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Conserved domains on  [gi|1063534949|ref|WP_069398201|]
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helicase-related protein [Mycobacterium shimoidei]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
5-643 2.59e-101

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 342.20  E-value: 2.59e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949    5 RITQPLLEAGTLALTAHERADLSLPEHSTTIEIELDGETFGAQWSGRSRQLSGDMLTERLQDYGQVGGLLRLDYDDHTYR 84
Cdd:COG0553     58 LELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLAL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949   85 LRLLPPGSAMQVPRPTSQPAVVQKPPAGTKAARRRATVDRQFHSDDKYDWGPGDNRTIGFLTEARVLLTDQLKAAGFDPF 164
Cdd:COG0553    138 LLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEA 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  165 EMVELRLQGEELATLDDFEELlavdvaNVDRMPHQAAAARHA--LSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAK 242
Cdd:COG0553    218 AVDAFRLRRLREALESLPAGL------KATLRPYQLEGAAWLlfLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  243 RVIVLCPAPLRDQWREEMnQKF--DMQFDVAYSGLD-------IGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDE---- 309
Cdd:COG0553    292 PVLIVAPTSLVGNWQREL-AKFapGLRVLVLDGTRErakganpFEDADLVITSYGLLRRDIELLAAVDWDLVILDEaqhi 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  310 --AHRaagagarKRRELVTALTTECRYAffLTATPVQNDLLELYRLVELLRPGTFRSEREFRREFMTSYDPRRPTDPAAL 387
Cdd:COG0553    371 knPAT-------KRAKAVRALKARHRLA--LTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERL 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  388 RSLISNAMIRTTRAQAGVDRVTRKPIDIGIDLGPRERELYALSTDLLRNVMTSpGDTMRRRSLALRLtaspfsmgTTALR 467
Cdd:COG0553    442 RRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEG-AEGIRRRGLILAA--------LTRLR 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  468 MAERHPdehvRKVLTEIGHFAmdiSGSAREDRALDITHRWLKDHGRVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSP 547
Cdd:COG0553    513 QICSHP----ALLLEEGAELS---GRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSA 585
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  548 SERASTIAAFRSGEAP--IMVSTDSGAEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVDRLTQPRNeVFVANLYARGTIDQ 625
Cdd:COG0553    586 EERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD-VQVYKLVAEGTIEE 664
                          650
                   ....*....|....*...
gi 1063534949  626 SVYQLLADKLRMFELLFG 643
Cdd:COG0553    665 KILELLEEKRALAESVLG 682
Siva super family cl09371
Cd27 binding protein (Siva); Siva binds to the CD27 cytoplasmic tail. It has a DD homology ...
1505-1603 4.57e-04

Cd27 binding protein (Siva); Siva binds to the CD27 cytoplasmic tail. It has a DD homology region, a box-B-like ring finger, and a zinc finger-like domain. Overexpression of Siva in various cell lines induces apoptosis, suggesting an important role for Siva in the CD27-transduced apoptotic pathway. Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis. Indeed, the unique amphipathic helical region (SAH) present in Siva-1 is required for its binding to BCL-X(L) and sensitising cells to UV radiation. Natural complexes of Siva-1/BCL-X(L) are detected in HUT78 and murine thymocyte, suggesting a potential role for Siva-1 in regulating T cell homeostasis. This family contains both Siva-1 and the shorter Siva-2 lacking the sequence coded by exon 2. It has been suggested that Siva-2 could regulate the function of Siva-1.


The actual alignment was detected with superfamily member pfam05458:

Pssm-ID: 283184  Cd Length: 173  Bit Score: 43.00  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949 1505 DGHFYRASTSALCTS--CRTWACRAC-DGVDHRSSidCPSCDRPVCRRCLeqshtvvdaqcllchdRPCPQCGrdpeVLA 1581
Cdd:pfam05458   90 DGKLMRATAQSSEASptGASIACSSCvRSVDGKAV--CSQCERALCGQCV----------------RTCSGCS----SLA 147
                           90       100
                   ....*....|....*....|..
gi 1063534949 1582 CSICGRSMCSNCRVQELCPACS 1603
Cdd:pfam05458  148 CSLCTLVDYSDQYEKVLCTSCS 169
zf-UDP super family cl48257
Zinc-binding RING-finger; This RING/U-box type zinc-binding domain is frequently found in the ...
2034-2093 8.20e-04

Zinc-binding RING-finger; This RING/U-box type zinc-binding domain is frequently found in the catalytic subunit (irx3) of cellulose synthase. The enzymic class is EC:2.4.1.12, whereby the synthase removes the glucose from UDP-glucose and adds it to the growing cellulose, thereby releasing UDP. The domain-structure is treble-clef like (PDB:1weo).


The actual alignment was detected with superfamily member pfam14569:

Pssm-ID: 464209 [Multi-domain]  Cd Length: 75  Bit Score: 40.02  E-value: 8.20e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063534949 2034 LCKYCDSTICTICTDNLVSCDCCQATICRRCV--REPHANLWLCPACATMRRPTRSEARRHG 2093
Cdd:pfam14569    7 ICQICGDDVGLTDDGELFVACNECAFPVCRPCyeYERKDGNQCCPQCKTRYKRHKGSPRVEG 68
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
5-643 2.59e-101

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 342.20  E-value: 2.59e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949    5 RITQPLLEAGTLALTAHERADLSLPEHSTTIEIELDGETFGAQWSGRSRQLSGDMLTERLQDYGQVGGLLRLDYDDHTYR 84
Cdd:COG0553     58 LELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLAL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949   85 LRLLPPGSAMQVPRPTSQPAVVQKPPAGTKAARRRATVDRQFHSDDKYDWGPGDNRTIGFLTEARVLLTDQLKAAGFDPF 164
Cdd:COG0553    138 LLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEA 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  165 EMVELRLQGEELATLDDFEELlavdvaNVDRMPHQAAAARHA--LSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAK 242
Cdd:COG0553    218 AVDAFRLRRLREALESLPAGL------KATLRPYQLEGAAWLlfLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  243 RVIVLCPAPLRDQWREEMnQKF--DMQFDVAYSGLD-------IGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDE---- 309
Cdd:COG0553    292 PVLIVAPTSLVGNWQREL-AKFapGLRVLVLDGTRErakganpFEDADLVITSYGLLRRDIELLAAVDWDLVILDEaqhi 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  310 --AHRaagagarKRRELVTALTTECRYAffLTATPVQNDLLELYRLVELLRPGTFRSEREFRREFMTSYDPRRPTDPAAL 387
Cdd:COG0553    371 knPAT-------KRAKAVRALKARHRLA--LTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERL 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  388 RSLISNAMIRTTRAQAGVDRVTRKPIDIGIDLGPRERELYALSTDLLRNVMTSpGDTMRRRSLALRLtaspfsmgTTALR 467
Cdd:COG0553    442 RRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEG-AEGIRRRGLILAA--------LTRLR 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  468 MAERHPdehvRKVLTEIGHFAmdiSGSAREDRALDITHRWLKDHGRVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSP 547
Cdd:COG0553    513 QICSHP----ALLLEEGAELS---GRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSA 585
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  548 SERASTIAAFRSGEAP--IMVSTDSGAEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVDRLTQPRNeVFVANLYARGTIDQ 625
Cdd:COG0553    586 EERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD-VQVYKLVAEGTIEE 664
                          650
                   ....*....|....*...
gi 1063534949  626 SVYQLLADKLRMFELLFG 643
Cdd:COG0553    665 KILELLEEKRALAESVLG 682
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
191-694 7.48e-61

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 226.87  E-value: 7.48e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  191 ANVDRMPHQAAAARHALSRLR-GRAILADEVGLGKTIEAGLAVKELTLRGlAKRVIVLCPAPLRDQWREEMNQKFDMQFD 269
Cdd:NF038318    26 ADIDPNPHQINAFCAAIAALKtGGIILADEVGLGKTIEAGLVLKYVLESG-AKKILIILPANLRKQWEIELEEKFDLESL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  270 V-------------AYSGLDIGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEA-HRAAGAGARKRRELVTALTTECRyA 335
Cdd:NF038318   105 IldsltvekdakkwNKRLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAhNLRNVHKGGKRAKNLYELTKGIP-K 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  336 FFLTATPVQNDLLELYRLVELLRPGTFRSEREFRREFMtsydprRPTDPAALRSLISNAMIRTTRAQAG--VDRVTRKPI 413
Cdd:NF038318   184 ILLTATPLQNSLLDLYGLVSFIDPRIFGSEKVFSKRYI------KDEDYSDLKRELSPVLYRTLRKDVAdyMQFKKRKCI 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  414 DIGIDLGPRERELYALSTDLL-RNVMTSPGDTMR-------RR-----SLAL---------RLTA--------------- 456
Cdd:NF038318   258 TVDFELSPDEIELYVRVNNFLkRDILYSIPTSNRtliilviRKllassSFALaetfevlkkRLEKlkegtrsanaqegfd 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  457 ------------SPFSMGTTALRMAERHPDEHVRKVLTEIGHFAMDISGSARED---RALDITHRWLKDHG---RVLIFT 518
Cdd:NF038318   338 lfwsfvedeideSGFEEKQDELYTRQKEFIQHEIDEVDAIIDVAKRIKTNAKVTalkTALEIAFEYQREEGiaqKVVVFT 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  519 QHTDT---VTGLLRRMELEGLRARAFHGSMSPSE-----RA-------------------STIAAFRSgEAPIMVSTDSG 571
Cdd:NF038318   418 ESKRTqkyIAEELRKSGYEGEDILLFNGDFDDAMtkeiyRAwqvknygkanygrsveykhAIVDYFKN-NAKILIVTDAG 496
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  572 AEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVDRLTQpRNEVFVANLY-ARGTIDQSVYQLLADKLRMFELLFGQVTTILG 650
Cdd:NF038318   497 SEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQ-KNDVVAINLLnTQNVADKRVYEILSEKFELFEGVFGASDIALG 575
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063534949  651 ELDDSKSatFESRVLD--------------------ALFAESDSKMQELLSELGTELADARERA 694
Cdd:NF038318   576 LLESGTD--FEKRVLQiyqscdttaefkkefdklekKLDAKRNKKARELRSLLITESSEAKKQA 637
DISARM_DrmD NF038317
DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component ...
196-997 5.71e-46

DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase.


