlLSGTPSLSRPFDIFHQIDMLWPGLLG-RDKF 386
Cdd:cd18069 154 ----STSQALKNIRSRRRIV-LTGYPLQNNLIEYWCMVDFVRPDFLGtRQEF 200
|
|
| DpdE |
NF041062 |
protein DpdE; |
223-366 |
2.42e-09 |
|
protein DpdE;
Pssm-ID: 468989 [Multi-domain] Cd Length: 1048 Bit Score: 61.91 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 223 RCLIADEMGLGKTLQA-IAIACCFM--SEGSILVVCPAILRYSWAEELE---HWLPFcLPADIHLVfGHEnNPANLKKWP 296
Cdd:NF041062 172 RYLLADEVGLGKTIEAgLVIRQHLLdnPDARVLVLVPDALVRQWRRELRdkfFLDDF-PGARVRVL-SHE-EPERWEPLL 248
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1366038577 297 RVVvisytmlhhlqksmldrewALLIVDESHHVRCTKKKSEPREI---KAVLDVARKVKRIVLLSGTPSLSRP 366
Cdd:NF041062 249 DAP-------------------DLLVVDEAHQLARLAWSGDPPERaryRELAALAHAAPRLLLLSATPVLGNE 302
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
182-394 |
6.56e-09 |
|
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: 58.09 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 182 RPEHLLDDKVDELIGKLPKRLLDsllpFQLEGVRFGLQRGGRC---LIADEMGLGKTLQAIAIACCFMSE----GSILVV 254
Cdd:cd18054 1 RPRFVALKKQPSYIGGENLELRD----YQLEGLNWLAHSWCKNnsvILADEMGLGKTIQTISFLSYLFHQhqlyGPFLLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 255 CPAILRYSWAEELEHWLPfclpaDIHLV--FGHENNPANLKKWP-----------RVVVISYTMLHHLQKSMLDREWALL 321
Cdd:cd18054 77 VPLSTLTSWQREFEIWAP-----EINVVvyIGDLMSRNTIREYEwihsqtkrlkfNALITTYEILLKDKTVLGSINWAFL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1366038577 322 IVDESHHVrctkKKSEPREIKAVLDVarKVKRIVLLSGTP---SLSRPFDIFHqidMLWPgllgrDKFKFGETYCD 394
Cdd:cd18054 152 GVDEAHRL----KNDDSLLYKTLIDF--KSNHRLLITGTPlqnSLKELWSLLH---FIMP-----EKFEFWEDFEE 213
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
205-432 |
8.69e-09 |
|
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: 57.33 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 205 SLLPFQLEGVRFGL---QRGGRCLIADEMGLGKTLQAIAIACCFMS----EGSILVVCPAILRYSWAEELEHWLP----F 273
Cdd:cd18065 15 TLRDYQVRGLNWMIslyENGVNGILADEMGLGKTLQTIALLGYLKHyrniPGPHMVLVPKSTLHNWMNEFKRWVPslraV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 274 CLPADIHLVFGHENNPANLKKWPrVVVISYTMLHHLQKSMLDREWALLIVDESHHVRCTKKKsepreikaVLDVARKVKR 353
Cdd:cd18065 95 CLIGDKDARAAFIRDVMMPGEWD-VCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSK--------LSEIVREFKT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 354 I--VLLSGTPSLSRPFDIFHQIDMLWPGLLGR-DKFkfgETYCDAKYVRGVQGKVfqdfskgtrlEELNMLLtRTVMIRR 430
Cdd:cd18065 166 TnrLLLTGTPLQNNLHELWALLNFLLPDVFNSaDDF---DSWFDTKNCLGDQKLV----------ERLHAVL-KPFLLRR 231
|
..
