NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2004339518|ref|WP_206768020|]
View 

MULTISPECIES: DNA repair helicase XPB [Brevibacillus]

Protein Classification

Ercc3/Rad25/XPB family helicase( domain architecture ID 1004556)

Ercc3/Rad25/XPB family helicase (also known as RepB/Ssl2/haywire) is a core subunit of the eukaryotic basal transcription factor complex TFIIH and is involved in nucleotide excision repair (NER) of DNA and in RNA transcription by RNA polymerase II

CATH:  3.40.50.300
EC:  3.6.4.12
Gene Ontology:  GO:0003677|GO:0003678|GO:0005524
PubMed:  8202161
SCOP:  4000282

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
rad25 super family cl36703
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
1-548 3.32e-100

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00603:

Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 319.05  E-value: 3.32e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518   1 MSYRPD---LPLIVQSDRTILLETQHPLFPEARQAISGFTELIKNPEYIHTYRITPLSLWNAAASGLTSQEVTDVLGSYS 77
Cdd:TIGR00603   6 LELKPDhgsRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEVLGRLS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518  78 KYGVPPTIVKEIEDTMRKYGLFRL----------------------------ERI----GDQLVLM-------------- 111
Cdd:TIGR00603  86 KTPIPKGIIEFIRLCTQSYGKVKLvlkhnryfvesphpevlqrllkdpviapCRIdpteEESLQTPtygskedfiinkpg 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 112 --------------SEDPLLLAEVTSYKSIAALFENE-------FVIKSYARGLIKQELIKLGFPVqdLAGY-----TEG 165
Cdd:TIGR00603 166 ftggasagqleanqGESAVPKDIADFYELEEEEEDEDeetathsFEIDQEQVEEVKKRCIELDYPL--LEEYdfrndTVN 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 166 ESCAVSLRETTSrgrafsLRPYQKEAVDAFYSGGAVTggSGVLVLPCGAGKTVIGLGAICQLQTATLILTTNTTSVRQWI 245
Cdd:TIGR00603 244 PDLNIDLKPTTQ------IRPYQEKSLSKMFGNGRAR--SGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 246 AELLDKTGLDPNMVGEYTGDNKEvKPITVATYQILTY------RPTAEDDFPHLKLFSERDWGLIIYDEVHLLPAPIFR- 318
Cdd:TIGR00603 316 QQFKMWSTIDDSQICRFTSDAKE-RFHGEAGVVVSTYsmvahtGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRr 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 319 VTSGIQATRRLGLTATLVREDGREEDVFTLIGPKKYEVPWKVMEEQGWIAEAHCREIRLPFEPKWREAYAHATARQKFRI 398
Cdd:TIGR00603 395 VLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLL 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 399 AAENPKKLEVVRELLERHAH--DRVLIIGQYIDQLEQMATALQLPLITGKVPDKERELLYTQFKKGEITRLI-VSKVANF 475
Cdd:TIGR00603 475 YVMNPNKFRACQFLIRFHEQrgDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIfLSKVGDT 554
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2004339518 476 AVDLPDANVAIQISGTYGSRQEEAQRLGRILRPK--TDDN--TAHFYTLVTRDTREQEFSLHRQLFLVEQGYPYDII 548
Cdd:TIGR00603 555 SIDLPEANVLIQISSHYGSRRQEAQRLGRILRAKkgSDAEeyNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVI 631
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
1-548 3.32e-100

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 319.05  E-value: 3.32e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518   1 MSYRPD---LPLIVQSDRTILLETQHPLFPEARQAISGFTELIKNPEYIHTYRITPLSLWNAAASGLTSQEVTDVLGSYS 77
Cdd:TIGR00603   6 LELKPDhgsRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEVLGRLS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518  78 KYGVPPTIVKEIEDTMRKYGLFRL----------------------------ERI----GDQLVLM-------------- 111
Cdd:TIGR00603  86 KTPIPKGIIEFIRLCTQSYGKVKLvlkhnryfvesphpevlqrllkdpviapCRIdpteEESLQTPtygskedfiinkpg 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 112 --------------SEDPLLLAEVTSYKSIAALFENE-------FVIKSYARGLIKQELIKLGFPVqdLAGY-----TEG 165
Cdd:TIGR00603 166 ftggasagqleanqGESAVPKDIADFYELEEEEEDEDeetathsFEIDQEQVEEVKKRCIELDYPL--LEEYdfrndTVN 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 166 ESCAVSLRETTSrgrafsLRPYQKEAVDAFYSGGAVTggSGVLVLPCGAGKTVIGLGAICQLQTATLILTTNTTSVRQWI 245
Cdd:TIGR00603 244 PDLNIDLKPTTQ------IRPYQEKSLSKMFGNGRAR--SGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 246 AELLDKTGLDPNMVGEYTGDNKEvKPITVATYQILTY------RPTAEDDFPHLKLFSERDWGLIIYDEVHLLPAPIFR- 318
Cdd:TIGR00603 316 QQFKMWSTIDDSQICRFTSDAKE-RFHGEAGVVVSTYsmvahtGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRr 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 319 VTSGIQATRRLGLTATLVREDGREEDVFTLIGPKKYEVPWKVMEEQGWIAEAHCREIRLPFEPKWREAYAHATARQKFRI 398
Cdd:TIGR00603 395 VLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLL 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 399 AAENPKKLEVVRELLERHAH--DRVLIIGQYIDQLEQMATALQLPLITGKVPDKERELLYTQFKKGEITRLI-VSKVANF 475
Cdd:TIGR00603 475 YVMNPNKFRACQFLIRFHEQrgDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIfLSKVGDT 554
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2004339518 476 AVDLPDANVAIQISGTYGSRQEEAQRLGRILRPK--TDDN--TAHFYTLVTRDTREQEFSLHRQLFLVEQGYPYDII 548
Cdd:TIGR00603 555 SIDLPEANVLIQISSHYGSRRQEAQRLGRILRAKkgSDAEeyNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVI 631
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
177-552 2.85e-98