Pssm-ID: 468471 [Multi-domain]  Cd Length: 1023  Bit Score: 181.97  E-value: 5.71e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  196 MPHQAAAARHALSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFDVAYS-- 273
Cdd:NF038317   110 EDYQLEPLVRALDMPRVNLLIADDVGLGKTIEAGLVIQELLLRHRARRVLIVCPASLQEKWRDEMREKFGLDFRIVDSey 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  274 --------GLDI---GSQDKLIVSLAL-----GTRHI----GKLAKTP--WDIVIVDE------AHRAAGAGARKRRELV 325
Cdd:NF038317   190 vaqlrrerGLHAnpwTSFPRLIVSMDWlrgerAQRLLrdvlPAHADTPraFDLLIVDEahnvapASPSKYAVDSQRTRLI 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  326 TALTTECRYAFFLTATPVQndlleLYR-----LVELLrpgtfrserefrrefmtsyDPRR-----PTDPAALRSlisnAM 395
Cdd:NF038317   270 RDLAPHFEHRLFLSATPHN-----GYSesftaLLELL-------------------DPQRfargvPPDEKQLDE----VM 321
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  396 IR-----TTRAQAGVDRVTRKPIDIGIDLGPRERELYALSTDLLRNVMTSPGDTMRRRSLAL-------RLTASPFSMGT 463
Cdd:NF038317   322 VRrlksdLVDRDGSPRFPERELEALPVDYSADEREIHELLDEYTELRRKRLAGKRGRRAADFvtlllkkRLFSSPAAFAR 401
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  464 T------------ALRMAERHPDEHVRK---------------------VLTEIGHFAMDISGSARED----RALDITHR 506
Cdd:NF038317   402 TlevhratlergaARGGPLSDDERLLRDdvlddeedyaddelleeaedeALEEASELSPPLTAEERALlerlRAWAERAE 481
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  507 ------------WLKDH---------GRVLIFTQHTDTVTGLLRRMELEGL---RARAFHGSMSPSERASTIAAFRS--G 560
Cdd:NF038317   482 arpdskaralidWLRANlrpggrwtnERVIVFTEYRDTLRWLVELLAAEGYggdRLALLHGGMDDDERERIKAAFQAdpS 561
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  561 EAP--IMVSTDSGAEGQNLQ-FCNCVLNYDLPWNPMRIEQRIGRVDRLTQPRNEVFVANLYARGTIDQSVYQL-----LA 632
Cdd:NF038317   562 EHPvrILLATDAASEGIDLQnHCHRLIHYDIPWNPNRLEQRNGRIDRHGQRADPVLIWHFVGKGTEGAAEGDLefldrLA 641
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  633 DKLrmfellfGQVTTILGELddsksatfeSRVLDAlfaesdsKMQELLS----ELGTELADARERASTLIAADSGLSKWM 708
Cdd:NF038317   642 RKV-------ATIREDLGSV---------NPVIAD-------QVERLLLgrrrDLDTEAAEIEAAKRRELAAERELREQL 698
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  709 TSALDHREGLTKEGstDLAPEIrrrarirqrrvqawVRRVLK-ALDA------QILHDTGDGEGAFLTAQLGEEVADELg 781
Cdd:NF038317   699 ERLHEQLEESREEL--HLTPAN--------------IRRVVDtALELagqpplVPVGDPGPDGRVFEVPALSGSWARAL- 761
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  782 gRTLLH---------LAFDRHGLENHPDAELCAVGSPVFDELLGLLR-----VRGDMH-ATVPVIPEDLGPSPFhhaptI 846
Cdd:NF038317   762 -DGLRHplhtgqirpITFDPEVAKGRDDVVLVHLNHPLVQMSLRLLRaavwsDDKPLHrVTAVVVPDDGLEEPA-----V 835
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  847 TLVRR-------------RLVPSGTWSGQATFRaRIGEAEITEHIItaevngtkEVRLPRrplqEGESLPAVFDEPAKVI 913
Cdd:NF038317   836 AALSRlvlvggdgarlheELLLAGGWLRDGRFR-RLEGVTDVEALL--------DAALPS----GRPAPPAVRDRLAERW 902
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  914 AAFESSVAGHLEKLRRDRAEEVE-----RQQALE------LERIRRGYQAQIDEAPHEDKArlrrALYSEERRLTRRPDV 982
Cdd:NF038317   903 PRLRERLEEALEARARDRLDALErtladRGEAEAqriravLDELRATLREALAEDEEPEQL----ALFSEDERRQLRRDR 978
                          970
                   ....*....|....*.
gi 1063534949  983 RA-RAKLLALTLDEDD 997
Cdd:NF038317   979 RAlERRLARLPEERER 994
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
196-383 7.07e-45

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: 162.07  E-value: 7.07e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  196 MPHQAAAARHALSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFDVAYS-- 273
Cdd:cd18011      2 LPHQIDAVLRALRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLILDRet 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  274 --------GLDIGSQDKLIVSLALGTRHI---GKLAKTPWDIVIVDE---AHRAAGAGARKRRELVTALTTECRYAFFLT 339
Cdd:cd18011     82 aaqlrrliGNPFEEFPIVIVSLDLLKRSEerrGLLLSEEWDLVVVDEahkLRNSGGGKETKRYKLGRLLAKRARHVLLLT 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1063534949  340 ATPVQNDLLELYRLVELLRPGTFRSEREFRREfmtsyDPRRPTD 383
Cdd:cd18011    162 ATPHNGKEEDFRALLSLLDPGRFAVLGRFLRL-----DGLREVL 200
DpdE NF041062
protein DpdE;
191-702 8.12e-36

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 149.35  E-value: 8.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  191 ANVDRMPHQAAAARHALSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQfDV 270
Cdd:NF041062   150 SAVELEPHQVAVVRRVLQDPVQRYLLADEVGLGKTIEAGLVIRQHLLDNPDARVLVLVPDALVRQWRRELRDKFFLD-DF 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  271 AYSGLDIGSQDKLIVSLALGTRHigklaktpwDIVIVDE-------AHRAAGAGARKRRELvTALTTECRYAFFLTATPV 343
Cdd:NF041062   229 PGARVRVLSHEEPERWEPLLDAP---------DLLVVDEahqlarlAWSGDPPERARYREL-AALAHAAPRLLLLSATPV 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  344 QND---------LL--ELYRLVEL-------------------LRPGT---------------FRSEREFRR---EFMTS 375
Cdd:NF041062   299 LGNeetflallhLLdpDLYPLDDLeafrerleereelgrlvlgLDPDNpnfllrqaldelralFPEDEELQElaeELLPL 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  376 YDPRRPTDP-------AALRSLISNA------MIRTTRAQA--------GVDRVTRKPIDIGiDLGPRERELYALSTDLL 434
Cdd:NF041062   379 LDEFDDEEPeeraravSALRAHISETyrlhrrMIRNRRSSVlgadylvpGRAGPRVLVWESP-AREAADEALEDWREEAA 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  435 RNVMTSPGDTMRRRSLALRLTASPFSMGTTALRMAER--HPDEHVRKVLTEIGHFAMDISGSAREDRALDITHR---WL- 508
Cdd:NF041062   458 LLDAESDPAARAAYARALAWLVARLGGPDDLAALLRWrlRGDAASADLAGERELLEALIAALEDEAKDADLLAAladWLl 537
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  509 ---KDHGRVLIFTQHTDTVTGLLRRMELEGL-RARAFHGSMSPSERASTIAAFRSG-EAPIMVSTDSGAEGQNLQFCNCV 583
Cdd:NF041062   538 pllRGSGKAVVFCGDGSLADHLAAALARLGAgSVERHLSGQGADQAERAVRAFRQDpSARVLVCDRSGEEGLNLQGADRL 617
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  584 LNYDLPWNPMRIEQRIGRVDRLTQPRNEVFVANLYARGTIDQSVY----QLLADKLRMFEllfGQVTTILGELDDsksat 659
Cdd:NF041062   618 VHLDLPWSPNRLEQRIGRLDRYASLRGGRPVESYVLAPSDDDSLYsawaDLLREGFGVFD---RSVASLQDALDE----- 689
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1063534949  660 FESRVLDALFAESDSKMQELLSELGTELADARERASTLIAADS 702
Cdd:NF041062   690 GLDEAWRALLEEGPEALLEAIARLRGELARERRRIDEQDALDS 732
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
193-713 2.85e-28

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 124.56  E-value: 2.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  193 VDRMPHQAAAARHALSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQF---- 268
Cdd:PRK04914   151 ASLIPHQLYIAHEVGRRHAPRVLLADEVGLGKTIEAGMIIHQQLLTGRAERVLILVPETLQHQWLVEMLRRFNLRFslfd 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  269 DVAYSGLDIGS-----QDKL-IVSLALGTRH---IGKLAKTPWDIVIVDEAHRAAGAGARKRRE--LVTALTTECRYAFF 337
Cdd:PRK04914   231 EERYAEAQHDAdnpfeTEQLvICSLDFLRRNkqrLEQALAAEWDLLVVDEAHHLVWSEEAPSREyqVVEQLAEVIPGVLL 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  338 LTATPVQNDLLELY-RLvELLRPGTFRSEREFRREfMTSYdprRPTDPAAlRSLISNAMIRTTRAQAGVDRVTRKPID-- 414
Cdd:PRK04914   311 LTATPEQLGQESHFaRL-RLLDPDRFHDYEAFVEE-QQQY---RPVADAV-QALLAGEKLSDDALNALGELLGEQDIEpl 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  415 IGIDLGPRERELYAlSTDLLRNVMTSPGdTMR------RRSLA----LRLTASPFSMGTTALRMAERHPDEHVRKVLT-E 483
Cdd:PRK04914   385 LQAANSDSEEAQAA-RQELISELLDRHG-TGRvlfrntRAAVKgfpkRELHPIPLPLPEQYQTAIKVSLEARARDMLYpE 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  484 IGHFAMDISGS-AREDRALDITHRWLKDHGR--VLIFTQHTDTVTGL---LRrmELEGLRARAFHGSMSPSERASTIAAF 557
Cdd:PRK04914   463 QIYQEFEDNATwWNFDPRVEWLIDFLKSHRSekVLVICAKAATALQLeqaLR--EREGIRAAVFHEGMSIIERDRAAAYF 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  558 RSGE--APIMVSTDSGAEGQNLQF-CNCVLnYDLPWNPMRIEQRIGRVDRLTQPRN-EVFVAnlYARGTIDQSVYQLLAD 633
Cdd:PRK04914   541 ADEEdgAQVLLCSEIGSEGRNFQFaSHLVL-FDLPFNPDLLEQRIGRLDRIGQKHDiQIHVP--YLEGTAQERLFRWYHE 617
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  634 KLRMFEL-------LFGQVTTilgELDDSKSATFESRVLDALFAESDSKMQELLSELGT------ELADAR-ERASTLIA 699
Cdd:PRK04914   618 GLNAFEHtcptgraLYDEFGD---ELIPYLASPDDTDGLDELIAETREQHEALKAQLEQgrdrllELNSCGgEKAQALAE 694
                          570       580
                   ....*....|....*....|
gi 1063534949  700 A------DSGLSKWMTSALD 713
Cdd:PRK04914   695 AiaeqddDTNLVNFALNLFD 714
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
508-604 2.72e-25

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 102.29  E-value: 2.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  508 LKDHGRVLIFTQHTDTV-TGLLRrmELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNY 586
Cdd:pfam00271   12 KERGGKVLIFSQTKKTLeAELLL--EKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINY 89
                           90
                   ....*....|....*...
gi 1063534949  587 DLPWNPMRIEQRIGRVDR 604
Cdd:pfam00271   90 DLPWNPASYIQRIGRAGR 107
HELICc smart00490
helicase superfamily c-terminal domain;
522-604 1.30e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.96  E-value: 1.30e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949   522 DTVTGLLRRMeleGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNYDLPWNPMRIEQRIGR 601
Cdd:smart00490    1 EELAELLKEL---GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ...
gi 1063534949   602 VDR 604
Cdd:smart00490   78 AGR 80
Siva pfam05458
Cd27 binding protein (Siva); Siva binds to the CD27 cytoplasmic tail. It has a DD homology ...
1505-1603 4.57e-04

Cd27 binding protein (Siva); Siva binds to the CD27 cytoplasmic tail. It has a DD homology region, a box-B-like ring finger, and a zinc finger-like domain. Overexpression of Siva in various cell lines induces apoptosis, suggesting an important role for Siva in the CD27-transduced apoptotic pathway. Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis. Indeed, the unique amphipathic helical region (SAH) present in Siva-1 is required for its binding to BCL-X(L) and sensitising cells to UV radiation. Natural complexes of Siva-1/BCL-X(L) are detected in HUT78 and murine thymocyte, suggesting a potential role for Siva-1 in regulating T cell homeostasis. This family contains both Siva-1 and the shorter Siva-2 lacking the sequence coded by exon 2. It has been suggested that Siva-2 could regulate the function of Siva-1.


Pssm-ID: 283184  Cd Length: 173  Bit Score: 43.00  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949 1505 DGHFYRASTSALCTS--CRTWACRAC-DGVDHRSSidCPSCDRPVCRRCLeqshtvvdaqcllchdRPCPQCGrdpeVLA 1581
Cdd:pfam05458   90 DGKLMRATAQSSEASptGASIACSSCvRSVDGKAV--CSQCERALCGQCV----------------RTCSGCS----SLA 147
                           90       100
                   ....*....|....*....|..
gi 1063534949 1582 CSICGRSMCSNCRVQELCPACS 1603
Cdd:pfam05458  148 CSLCTLVDYSDQYEKVLCTSCS 169
zf-UDP pfam14569
Zinc-binding RING-finger; This RING/U-box type zinc-binding domain is frequently found in the ...
2034-2093 8.20e-04

Zinc-binding RING-finger; This RING/U-box type zinc-binding domain is frequently found in the catalytic subunit (irx3) of cellulose synthase. The enzymic class is EC:2.4.1.12, whereby the synthase removes the glucose from UDP-glucose and adds it to the growing cellulose, thereby releasing UDP. The domain-structure is treble-clef like (PDB:1weo).