gi 1366038577 431 LK 432
Cdd:cd18065 232 IK 233
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
225-381 |
9.83e-09 |
|
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: 57.75 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 225 LIADEMGLGKTLQAIAIACCFMS----EGSILVVCPAILRYSWAEELEHWLPFCLPADihlvfgHENNPANLKKWP---- 296
Cdd:cd18062 46 ILADEMGLGKTIQTIALITYLMEhkriNGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS------YKGSPAARRAFVpqlr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 297 ----RVVVISYTMLHHLQKSMLDREWALLIVDESHhvrctKKKSEPREIKAVLDVARKVKRIVLLSGTPSLSRPFDIFHQ 372
Cdd:cd18062 120 sgkfNVLLTTYEYIIKDKQILAKIRWKYMIVDEGH-----RMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWAL 194
|
....*....
gi 1366038577 373 IDMLWPGLL 381
Cdd:cd18062 195 LNFLLPTIF 203
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
206-373 |
1.78e-08 |
|
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: 56.60 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGLQ---RGGRCLIADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYSWAEELEHWLP----FC 274
Cdd:cd18053 21 LRDYQLNGLNWLAHswcKGNSCILADEMGLGKTIQTISFLNYLFHEhqlyGPFLLVVPLSTLTSWQREIQTWAPqmnaVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 275 LPADI---HLVFGHE-NNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHHVrctkKKSEPREIKAVLDVarK 350
Cdd:cd18053 101 YLGDInsrNMIRTHEwMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRL----KNDDSLLYKTLIDF--K 174
|
170 180
....*....|....*....|....*.
gi 1366038577 351 VKRIVLLSGTP---SLSRPFDIFHQI 373
Cdd:cd18053 175 SNHRLLITGTPlqnSLKELWSLLHFI 200
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
221-360 |
5.12e-08 |
|
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: 53.18 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 221 GGRCLIADEMGLGKTLQA-IAIACCFMSEGS-ILVVCPAI-LRYSWAEELEHWLPfcLPADIHLVFGHENNPANLKKW-- 295
Cdd:cd00046 1 GENVLITAPTGSGKTLAAlLAALLLLLKKGKkVLVLVPTKaLALQTAERLRELFG--PGIRVAVLVGGSSAEEREKNKlg 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1366038577 296 -PRVVVISYTMLHHLQKSML---DREWALLIVDESHHVRcTKKKSEPREIKAVLDVARKVKRIVLLSGT 360
Cdd:cd00046 79 dADIIIATPDMLLNLLLREDrlfLKDLKLIIVDEAHALL-IDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
206-385 |
5.74e-08 |
|
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: 55.28 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRF-------GLQR-----GGRCLIADEMGLGKTLQAIA----IACCFMSEG--SILVVCPAILRYSWAEEL 267
Cdd:cd18068 1 LKPHQVDGVQFmwdccceSLKKtkkspGSGCILAHCMGLGKTLQVVTflhtVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 268 EHWLPFCLP------ADIHLVFGHENNPANLKKW---PRVVVISYTMLHHL----------------QKSMLDREWALLI 322
Cdd:cd18068 81 EKWQEGLKDeekievNELATYKRPQERSYKLQRWqeeGGVMIIGYDMYRILaqernvksreklkeifNKALVDPGPDFVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1366038577 323 VDESHhvrctKKKSEPREI-KAVLDVarKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLLGRDK 385
Cdd:cd18068 161 CDEGH-----ILKNEASAVsKAMNSI--RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIK 217
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
206-361 |
7.10e-08 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are 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: 350684 [Multi-domain] Cd Length: 146 Bit Score: 53.08 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVR--FGLQRGGRCLIADEMGLGKTLQAIAIACCFmSEGSILVVCPAI-LRYSWAEELEHWLPfclPADIHLV 282
Cdd:cd17926 1 LRPYQEEALEawLAHKNNRRGILVLPTGSGKTLTALALIAYL-KELRTLIVVPTDaLLDQWKERFEDFLG---DSSIGLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 283 FGHENNPANLKKwprVVVISYTMLHHLQK--SMLDREWALLIVDESHHVrCTKKksepreIKAVLDVARKvKRIVLLSGT 360
Cdd:cd17926 77 GGGKKKDFDDAN---VVVATYQSLSNLAEeeKDLFDQFGLLIVDEAHHL-PAKT------FSEILKELNA-KYRLGLTAT 145
|
.