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 309.26  E-value: 2.85e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 177 SRGRAFSLRPYQKEAVDAFYSGGAVTGGSGVLVLPCGAGKTVIGLGAICQLQTA--TLILTTNTTSVRQWIAELLDKTGL 254
Cdd:COG1061    74 ASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGkrVLVLVPRRELLEQWAEELRRFLGD 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 255 DPNmvgeYTGDNKEVKPITVATYQILTYRptaeddfPHLKLFsERDWGLIIYDEVHLLPAPIFR-VTSGIQATRRLGLTA 333
Cdd:COG1061   154 PLA----GGGKKDSDAPITVATYQSLARR-------AHLDEL-GDRFGLVIIDEAHHAGAPSYRrILEAFPAAYRLGLTA 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 334 TLVREDGREEDVFTLIGpKKYEVPWKVMEEQGWIAEAHCREIRLPFEPKwREAYAHATARQKFRIAAENPKKLEVVRELL 413
Cdd:COG1061   222 TPFRSDGREILLFLFDG-IVYEYSLKEAIEDGYLAPPEYYGIRVDLTDE-RAEYDALSERLREALAADAERKDKILRELL 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 414 ERHAHD-RVLIIGQYIDQLEQMATALQ-----LPLITGKVPDKERELLYTQFKKGEITRLIVSKVANFAVDLPDANVAIQ 487
Cdd:COG1061   300 REHPDDrKTLVFCSSVDHAEALAELLNeagirAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004339518 488 ISGTyGSRQEEAQRLGRILRPKTDDNTAHFYTLVTRDTREQEFSLHRQLFLVeqGYPYDIIESET 552
Cdd:COG1061   380 LRPT-GSPREFIQRLGRGLRPAPGKEDALVYDFVGNDVPVLEELAKDLRDLA--GYRVEFLDEEE 441
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
170-341 9.82e-69

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 219.10  E-value: 9.82e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 170 VSLRETTSrgrafsLRPYQKEAVDAFYSGGavTGGSGVLVLPCGAGKTVIGLGAICQLQTATLILTTNTTSVRQWIAELL 249
Cdd:cd18029     1 IDLKPSTQ------LRPYQEKALSKMFGNG--RARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 250 DKTGLDPNMVGEYTGDNKE---VKPITVATYQILTYRptaEDDFPHLKLF----SERDWGLIIYDEVHLLPAPIFRVTSG 322
Cdd:cd18029    73 DWTTIDDEQIGRFTSDKKEifpEAGVTVSTYSMLANT---RKRSPESEKFmefiTEREWGLIILDEVHVVPAPMFRRVLT 149
                         170       180
                  ....*....|....*....|
gi 2004339518 323 IQAT-RRLGLTATLVREDGR 341
Cdd:cd18029   150 LQKAhCKLGLTATLVREDDK 169
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
363-548 1.23e-47

ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 and XPB helicases.


Pssm-ID: 406585  Cd Length: 248  Bit Score: 166.24  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 363 EQGWIAEAHCREIRLPFEPKWREAYAHATARQKFRIAAENPKKLEVVRELLERHAH--DRVLIIGQYIDQLEQMATALQL 440
Cdd:pfam16203   3 EKGHIANVQCAEVWCPMTAEFYREYLRSKSRKKRLLYVMNPNKFRACQFLIRYHERrgDKIIVFSDNVFALKEYAKKLNK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 441 PLITGKVPDKERELLYTQFKKGEITRLI-VSKVANFAVDLPDANVAIQISGTYGSRQEEAQRLGRILRPKTDDNT----A 515
Cdd:pfam16203  83 PYIYGGTSQAERMRILQNFKHNPNVNTIfLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRSNDegfnA 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2004339518 516 HFYTLVTRDTREQEFSLHRQLFLVEQGYPYDII 548
Cdd:pfam16203 163 FFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVI 195
DEXDc smart00487
DEAD-like helicases superfamily;
182-338 4.07e-17