Pssm-ID: 464209 [Multi-domain]  Cd Length: 75  Bit Score: 40.02  E-value: 8.20e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063534949 2034 LCKYCDSTICTICTDNLVSCDCCQATICRRCV--REPHANLWLCPACATMRRPTRSEARRHG 2093
Cdd:pfam14569    7 ICQICGDDVGLTDDGELFVACNECAFPVCRPCyeYERKDGNQCCPQCKTRYKRHKGSPRVEG 68
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
1525-1588 3.25e-03

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.18  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949 1525 CRACDGVDHRSSiDCPSCDRPV------CRRCLEQSH----------TVVDAQCLLCHD-----RPCPQCGRDPEVLACS 1583
Cdd:PTZ00368     3 CYRCGGVGHQSR-ECPNSAPAGaakarpCYKCGEPGHlsrecpsapgGRGERSCYNCGKtghlsRECPEAPPGSGPRSCY 81

                   ....*
gi 1063534949 1584 ICGRS 1588
Cdd:PTZ00368    82 NCGQT 86
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
2043-2078 4.80e-03

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the second PHD finger.


Pssm-ID: 277007 [Multi-domain]  Cd Length: 43  Bit Score: 36.87  E-value: 4.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1063534949 2043 CTICTD--NLVSCDCCQATICRRCVREPHANL----WLCPAC 2078
Cdd:cd15532      2 CRVCKDggELLCCDGCPSSYHLHCLNPPLAEIpdgdWFCPRC 43
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
5-643 2.59e-101

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 342.20  E-value: 2.59e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949    5 RITQPLLEAGTLALTAHERADLSLPEHSTTIEIELDGETFGAQWSGRSRQLSGDMLTERLQDYGQVGGLLRLDYDDHTYR 84
Cdd:COG0553     58 LELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLAL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949   85 LRLLPPGSAMQVPRPTSQPAVVQKPPAGTKAARRRATVDRQFHSDDKYDWGPGDNRTIGFLTEARVLLTDQLKAAGFDPF 164
Cdd:COG0553    138 LLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEA 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  165 EMVELRLQGEELATLDDFEELlavdvaNVDRMPHQAAAARHA--LSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAK 242
Cdd:COG0553    218 AVDAFRLRRLREALESLPAGL------KATLRPYQLEGAAWLlfLRRLGLGGLLADDMGLGKTIQALALLLELKERGLAR 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  243 RVIVLCPAPLRDQWREEMnQKF--DMQFDVAYSGLD-------IGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDE---- 309
Cdd:COG0553    292 PVLIVAPTSLVGNWQREL-AKFapGLRVLVLDGTRErakganpFEDADLVITSYGLLRRDIELLAAVDWDLVILDEaqhi 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  310 --AHRaagagarKRRELVTALTTECRYAffLTATPVQNDLLELYRLVELLRPGTFRSEREFRREFMTSYDPRRPTDPAAL 387
Cdd:COG0553    371 knPAT-------KRAKAVRALKARHRLA--LTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEALERL 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  388 RSLISNAMIRTTRAQAGVDRVTRKPIDIGIDLGPRERELYALSTDLLRNVMTSpGDTMRRRSLALRLtaspfsmgTTALR 467
Cdd:COG0553    442 RRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEG-AEGIRRRGLILAA--------LTRLR 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  468 MAERHPdehvRKVLTEIGHFAmdiSGSAREDRALDITHRWLKDHGRVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSP 547
Cdd:COG0553    513 QICSHP----ALLLEEGAELS---GRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSA 585
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  548 SERASTIAAFRSGEAP--IMVSTDSGAEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVDRLTQPRNeVFVANLYARGTIDQ 625
Cdd:COG0553    586 EERDELVDRFQEGPEApvFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD-VQVYKLVAEGTIEE 664
                          650
                   ....*....|....*...
gi 1063534949  626 SVYQLLADKLRMFELLFG 643
Cdd:COG0553    665 KILELLEEKRALAESVLG 682
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
191-694 7.48e-61

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 226.87  E-value: 7.48e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  191 ANVDRMPHQAAAARHALSRLR-GRAILADEVGLGKTIEAGLAVKELTLRGlAKRVIVLCPAPLRDQWREEMNQKFDMQFD 269
Cdd:NF038318    26 ADIDPNPHQINAFCAAIAALKtGGIILADEVGLGKTIEAGLVLKYVLESG-AKKILIILPANLRKQWEIELEEKFDLESL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  270 V-------------AYSGLDIGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEA-HRAAGAGARKRRELVTALTTECRyA 335
Cdd:NF038318   105 IldsltvekdakkwNKRLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAhNLRNVHKGGKRAKNLYELTKGIP-K 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  336 FFLTATPVQNDLLELYRLVELLRPGTFRSEREFRREFMtsydprRPTDPAALRSLISNAMIRTTRAQAG--VDRVTRKPI 413
Cdd:NF038318   184 ILLTATPLQNSLLDLYGLVSFIDPRIFGSEKVFSKRYI------KDEDYSDLKRELSPVLYRTLRKDVAdyMQFKKRKCI 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  414 DIGIDLGPRERELYALSTDLL-RNVMTSPGDTMR-------RR-----SLAL---------RLTA--------------- 456
Cdd:NF038318   258 TVDFELSPDEIELYVRVNNFLkRDILYSIPTSNRtliilviRKllassSFALaetfevlkkRLEKlkegtrsanaqegfd 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  457 ------------SPFSMGTTALRMAERHPDEHVRKVLTEIGHFAMDISGSARED---RALDITHRWLKDHG---RVLIFT 518
Cdd:NF038318   338 lfwsfvedeideSGFEEKQDELYTRQKEFIQHEIDEVDAIIDVAKRIKTNAKVTalkTALEIAFEYQREEGiaqKVVVFT 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  519 QHTDT---VTGLLRRMELEGLRARAFHGSMSPSE-----RA-------------------STIAAFRSgEAPIMVSTDSG 571
Cdd:NF038318   418 ESKRTqkyIAEELRKSGYEGEDILLFNGDFDDAMtkeiyRAwqvknygkanygrsveykhAIVDYFKN-NAKILIVTDAG 496
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  572 AEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVDRLTQpRNEVFVANLY-ARGTIDQSVYQLLADKLRMFELLFGQVTTILG 650
Cdd:NF038318   497 SEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQ-KNDVVAINLLnTQNVADKRVYEILSEKFELFEGVFGASDIALG 575
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063534949  651 ELDDSKSatFESRVLD--------------------ALFAESDSKMQELLSELGTELADARERA 694
Cdd:NF038318   576 LLESGTD--FEKRVLQiyqscdttaefkkefdklekKLDAKRNKKARELRSLLITESSEAKKQA 637
DISARM_DrmD NF038317
DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component ...
196-997 5.71e-46

DISARM system SNF2-like helicase DrmD, long form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase.


Pssm-ID: 468471 [Multi-domain]  Cd Length: 1023  Bit Score: 181.97  E-value: 5.71e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  196 MPHQAAAARHALSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFDVAYS-- 273
Cdd:NF038317   110 EDYQLEPLVRALDMPRVNLLIADDVGLGKTIEAGLVIQELLLRHRARRVLIVCPASLQEKWRDEMREKFGLDFRIVDSey 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  274 --------GLDI---GSQDKLIVSLAL-----GTRHI----GKLAKTP--WDIVIVDE------AHRAAGAGARKRRELV 325
Cdd:NF038317   190 vaqlrrerGLHAnpwTSFPRLIVSMDWlrgerAQRLLrdvlPAHADTPraFDLLIVDEahnvapASPSKYAVDSQRTRLI 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  326 TALTTECRYAFFLTATPVQndlleLYR-----LVELLrpgtfrserefrrefmtsyDPRR-----PTDPAALRSlisnAM 395
Cdd:NF038317   270 RDLAPHFEHRLFLSATPHN-----GYSesftaLLELL-------------------DPQRfargvPPDEKQLDE----VM 321
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  396 IR-----TTRAQAGVDRVTRKPIDIGIDLGPRERELYALSTDLLRNVMTSPGDTMRRRSLAL-------RLTASPFSMGT 463
Cdd:NF038317   322 VRrlksdLVDRDGSPRFPERELEALPVDYSADEREIHELLDEYTELRRKRLAGKRGRRAADFvtlllkkRLFSSPAAFAR 401
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  464 T------------ALRMAERHPDEHVRK---------------------VLTEIGHFAMDISGSARED----RALDITHR 506
Cdd:NF038317   402 TlevhratlergaARGGPLSDDERLLRDdvlddeedyaddelleeaedeALEEASELSPPLTAEERALlerlRAWAERAE 481
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  507 ------------WLKDH---------GRVLIFTQHTDTVTGLLRRMELEGL---RARAFHGSMSPSERASTIAAFRS--G 560
Cdd:NF038317   482 arpdskaralidWLRANlrpggrwtnERVIVFTEYRDTLRWLVELLAAEGYggdRLALLHGGMDDDERERIKAAFQAdpS 561
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  561 EAP--IMVSTDSGAEGQNLQ-FCNCVLNYDLPWNPMRIEQRIGRVDRLTQPRNEVFVANLYARGTIDQSVYQL-----LA 632
Cdd:NF038317   562 EHPvrILLATDAASEGIDLQnHCHRLIHYDIPWNPNRLEQRNGRIDRHGQRADPVLIWHFVGKGTEGAAEGDLefldrLA 641
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  633 DKLrmfellfGQVTTILGELddsksatfeSRVLDAlfaesdsKMQELLS----ELGTELADARERASTLIAADSGLSKWM 708
Cdd:NF038317   642 RKV-------ATIREDLGSV---------NPVIAD-------QVERLLLgrrrDLDTEAAEIEAAKRRELAAERELREQL 698
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  709 TSALDHREGLTKEGstDLAPEIrrrarirqrrvqawVRRVLK-ALDA------QILHDTGDGEGAFLTAQLGEEVADELg 781
Cdd:NF038317   699 ERLHEQLEESREEL--HLTPAN--------------IRRVVDtALELagqpplVPVGDPGPDGRVFEVPALSGSWARAL- 761
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  782 gRTLLH---------LAFDRHGLENHPDAELCAVGSPVFDELLGLLR-----VRGDMH-ATVPVIPEDLGPSPFhhaptI 846
Cdd:NF038317   762 -DGLRHplhtgqirpITFDPEVAKGRDDVVLVHLNHPLVQMSLRLLRaavwsDDKPLHrVTAVVVPDDGLEEPA-----V 835
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  847 TLVRR-------------RLVPSGTWSGQATFRaRIGEAEITEHIItaevngtkEVRLPRrplqEGESLPAVFDEPAKVI 913
Cdd:NF038317   836 AALSRlvlvggdgarlheELLLAGGWLRDGRFR-RLEGVTDVEALL--------DAALPS----GRPAPPAVRDRLAERW 902
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  914 AAFESSVAGHLEKLRRDRAEEVE-----RQQALE------LERIRRGYQAQIDEAPHEDKArlrrALYSEERRLTRRPDV 982
Cdd:NF038317   903 PRLRERLEEALEARARDRLDALErtladRGEAEAqriravLDELRATLREALAEDEEPEQL----ALFSEDERRQLRRDR 978
                          970
                   ....*....|....*.
gi 1063534949  983 RA-RAKLLALTLDEDD 997
Cdd:NF038317   979 RAlERRLARLPEERER 994
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
196-383 7.07e-45

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: 162.07  E-value: 7.07e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  196 MPHQAAAARHALSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFDVAYS-- 273
Cdd:cd18011      2 LPHQIDAVLRALRKPPVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLILDRet 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  274 --------GLDIGSQDKLIVSLALGTRHI---GKLAKTPWDIVIVDE---AHRAAGAGARKRRELVTALTTECRYAFFLT 339
Cdd:cd18011     82 aaqlrrliGNPFEEFPIVIVSLDLLKRSEerrGLLLSEEWDLVVVDEahkLRNSGGGKETKRYKLGRLLAKRARHVLLLT 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1063534949  340 ATPVQNDLLELYRLVELLRPGTFRSEREFRREfmtsyDPRRPTD 383
Cdd:cd18011    162 ATPHNGKEEDFRALLSLLDPGRFAVLGRFLRL-----DGLREVL 200
DpdE NF041062
protein DpdE;
191-702 8.12e-36