gi 1366038577 361 P 361
Cdd:cd17926 146 P 146
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
191-381 |
7.27e-08 |
|
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: 55.07 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 191 VDELIGKLPKRLLDSLLP-FQLEGVRFGLQRGGRCL---IADEMGLGKTLQAIAIACCFMSE----GSILVVCPAILRYS 262
Cdd:cd18063 8 ITERVEKQSSLLINGTLKhYQLQGLEWMVSLYNNNLngiLADEMGLGKTIQTIALITYLMEHkrlnGPYLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 263 WAEELEHWLPFCLPadihlvFGHENNPANLKKW-PR-------VVVISYTMLHHLQKSMLDREWALLIVDESHhvrctKK 334
Cdd:cd18063 88 WTYEFDKWAPSVVK------ISYKGTPAMRRSLvPQlrsgkfnVLLTTYEYIIKDKHILAKIRWKYMIVDEGH-----RM 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1366038577 335 KSEPREIKAVLDVARKVKRIVLLSGTPSLSRPFDIFHQIDMLWPGLL 381
Cdd:cd18063 157 KNHHCKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIF 203
|
|
| DEXHc_XPB |
cd18029 |
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ... |
208-329 |
1.69e-07 |
|
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain] Cd Length: 169 Bit Score: 52.30 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 208 PFQLEGVR--FGLQRGGRCLIADEMGLGKTLQAIAIACCFMSegSILVVCPAILR-YSWAEELEHWlpfCLPADIHL-VF 283
Cdd:cd18029 11 PYQEKALSkmFGNGRARSGVIVLPCGAGKTLVGITAACTIKK--STLVLCTSAVSvEQWRRQFLDW---TTIDDEQIgRF 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1366038577 284 GHENNPanlKKWPRVVVIS-YTML-------HHLQKSM---LDREWALLIVDESHHV 329
Cdd:cd18029 86 TSDKKE---IFPEAGVTVStYSMLantrkrsPESEKFMefiTEREWGLIILDEVHVV 139
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
206-430 |
1.79e-07 |
|
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: 53.52 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVR---FGLQRGGRCLIADEMGLGKTLQAIAiaccFMSE-------GSILVVCPAILRYSWAEELEHWLP--- 272
Cdd:cd18060 1 LREYQLEGVNwllFNWYNRQNCILADEMGLGKTIQSIA----FLQEvynvgihGPFLVIAPLSTITNWEREFNTWTEmnt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 273 ------------------FCLPADIHLVFGHENNPAnlkkwprvVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKK 334
Cdd:cd18060 77 ivyhgslasrqmiqqyemYCKDSRGRLIPGAYKFDA--------LITTFEMILSDCPELREIEWRCVIIDEAH--RLKNR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 335 KSEPREIKAVLDVARKvkriVLLSGTPSLSRPFDIFHQIDMLWPgllgrdkfkfGETYCDAKYVRGvqgkvFQDFSKGTR 414
Cdd:cd18060 147 NCKLLDSLKHMDLEHK----VLLTGTPLQNTVEELFSLLHFLEP----------SQFPSESEFLKD-----FGDLKTEEQ 207
|
250
....*....|....*.