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 79.84  E-value: 4.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518  182 FSLRPYQKEAVDAFYSGGavtgGSGVLVLPCGAGKTVIGLGAICQL-----QTATLILTTNTTSVRQWIAELLDKTGLDP 256
Cdd:smart00487   7 EPLRPYQKEAIEALLSGL----RDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518  257 NM-VGEYTGDN---------KEVKPITVATYQILTyrptaedDFPHLKLFSERDWGLIIYDEVHLLPAPIFR------VT 320
Cdd:smart00487  83 LKvVGLYGGDSkreqlrkleSGKTDILVTTPGRLL-------DLLENDKLSLSNVDLVILDEAHRLLDGGFGdqleklLK 155
                          170
                   ....*....|....*...
gi 2004339518  321 SGIQATRRLGLTATLVRE 338
Cdd:smart00487 156 LLPKNVQLLLLSATPPEE 173
uvsW PHA02558
UvsW helicase; Provisional
185-335 1.71e-05

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 47.31  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 185 RPYQKEAVdafYSGgaVTGGSGVLVLPCGAGKTVIglgaICQL--------QTATLILTTNTTSVRQWIAELLDkTGLDP 256
Cdd:PHA02558  116 HWYQYDAV---YEG--LKNNRRLLNLPTSAGKSLI----QYLLsryylenyEGKVLIIVPTTSLVTQMIDDFVD-YRLFP 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 257 --NMVGEYTGDNKEV-KPITVATYQILTYRPTaeddfphlKLFSerDWGLIIYDEVHLLPAP--IFRVTSGIQATRRLGL 331
Cdd:PHA02558  186 reAMHKIYSGTAKDTdAPIVVSTWQSAVKQPK--------EWFD--QFGMVIVDECHLFTGKslTSIITKLDNCKFKFGL 255

                  ....
gi 2004339518 332 TATL 335
Cdd:PHA02558  256 TGSL 259
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
1-548 3.32e-100

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 319.05  E-value: 3.32e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518   1 MSYRPD---LPLIVQSDRTILLETQHPLFPEARQAISGFTELIKNPEYIHTYRITPLSLWNAAASGLTSQEVTDVLGSYS 77
Cdd:TIGR00603   6 LELKPDhgsRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEVLGRLS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518  78 KYGVPPTIVKEIEDTMRKYGLFRL----------------------------ERI----GDQLVLM-------------- 111
Cdd:TIGR00603  86 KTPIPKGIIEFIRLCTQSYGKVKLvlkhnryfvesphpevlqrllkdpviapCRIdpteEESLQTPtygskedfiinkpg 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 112 --------------SEDPLLLAEVTSYKSIAALFENE-------FVIKSYARGLIKQELIKLGFPVqdLAGY-----TEG 165
Cdd:TIGR00603 166 ftggasagqleanqGESAVPKDIADFYELEEEEEDEDeetathsFEIDQEQVEEVKKRCIELDYPL--LEEYdfrndTVN 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 166 ESCAVSLRETTSrgrafsLRPYQKEAVDAFYSGGAVTggSGVLVLPCGAGKTVIGLGAICQLQTATLILTTNTTSVRQWI 245
Cdd:TIGR00603 244 PDLNIDLKPTTQ------IRPYQEKSLSKMFGNGRAR--SGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 246 AELLDKTGLDPNMVGEYTGDNKEvKPITVATYQILTY------RPTAEDDFPHLKLFSERDWGLIIYDEVHLLPAPIFR- 318
Cdd:TIGR00603 316 QQFKMWSTIDDSQICRFTSDAKE-RFHGEAGVVVSTYsmvahtGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRr 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 319 VTSGIQATRRLGLTATLVREDGREEDVFTLIGPKKYEVPWKVMEEQGWIAEAHCREIRLPFEPKWREAYAHATARQKFRI 398
Cdd:TIGR00603 395 VLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLL 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 399 AAENPKKLEVVRELLERHAH--DRVLIIGQYIDQLEQMATALQLPLITGKVPDKERELLYTQFKKGEITRLI-VSKVANF 475
Cdd:TIGR00603 475 YVMNPNKFRACQFLIRFHEQrgDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIfLSKVGDT 554
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2004339518 476 AVDLPDANVAIQISGTYGSRQEEAQRLGRILRPK--TDDN--TAHFYTLVTRDTREQEFSLHRQLFLVEQGYPYDII 548
Cdd:TIGR00603 555 SIDLPEANVLIQISSHYGSRRQEAQRLGRILRAKkgSDAEeyNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVI 631
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
177-552 2.85e-98