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 149.35  E-value: 8.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  191 ANVDRMPHQAAAARHALSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQfDV 270
Cdd:NF041062   150 SAVELEPHQVAVVRRVLQDPVQRYLLADEVGLGKTIEAGLVIRQHLLDNPDARVLVLVPDALVRQWRRELRDKFFLD-DF 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  271 AYSGLDIGSQDKLIVSLALGTRHigklaktpwDIVIVDE-------AHRAAGAGARKRRELvTALTTECRYAFFLTATPV 343
Cdd:NF041062   229 PGARVRVLSHEEPERWEPLLDAP---------DLLVVDEahqlarlAWSGDPPERARYREL-AALAHAAPRLLLLSATPV 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  344 QND---------LL--ELYRLVEL-------------------LRPGT---------------FRSEREFRR---EFMTS 375
Cdd:NF041062   299 LGNeetflallhLLdpDLYPLDDLeafrerleereelgrlvlgLDPDNpnfllrqaldelralFPEDEELQElaeELLPL 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  376 YDPRRPTDP-------AALRSLISNA------MIRTTRAQA--------GVDRVTRKPIDIGiDLGPRERELYALSTDLL 434
Cdd:NF041062   379 LDEFDDEEPeeraravSALRAHISETyrlhrrMIRNRRSSVlgadylvpGRAGPRVLVWESP-AREAADEALEDWREEAA 457
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  435 RNVMTSPGDTMRRRSLALRLTASPFSMGTTALRMAER--HPDEHVRKVLTEIGHFAMDISGSAREDRALDITHR---WL- 508
Cdd:NF041062   458 LLDAESDPAARAAYARALAWLVARLGGPDDLAALLRWrlRGDAASADLAGERELLEALIAALEDEAKDADLLAAladWLl 537
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  509 ---KDHGRVLIFTQHTDTVTGLLRRMELEGL-RARAFHGSMSPSERASTIAAFRSG-EAPIMVSTDSGAEGQNLQFCNCV 583
Cdd:NF041062   538 pllRGSGKAVVFCGDGSLADHLAAALARLGAgSVERHLSGQGADQAERAVRAFRQDpSARVLVCDRSGEEGLNLQGADRL 617
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  584 LNYDLPWNPMRIEQRIGRVDRLTQPRNEVFVANLYARGTIDQSVY----QLLADKLRMFEllfGQVTTILGELDDsksat 659
Cdd:NF041062   618 VHLDLPWSPNRLEQRIGRLDRYASLRGGRPVESYVLAPSDDDSLYsawaDLLREGFGVFD---RSVASLQDALDE----- 689
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1063534949  660 FESRVLDALFAESDSKMQELLSELGTELADARERASTLIAADS 702
Cdd:NF041062   690 GLDEAWRALLEEGPEALLEAIARLRGELARERRRIDEQDALDS 732
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
494-614 7.39e-33

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: 124.90  E-value: 7.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  494 SAREDRALDITHRWLKDHGRVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGEAP--IMVSTDSG 571
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1063534949  572 AEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVDRLTQPRnEVFV 614
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKK-PVVV 131
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
193-713 2.85e-28

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 124.56  E-value: 2.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  193 VDRMPHQAAAARHALSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQF---- 268
Cdd:PRK04914   151 ASLIPHQLYIAHEVGRRHAPRVLLADEVGLGKTIEAGMIIHQQLLTGRAERVLILVPETLQHQWLVEMLRRFNLRFslfd 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  269 DVAYSGLDIGS-----QDKL-IVSLALGTRH---IGKLAKTPWDIVIVDEAHRAAGAGARKRRE--LVTALTTECRYAFF 337
Cdd:PRK04914   231 EERYAEAQHDAdnpfeTEQLvICSLDFLRRNkqrLEQALAAEWDLLVVDEAHHLVWSEEAPSREyqVVEQLAEVIPGVLL 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  338 LTATPVQNDLLELY-RLvELLRPGTFRSEREFRREfMTSYdprRPTDPAAlRSLISNAMIRTTRAQAGVDRVTRKPID-- 414
Cdd:PRK04914   311 LTATPEQLGQESHFaRL-RLLDPDRFHDYEAFVEE-QQQY---RPVADAV-QALLAGEKLSDDALNALGELLGEQDIEpl 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  415 IGIDLGPRERELYAlSTDLLRNVMTSPGdTMR------RRSLA----LRLTASPFSMGTTALRMAERHPDEHVRKVLT-E 483
Cdd:PRK04914   385 LQAANSDSEEAQAA-RQELISELLDRHG-TGRvlfrntRAAVKgfpkRELHPIPLPLPEQYQTAIKVSLEARARDMLYpE 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  484 IGHFAMDISGS-AREDRALDITHRWLKDHGR--VLIFTQHTDTVTGL---LRrmELEGLRARAFHGSMSPSERASTIAAF 557
Cdd:PRK04914   463 QIYQEFEDNATwWNFDPRVEWLIDFLKSHRSekVLVICAKAATALQLeqaLR--EREGIRAAVFHEGMSIIERDRAAAYF 540
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  558 RSGE--APIMVSTDSGAEGQNLQF-CNCVLnYDLPWNPMRIEQRIGRVDRLTQPRN-EVFVAnlYARGTIDQSVYQLLAD 633
Cdd:PRK04914   541 ADEEdgAQVLLCSEIGSEGRNFQFaSHLVL-FDLPFNPDLLEQRIGRLDRIGQKHDiQIHVP--YLEGTAQERLFRWYHE 617
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  634 KLRMFEL-------LFGQVTTilgELDDSKSATFESRVLDALFAESDSKMQELLSELGT------ELADAR-ERASTLIA 699
Cdd:PRK04914   618 GLNAFEHtcptgraLYDEFGD---ELIPYLASPDDTDGLDELIAETREQHEALKAQLEQgrdrllELNSCGgEKAQALAE 694
                          570       580
                   ....*....|....*....|
gi 1063534949  700 A------DSGLSKWMTSALD 713
Cdd:PRK04914   695 AiaeqddDTNLVNFALNLFD 714
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
196-359 1.42e-25

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: 105.73  E-value: 1.42e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  196 MPHQAAAARHALSRL--RGRAILADEVGLGKTIEA-GLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNqKFDMQFDVA- 271
Cdd:cd17919      2 RPYQLEGLNFLLELYenGPGGILADEMGLGKTLQAiAFLAYLLKEGKERGPVLVVCPLSVLENWEREFE-KWTPDLRVVv 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  272 -----------YSGLDIGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArKRRELVTALTTECRYAffLTA 340
Cdd:cd17919     81 yhgsqreraqiRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKS-QLSKALKALRAKRRLL--LTG 157
                          170
                   ....*....|....*....
gi 1063534949  341 TPVQNDLLELYRLVELLRP 359
Cdd:cd17919    158 TPLQNNLEELWALLDFLDP 176
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
508-604 2.72e-25

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 102.29  E-value: 2.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  508 LKDHGRVLIFTQHTDTV-TGLLRrmELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNY 586
Cdd:pfam00271   12 KERGGKVLIFSQTKKTLeAELLL--EKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLVINY 89
                           90
                   ....*....|....*...
gi 1063534949  587 DLPWNPMRIEQRIGRVDR 604
Cdd:pfam00271   90 DLPWNPASYIQRIGRAGR 107
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
465-675 1.03e-22

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 105.97  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  465 ALRMAERHPDEH--VRKVLTEIghfamdisgsareDRALDIthrwlKDHGRVLIFTQHTDTVTGLLRRMELEGLRARAFH 542
Cdd:COG1111    323 AMRLAEEADIEHpkLSKLREIL-------------KEQLGT-----NPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFV 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  543 G--------SMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVDRLTQPRneVFV 614
Cdd:COG1111    385 GqaskegdkGLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGR--VVV 462
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063534949  615 anLYARGTIDQSVYQLLADKLRMFELLFGQVTTILGELDDSKSATFESRVLDALFAESDSK 675
Cdd:COG1111    463 --LIAKGTRDEAYYWSSRRKEKKMKSILKKLKKLLDKQEKEKLKESAQATLDEFESIKELA 521
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
196-368 5.55e-20

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: 90.34  E-value: 5.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  196 MPHQAAAARHALSRlRGRAILADEVGLGKTIEA-GLAvkeltlrgLAKR----VIVLCPAPLRDQWREEMnQKFDMQFDV 270
Cdd:cd18010      2 LPFQREGVCFALRR-GGRVLIADEMGLGKTVQAiAIA--------AYYReewpLLIVCPSSLRLTWADEI-ERWLPSLPP 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  271 AYSGLDIGSQDKL--------IVSLALGTRHIGKLAKTPWDIVIVDEaHRAAGAGARKRRELVTALTTECRYAFFLTATP 342
Cdd:cd18010     72 DDIQVIVKSKDGLrdgdakvvIVSYDLLRRLEKQLLARKFKVVICDE-SHYLKNSKAKRTKAALPLLKRAKRVILLSGTP 150
                          170       180
                   ....*....|....*....|....*.
gi 1063534949  343 VQNDLLELYRLVELLRPGTFRSEREF 368
Cdd:cd18010    151 ALSRPIELFTQLDALDPKLFGRFHDF 176
HELICc smart00490
helicase superfamily c-terminal domain;
522-604 1.30e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.96  E-value: 1.30e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949   522 DTVTGLLRRMeleGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNYDLPWNPMRIEQRIGR 601
Cdd:smart00490    1 EELAELLKEL---GIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ...
gi 1063534949   602 VDR 604
Cdd:smart00490   78 AGR 80
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
197-397 1.75e-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: 90.04  E-value: 1.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  197 PHQAAAARHALSRLRGR-------AILADEVGLGKTIEAGLAVKEL-----TLRGLAKRVIVLCPAPLRDQWREEMN--- 261
Cdd:cd18004      3 PHQREGVQFLYDCLTGRrgyggggAILADEMGLGKTLQAIALVWTLlkqgpYGKPTAKKALIVCPSSLVGNWKAEFDkwl 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  262 ----------------QKFDMQFDVAYSGLDIgsqdkLIVSLALGTRHIGKLAKT-PWDIVIVDEAHRAAGAGArKRREL 324
Cdd:cd18004     83 glrrikvvtadgnakdVKASLDFFSSASTYPV-----LIISYETLRRHAEKLSKKiSIDLLICDEGHRLKNSES-KTTKA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  325 VTALTTECRyaFFLTATPVQNDLLELYRLVELLRPGTFRSEREFRREFMT----SYDPRRPTD--------PAALRSLIS 392
Cdd:cd18004    157 LNSLPCRRR--LLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpilrSRDPDASEEdkelgaerSQELSELTS 234

                   ....*
gi 1063534949  393 NAMIR 397
Cdd:cd18004    235 RFILR 239
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
197-759 1.01e-17

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 89.31  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  197 PHQAAA---ARHALSRLRGRAILADEVGLGKTIEAGLAVKELtlrGLAKRVIVLCPAP-LRDQWREEMNQKFDmqfDVAY 272
Cdd:COG1061     83 PYQQEAleaLLAALERGGGRGLVVAPTGTGKTVLALALAAEL---LRGKRVLVLVPRReLLEQWAEELRRFLG---DPLA 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  273 SGLDIGSQDKLIV----SLAlGTRHIGKLAKTpWDIVIVDEAHRAAGAgarKRRELVTALTTECRYAffLTATPvqndll 348
Cdd:COG1061    157 GGGKKDSDAPITVatyqSLA-RRAHLDELGDR-FGLVIIDEAHHAGAP---SYRRILEAFPAAYRLG--LTATP------ 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  349 elyrlvellrpgtFRSERefRREFMTSYDPRRPTDPaaLRSLISNAMIRttraqagvdrvtrkpidigidlgprERELYA 428
Cdd:COG1061    224 -------------FRSDG--REILLFLFDGIVYEYS--LKEAIEDGYLA-------------------------PPEYYG 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  429 LSTDLlrnvmtspgdtmrrrslalrltaspfsmgtTALRMAERHPDEHVRKVLTeighfamdisgsAREDRALDITHRWL 508
Cdd:COG1061    262 IRVDL------------------------------TDERAEYDALSERLREALA------------ADAERKDKILRELL 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  509 KDHG---RVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGqnlqfcncvln 585
Cdd:COG1061    300 REHPddrKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEG----------- 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  586 YDLPW-----------NPMRIEQRIGRVDRLTQPRNEVFVANLYARgtiDQSVYQLLADKLRMFELLFGQVTTILGELDD 654
Cdd:COG1061    369 VDVPRldvaillrptgSPREFIQRLGRGLRPAPGKEDALVYDFVGN---DVPVLEELAKDLRDLAGYRVEFLDEEESEEL 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  655 SKSATFESRVLDALFAESDSKMQELLSELGTELADARERASTLIAADSGLSKWMTSALDHREGLTKEGSTDLAPEIRRRA 734
Cdd:COG1061    446 ALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLK 525
                          570       580
                   ....*....|....*....|....*
gi 1063534949  735 RIRQRRVQAWVRRVLKALDAQILHD 759
Cdd:COG1061    526 LLLLLLLLLLLELLELLAALLRLEE 550
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
486-604 1.26e-17