gi 1366038577 415 LEELNMLLtRTVMIRR 430
Cdd:cd18060 208 VQKLQAIL-KPMMLRR 222
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
206-378 |
4.28e-07 |
|
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: 52.35 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVR---FGLQRGGRCLIADEMGLGKTLQAIAiaccFMSE-------GSILVVCPAILRYSWAEELEHWlpfcl 275
Cdd:cd18058 1 LREYQLEGMNwllFNWYNRKNCILADEMGLGKTIQSIT----FLSEiflmgirGPFLIIAPLSTITNWEREFRTW----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 276 pADIHLVFGH-------------------ENNPANLKKWPRVVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKKKS 336
Cdd:cd18058 72 -TEMNAIVYHgsqisrqmiqqyemyyrdeQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAH--RLKNRNC 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1366038577 337 EPREIKAVLDVARKvkriVLLSGTPSLSRPFDIFHQIDMLWP 378
Cdd:cd18058 149 KLLEGLKLMALEHK----VLLTGTPLQNSVEELFSLLNFLEP 186
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
206-361 |
1.26e-06 |
|
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: 50.08 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVRFGL---QRGGRCLIADEMGLGKTLQAIAiaccFMS-------EGSILVVCPAILRYSWAEELEHWLPFCL 275
Cdd:cd17998 1 LKDYQLIGLNWLNllyQKKLSGILADEMGLGKTIQVIA----FLAylkeigiPGPHLVVVPSSTLDNWLREFKRWCPSLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 276 padIHLVFGHENNPANLK--------KWpRVVVISYTML--HHLQKSMLDR-EWALLIVDESHHVrctkKKSEPREIKAV 344
Cdd:cd17998 77 ---VEPYYGSQEERKHLRydilkgleDF-DVIVTTYNLAtsNPDDRSFFKRlKLNYVVYDEGHML----KNMTSERYRHL 148
|
170
....*....|....*..
gi 1366038577 345 LDVaRKVKRIvLLSGTP 361
Cdd:cd17998 149 MTI-NANFRL-LLTGTP 163
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
206-402 |
1.37e-06 |
|
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: 50.80 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVR---FGLQRGGRCLIADEMGLGKTLQAIAiaccFMSE-------GSILVVCPAILRYSWAEELEHWLPFcl 275
Cdd:cd18059 1 LREYQLEGVNwllFNWYNTRNCILADEMGLGKTIQSIT----FLYEiylkgihGPFLVIAPLSTIPNWEREFRTWTEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 276 paDIHLVFGHENNPANLKKWP-----------------RVVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKKKSEP 338
Cdd:cd18059 75 --NVVVYHGSQASRRTIQLYEmyfkdpqgrvikgsykfHAIITTFEMILTDCPELRNIPWRCVVIDEAH--RLKNRNCKL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1366038577 339 REIKAVLDVARKvkriVLLSGTPSLSRPFDIFHQIDMLWPGLLGRDKfKFGETYCDAKYVRGVQ 402
Cdd:cd18059 151 LEGLKMMDLEHK----VLLTGTPLQNTVEELFSLLHFLEPSRFPSET-TFMQEFGDLKTEEQVQ 209
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|
| PRK04914 |
PRK04914 |
RNA polymerase-associated protein RapA; |
205-361 |
1.38e-06 |
|
RNA polymerase-associated protein RapA;
Pssm-ID: 235319 [Multi-domain] Cd Length: 956 Bit Score: 52.92 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 205 SLLPFQL----E-GVRFGlqrgGRCLIADEMGLGKTLQAiaiaccfmseGSI-------------LVVCPAILRYSWAEE 266
Cdd:PRK04914 152 SLIPHQLyiahEvGRRHA----PRVLLADEVGLGKTIEA----------GMIihqqlltgraervLILVPETLQHQWLVE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 267 L--EHWLPFCL-----PADIhlvFGHENNP---ANLkkwprvVVISYTML---HHLQKSMLDREWALLIVDESHHVRCTK 333
Cdd:PRK04914 218 MlrRFNLRFSLfdeerYAEA---QHDADNPfetEQL------VICSLDFLrrnKQRLEQALAAEWDLLVVDEAHHLVWSE 288
|
170 180
....*....|....*....|....*...