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 309.26  E-value: 2.85e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 177 SRGRAFSLRPYQKEAVDAFYSGGAVTGGSGVLVLPCGAGKTVIGLGAICQLQTA--TLILTTNTTSVRQWIAELLDKTGL 254
Cdd:COG1061    74 ASGTSFELRPYQQEALEALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGkrVLVLVPRRELLEQWAEELRRFLGD 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 255 DPNmvgeYTGDNKEVKPITVATYQILTYRptaeddfPHLKLFsERDWGLIIYDEVHLLPAPIFR-VTSGIQATRRLGLTA 333
Cdd:COG1061   154 PLA----GGGKKDSDAPITVATYQSLARR-------AHLDEL-GDRFGLVIIDEAHHAGAPSYRrILEAFPAAYRLGLTA 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 334 TLVREDGREEDVFTLIGpKKYEVPWKVMEEQGWIAEAHCREIRLPFEPKwREAYAHATARQKFRIAAENPKKLEVVRELL 413
Cdd:COG1061   222 TPFRSDGREILLFLFDG-IVYEYSLKEAIEDGYLAPPEYYGIRVDLTDE-RAEYDALSERLREALAADAERKDKILRELL 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 414 ERHAHD-RVLIIGQYIDQLEQMATALQ-----LPLITGKVPDKERELLYTQFKKGEITRLIVSKVANFAVDLPDANVAIQ 487
Cdd:COG1061   300 REHPDDrKTLVFCSSVDHAEALAELLNeagirAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAIL 379
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004339518 488 ISGTyGSRQEEAQRLGRILRPKTDDNTAHFYTLVTRDTREQEFSLHRQLFLVeqGYPYDIIESET 552
Cdd:COG1061   380 LRPT-GSPREFIQRLGRGLRPAPGKEDALVYDFVGNDVPVLEELAKDLRDLA--GYRVEFLDEEE 441
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
170-341 9.82e-69

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 219.10  E-value: 9.82e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 170 VSLRETTSrgrafsLRPYQKEAVDAFYSGGavTGGSGVLVLPCGAGKTVIGLGAICQLQTATLILTTNTTSVRQWIAELL 249
Cdd:cd18029     1 IDLKPSTQ------LRPYQEKALSKMFGNG--RARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 250 DKTGLDPNMVGEYTGDNKE---VKPITVATYQILTYRptaEDDFPHLKLF----SERDWGLIIYDEVHLLPAPIFRVTSG 322
Cdd:cd18029    73 DWTTIDDEQIGRFTSDKKEifpEAGVTVSTYSMLANT---RKRSPESEKFmefiTEREWGLIILDEVHVVPAPMFRRVLT 149
                         170       180
                  ....*....|....*....|
gi 2004339518 323 IQAT-RRLGLTATLVREDGR 341
Cdd:cd18029   150 LQKAhCKLGLTATLVREDDK 169
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
372-521 7.02e-60

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 195.16  E-value: 7.02e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 372 CREIRLPFEPKWREAYAHATA-RQKFRIAAENPKKLEVVRELLERHA-HDRVLIIGQYIDQLEQMATALQLPLITGKVPD 449
Cdd:cd18789     1 CAEIRCPMTPEFYREYLGLGAhRKRRLLAAMNPNKLRALEELLKRHEqGDKIIVFTDNVEALYRYAKRLLKPFITGETPQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2004339518 450 KERELLYTQFKKGEITRLIVSKVANFAVDLPDANVAIQISGTYGSRQEEAQRLGRILRPKTDDN-TAHFYTLV 521
Cdd:cd18789    81 SEREEILQNFREGEYNTLVVSKVGDEGIDLPEANVAIQISGHGGSRRQEAQRLGRILRPKKGGGkNAFFYSLV 153
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
363-548 1.23e-47

ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 and XPB helicases.


Pssm-ID: 406585  Cd Length: 248  Bit Score: 166.24  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 363 EQGWIAEAHCREIRLPFEPKWREAYAHATARQKFRIAAENPKKLEVVRELLERHAH--DRVLIIGQYIDQLEQMATALQL 440
Cdd:pfam16203   3 EKGHIANVQCAEVWCPMTAEFYREYLRSKSRKKRLLYVMNPNKFRACQFLIRYHERrgDKIIVFSDNVFALKEYAKKLNK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 441 PLITGKVPDKERELLYTQFKKGEITRLI-VSKVANFAVDLPDANVAIQISGTYGSRQEEAQRLGRILRPKTDDNT----A 515
Cdd:pfam16203  83 PYIYGGTSQAERMRILQNFKHNPNVNTIfLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRSNDegfnA 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2004339518 516 HFYTLVTRDTREQEFSLHRQLFLVEQGYPYDII 548
Cdd:pfam16203 163 FFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVI 195
Helicase_C_3 pfam13625
Helicase conserved C-terminal domain; This domain family is found in a wide variety of ...
9-130 1.85e-38

Helicase conserved C-terminal domain; This domain family is found in a wide variety of helicases and helicase-related proteins.


Pssm-ID: 463939 [Multi-domain]  Cd Length: 121  Bit Score: 137.25  E-value: 1.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518   9 LIVQSDRTILLETqhPLFPEARQAISGFTELIKnPEYIHTYRITPLSLWNAAASGLTSQEVTDVLGSYSKYGVPPTIVKE 88
Cdd:pfam13625   1 LIVQADLTILLPG--PLAPEARDFLAAFAELES-RGHAHTYRLTPLSLRRALDAGLTAEDILDFLERHSKYPVPQALEYL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2004339518  89 IEDTMRKYGLFRLERiGDQLVLMSEDPLLLAEVTSYKSIAAL 130
Cdd:pfam13625  78 IRDVARRHGRLRLGL-GASSYLRSDDPAVLAELLADPRIAPL 118
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
184-335 1.06e-30