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 81.01  E-value: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  486 HFAMDISGSAREDRALDITHRWLKDhGRVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGEAPIM 565
Cdd:cd18787      3 QLYVVVEEEEKKLLLLLLLLEKLKP-GKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVL 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1063534949  566 VSTDSGAEGQNLQFCNCVLNYDLPWNPmriEQ---RIGRVDR 604
Cdd:cd18787     82 VATDVAARGLDIPGVDHVINYDLPRDA---EDyvhRIGRTGR 120
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
207-399 1.47e-17

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: 83.77  E-value: 1.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  207 LSRLR----GrAILADEVGLGKTIEAgLAV----KEltlRGLAKRVIVLCPAPLRDQWREEMnQKFDMQFDVA-YSG--- 274
Cdd:cd18012     16 LSFLRhyglG-GILADDMGLGKTLQT-LALllsrKE---EGRKGPSLVVAPTSLIYNWEEEA-AKFAPELKVLvIHGtkr 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  275 -----LDIGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArKRRELVTALTTecRYAFFLTATPVQNDLLE 349
Cdd:cd18012     90 kreklRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQT-KTAKAVKALKA--DHRLALTGTPIENHLGE 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063534949  350 LYRLVELLRPGTFRSEREFRREF-MTSYDPRRPTDPAALRSLISNAMIRTT 399
Cdd:cd18012    167 LWSIFDFLNPGLLGSYKRFKKRFaKPIEKDGDEEALEELKKLISPFILRRL 217
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
196-397 2.13e-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: 80.79  E-value: 2.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  196 MPHQaaaaRHALSRLRGRA-ILADEVGLGKTIEAgLA-------------------VKELTLRGLAKRVIVLCPAPLRDQ 255
Cdd:cd18008      2 LPYQ----KQGLAWMLPRGgILADEMGLGKTIQA-LAlilatrpqdpkipeeleenSSDPKKLYLSKTTLIVVPLSLLSQ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  256 WREEMNQKFD---------------------MQFDV---AYSGLDI-GSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEA 310
Cdd:cd18008     77 WKDEIEKHTKpgslkvyvyhgskriksieelSDYDIvitTYGTLASeFPKNKKGGGRDSKEKEASPLHRIRWYRVILDEA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  311 HRAAGAGARKRReLVTALTTECRYAffLTATPVQNDLLELYRLVELLRPGTFRSEREFRREFMTSYDPRRPTDPAALRSL 390
Cdd:cd18008    157 HNIKNRSTKTSR-AVCALKAERRWC--LTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRKALERLQAL 233

                   ....*..
gi 1063534949  391 ISNAMIR 397
Cdd:cd18008    234 LKPILLR 240
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
198-402 5.41e-16

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: 80.81  E-value: 5.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  198 HQAAAARHALSRLRGRA---ILADEVGLGKTIEA---GLAVKEL-TLRGLAkrVIVLCPAPLRDQWREEMNQ-------- 262
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrggILADEMGLGKTLQTislLLYLKHVdKNWGGP--TLIVVPLSLLHNWMNEFERwvsppalr 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  263 ------KFDMQFDVAYSGLDIGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArKRRELVTALTTecRYAF 336
Cdd:pfam00176   79 vvvlhgNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKS-KLSKALKSLKT--RNRW 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063534949  337 FLTATPVQNDLLELYRLVELLRPGTFRSEREFRREFmtSYDPRRPTDP---AALRSLISNAMIRTTRAQ 402
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWF--DRPIERGGGKkgvSRLHKLLKPFLLRRTKKD 222
DEXDc smart00487
DEAD-like helicases superfamily;
197-366 1.11e-15

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 77.92  E-value: 1.11e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949   197 PHQAAAARHALSRLRGrAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCP-APLRDQWREEMNQKFDMQFDVA---Y 272
Cdd:smart00487   11 PYQKEAIEALLSGLRD-VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPSLGLKVvglY 89
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949   273 SGLDIGSQDKLIVS----LALGT-----RHI--GKLAKTPWDIVIVDEAHRAAGAGARKRRELVTALTTECRYAFFLTAT 341
Cdd:smart00487   90 GGDSKREQLRKLESgktdILVTTpgrllDLLenDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLSAT 169
                           170       180
                    ....*....|....*....|....*...
gi 1063534949   342 P---VQNDLLELYRLVELLRPGTFRSER 366
Cdd:smart00487  170 PpeeIENLLELFLNDPVFIDVGFTPLEP 197
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
214-379 1.52e-14

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: 75.08  E-value: 1.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  214 AILADEVGLGKTIEAGLAV--------KELTLRGLakRVIVLCPAPLRDQWREEMNQKFDMQFD--VAYSG--------- 274
Cdd:cd17999     22 GILCDDMGLGKTLQTLCILasdhhkraNSFNSENL--PSLVVCPPTLVGHWVAEIKKYFPNAFLkpLAYVGppqerrrlr 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  275 LDIGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArKRRELVTALTTECRyaFFLTATPVQNDLLELYRLV 354
Cdd:cd17999    100 EQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKT-KLSKAVKQLKANHR--LILSGTPIQNNVLELWSLF 176
                          170       180
                   ....*....|....*....|....*....
gi 1063534949  355 ELLRPGTFRSEREFRREF----MTSYDPR 379
Cdd:cd17999    177 DFLMPGYLGTEKQFQRRFlkpiLASRDSK 205
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
209-372 2.76e-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: 74.50  E-value: 2.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  209 RLRGR--AILADEVGLGKTIEAGLAVKELTLRG------LAKRVIVLCPAPLRDQWREEMnQKFDMQFDVAYSGLDigsQ 280
Cdd:cd18066     20 RVNERfgAILADEMGLGKTLQCISLIWTLLRQGpyggkpVIKRALIVTPGSLVKNWKKEF-QKWLGSERIKVFTVD---Q 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  281 DK-------------LIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArkrrELVTALTT-ECRYAFFLTATPVQND 346
Cdd:cd18066     96 DHkveefiasplysvLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSI----KTTTALTSlSCERRIILTGTPIQND 171
                          170       180
                   ....*....|....*....|....*.
gi 1063534949  347 LLELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd18066    172 LQEFFALIDFVNPGILGSLSTYRKVY 197
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
495-604 4.52e-14

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 76.72  E-value: 4.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  495 AREDRALDITHRWLKDH--GRVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGA 572
Cdd:COG0513    223 VDKRDKLELLRRLLRDEdpERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAA 302
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1063534949  573 EG---QNLQFcncVLNYDLPWNPmriEQ---RIGRVDR 604
Cdd:COG0513    303 RGidiDDVSH---VINYDLPEDP---EDyvhRIGRTGR 334
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
215-359 1.28e-13

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: 71.59  E-value: 1.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIE--AGLAVKELTLRGLaKRVIVLCPAPLRDQWREEMNQKFDmQFDVAY---SGLDIGSQDK------- 282
Cdd:cd18000     23 ILGDEMGLGKTIQiiAFLAALHHSKLGL-GPSLIVCPATVLKQWVKEFHRWWP-PFRVVVlhsSGSGTGSEEKlgsierk 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  283 -------------LIVSLALGTRHIGKLAKTPWDIVIVDEahraagagARKRRELVTALTTECR-----YAFFLTATPVQ 344
Cdd:cd18000    101 sqlirkvvgdggiLITTYEGFRKHKDLLLNHNWQYVILDE--------GHKIRNPDAEITLACKqlrtpHRLILSGTPIQ 172
                          170
                   ....*....|....*
gi 1063534949  345 NDLLELYRLVELLRP 359
Cdd:cd18000    173 NNLKELWSLFDFVFP 187
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
214-372 3.47e-13

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: 71.25  E-value: 3.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  214 AILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFDVAYSGLDIGSQDK----------- 282
Cdd:cd18001     22 GILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFHGTSKKERERnleriqrgggv 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  283 LIVSLALGTRHIGKLAKTP-----WDIVIVDEaHRAAGAGARKRRELVTALTTECRyaFFLTATPVQNDLLELYRLVELL 357
Cdd:cd18001    102 LLTTYGMVLSNTEQLSADDhdefkWDYVILDE-GHKIKNSKTKSAKSLREIPAKNR--IILTGTPIQNNLKELWALFDFA 178
                          170
                   ....*....|....*.
gi 1063534949  358 RPGTFR-SEREFRREF 372
Cdd:cd18001    179 CNGSLLgTRKTFKMEF 194
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
211-397 2.19e-12

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: 68.54  E-value: 2.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  211 RGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQfDVAYSGLDIGSQ---------- 280
Cdd:cd18060     19 RQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMN-TIVYHGSLASRQmiqqyemyck 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  281 -------------DKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAagagarKRR--ELVTALT-TECRYAFFLTATPVQ 344
Cdd:cd18060     98 dsrgrlipgaykfDALITTFEMILSDCPELREIEWRCVIIDEAHRL------KNRncKLLDSLKhMDLEHKVLLTGTPLQ 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063534949  345 NDLLELYRLVELLRPGTFRSEREFRREFMtsyDPRRPTDPAALRSLISNAMIR 397
Cdd:cd18060    172 NTVEELFSLLHFLEPSQFPSESEFLKDFG---DLKTEEQVQKLQAILKPMMLR 221
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
215-372 2.68e-12

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: 68.43  E-value: 2.68e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKELTLRGlAKRVIVLCPAPLR--DQWREE------MN--------------QKFDMQFDVAY 272
Cdd:cd17995     23 ILADEMGLGKTIQSIAFLEHLYQVE-GIRGPFLVIAPLStiPNWQREfetwtdMNvvvyhgsgesrqiiQQYEMYFKDAQ 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  273 SGLD--IGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAagagarKRR-----ELVTALTTECRyaFFLTATPVQN 345
Cdd:cd17995    102 GRKKkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRL------KNRnskllQGLKKLTLEHK--LLLTGTPLQN 173
                          170       180
                   ....*....|....*....|....*..
gi 1063534949  346 DLLELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd17995    174 NTEELWSLLNFLEPEKFPSSEEFLEEF 200
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
215-657 7.45e-12

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 70.99  E-value: 7.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKELT-LRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFDVAYSG------------LDIGSQD 281
Cdd:PLN03142   192 ILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGnpeerahqreelLVAGKFD 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  282 KLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAgarKRRELVTALTTECRYAFFLTATPVQNDLLELYRLVELLRPGT 361
Cdd:PLN03142   272 VCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNE---NSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEI 348
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  362 FRSEREFRREFMTSYDPRRPTDPAALRSLISNAMIRttRAQAGVDR--VTRKPIDIGIDLGPRERELYA--LSTDLlrNV 437
Cdd:PLN03142   349 FSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLR--RLKSDVEKglPPKKETILKVGMSQMQKQYYKalLQKDL--DV 424
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  438 MTSPGDTMRRRSLALRLTA---SPFsmgttALRMAERHP----DEHvrkVLTEIGHFAMdisgsaredraLDITHRWLKD 510
Cdd:PLN03142   425 VNAGGERKRLLNIAMQLRKccnHPY-----LFQGAEPGPpyttGEH---LVENSGKMVL-----------LDKLLPKLKE 485
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  511 HG-RVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFR---SGEAPIMVSTDSGAEGQNLQFCNCVLNY 586
Cdd:PLN03142   486 RDsRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNkpgSEKFVFLLSTRAGGLGINLATADIVILY 565
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063534949  587 DLPWNPMRIEQRIGRVDRLTQPRnEVFVANLYARGTIDQSVYQLLADKLRMFELLFGQvttilGELDDSKS 657
Cdd:PLN03142   566 DSDWNPQVDLQAQDRAHRIGQKK-EVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ-----GRLAEQKT 630
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
211-397 8.49e-12

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: 66.99  E-value: 8.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  211 RGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFdVAYSGLDIGSQ---------- 280
Cdd:cd18058     19 RKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNA-IVYHGSQISRQmiqqyemyyr 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  281 -------------DKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArKRRELVTALTTEcrYAFFLTATPVQNDL 347
Cdd:cd18058     98 deqgnplsgifkfQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNC-KLLEGLKLMALE--HKVLLTGTPLQNSV 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1063534949  348 LELYRLVELLRPGTFRSEREFRREFMtsyDPRRPTDPAALRSLISNAMIR 397
Cdd:cd18058    175 EELFSLLNFLEPSQFPSETTFLEEFG---DLKTEEQVKKLQSILKPMMLR 221
PTZ00110 PTZ00110
helicase; Provisional
506-604 2.95e-11

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 68.65  E-value: 2.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  506 RWLKDHGRVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLN 585
Cdd:PTZ00110   372 RIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVIN 451
                           90       100
                   ....*....|....*....|..
gi 1063534949  586 YDLpwnPMRIE---QRIGRVDR 604
Cdd:PTZ00110   452 FDF---PNQIEdyvHRIGRTGR 470
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
215-372 1.18e-10

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: 63.94  E-value: 1.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIE--AGLA-------------------VKELTLRGLAKRVIVLCPAPLRDQWREEMN------------ 261
Cdd:cd18005     23 ILGDDMGLGKTVQviAFLAavlgktgtrrdrennrprfKKKPPASSAKKPVLIVAPLSVLYNWKDELDtwghfevgvyhg 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  262 QKFDMQFDVAysgLDIGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEaHRAAGAGARKRRELVTALTTECRYAffLTAT 341
Cdd:cd18005    103 SRKDDELEGR---LKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADE-AHRIKNPKSKLTQAMKELKCKVRIG--LTGT 176
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1063534949  342 PVQNDLLELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd18005    177 LLQNNMKELWCLLDWAVPGALGSRSQFKKHF 207
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
215-372 1.19e-10

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: 63.51  E-value: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMN--------------------QKFDMQFDVAYSG 274
Cdd:cd18059     23 ILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRtwtelnvvvyhgsqasrrtiQLYEMYFKDPQGR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  275 LDIGSQD--KLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGagarKRRELVTALTT-ECRYAFFLTATPVQNDLLELY 351
Cdd:cd18059    103 VIKGSYKfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKN----RNCKLLEGLKMmDLEHKVLLTGTPLQNTVEELF 178
                          170       180
                   ....*....|....*....|.
gi 1063534949  352 RLVELLRPGTFRSEREFRREF 372
Cdd:cd18059    179 SLLHFLEPSRFPSETTFMQEF 199
PRK13766 PRK13766
Hef nuclease; Provisional
498-716 5.82e-10

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 64.51  E-value: 5.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  498 DRALDITHRWLKDHG--RVLIFTQHTDTVTGLLRRMELEGLRARAFHGS--------MSPSERASTIAAFRSGEAPIMVS 567
Cdd:PRK13766   350 EKLREIVKEQLGKNPdsRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVS 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  568 TDSGAEGQNLQFCNCVLNYDlpwnP----MRIEQRIGRVDRLTQPRneVFVanLYARGTIDQSVYQL-LADKLRMFELLF 642
Cdd:PRK13766   430 TSVAEEGLDIPSVDLVIFYE----PvpseIRSIQRKGRTGRQEEGR--VVV--LIAKGTRDEAYYWSsRRKEKKMKEELK 501
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063534949  643 GqvttILGELDDSKSATFESRVLDALFAESDSKMQELLSELGTELADARERASTLIAADSGLSKWMTSALDHRE 716
Cdd:PRK13766   502 N----LKGILNKKLQELDEEQKGEEEEKDEQLSLDDFVKSKGKEEEEEEEKEEKDKETEEDEPEGPKIIVDSRE 571
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
215-372 1.02e-09

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: 60.98  E-value: 1.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAgLAVkeltLRGLAKR------VIVLCPAPLRDQWREEMNqKFDMQFDV-AYSGldiGSQDK----- 282
Cdd:cd18002     23 ILADEMGLGKTVQS-IAV----LAHLAEEhniwgpFLVIAPASTLHNWQQEIS-RFVPQFKVlPYWG---NPKDRkvlrk 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  283 ----------------LIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGARKRRELvtaLTTECRYAFFLTATPVQND 346
Cdd:cd18002     94 fwdrknlytrdapfhvVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL---LSFHCRNRLLLTGTPIQNS 170
                          170       180
                   ....*....|....*....|....*.
gi 1063534949  347 LLELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd18002    171 MAELWALLHFIMPTLFDSHDEFNEWF 196
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
197-397 1.79e-09

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: 60.14  E-value: 1.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  197 PHQAAAARHALSRLRGR--AILADEVGLGKTIEA--GLAVKELTLrGLAKRVIVLCPAPLRDQWREEMNQ---------- 262
Cdd:cd18006      3 PYQLEGVNWLLQCRAEQhgCILGDEMGLGKTCQTisLLWYLAGRL-KLLGPFLVLCPLSVLDNWKEELNRfapdlsvity 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  263 ------KFDMQFDVaYSGLDIgsqDKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGARKRRELVTALTTECryaF 336
Cdd:cd18006     82 mgdkekRLDLQQDI-KSTNRF---HVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFR---L 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063534949  337 FLTATPVQNDLLELYRLVELLRPGTFRSEREFRreFMTSYDPRRpTDPAA---LRSLISNAMIR 397
Cdd:cd18006    155 LLTGTPIQNSLQELYALLSFIEPNVFPKDKLDD--FIKAYSETD-DESETveeLHLLLQPFLLR 215
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
197-372 8.03e-09

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: 58.64  E-value: 8.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  197 PHQAAAARHALSRLRGR-------AILADEVGLGKTIEAGLAVKELTLRG-----LAKRVIVLCPAPLRDQWREEMNQKf 264
Cdd:cd18067      3 PHQREGVKFLYRCVTGRrirgshgCIMADEMGLGKTLQCITLMWTLLRQSpqckpEIDKAIVVSPSSLVKNWANELGKW- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  265 dMQFDVAYSGLDIGSQDK--------------------LIVSLALGTRHIGKLAKTPWDIVIVDEAHRAagagarKRREL 324
Cdd:cd18067     82 -LGGRLQPLAIDGGSKKEidrklvqwasqqgrrvstpvLIISYETFRLHVEVLQKGEVGLVICDEGHRL------KNSDN 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063534949  325 VT--ALTT-ECRYAFFLTATPVQNDLLELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd18067    155 QTyqALDSlNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNF 205
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
211-372 8.22e-09

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: 58.09  E-value: 8.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  211 RGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREE--------------------MNQKFDMQFDV 270
Cdd:cd18061     19 RRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREfrtwtdlnvvvyhgslisrqMIQQYEMYFRD 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  271 AYSGLDIGSQ--DKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGagarKRRELVTALT-TECRYAFFLTATPVQNDL 347
Cdd:cd18061     99 SQGRIIRGAYrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKN----KNCKLLEGLKlMNLEHKVLLTGTPLQNTV 174
                          170       180
                   ....*....|....*....|....*
gi 1063534949  348 LELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd18061    175 EELFSLLHFLEPLRFPSESTFMQEF 199
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
215-373 1.79e-08

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: 56.98  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIE-----AGLAVKEltlrGLAKRVIVLCPAPLRDQWREEMnQKFDMQFDV-AYsgldIGSQDKL----- 283
Cdd:cd18003     23 ILADEMGLGKTIQtiallAHLACEK----GNWGPHLIVVPTSVMLNWEMEF-KRWCPGFKIlTY----YGSAKERklkrq 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  284 -----------IVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArKRRELVTALTTECRyaFFLTATPVQNDLLELYR 352
Cdd:cd18003     94 gwmkpnsfhvcITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKS-QRWQTLLNFNTQRR--LLLTGTPLQNSLMELWS 170
                          170       180
                   ....*....|....*....|.
gi 1063534949  353 LVELLRPGTFRSEREFRREFM 373
Cdd:cd18003    171 LMHFLMPHIFQSHQEFKEWFS 191
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
214-372 2.56e-08

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: 56.29  E-value: 2.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  214 AILADEVGLGKTIEAGLAVKELTLRGLAKRVIvLCPAPLRD--QWREEMNQKFDMQFDVAYSGLDIgsqdkLIVSLALGT 291
Cdd:cd17994     22 TILADEMGLGKTIQTIVFLYSLYKEGHSKGPF-LVSAPLSTiiNWEREFEMWAPDFYVVTYVGDHV-----LLTSYELIS 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  292 RHIGKLAKTPWDIVIVDEAHRAAGAGARKRRELVTaltTECRYAFFLTATPVQNDLLELYRLVELLRPGTFRSEREFRRE 371
Cdd:cd17994     96 IDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNS---YKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEE 172

                   .
gi 1063534949  372 F 372
Cdd:cd17994    173 F 173
PRK04537 PRK04537
ATP-dependent RNA helicase RhlB; Provisional
513-628 3.06e-08

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 235307 [Multi-domain]  Cd Length: 572  Bit Score: 58.81  E-value: 3.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  513 RVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNYDLPWNP 592
Cdd:PRK04537   259 RTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDA 338
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1063534949  593 MRIEQRIGRVDRLTQPRNEV-FVANLYARGTIDQSVY 628
Cdd:PRK04537   339 EDYVHRIGRTARLGEEGDAIsFACERYAMSLPDIEAY 375
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
214-362 9.23e-08

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: 54.31  E-value: 9.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  214 AILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNqKF--DMQFDVAYsgldiGSQDK--------- 282
Cdd:cd17998     22 GILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFK-RWcpSLKVEPYY-----GSQEErkhlrydil 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  283 -------LIVS---LALGTRHIGKLAKT-PWDIVIVDEAHRAAGAGARKRRELvtaLTTECRYAFFLTATPVQNDLLELY 351
Cdd:cd17998     96 kgledfdVIVTtynLATSNPDDRSFFKRlKLNYVVYDEGHMLKNMTSERYRHL---MTINANFRLLLTGTPLQNNLLELM 172
                          170
                   ....*....|.
gi 1063534949  352 RLVELLRPGTF 362
Cdd:cd17998    173 SLLNFIMPKPF 183
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
215-372 1.14e-07

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: 55.08  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCPAPLRDQWREEMnQKFDMQFDVA-YSGlDIGSQDKL---------- 283
Cdd:cd18009     26 ILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEF-ARFTPSVPVLlYHG-TKEERERLrkkimkregt 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  284 -------IVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGARKRRELVTaLTTECRyaFFLTATPVQNDLLELYRLVEL 356
Cdd:cd18009    104 lqdfpvvVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKT-FNSDNR--LLLTGTPLQNNLSELWSLLNF 180
                          170
                   ....*....|....*.
gi 1063534949  357 LRPGTFRSEREFRREF 372
Cdd:cd18009    181 LLPDVFDDLSSFESWF 196
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
196-362 2.24e-07

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 54.02  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  196 MPHQaaaaRHALSRLRGR-------AILADEVGLGKTI------------------EAGLAVKELTLRGLAKRV-----I 245
Cdd:cd18072      2 LLHQ----KQALAWLLWRerqkprgGILADDMGLGKTLtmialilaqkntqnrkeeEKEKALTEWESKKDSTLVpsagtL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  246 VLCPAPLRDQWREEMNQKFDMQFDVAY---------SGLDIGSQDKLIVSLALGTRHIGKLAKTP---------WDIVIV 307
Cdd:cd18072     78 VVCPASLVHQWKNEVESRVASNKLRVClyhgpnrerIGEVLRDYDIVITTYSLVAKEIPTYKEESrssplfriaWARIIL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063534949  308 DEAHRAAGAGARKRRElVTALTTECRYAffLTATPVQNDLLELYRLVELLRPGTF 362
Cdd:cd18072    158 DEAHNIKNPKVQASIA-VCKLRAHARWA--LTGTPIQNNLLDMYSLLKFLRCSPF 209
PRK10590 PRK10590
ATP-dependent RNA helicase RhlE; Provisional
513-604 2.69e-07

ATP-dependent RNA helicase RhlE; Provisional


Pssm-ID: 236722 [Multi-domain]  Cd Length: 456  Bit Score: 55.58  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  513 RVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNYDLPWNP 592
Cdd:PRK10590   247 QVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVP 326
                           90
                   ....*....|..
gi 1063534949  593 MRIEQRIGRVDR 604
Cdd:PRK10590   327 EDYVHRIGRTGR 338
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
210-397 3.43e-07