gi 1366038577 334 KKSEpREIKAVLDVARKVKRIVLLSGTP 361
Cdd:PRK04914 289 EAPS-REYQVVEQLAEVIPGVLLLTATP 315
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
206-378 |
1.00e-04 |
|
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: 45.00 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVR---FGLQRGGRCLIADEMGLGKTLQAIAiaccFMSE-------GSILVVCPAILRYSWAEELEHWlpfcl 275
Cdd:cd18061 1 LREYQLEGLNwllFNWYNRRNCILADEMGLGKTIQSIT----FLYEilltgirGPFLIIAPLSTIANWEREFRTW----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 276 pADIHLVFGHEN--NPANLKKWP-----------------RVVVISYTMLHHLQKSMLDREWALLIVDESHhvRCTKKKS 336
Cdd:cd18061 72 -TDLNVVVYHGSliSRQMIQQYEmyfrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAH--RLKNKNC 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1366038577 337 EPREIKAVLDVARKvkriVLLSGTPSLSRPFDIFHQIDMLWP 378
Cdd:cd18061 149 KLLEGLKLMNLEHK----VLLTGTPLQNTVEELFSLLHFLEP 186
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
205-328 |
6.40e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.89 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 205 SLLPFQLEGVR----FGLQRGGRCLIADEMGLGKTLQAIAIACCFMSEGSI---LVVCPAI-LRYSWAEELEHWLPFCLP 276
Cdd:pfam04851 3 ELRPYQIEAIEnlleSIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIkkvLFLVPRKdLLEQALEEFKKFLPNYVE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1366038577 277 ADIhlVFGHENNPANLKKWpRVVVISYTMLH---HLQKSMLDRE-WALLIVDESHH 328
Cdd:pfam04851 83 IGE--IISGDKKDESVDDN-KIVVTTIQSLYkalELASLELLPDfFDVIIIDEAHR 135
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
578-637 |
1.34e-03 |
|
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: 38.84 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 578 QLSSEVKIaIVGITAGGVGLDFSSATHVVFLELPQSPSLMLQAEDRAHRRGQTNAVNIYF 637
Cdd:cd18785 18 EIASSLEI-LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILF 76
|
|
| McrA |
COG1403 |
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms]; |
1131-1163 |
5.59e-03 |
|
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
Pssm-ID: 441013 [Multi-domain] Cd Length: 64 Bit Score: 36.50 E-value: 5.59e-03
10 20 30
....*....|....*....|....*....|...
gi 1366038577 1131 GNAWHADHLVPVYLGGGEcRLENMRTLCVACHS 1163
Cdd:COG1403 31 GDALEVDHIIPRSRGGTD-TWENLVLLCRRCNR 62
|
|
| rad25 |
TIGR00603 |
DNA repair helicase rad25; All proteins in this family for which functions are known are ... |
206-329 |
6.54e-03 |
|
DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273168 [Multi-domain] Cd Length: 732 Bit Score: 40.94 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1366038577 206 LLPFQLEGVR--FGLQRGGRCLIADEMGLGKTLQAIAIACCFmsEGSILVVC-PAILRYSWAEELEHWlpfCLPADIHL- 281
Cdd:TIGR00603 256 IRPYQEKSLSkmFGNGRARSGIIVLPCGAGKSLVGVTAACTV--KKSCLVLCtSAVSVEQWKQQFKMW---STIDDSQIc 330
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1366038577 282 VFGHENnpanlKKWPR----VVVISYTMLHHLQKS----------MLDREWALLIVDESHHV 329
Cdd:TIGR00603 331 RFTSDA-----KERFHgeagVVVSTYSMVAHTGKRsyesekvmewLTNREWGLILLDEVHVV 387
|
|
| HNHc |
cd00085 |
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ... |
1126-1166 |
7.24e-03 |
|
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.
Pssm-ID: 238038 [Multi-domain] Cd Length: 57 Bit Score: 35.91 E-value: 7.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1366038577 1126 KDPTEGNAWHADHLVPVYlGGGECRLENMRTLCVACHSDVT 1166
Cdd:cd00085 18 GKPGGTEGLEVDHIIPLS-DGGNNDLDNLVLLCRKCHRKKH 57
|
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