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 116.64  E-value: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 184 LRPYQKEAVDAFYsgGAVTGGSGVLVLPCGAGKTVIGLGAICQLQTA-TLILTTNTTSVRQWIAELLDKTGLDpnMVGEY 262
Cdd:cd17926     1 LRPYQEEALEAWL--AHKNNRRGILVLPTGSGKTLTALALIAYLKELrTLIVVPTDALLDQWKERFEDFLGDS--SIGLI 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2004339518 263 TGDNKEVK---PITVATYQILTYRPTAEDDFPHlklfserDWGLIIYDEVHLLPAPIFRVT-SGIQATRRLGLTATL 335
Cdd:cd17926    77 GGGKKKDFddaNVVVATYQSLSNLAEEEKDLFD-------QFGLLIVDEAHHLPAKTFSEIlKELNAKYRLGLTATP 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
182-337 5.95e-19

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 83.88  E-value: 5.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 182 FSLRPYQKEAVDAFYSGGAVTGGSGVLVLPCGAGKTVIGLGAICQLQTA-----TLILTTNTTSVRQWIAELLDKTGLDP 256
Cdd:pfam04851   2 LELRPYQIEAIENLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKgpikkVLFLVPRKDLLEQALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 257 NMVGEYTGDNKEV----KPITVATYQILtyrpTAEDDFPHLKLFSERdWGLIIYDEVHLLPAPIFR-VTSGIQATRRLGL 331
Cdd:pfam04851  82 EIGEIISGDKKDEsvddNKIVVTTIQSL----YKALELASLELLPDF-FDVIIIDEAHRSGASSYRnILEYFKPAFLLGL 156

                  ....*.
gi 2004339518 332 TATLVR 337
Cdd:pfam04851 157 TATPER 162
DEXDc smart00487
DEAD-like helicases superfamily;
182-338 4.07e-17

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 79.84  E-value: 4.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518  182 FSLRPYQKEAVDAFYSGGavtgGSGVLVLPCGAGKTVIGLGAICQL-----QTATLILTTNTTSVRQWIAELLDKTGLDP 256
Cdd:smart00487   7 EPLRPYQKEAIEALLSGL----RDVILAAPTGSGKTLAALLPALEAlkrgkGGRVLVLVPTRELAEQWAEELKKLGPSLG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518  257 NM-VGEYTGDN---------KEVKPITVATYQILTyrptaedDFPHLKLFSERDWGLIIYDEVHLLPAPIFR------VT 320
Cdd:smart00487  83 LKvVGLYGGDSkreqlrkleSGKTDILVTTPGRLL-------DLLENDKLSLSNVDLVILDEAHRLLDGGFGdqleklLK 155
                          170
                   ....*....|....*...
gi 2004339518  321 SGIQATRRLGLTATLVRE 338
Cdd:smart00487 156 LLPKNVQLLLLSATPPEE 173
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
183-528 1.57e-13

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 73.34  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 183 SLRPYQKEAVDAFYSGGAVTGGsGVLVLPCGAGKTVIGLGAICQLQTA-----TLILTTnTTSVRQWIAELLdKTGLDPN 257
Cdd:COG0553   241 TLRPYQLEGAAWLLFLRRLGLG-GLLADDMGLGKTIQALALLLELKERglarpVLIVAP-TSLVGNWQRELA-KFAPGLR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 258 mVGEYTGDNKEVKPIT-VATYQIL--TYrPTAEDDFPHLKlfsERDWGLIIYDEVHLL---PAPIFRVTSGIQATRRLGL 331
Cdd:COG0553   318 -VLVLDGTRERAKGANpFEDADLVitSY-GLLRRDIELLA---AVDWDLVILDEAQHIknpATKRAKAVRALKARHRLAL 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 332 TATLVRedGREED---VFTLIGP----------KKYEVP-----WKVMEE-QGWIA----------------EAHCREIR 376
Cdd:COG0553   393 TGTPVE--NRLEElwsLLDFLNPgllgslkafrERFARPiekgdEEALERlRRLLRpfllrrtkedvlkdlpEKTEETLY 470
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 377 LPFEPKWREAYAHAT---------------------ARQKFRIAAENPK--------------KLEVVRELLERH--AHD 419
Cdd:COG0553   471 VELTPEQRALYEAVLeylrrelegaegirrrglilaALTRLRQICSHPAllleegaelsgrsaKLEALLELLEELlaEGE 550
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 420 RVLIIGQYIDQLEQMATALQ-----LPLITGKVPDKERELLYTQFKKG-EITRLIVS-KVANFAVDLPDANVAI------ 486
Cdd:COG0553   551 KVLVFSQFTDTLDLLEERLEergieYAYLHGGTSAEERDELVDRFQEGpEAPVFLISlKAGGEGLNLTAADHVIhydlww 630
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 2004339518 487 --QIsgtygsrqeEAQRLGRILRPKtDDNTAHFYTLVTRDTREQ 528
Cdd:COG0553   631 npAV---------EEQAIDRAHRIG-QTRDVQVYKLVAEGTIEE 664
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
404-509 4.25e-13

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: 65.69  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 404 KKLEVVRELLERHAHDRVLIIGQYIDQLE--QMATALQLP--LITGKVPDKERELLYTQFKKGEITRLIVSKVANFAVDL 479
Cdd:pfam00271   1 EKLEALLELLKKERGGKVLIFSQTKKTLEaeLLLEKEGIKvaRLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2004339518 480 PDANVAIQISGTYGSRQEEaQRLGRILRPK 509
Cdd:pfam00271  81 PDVDLVINYDLPWNPASYI-QRIGRAGRAG 109
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
184-334 6.07e-10