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: 53.63  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  210 LRGrAILADEVGLGKTIEAGLAVkeltlrgLAKRVIVLCPAPLRDQWREEMNQKF-DMQFDV-AYSGLD-------IGSQ 280
Cdd:cd18071     48 VRG-GILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVkPGQLKVyTYHGGErnrdpklLSKY 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  281 DKLI-----VSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGARKRReLVTALTTECRYAffLTATPVQNDLLELYRLVE 355
Cdd:cd18071    120 DIVLttyntLASDFGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTK-AVLNLSSERRWV--LTGTPIQNSPKDLGSLLS 196
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1063534949  356 LLRPGTFRSEREFRREFMTsydPRRPTDPAA---LRSLISNAMIR 397
Cdd:cd18071    197 FLHLKPFSNPEYWRRLIQR---PLTMGDPTGlkrLQVLMKQITLR 238
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
197-372 3.99e-07

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: 53.28  E-value: 3.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  197 PHQAAAAR-------HALSRLRGRA----ILADEVGLGKTIEAgLAVKELTLRGL-AKRVIVLCPAPLRDQWREEMNQ-- 262
Cdd:cd18069      3 PHQIGGIRflydniiESLERYKGSSgfgcILAHSMGLGKTLQV-ISFLDVLLRHTgAKTVLAIVPVNTLQNWLSEFNKwl 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  263 -KFDMQFDVAYSGLDI---GSQDKLIVSLA---LGTRHIG----------KLAKTPwDIVIVDEAhraagagarKRRELV 325
Cdd:cd18069     82 pPPEALPNVRPRPFKVfilNDEHKTTAARAkviEDWVKDGgvllmgyemfRLRPGP-DVVICDEG---------HRIKNC 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063534949  326 TALTTE------CRYAFFLTATPVQNDLLELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd18069    152 HASTSQalknirSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 204
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
214-372 5.17e-07

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: 53.14  E-value: 5.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  214 AILADEVGLGKTIEA-GLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFDVAYSG-----------LDIGSQD 281
Cdd:cd18063     45 GILADEMGLGKTIQTiALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGtpamrrslvpqLRSGKFN 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  282 KLIVSLA--LGTRHIgkLAKTPWDIVIVDEAHRAAGAGARKRRELVTALTTECRyaFFLTATPVQNDLLELYRLVELLRP 359
Cdd:cd18063    125 VLLTTYEyiIKDKHI--LAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRR--ILLTGTPLQNKLPELWALLNFLLP 200
                          170
                   ....*....|...
gi 1063534949  360 GTFRSEREFRREF 372
Cdd:cd18063    201 TIFKSCSTFEQWF 213
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
196-372 5.21e-07

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: 53.06  E-value: 5.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  196 MPHQAAAARHALSRLRGRA---------ILADEVGLGKTIEAgLAVKELTLRGL--AKRVIVLCPAPLRDQWREEMN--- 261
Cdd:cd18007      2 KPHQVEGVRFLWSNLVGTDvgsdegggcILAHTMGLGKTLQV-ITFLHTYLAAAprRSRPLVLCPASTLYNWEDEFKkwl 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  262 ----------------QKFDMQFDVAYSGldigSQDK--LIVSLALGTRHIGKLAKTPW--------------DIVIVDE 309
Cdd:cd18007     81 ppdlrpllvlvslsasKRADARLRKINKW----HKEGgvLLIGYELFRNLASNATTDPRlkqefiaalldpgpDLLVLDE 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063534949  310 AHRAagagarkRRE---LVTALT---TECRYAffLTATPVQNDLLELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd18007    157 GHRL-------KNEksqLSKALSkvkTKRRIL--LTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
214-372 5.38e-07

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: 53.12  E-value: 5.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  214 AILADEVGLGKTIEA-GLAVKELTLRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFDVAYSG-----------LDIGSQD 281
Cdd:cd18062     45 GILADEMGLGKTIQTiALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVSYKGspaarrafvpqLRSGKFN 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  282 KLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGARKRRELVTALTTECRyaFFLTATPVQNDLLELYRLVELLRPGT 361
Cdd:cd18062    125 VLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRR--LLLTGTPLQNKLPELWALLNFLLPTI 202
                          170
                   ....*....|.
gi 1063534949  362 FRSEREFRREF 372
Cdd:cd18062    203 FKSCSTFEQWF 213
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
197-379 5.38e-07

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: 52.74  E-value: 5.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  197 PHQAAAARHALSRLRGrAILADeVGLGKTIEAGLAVKELTLRGLAKRVIVLcpAPLR---DQWREEMNQkfdmqfdvaYS 273
Cdd:cd18013      3 PYQKVAINFIIEHPYC-GLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVI--APLRvarSTWPDEVEK---------WN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  274 GLdigsqDKLIVSLALGT-RHIGKLAKTPWDI-----------------------VIVDEaHRAAGAGARKRRELVTALT 329
Cdd:cd18013     70 HL-----RNLTVSVAVGTeRQRSKAANTPADLyvinrenlkwlvnksgdpwpfdmVVIDE-LSSFKSPRSKRFKALRKVR 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1063534949  330 TECRYAFFLTATPVQNDLLELYRLVELLRpgtfRSEREFRreFMTSYDPR 379
Cdd:cd18013    144 PVIKRLIGLTGTPSPNGLMDLWAQIALLD----QGERLGR--SITAYRER 187
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
215-374 7.30e-07

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: 52.37  E-value: 7.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKEL-----------------TLRG----LAK-----RVIVLCPAPlrDQWREEMNQKFDMQF 268
Cdd:cd17996     26 ILADEMGLGKTIQTISLITYLmekkknngpylvivplsTLSNwvseFEKwapsvSKIVYKGTP--DVRKKLQSQIRAGKF 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  269 DVAYSGLDIGSQDKLivslalgtrhigKLAKTPWDIVIVDEAHRAAGAGARKRRELVTALTTecRYAFFLTATPVQNDLL 348
Cdd:cd17996    104 NVLLTTYEYIIKDKP------------LLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHA--RYRLLLTGTPLQNNLP 169
                          170       180
                   ....*....|....*....|....*.
gi 1063534949  349 ELYRLVELLRPGTFRSEREFRREFMT 374
Cdd:cd17996    170 ELWALLNFLLPKIFKSCKTFEQWFNT 195
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
513-604 7.51e-07

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 54.15  E-value: 7.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  513 RVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNYDLPWNP 592
Cdd:PRK01297   337 RVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDP 416
                           90
                   ....*....|..
gi 1063534949  593 MRIEQRIGRVDR 604
Cdd:PRK01297   417 DDYVHRIGRTGR 428
PTZ00424 PTZ00424
helicase 45; Provisional
524-604 8.00e-07

helicase 45; Provisional


Pssm-ID: 185609 [Multi-domain]  Cd Length: 401  Bit Score: 53.68  E-value: 8.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  524 VTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVD 603
Cdd:PTZ00424   280 VDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSG 359

                   .
gi 1063534949  604 R 604
Cdd:PTZ00424   360 R 360
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
214-375 1.99e-06

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: 51.20  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  214 AILADEVGLGKTIEAglavkeLTLRGLAKRV-------IVLCPAPLRDQWREEMNQKFDMQFDVAYSG------------ 274
Cdd:cd18064     37 GILADEMGLGKTLQT------ISLLGYMKHYrnipgphMVLVPKSTLHNWMAEFKRWVPTLRAVCLIGdkdqraafvrdv 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  275 LDIGSQDKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArKRRELVTALTTECRyaFFLTATPVQNDLLELYRLV 354
Cdd:cd18064    111 LLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKS-KLSEIVREFKTTNR--LLLTGTPLQNNLHELWALL 187
                          170       180
                   ....*....|....*....|.
gi 1063534949  355 ELLRPGTFRSEREFRREFMTS 375
Cdd:cd18064    188 NFLLPDVFNSAEDFDSWFDTN 208
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
215-368 2.98e-06

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: 50.43  E-value: 2.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEA----GLAVKELTLRGLAKRVIVLC--PAPLR--DQWREEMNQkfdmqfdVAYSGlDIGSQD----- 281
Cdd:cd17993     24 ILADEMGLGKTVQTisflSYLFHSQQQYGPFLVVVPLStmPAWQRefAKWAPDMNV-------IVYLG-DIKSRDtirey 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  282 --------KLIVSLALGTRHI-----GKLAKTPWDIVIVDEAHRAagagarKRRE--LVTALT---TECRyaFFLTATPV 343
Cdd:cd17993     96 efyfsqtkKLKFNVLLTTYEIilkdkAFLGSIKWQYLAVDEAHRL------KNDEslLYEALKefkTNNR--LLITGTPL 167
                          170       180
                   ....*....|....*....|....*
gi 1063534949  344 QNDLLELYRLVELLRPGTFRSEREF 368
Cdd:cd17993    168 QNSLKELWALLHFLMPGKFDIWEEF 192
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
513-604 3.10e-06

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 48.89  E-value: 3.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  513 RVLIFTQHTDTVTGLLRRME--LEGLRARAFHGS--------MSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNC 582
Cdd:cd18801     32 RVIIFSEFRDSAEEIVNFLSkiRPGIRATRFIGQasgksskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDL 111
                           90       100
                   ....*....|....*....|..
gi 1063534949  583 VLNYDLPWNPMRIEQRIGRVDR 604
Cdd:cd18801    112 IICYDASPSPIRMIQRMGRTGR 133
PRK11634 PRK11634
ATP-dependent RNA helicase DeaD; Provisional
490-700 7.25e-06

ATP-dependent RNA helicase DeaD; Provisional


Pssm-ID: 236941 [Multi-domain]  Cd Length: 629  Bit Score: 51.00  E-value: 7.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  490 DISGS------AREDRALDithRWLK--DHGRVLIFTQHTDTVTGLLRRMELEGLRARAFHGSMSPSERASTIAAFRSGE 561
Cdd:PRK11634   219 DISQSywtvwgMRKNEALV---RFLEaeDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGR 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  562 APIMVSTDSGAEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVDRLTQP-RNEVFVANLYARgtidqsvyqLLADKLRMFEL 640
Cdd:PRK11634   296 LDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAgRALLFVENRERR---------LLRNIERTMKL 366
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063534949  641 LFGQVTTILGEL-DDSKSATFESRVLDALFAESDSKMQELLSELGTELADARERASTLIAA 700
Cdd:PRK11634   367 TIPEVELPNAELlGKRRLEKFAAKVQQQLESSDLDQYRALLAKIQPTAEGEELDLETLAAA 427
SF2_C_dicer cd18802
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ...
506-601 8.81e-06

C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains 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: 350189 [Multi-domain]  Cd Length: 142  Bit Score: 47.59  E-value: 8.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  506 RWLKDHGRVLIFTqHTDTVTGllrrmelEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLN 585
Cdd:cd18802     43 RLLKEHPSTLAFI-RCGFLIG-------RGNSSQRKRSLMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIR 114
                           90
                   ....*....|....*.
gi 1063534949  586 YDLPWNPMRIEQRIGR 601
Cdd:cd18802    115 FDLPKTLRSYIQSRGR 130
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
214-375 9.34e-06

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: 49.25  E-value: 9.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  214 AILADEVGLGKTIEAGLAVKELT-LRGLAKRVIVLCPAPLRDQWREEMNQKFDMQFDVAYSG------------LDIGSQ 280
Cdd:cd18065     37 GILADEMGLGKTLQTIALLGYLKhYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVCLIGdkdaraafirdvMMPGEW 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  281 DKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArKRRELVTALTTECRyaFFLTATPVQNDLLELYRLVELLRPG 360
Cdd:cd18065    117 DVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKS-KLSEIVREFKTTNR--LLLTGTPLQNNLHELWALLNFLLPD 193
                          170
                   ....*....|....*
gi 1063534949  361 TFRSEREFRREFMTS 375
Cdd:cd18065    194 VFNSADDFDSWFDTK 208
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
215-372 1.64e-05

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: 48.09  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIE--AGLA-VKELtlRGLAKRVIVLCPAPLRDQWREEMNQ--------KF----DMQFDVAYSGLDIGS 279
Cdd:cd17997     26 ILADEMGLGKTLQtiSLLGyLKHY--KNINGPHLIIVPKSTLDNWMREFKRwcpslrvvVLigdkEERADIIRDVLLPGK 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  280 QDKLIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGArKRRELVTALTTecRYAFFLTATPVQNDLLELYRLVELLRP 359
Cdd:cd17997    104 FDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKS-KLSQIVRLFNS--RNRLLLTGTPLQNNLHELWALLNFLLP 180
                          170
                   ....*....|...
gi 1063534949  360 GTFRSEREFRREF 372
Cdd:cd17997    181 DVFTSSEDFDEWF 193
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
215-397 2.81e-05

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: 47.75  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKELTLRGLAKRViVLCPAPLRD--QWREEMN-----------------------QKFDMQFD 269
Cdd:cd18057     23 ILADEMGLGKTVQTIVFLYSLYKEGHSKGP-YLVSAPLSTiiNWEREFEmwapdfyvvtytgdkesrsvireNEFSFEDN 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  270 VAYSGLDIGSQDK--------LIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGARKRRELVTaltTECRYAFFLTAT 341
Cdd:cd18057    102 AIRSGKKVFRMKKeaqikfhvLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNS---YKIDYKLLLTGT 178
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063534949  342 PVQNDLLELYRLVELLRPGTFRSEREFRREFMtsyDPRRPTDPAALRSLISNAMIR 397
Cdd:cd18057    179 PLQNNLEELFHLLNFLTPERFNNLEGFLEEFA---DISKEDQIKKLHDLLGPHMLR 231
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
215-372 4.09e-05

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: 47.37  E-value: 4.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKELTLRGLAKRVIvLCPAPLRD--QWREEmnqkFDMQFDVAYSGLDIGSQDK---------- 282
Cdd:cd18056     23 ILADEMGLGKTVQTAVFLYSLYKEGHSKGPF-LVSAPLSTiiNWERE----FEMWAPDMYVVTYVGDKDSraiirenefs 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  283 -------------------------LIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGARKRRELVTaltTECRYAFF 337
Cdd:cd18056     98 fednairggkkasrmkkeasvkfhvLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNG---YSLQHKLL 174
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1063534949  338 LTATPVQNDLLELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd18056    175 LTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF 209
ResIII pfam04851
Type III restriction enzyme, res subunit;
197-309 5.15e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 45.74  E-value: 5.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  197 PHQAAAAR---HALSRLRGRAILADEVGLGKTIEAGLAVKELTLRGLAKRVIVLCP-APLRDQWREEMNQKFDMQFDVA- 271
Cdd:pfam04851    6 PYQIEAIEnllESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNYVEIGe 85
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1063534949  272 -YSGLD-----------IGSQDKLIVSLALGTRHIGKLAktpWDIVIVDE 309
Cdd:pfam04851   86 iISGDKkdesvddnkivVTTIQSLYKALELASLELLPDF---FDVIIIDE 132
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
215-371 2.15e-04

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: 45.00  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKEL-TLRGLAKRVIVLCPAPLRDQWREEMNQ-KFDMQFdVAYSGlDIGSQDK---------- 282
Cdd:cd18054     43 ILADEMGLGKTIQTISFLSYLfHQHQLYGPFLLVVPLSTLTSWQREFEIwAPEINV-VVYIG-DLMSRNTireyewihsq 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  283 --------LIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGARKRRELVTaltTECRYAFFLTATPVQNDLLELYRLV 354
Cdd:cd18054    121 tkrlkfnaLITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLID---FKSNHRLLITGTPLQNSLKELWSLL 197
                          170
                   ....*....|....*..
gi 1063534949  355 ELLRPGTFRSEREFRRE 371
Cdd:cd18054    198 HFIMPEKFEFWEDFEED 214
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
498-601 2.66e-04

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases 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: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 43.41  E-value: 2.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  498 DRALDITHRWLKDHGRVLIFT---QHTDTVTGLLRRM---ELEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSG 571
Cdd:cd18796     25 ADAYAEVIFLLERHKSTLVFTntrSQAERLAQRLRELcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSL 104
                           90       100       110
                   ....*....|....*....|....*....|
gi 1063534949  572 AEGQNLQFCNCVLNYDLPWNPMRIEQRIGR 601
Cdd:cd18796    105 ELGIDIGDVDLVIQIGSPKSVARLLQRLGR 134
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
215-372 2.67e-04

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: 44.62  E-value: 2.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKELTLRGLAKRVIvLCPAPLRD--QWREEMNQKFDMQFDVAYSG------------------ 274
Cdd:cd18055     23 ILADEMGLGKTIQTIVFLYSLYKEGHTKGPF-LVSAPLSTiiNWEREFQMWAPDFYVVTYTGdkdsraiirenefsfddn 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  275 ----------LDIGSQDK---LIVSLALGTRHIGKLAKTPWDIVIVDEAHRAAGAGARKRRELVTaltTECRYAFFLTAT 341
Cdd:cd18055    102 avkggkkafkMKREAQVKfhvLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNG---YKIDHKLLLTGT 178
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1063534949  342 PVQNDLLELYRLVELLRPGTFRSEREFRREF 372
Cdd:cd18055    179 PLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
215-309 2.70e-04

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: 43.16  E-value: 2.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEAGLAVKELTLRGlAKRVIVLCP-APLRDQWREEMNQKFDMQFDVAY--SGLD-------IGSQDKLI 284
Cdd:cd00046      5 LITAPTGSGKTLAALLAALLLLLKK-GKKVLVLVPtKALALQTAERLRELFGPGIRVAVlvGGSSaeereknKLGDADII 83
                           90       100
                   ....*....|....*....|....*....
gi 1063534949  285 V----SLALGTRHIGKLAKTPWDIVIVDE 309
Cdd:cd00046     84 IatpdMLLNLLLREDRLFLKDLKLIIVDE 112
Siva pfam05458
Cd27 binding protein (Siva); Siva binds to the CD27 cytoplasmic tail. It has a DD homology ...
1505-1603 4.57e-04

Cd27 binding protein (Siva); Siva binds to the CD27 cytoplasmic tail. It has a DD homology region, a box-B-like ring finger, and a zinc finger-like domain. Overexpression of Siva in various cell lines induces apoptosis, suggesting an important role for Siva in the CD27-transduced apoptotic pathway. Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis. Indeed, the unique amphipathic helical region (SAH) present in Siva-1 is required for its binding to BCL-X(L) and sensitising cells to UV radiation. Natural complexes of Siva-1/BCL-X(L) are detected in HUT78 and murine thymocyte, suggesting a potential role for Siva-1 in regulating T cell homeostasis. This family contains both Siva-1 and the shorter Siva-2 lacking the sequence coded by exon 2. It has been suggested that Siva-2 could regulate the function of Siva-1.


Pssm-ID: 283184  Cd Length: 173  Bit Score: 43.00  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949 1505 DGHFYRASTSALCTS--CRTWACRAC-DGVDHRSSidCPSCDRPVCRRCLeqshtvvdaqcllchdRPCPQCGrdpeVLA 1581
Cdd:pfam05458   90 DGKLMRATAQSSEASptGASIACSSCvRSVDGKAV--CSQCERALCGQCV----------------RTCSGCS----SLA 147
                           90       100
                   ....*....|....*....|..
gi 1063534949 1582 CSICGRSMCSNCRVQELCPACS 1603
Cdd:pfam05458  148 CSLCTLVDYSDQYEKVLCTSCS 169
zf-UDP pfam14569
Zinc-binding RING-finger; This RING/U-box type zinc-binding domain is frequently found in the ...
2034-2093 8.20e-04

Zinc-binding RING-finger; This RING/U-box type zinc-binding domain is frequently found in the catalytic subunit (irx3) of cellulose synthase. The enzymic class is EC:2.4.1.12, whereby the synthase removes the glucose from UDP-glucose and adds it to the growing cellulose, thereby releasing UDP. The domain-structure is treble-clef like (PDB:1weo).


Pssm-ID: 464209 [Multi-domain]  Cd Length: 75  Bit Score: 40.02  E-value: 8.20e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063534949 2034 LCKYCDSTICTICTDNLVSCDCCQATICRRCV--REPHANLWLCPACATMRRPTRSEARRHG 2093
Cdd:pfam14569    7 ICQICGDDVGLTDDGELFVACNECAFPVCRPCyeYERKDGNQCCPQCKTRYKRHKGSPRVEG 68
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
215-371 1.05e-03

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: 43.11  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  215 ILADEVGLGKTIEA----GLAVKELTLRGlakRVIVLCPAPLRDQWREEMNQKFDMQFDVAYSGlDIGSQD--------- 281
Cdd:cd18053     43 ILADEMGLGKTIQTisflNYLFHEHQLYG---PFLLVVPLSTLTSWQREIQTWAPQMNAVVYLG-DINSRNmirthewmh 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  282 ----KLIVSLALGTRHI-----GKLAKTPWDIVIVDEAHRAAGAGARKRRelvTALTTECRYAFFLTATPVQNDLLELYR 352
Cdd:cd18053    119 pqtkRLKFNILLTTYEIllkdkSFLGGLNWAFIGVDEAHRLKNDDSLLYK---TLIDFKSNHRLLITGTPLQNSLKELWS 195
                          170
                   ....*....|....*....
gi 1063534949  353 LVELLRPGTFRSEREFRRE 371
Cdd:cd18053    196 LLHFIMPEKFSSWEDFEEE 214
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
501-604 1.33e-03

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. 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: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 41.04  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  501 LDITHRWLKD---HGRVLIF--TQH-TDTVTGLLRRmelEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDS---G 571
Cdd:cd18794     17 KLDLLKRIKVehlGGSGIIYclSRKeCEQVAARLQS---KGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAfgmG 93
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1063534949  572 AEGQNLQFcncVLNYDLPWNPMRIEQRIGRVDR 604
Cdd:cd18794     94 IDKPDVRF---VIHYSLPKSMESYYQESGRAGR 123
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
521-568 1.38e-03

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 43.59  E-value: 1.38e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1063534949  521 TDTVTGLLRRmelEGLRARAFHGSMSPSERASTIAAFRSGEAPIMVST 568
Cdd:COG0514    243 VEELAEWLRE---AGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT 287
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
535-608 1.98e-03

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 43.24  E-value: 1.98e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063534949  535 GLRARAFHGSMSPSERASTIAAFRSGEAPIMVSTDSGAEGQNLQFCNCVLNYDLPWNPMRIEQRIGRVDRLTQP 608
Cdd:PLN00206   392 GLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEK 465
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
1525-1588 3.25e-03

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.18  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949 1525 CRACDGVDHRSSiDCPSCDRPV------CRRCLEQSH----------TVVDAQCLLCHD-----RPCPQCGRDPEVLACS 1583
Cdd:PTZ00368     3 CYRCGGVGHQSR-ECPNSAPAGaakarpCYKCGEPGHlsrecpsapgGRGERSCYNCGKtghlsRECPEAPPGSGPRSCY 81

                   ....*
gi 1063534949 1584 ICGRS 1588
Cdd:PTZ00368    82 NCGQT 86
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
2043-2078 4.80e-03

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the second PHD finger.


Pssm-ID: 277007 [Multi-domain]  Cd Length: 43  Bit Score: 36.87  E-value: 4.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1063534949 2043 CTICTD--NLVSCDCCQATICRRCVREPHANL----WLCPAC 2078
Cdd:cd15532      2 CRVCKDggELLCCDGCPSSYHLHCLNPPLAEIpdgdWFCPRC 43
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
303-383 5.38e-03

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: 41.03  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063534949  303 DIVIVDEAHRAAGAGARKRRELVTALTtecRYAFFLTATPVQNDLLELYRLVELLRPGTFRSEREFRREFMTSYDPRRPT 382
Cdd:cd18068    157 DFVVCDEGHILKNEASAVSKAMNSIRT---KRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCA 233

                   .
gi 1063534949  383 D 383
Cdd:cd18068    234 D 234
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
2039-2078 5.55e-03

Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 37.00  E-value: 5.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1063534949 2039 DSTICTICTD---NLVSCDCCQATICRRCVREP--HANLwLCPAC 2078
Cdd:cd16620      2 DELKCPICKDlmkDAVLTPCCGNSFCDECIRTAllEEDF-TCPTC 45
RecG COG1200
RecG-like helicase [Replication, recombination and repair];
542-568 7.39e-03

RecG-like helicase [Replication, recombination and repair];


Pssm-ID: 440813 [Multi-domain]  Cd Length: 684  Bit Score: 41.57  E-value: 7.39e-03
                           10        20
                   ....*....|....*....|....*..
gi 1063534949  542 HGSMSPSERASTIAAFRSGEAPIMVST 568
Cdd:COG1200    510 HGRMKPAEKDAVMAAFKAGEIDVLVAT 536
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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