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: 58.73  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 184 LRPYQKEAVdAFYSGGAVTGGSGVLVLPCGAGKTVIGLGAICQL------QTATLILTTNTTsVRQWIAELLDKTgldPN 257
Cdd:cd17919     1 LRPYQLEGL-NFLLELYENGPGGILADEMGLGKTLQAIAFLAYLlkegkeRGPVLVVCPLSV-LENWEREFEKWT---PD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 258 M-VGEYTGDNKEVKPITVATYQ-----ILTYRPTAEDDFPHLKLFserDWGLIIYDEVHLLPAP---IFRVTSGIQATRR 328
Cdd:cd17919    76 LrVVVYHGSQRERAQIRAKEKLdkfdvVLTTYETLRRDKASLRKF---RWDLVVVDEAHRLKNPksqLSKALKALRAKRR 152

                  ....*.
gi 2004339518 329 LGLTAT 334
Cdd:cd17919   153 LLLTGT 158
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
184-348 9.49e-10

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 57.57  E-value: 9.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 184 LRPYQKEAVDAfySGGAVTGG--SGVLVLPCGAGKTVIGLGAICQLQTAT-----LILTTNTTSVRQwiAELLDKTGLDP 256
Cdd:cd18032     1 PRYYQQEAIEA--LEEAREKGqrRALLVMATGTGKTYTAAFLIKRLLEANrkkriLFLAHREELLEQ--AERSFKEVLPD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 257 NMVGEYTGDNKEV--KPITVATYQILTYRptaeddfPHLKLFSERDWGLIIYDEVHLLPAPIFR-----VTSGIQatrrL 329
Cdd:cd18032    77 GSFGNLKGGKKKPddARVVFATVQTLNKR-------KRLEKFPPDYFDLIIIDEAHHAIASSYRkileyFEPAFL----L 145
                         170
                  ....*....|....*....
gi 2004339518 330 GLTATLVREDGReeDVFTL 348
Cdd:cd18032   146 GLTATPERTDGL--DTYEL 162
HELICc smart00490
helicase superfamily c-terminal domain;
429-509 2.26e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 54.14  E-value: 2.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518  429 DQLEQMATALQLP--LITGKVPDKERELLYTQFKKGEITRLIVSKVANFAVDLPDANVAIqISGTYGSRQEEAQRLGRIL 506
Cdd:smart00490   1 EELAELLKELGIKvaRLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVI-IYDLPWSPASYIQRIGRAG 79

                   ...
gi 2004339518  507 RPK 509
Cdd:smart00490  80 RAG 82
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
203-334 4.35e-09

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: 55.10  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 203 GGSGVLVLPCGAGKTVI-GLGAICQLQTA---TLILTTNTTSVRQWIAELldKTGLDPN-----MVGEYTGDNKEVK--- 270
Cdd:cd00046     1 GENVLITAPTGSGKTLAaLLAALLLLLKKgkkVLVLVPTKALALQTAERL--RELFGPGirvavLVGGSSAEEREKNklg 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004339518 271 --PITVATYQiltyrpTAEDDFPHLKLFSERDWGLIIYDEVHLLP---APIFRVTSGIQA-----TRRLGLTAT 334
Cdd:cd00046    79 daDIIIATPD------MLLNLLLREDRLFLKDLKLIIVDEAHALLidsRGALILDLAVRKaglknAQVILLSAT 146
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
184-350 2.12e-07

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: 51.52  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 184 LRPYQKEAVdafysGGAVTGGSGVLVLP--CGAGKTVIGLGAICQLQTAT-----LILTTnTTSVRQWIAELLDKTGLDP 256
Cdd:cd18011     1 PLPHQIDAV-----LRALRKPPVRLLLAdeVGLGKTIEAGLIIKELLLRGdakrvLILCP-ASLVEQWQDELQDKFGLPF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 257 --------NMVGEYTGDNKEVKPITVATYQiltyrpTAEDDFPHLKLFSERDWGLIIYDEVHLLpapifRVTSGIQATRR 328
Cdd:cd18011    75 lildretaAQLRRLIGNPFEEFPIVIVSLD------LLKRSEERRGLLLSEEWDLVVVDEAHKL-----RNSGGGKETKR 143
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2004339518 329 --------------LGLTATLVRedGREEDVFTLIG 350
Cdd:cd18011   144 yklgrllakrarhvLLLTATPHN--GKEEDFRALLS 177
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
183-335 2.55e-07

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 51.11  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 183 SLRPYQKEAVDAFYSggavTGGSGVLVLPCGAGKTVIGLGAICQ--LQTATLILTTNTTS--VRQWIAELLDKTGLDPNM 258
Cdd:cd17921     1 LLNPIQREALRALYL----SGDSVLVSAPTSSGKTLIAELAILRalATSGGKAVYIAPTRalVNQKEADLRERFGPLGKN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 259 VGEYTGDNKEVK------PITVATY---QILTYRPTAEDDFPHlklfserdwGLIIYDEVHLLPAP---------IFRVT 320
Cdd:cd17921    77 VGLLTGDPSVNKlllaeaDILVATPeklDLLLRNGGERLIQDV---------RLVVVDEAHLIGDGergvvlellLSRLL 147
                         170
                  ....*....|....*
gi 2004339518 321 SGIQATRRLGLTATL 335
Cdd:cd17921   148 RINKNARFVGLSATL 162
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
405-507 2.32e-06

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: 47.09  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 405 KLEVVRELLERHAH--DRVLIIGQY---IDQLEQMATALQLP--LITGKVPDKERELLYTQFKKG-EITRLIVS-KVANF 475
Cdd:cd18793    12 KLEALLELLEELREpgEKVLIFSQFtdtLDILEEALRERGIKylRLDGSTSSKERQKLVDRFNEDpDIRVFLLStKAGGV 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2004339518 476 AVDLPDANVAI--------QIsgtygsrqeEAQRLGRILR 507
Cdd:cd18793    92 GLNLTAANRVIlydpwwnpAV---------EEQAIDRAHR 122
DEXHc_RLR cd18036
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ...
182-310 4.34e-06

DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) 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: 350794 [Multi-domain]  Cd Length: 204  Bit Score: 47.86  E-value: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 182 FSLRPYQKEAVDAfysggAVTGGSGVLVLPCGAGKTVIGLGAI--------CQLQTATLILTTNTTSVRQWIAELLDKTG 253
Cdd:cd18036     1 LELRNYQLELVLP-----ALRGKNTIICAPTGSGKTRVAVYICrhhlekrrSAGEKGRVVVLVNKVPLVEQQLEKFFKYF 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004339518 254 LDPNMVGEYTGDNKEVKP---------ITVATYQIL--TYRPTAEDDFPHLKLFSerdwgLIIYDEVH 310
Cdd:cd18036    76 RKGYKVTGLSGDSSHKVSfgqivkasdVIICTPQILinNLLSGREEERVYLSDFS-----LLIFDECH 138
uvsW PHA02558
UvsW helicase; Provisional
185-335 1.71e-05

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 47.31  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 185 RPYQKEAVdafYSGgaVTGGSGVLVLPCGAGKTVIglgaICQL--------QTATLILTTNTTSVRQWIAELLDkTGLDP 256
Cdd:PHA02558  116 HWYQYDAV---YEG--LKNNRRLLNLPTSAGKSLI----QYLLsryylenyEGKVLIIVPTTSLVTQMIDDFVD-YRLFP 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 257 --NMVGEYTGDNKEV-KPITVATYQILTYRPTaeddfphlKLFSerDWGLIIYDEVHLLPAP--IFRVTSGIQATRRLGL 331
Cdd:PHA02558  186 reAMHKIYSGTAKDTdAPIVVSTWQSAVKQPK--------EWFD--QFGMVIVDECHLFTGKslTSIITKLDNCKFKFGL 255

                  ....
gi 2004339518 332 TATL 335
Cdd:PHA02558  256 TGSL 259
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
184-342 2.67e-05

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: 45.83  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 184 LRPYQKEAVDAFYsGGAVTGGSGVLVLPCGAGKTV--IGLGAICQLQTAT------------------------LILTTN 237
Cdd:cd18005     1 LRDYQREGVEFMY-DLYKNGRGGILGDDMGLGKTVqvIAFLAAVLGKTGTrrdrennrprfkkkppassakkpvLIVAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 238 TTsVRQWIAELlDKTGldPNMVGEYTGDNKEVKP----------ITVATYQilTYRPTAEDdfphlklFSERDWGLIIYD 307
Cdd:cd18005    80 SV-LYNWKDEL-DTWG--HFEVGVYHGSRKDDELegrlkagrleVVVTTYD--TLRRCIDS-------LNSINWSAVIAD 146
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2004339518 308 EVHLLPAPIFRVTSGIQ---ATRRLGLTATLVREDGRE 342
Cdd:cd18005   147 EAHRIKNPKSKLTQAMKelkCKVRIGLTGTLLQNNMKE 184
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
182-311 4.76e-05

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex 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. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family 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: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 44.73  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 182 FSLRPYQKEAVDAfysggAVTGGSGVLVLPCGAGKTVIGLgAIC--------QLQTATLILTTNTTSVRQWIAELLDK-T 252
Cdd:cd17927     1 FKPRNYQLELAQP-----ALKGKNTIICLPTGSGKTFVAV-LICehhlkkfpAGRKGKVVFLANKVPLVEQQKEVFRKhF 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004339518 253 GLDPNMVGEYTGDNK---------EVKPITVATYQILtyrptaEDDFPHLKLFSERDWGLIIYDEVHL 311
Cdd:cd17927    75 ERPGYKVTGLSGDTSenvsveqivESSDVIIVTPQIL------VNDLKSGTIVSLSDFSLLVFDECHN 136
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
180-312 7.19e-05

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


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 45.70  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 180 RAFSLRPYQKEAVDAfysggaVTGGSGVLVL-PCGAGKTVIGLGAICQ-LQ-------TATLILTTNttsvrQWIAELLD 250
Cdd:COG4581    22 RGFELDPFQEEAILA------LEAGRSVLVAaPTGSGKTLVAEFAIFLaLArgrrsfyTAPIKALSN-----QKFFDLVE 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004339518 251 KTGldPNMVGEYTGD---NKEVkPITVATYQILtyRPTAEDDFPHLklfseRDWGLIIYDEVHLL 312
Cdd:COG4581    91 RFG--AENVGLLTGDasvNPDA-PIVVMTTEIL--RNMLYREGADL-----EDVGVVVMDEFHYL 145
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
182-312 1.60e-04

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 44.50  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 182 FSLRPYQKEAVDAfysgGAVTGGSGVLVLPCGAGKTVIGLGAICQLqtatliLTTNTTSV-------------RQWIAEl 248
Cdd:COG1204    21 EELYPPQAEALEA----GLLEGKNLVVSAPTASGKTLIAELAILKA------LLNGGKALyivplralasekyREFKRD- 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004339518 249 LDKTGLDpnmVGEYTGDNKEVKP------ITVATY----QILTYRPTAEDDFphlklfserdwGLIIYDEVHLL 312
Cdd:COG1204    90 FEELGIK---VGVSTGDYDSDDEwlgrydILVATPekldSLLRNGPSWLRDV-----------DLVVVDEAHLI 149
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
187-354 3.60e-04

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: 42.67  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 187 YQKEAVDAFYSGGAVTGGSGVLVLPCGAGKTVIGLGAI-----CQLQT--ATLILTTNTTsVRQWIAELLDKTGLDPNMV 259
Cdd:pfam00176   1 YQIEGVNWMLSLENNLGRGGILADEMGLGKTLQTISLLlylkhVDKNWggPTLIVVPLSL-LHNWMNEFERWVSPPALRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 260 GEYTGDNKE-----VKPITVATYQIL--TYrptaeDDFPHLK-LFSERDWGLIIYDEVHLLP---APIFRVTSGIQATRR 328
Cdd:pfam00176  80 VVLHGNKRPqerwkNDPNFLADFDVVitTY-----ETLRKHKeLLKKVHWHRIVLDEGHRLKnskSKLSKALKSLKTRNR 154
                         170       180
                  ....*....|....*....|....*....
gi 2004339518 329 LGLTATLVREDGreEDVFTL---IGPKKY 354
Cdd:pfam00176 155 WILTGTPLQNNL--EELWALlnfLRPGPF 181
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
185-338 1.04e-03

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 39.92  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 185 RPYQKEAVDAFYSGGAVtggsgVLVLPCGAGKTVI-GLGAICQLQTA-----TLILTTNTTSVRQWIAELLDKT-GLDPN 257
Cdd:pfam00270   1 TPIQAEAIPAILEGRDV-----LVQAPTGSGKTLAfLLPALEALDKLdngpqALVLAPTRELAEQIYEELKKLGkGLGLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 258 MVGEYTGDNKEVK-------PITVATYQILtyrptaEDDFPHLKLFSERdwGLIIYDEVHLL-----PAPIFRVTSGIQA 325
Cdd:pfam00270  76 VASLLGGDSRKEQleklkgpDILVGTPGRL------LDLLQERKLLKNL--KLLVLDEAHRLldmgfGPDLEEILRRLPK 147
                         170
                  ....*....|....
gi 2004339518 326 TRR-LGLTATLVRE 338
Cdd:pfam00270 148 KRQiLLLSATLPRN 161
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
184-334 2.87e-03

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: 39.64  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 184 LRPYQKEAVD--AF---YsggavtGGSGVLVLPCGAGKTV--IGLGAICQLQTATLILTTNTTS--------VRQWIAEL 248
Cdd:cd17999     1 LRPYQQEGINwlAFlnkY------NLHGILCDDMGLGKTLqtLCILASDHHKRANSFNSENLPSlvvcpptlVGHWVAEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 249 ---LDKTGLDP-NMVGEYTGDNK-----EVKPITVATYQILtyRPTAEddfphlkLFSERDWGLIIYDEVHLLPAP---I 316
Cdd:cd17999    75 kkyFPNAFLKPlAYVGPPQERRRlreqgEKHNVIVASYDVL--RNDIE-------VLTKIEWNYCVLDEGHIIKNSktkL 145
                         170
                  ....*....|....*...
gi 2004339518 317 FRVTSGIQATRRLGLTAT 334
Cdd:cd17999   146 SKAVKQLKANHRLILSGT 163
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
393-487 3.25e-03

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: 37.87  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004339518 393 RQKFRIAAENPKKLEVVRELLERHAHDRVLIIGQYIDQLEQMATALQLP-----LITGKVPDKERELLYTQFKKGEITRL 467
Cdd:cd18787     2 KQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELgikvaALHGDLSQEERERALKKFRSGKVRVL 81
                          90       100
                  ....*....|....*....|..
gi 2004339518 468 IVSKVAnfA--VDLPDANVAIQ 487
Cdd:cd18787    82 VATDVA--ArgLDIPGVDHVIN 101
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH