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Conserved domains on  [gi|24662247|ref|NP_524020|]
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haywire, isoform A [Drosophila melanogaster]

Protein Classification

rad25 family protein( domain architecture ID 11489419)

rad25 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
70-795 0e+00

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: 1354.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247    70 DYRSQMQLRPDHGNRPLWVAPNGHVFLESFSPVYKHAHDFLIAISEPVCRPEHIHEYKLTAYSLYAAVSVGLQTHDIVEY 149
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   150 LKRLSKTSIPEGILEFIRLCTLSYGKVKLVLKHNKYFIESPHPEVLQKLLKDPVIQKCRLIRSEGEdfiqgtldgKAITQ 229
Cdd:TIGR00603  81 LGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEEE---------SLQTP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   230 FGTKLPPGATDKPTPD----PAAAAGADGTTAVPEDITDFYEKIDKEEEDEDeaNLKTVSFEVAQEKIEVIQKRCIEIEH 305
Cdd:TIGR00603 152 TYGSKEDFIINKPGFTggasAGQLEANQGESAVPKDIADFYELEEEEEDEDE--ETATHSFEIDQEQVEEVKKRCIELDY 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   306 PLLAEYDFRNDTNNPDINIDLKPAAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTACCTVRKRALVLCNSGV 385
Cdd:TIGR00603 230 PLLEEYDFRNDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   386 SVEQWKQQFKMWSTADDSMICRFTSEAKDKPMG-CGILVTTYSMITHTQKRSWEAEQTMRWLQEQEWGIMVLDEVHTIPA 464
Cdd:TIGR00603 310 SVEQWKQQFKMWSTIDDSQICRFTSDAKERFHGeAGVVVSTYSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   465 KMFRRVLTIVQSHCKLGLTATLLREDDKIADLNFLIGPKLYEANWLELQKKGYIARVQCAEVWCPMSPEFYREYLTTKTS 544
Cdd:TIGR00603 390 AMFRRVLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSR 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   545 KKMLLYVMNPSKFRSCQFLIKYHEQRGDKTIVFSDNVFALKHYAIKMNKPFIYGPTSQNERIQILQNFKFNSKVNTIFVS 624
Cdd:TIGR00603 470 KRMLLYVMNPNKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLS 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   625 KVADTSFDLPEANVLIQISSHGGSRRQEAQRLGRILRAKKGAIAEEYNAFFYTLVSQDTMEMSYSRKRQRFLVNQGYSYK 704
Cdd:TIGR00603 550 KVGDTSIDLPEANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAEEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFK 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   705 VITHLKGMDTDSDLMYGTQEEQGQLLQLVLSASDLDCEDEKLPGEPGYRPSG--------SGGAVRRVGGLSSMSGGDDA 776
Cdd:TIGR00603 630 VITHLPGMDNESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGEFGSRALGasrsmssaSGKAVRRGGSLSSLSGGDDM 709
                         730       740
                  ....*....|....*....|...
gi 24662247   777 IYYEHRKKNIGS----VHPLFKK 795
Cdd:TIGR00603 710 AYMEYRKPAIKKskkeVHPLFKK 732
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
70-795 0e+00

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: 1354.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247    70 DYRSQMQLRPDHGNRPLWVAPNGHVFLESFSPVYKHAHDFLIAISEPVCRPEHIHEYKLTAYSLYAAVSVGLQTHDIVEY 149
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   150 LKRLSKTSIPEGILEFIRLCTLSYGKVKLVLKHNKYFIESPHPEVLQKLLKDPVIQKCRLIRSEGEdfiqgtldgKAITQ 229
Cdd:TIGR00603  81 LGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEEE---------SLQTP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   230 FGTKLPPGATDKPTPD----PAAAAGADGTTAVPEDITDFYEKIDKEEEDEDeaNLKTVSFEVAQEKIEVIQKRCIEIEH 305
Cdd:TIGR00603 152 TYGSKEDFIINKPGFTggasAGQLEANQGESAVPKDIADFYELEEEEEDEDE--ETATHSFEIDQEQVEEVKKRCIELDY 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   306 PLLAEYDFRNDTNNPDINIDLKPAAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTACCTVRKRALVLCNSGV 385
Cdd:TIGR00603 230 PLLEEYDFRNDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   386 SVEQWKQQFKMWSTADDSMICRFTSEAKDKPMG-CGILVTTYSMITHTQKRSWEAEQTMRWLQEQEWGIMVLDEVHTIPA 464
Cdd:TIGR00603 310 SVEQWKQQFKMWSTIDDSQICRFTSDAKERFHGeAGVVVSTYSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   465 KMFRRVLTIVQSHCKLGLTATLLREDDKIADLNFLIGPKLYEANWLELQKKGYIARVQCAEVWCPMSPEFYREYLTTKTS 544
Cdd:TIGR00603 390 AMFRRVLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSR 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   545 KKMLLYVMNPSKFRSCQFLIKYHEQRGDKTIVFSDNVFALKHYAIKMNKPFIYGPTSQNERIQILQNFKFNSKVNTIFVS 624
Cdd:TIGR00603 470 KRMLLYVMNPNKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLS 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   625 KVADTSFDLPEANVLIQISSHGGSRRQEAQRLGRILRAKKGAIAEEYNAFFYTLVSQDTMEMSYSRKRQRFLVNQGYSYK 704
Cdd:TIGR00603 550 KVGDTSIDLPEANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAEEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFK 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   705 VITHLKGMDTDSDLMYGTQEEQGQLLQLVLSASDLDCEDEKLPGEPGYRPSG--------SGGAVRRVGGLSSMSGGDDA 776
Cdd:TIGR00603 630 VITHLPGMDNESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGEFGSRALGasrsmssaSGKAVRRGGSLSSLSGGDDM 709
                         730       740
                  ....*....|....*....|...
gi 24662247   777 IYYEHRKKNIGS----VHPLFKK 795
Cdd:TIGR00603 710 AYMEYRKPAIKKskkeVHPLFKK 732
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
512-757 7.04e-178

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: 509.83  E-value: 7.04e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   512 LQKKGYIARVQCAEVWCPMSPEFYREYLTTKTSKKMLLYVMNPSKFRSCQFLIKYHEQRGDKTIVFSDNVFALKHYAIKM 591
Cdd:pfam16203   1 LQEKGHIANVQCAEVWCPMTAEFYREYLRSKSRKKRLLYVMNPNKFRACQFLIRYHERRGDKIIVFSDNVFALKEYAKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   592 NKPFIYGPTSQNERIQILQNFKFNSKVNTIFVSKVADTSFDLPEANVLIQISSHGGSRRQEAQRLGRILRAKKGAIAEEY 671
Cdd:pfam16203  81 NKPYIYGGTSQAERMRILQNFKHNPNVNTIFLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRSNDEGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   672 NAFFYTLVSQDTMEMSYSRKRQRFLVNQGYSYKVITHLKGMDTDSDLMYGTQEEQGQLLQLVLSASDLDCEDEKLPGEPG 751
Cdd:pfam16203 161 NAFFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVITNLAGMEDEENLAYSTKEEQLELLQKVLAANDTDAEEEVIADDLG 240

                  ....*.
gi 24662247   752 YRPSGS 757
Cdd:pfam16203 241 KDRKGG 246
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
324-492 1.29e-109

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: 331.57  E-value: 1.29e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 324 IDLKPAAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTACCTVRKRALVLCNSGVSVEQWKQQFKMWSTADDS 403
Cdd:cd18029   1 IDLKPSTQLRPYQEKALSKMFGNGRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDWTTIDDE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 404 MICRFTSEAKDKPMGCGILVTTYSMITHTQKRSWEAEQTMRWLQEQEWGIMVLDEVHTIPAKMFRRVLTIVQSHCKLGLT 483
Cdd:cd18029  81 QIGRFTSDKKEIFPEAGVTVSTYSMLANTRKRSPESEKFMEFITEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLGLT 160

                ....*....
gi 24662247 484 ATLLREDDK 492
Cdd:cd18029 161 ATLVREDDK 169
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
332-705 1.70e-58

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 209.11  E-value: 1.70e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 332 LRPYQEKSLRKMFGNGRA--RSGVIVLPCGAGKSLVGVTACCTVR--KRALVLCNSGVSVEQWKQQFKMWSTaddsmicR 407
Cdd:COG1061  81 LRPYQQEALEALLAALERggGRGLVVAPTGTGKTVLALALAAELLrgKRVLVLVPRRELLEQWAEELRRFLG-------D 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 408 FTSEAKDKPMGCGILVTTYSMITHtqkrsweaEQTMRWLQEqEWGIMVLDEVHTIPAKMFRRVLTIVQSHCKLGLTATLL 487
Cdd:COG1061 154 PLAGGGKKDSDAPITVATYQSLAR--------RAHLDELGD-RFGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPF 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 488 REDDKIADLNFLIGpKLYEANWLELQKKGYIARVQCAEVWCPMSPEFyREYlttKTSKKMLLYVMNPSKFRSCQFLIKYH 567
Cdd:COG1061 225 RSDGREILLFLFDG-IVYEYSLKEAIEDGYLAPPEYYGIRVDLTDER-AEY---DALSERLREALAADAERKDKILRELL 299
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 568 EQRGD--KTIVFSDNVFALKHYA-----IKMNKPFIYGPTSQNERIQILQNFKfNSKVNTIFVSKVADTSFDLPEANVLI 640
Cdd:COG1061 300 REHPDdrKTLVFCSSVDHAEALAellneAGIRAAVVTGDTPKKEREEILEAFR-DGELRILVTVDVLNEGVDVPRLDVAI 378
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24662247 641 QISSHgGSRRQEAQRLGRILRAKKGaiaEEYnAFFYTLVSQDTMEMSYSRKRQRFLVnqGYSYKV 705
Cdd:COG1061 379 LLRPT-GSPREFIQRLGRGLRPAPG---KED-ALVYDFVGNDVPVLEELAKDLRDLA--GYRVEF 436
DEXDc smart00487
DEAD-like helicases superfamily;
324-498 1.30e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 84.85  E-value: 1.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247    324 IDLKPAAVLRPYQEKSLRKMFGNGRarSGVIVLPCGAGKSLVGVTAC-----CTVRKRALVLCNSGVSVEQWKQQFKMWS 398
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLR--DVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247    399 TADDSM-ICRFTSEAKDKPM------GCGILVTTYSMITHtqkrsweaEQTMRWLQEQEWGIMVLDEVHTIPAKMFRRVL 471
Cdd:smart00487  79 PSLGLKvVGLYGGDSKREQLrklesgKTDILVTTPGRLLD--------LLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190
                   ....*....|....*....|....*....|..
gi 24662247    472 TIVQSHCK-----LGLTATLLREDDKIADLNF 498
Cdd:smart00487 151 EKLLKLLPknvqlLLLSATPPEEIENLLELFL 182
uvsW PHA02558
UvsW helicase; Provisional
333-570 7.68e-03

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 39.61  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247  333 RPYQEKSLRKMFGNGRarsGVIVLPCGAGKSLVgvtACCTVR-------KRALVLCNSGVSVEQWKQQFKMWSTADDS-- 403
Cdd:PHA02558 116 HWYQYDAVYEGLKNNR---RLLNLPTSAGKSLI---QYLLSRyylenyeGKVLIIVPTTSLVTQMIDDFVDYRLFPREam 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247  404 -MICRFTSEAKDKPmgcgILVTTYSMItHTQKRSWeaeqtmrwlqEQEWGIMVLDEVHTIPAKMFRRVLTIVqSHC--KL 480
Cdd:PHA02558 190 hKIYSGTAKDTDAP----IVVSTWQSA-VKQPKEW----------FDQFGMVIVDECHLFTGKSLTSIITKL-DNCkfKF 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247  481 GLTATLlrEDDKIADLNF--LIGP--KLYEANwlELQKKGYIARVQCAEVWCPMSPEFyreylttktSKKMllyvmnpsK 556
Cdd:PHA02558 254 GLTGSL--RDGKANILQYvgLFGDifKPVTTS--QLMEEGQVTDLKINSIFLRYPDED---------RVKL--------K 312
                        250
                 ....*....|....*..
gi 24662247  557 FRSCQFLIKY---HEQR 570
Cdd:PHA02558 313 GEDYQEEIKYitsHTKR 329
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
70-795 0e+00

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: 1354.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247    70 DYRSQMQLRPDHGNRPLWVAPNGHVFLESFSPVYKHAHDFLIAISEPVCRPEHIHEYKLTAYSLYAAVSVGLQTHDIVEY 149
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   150 LKRLSKTSIPEGILEFIRLCTLSYGKVKLVLKHNKYFIESPHPEVLQKLLKDPVIQKCRLIRSEGEdfiqgtldgKAITQ 229
Cdd:TIGR00603  81 LGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEEE---------SLQTP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   230 FGTKLPPGATDKPTPD----PAAAAGADGTTAVPEDITDFYEKIDKEEEDEDeaNLKTVSFEVAQEKIEVIQKRCIEIEH 305
Cdd:TIGR00603 152 TYGSKEDFIINKPGFTggasAGQLEANQGESAVPKDIADFYELEEEEEDEDE--ETATHSFEIDQEQVEEVKKRCIELDY 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   306 PLLAEYDFRNDTNNPDINIDLKPAAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTACCTVRKRALVLCNSGV 385
Cdd:TIGR00603 230 PLLEEYDFRNDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   386 SVEQWKQQFKMWSTADDSMICRFTSEAKDKPMG-CGILVTTYSMITHTQKRSWEAEQTMRWLQEQEWGIMVLDEVHTIPA 464
Cdd:TIGR00603 310 SVEQWKQQFKMWSTIDDSQICRFTSDAKERFHGeAGVVVSTYSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   465 KMFRRVLTIVQSHCKLGLTATLLREDDKIADLNFLIGPKLYEANWLELQKKGYIARVQCAEVWCPMSPEFYREYLTTKTS 544
Cdd:TIGR00603 390 AMFRRVLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSR 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   545 KKMLLYVMNPSKFRSCQFLIKYHEQRGDKTIVFSDNVFALKHYAIKMNKPFIYGPTSQNERIQILQNFKFNSKVNTIFVS 624
Cdd:TIGR00603 470 KRMLLYVMNPNKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLS 549
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   625 KVADTSFDLPEANVLIQISSHGGSRRQEAQRLGRILRAKKGAIAEEYNAFFYTLVSQDTMEMSYSRKRQRFLVNQGYSYK 704
Cdd:TIGR00603 550 KVGDTSIDLPEANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAEEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFK 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   705 VITHLKGMDTDSDLMYGTQEEQGQLLQLVLSASDLDCEDEKLPGEPGYRPSG--------SGGAVRRVGGLSSMSGGDDA 776
Cdd:TIGR00603 630 VITHLPGMDNESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGEFGSRALGasrsmssaSGKAVRRGGSLSSLSGGDDM 709
                         730       740
                  ....*....|....*....|...
gi 24662247   777 IYYEHRKKNIGS----VHPLFKK 795
Cdd:TIGR00603 710 AYMEYRKPAIKKskkeVHPLFKK 732
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
512-757 7.04e-178

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: 509.83  E-value: 7.04e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   512 LQKKGYIARVQCAEVWCPMSPEFYREYLTTKTSKKMLLYVMNPSKFRSCQFLIKYHEQRGDKTIVFSDNVFALKHYAIKM 591
Cdd:pfam16203   1 LQEKGHIANVQCAEVWCPMTAEFYREYLRSKSRKKRLLYVMNPNKFRACQFLIRYHERRGDKIIVFSDNVFALKEYAKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   592 NKPFIYGPTSQNERIQILQNFKFNSKVNTIFVSKVADTSFDLPEANVLIQISSHGGSRRQEAQRLGRILRAKKGAIAEEY 671
Cdd:pfam16203  81 NKPYIYGGTSQAERMRILQNFKHNPNVNTIFLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRSNDEGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   672 NAFFYTLVSQDTMEMSYSRKRQRFLVNQGYSYKVITHLKGMDTDSDLMYGTQEEQGQLLQLVLSASDLDCEDEKLPGEPG 751
Cdd:pfam16203 161 NAFFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVITNLAGMEDEENLAYSTKEEQLELLQKVLAANDTDAEEEVIADDLG 240

                  ....*.
gi 24662247   752 YRPSGS 757
Cdd:pfam16203 241 KDRKGG 246
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
324-492 1.29e-109

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: 331.57  E-value: 1.29e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 324 IDLKPAAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTACCTVRKRALVLCNSGVSVEQWKQQFKMWSTADDS 403
Cdd:cd18029   1 IDLKPSTQLRPYQEKALSKMFGNGRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDWTTIDDE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 404 MICRFTSEAKDKPMGCGILVTTYSMITHTQKRSWEAEQTMRWLQEQEWGIMVLDEVHTIPAKMFRRVLTIVQSHCKLGLT 483
Cdd:cd18029  81 QIGRFTSDKKEIFPEAGVTVSTYSMLANTRKRSPESEKFMEFITEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLGLT 160

                ....*....
gi 24662247 484 ATLLREDDK 492
Cdd:cd18029 161 ATLVREDDK 169
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
523-679 2.47e-87

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: 272.59  E-value: 2.47e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 523 CAEVWCPMSPEFYREYLTTK-TSKKMLLYVMNPSKFRSCQFLIKYHEQrGDKTIVFSDNVFALKHYAIKMNKPFIYGPTS 601
Cdd:cd18789   1 CAEIRCPMTPEFYREYLGLGaHRKRRLLAAMNPNKLRALEELLKRHEQ-GDKIIVFTDNVEALYRYAKRLLKPFITGETP 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24662247 602 QNERIQILQNFKFNsKVNTIFVSKVADTSFDLPEANVLIQISSHGGSRRQEAQRLGRILRAKKGAiaeEYNAFFYTLV 679
Cdd:cd18789  80 QSEREEILQNFREG-EYNTLVVSKVGDEGIDLPEANVAIQISGHGGSRRQEAQRLGRILRPKKGG---GKNAFFYSLV 153
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
332-705 1.70e-58

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 209.11  E-value: 1.70e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 332 LRPYQEKSLRKMFGNGRA--RSGVIVLPCGAGKSLVGVTACCTVR--KRALVLCNSGVSVEQWKQQFKMWSTaddsmicR 407
Cdd:COG1061  81 LRPYQQEALEALLAALERggGRGLVVAPTGTGKTVLALALAAELLrgKRVLVLVPRRELLEQWAEELRRFLG-------D 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 408 FTSEAKDKPMGCGILVTTYSMITHtqkrsweaEQTMRWLQEqEWGIMVLDEVHTIPAKMFRRVLTIVQSHCKLGLTATLL 487
Cdd:COG1061 154 PLAGGGKKDSDAPITVATYQSLAR--------RAHLDELGD-RFGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTATPF 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 488 REDDKIADLNFLIGpKLYEANWLELQKKGYIARVQCAEVWCPMSPEFyREYlttKTSKKMLLYVMNPSKFRSCQFLIKYH 567
Cdd:COG1061 225 RSDGREILLFLFDG-IVYEYSLKEAIEDGYLAPPEYYGIRVDLTDER-AEY---DALSERLREALAADAERKDKILRELL 299
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 568 EQRGD--KTIVFSDNVFALKHYA-----IKMNKPFIYGPTSQNERIQILQNFKfNSKVNTIFVSKVADTSFDLPEANVLI 640
Cdd:COG1061 300 REHPDdrKTLVFCSSVDHAEALAellneAGIRAAVVTGDTPKKEREEILEAFR-DGELRILVTVDVLNEGVDVPRLDVAI 378
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24662247 641 QISSHgGSRRQEAQRLGRILRAKKGaiaEEYnAFFYTLVSQDTMEMSYSRKRQRFLVnqGYSYKV 705
Cdd:COG1061 379 LLRPT-GSPREFIQRLGRGLRPAPG---KED-ALVYDFVGNDVPVLEELAKDLRDLA--GYRVEF 436
Helicase_C_3 pfam13625
Helicase conserved C-terminal domain; This domain family is found in a wide variety of ...
86-209 4.07e-46

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: 160.36  E-value: 4.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247    86 LWVAPNGHVFLESfsPVYKHAHDFLIAISEPVCRpEHIHEYKLTAYSLYAAVSVGLQTHDIVEYLKRLSKTSIPEGILEF 165
Cdd:pfam13625   1 LIVQADLTILLPG--PLAPEARDFLAAFAELESR-GHAHTYRLTPLSLRRALDAGLTAEDILDFLERHSKYPVPQALEYL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 24662247   166 IRLCTLSYGKVKLVLkHNKYFIESPHPEVLQKLLKDPVIQKCRL 209
Cdd:pfam13625  78 IRDVARRHGRLRLGL-GASSYLRSDDPAVLAELLADPRIAPLGL 120
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
332-486 1.41e-39

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: 142.83  E-value: 1.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 332 LRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTACCTVRK-RALVLCNSGVSVEQWKQQFKMWSTadDSMICRFTS 410
Cdd:cd17926   1 LRPYQEEALEAWLAHKNNRRGILVLPTGSGKTLTALALIAYLKElRTLIVVPTDALLDQWKERFEDFLG--DSSIGLIGG 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24662247 411 EAKDKPMGCGILVTTYsmithtQKRSWEAEQTMRWLqeQEWGIMVLDEVHTIPAKMFRRVLTIVQSHCKLGLTATL 486
Cdd:cd17926  79 GKKKDFDDANVVVATY------QSLSNLAEEEKDLF--DQFGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
DEXDc smart00487
DEAD-like helicases superfamily;
324-498 1.30e-18

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 84.85  E-value: 1.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247    324 IDLKPAAVLRPYQEKSLRKMFGNGRarSGVIVLPCGAGKSLVGVTAC-----CTVRKRALVLCNSGVSVEQWKQQFKMWS 398
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLR--DVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247    399 TADDSM-ICRFTSEAKDKPM------GCGILVTTYSMITHtqkrsweaEQTMRWLQEQEWGIMVLDEVHTIPAKMFRRVL 471
Cdd:smart00487  79 PSLGLKvVGLYGGDSKREQLrklesgKTDILVTTPGRLLD--------LLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190
                   ....*....|....*....|....*....|..
gi 24662247    472 TIVQSHCK-----LGLTATLLREDDKIADLNF 498
Cdd:smart00487 151 EKLLKLLPknvqlLLLSATPPEEIENLLELFL 182
ResIII pfam04851
Type III restriction enzyme, res subunit;
331-488 1.07e-15

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 75.40  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   331 VLRPYQE---KSLRKMFGNGRARsGVIVLPCGAGKSLVGVTACCTVRK-----RALVLCNSGVSVEQWKQQFKMWSTADD 402
Cdd:pfam04851   3 ELRPYQIeaiENLLESIKNGQKR-GLIVMATGSGKTLTAAKLIARLFKkgpikKVLFLVPRKDLLEQALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   403 SmICRFTSEAKDKPM--GCGILVTTYSMIThtqkrSWEAEQTMRWLQEQeWGIMVLDEVHTIPAKMFRRVLTIVQSHCKL 480
Cdd:pfam04851  82 E-IGEIISGDKKDESvdDNKIVVTTIQSLY-----KALELASLELLPDF-FDVIIIDEAHRSGASSYRNILEYFKPAFLL 154

                  ....*...
gi 24662247   481 GLTATLLR 488
Cdd:pfam04851 155 GLTATPER 162
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
332-485 1.61e-13

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: 69.52  E-value: 1.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 332 LRPYQEKSLRKMFGNGRARSGVIVLPC-GAGKSLVGVTACCTVRK------RALVLC-NSgvSVEQWKQQFKMWstADDS 403
Cdd:cd17919   1 LRPYQLEGLNFLLELYENGPGGILADEmGLGKTLQAIAFLAYLLKegkergPVLVVCpLS--VLENWEREFEKW--TPDL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 404 MICRFTSEAKD--------KPMGCGILVTTYSMIthtqkrSWEAEqtmrWLQEQEWGIMVLDEVHTI---PAKMFRRVLT 472
Cdd:cd17919  77 RVVVYHGSQREraqirakeKLDKFDVVLTTYETL------RRDKA----SLRKFRWDLVVVDEAHRLknpKSQLSKALKA 146
                       170
                ....*....|...
gi 24662247 473 IvQSHCKLGLTAT 485
Cdd:cd17919 147 L-RAKRRLLLTGT 158
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
561-663 9.24e-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: 65.31  E-value: 9.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   561 QFLIKYHE-QRGDKTIVFSDNVFALKHYAIKMNKPF----IYGPTSQNERIQILQNFKfNSKVNTIFVSKVADTSFDLPE 635
Cdd:pfam00271   4 EALLELLKkERGGKVLIFSQTKKTLEAELLLEKEGIkvarLHGDLSQEEREEILEDFR-KGKIDVLVATDVAERGLDLPD 82
                          90       100
                  ....*....|....*....|....*...
gi 24662247   636 ANVLIQISSHgGSRRQEAQRLGRILRAK 663
Cdd:pfam00271  83 VDLVINYDLP-WNPASYIQRIGRAGRAG 109
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
330-695 4.26e-11

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 66.40  E-value: 4.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 330 AVLRPYQEKSLRKMFGNGRARSGVI----VlpcGAGKSLVGVTACCTVR-----KRALVLCNSGVsVEQWKQQFKMWSTA 400
Cdd:COG0553 240 ATLRPYQLEGAAWLLFLRRLGLGGLladdM---GLGKTIQALALLLELKerglaRPVLIVAPTSL-VGNWQRELAKFAPG 315
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 401 DDSMICRFTSEAKDKP---MGCGILVTTYSMIthtqkRSWEAEqtmrwLQEQEWGIMVLDEVHTI---PAKMFRRVLTIv 474
Cdd:COG0553 316 LRVLVLDGTRERAKGAnpfEDADLVITSYGLL-----RRDIEL-----LAAVDWDLVILDEAQHIknpATKRAKAVRAL- 384
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 475 QSHCKLGLTAT-----------LLR------------------------EDDKIADLNFLIGPKLY----EANWLELQKK 515
Cdd:COG0553 385 KARHRLALTGTpvenrleelwsLLDflnpgllgslkafrerfarpiekgDEEALERLRRLLRPFLLrrtkEDVLKDLPEK 464
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 516 gyiaRVQcaEVWCPMSPE---FYREYL---------TTKTSKKMLL-----------------------YVMNPSKFRSC 560
Cdd:COG0553 465 ----TEE--TLYVELTPEqraLYEAVLeylrrelegAEGIRRRGLIlaaltrlrqicshpallleegaeLSGRSAKLEAL 538
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 561 QFLIKYHEQRGDKTIVFS---DNVFALKHYAIKMNKP--FIYGPTSQNERIQILQNFKFNSKVNTIFVS-KVADTSFDLP 634
Cdd:COG0553 539 LELLEELLAEGEKVLVFSqftDTLDLLEERLEERGIEyaYLHGGTSAEERDELVDRFQEGPEAPVFLISlKAGGEGLNLT 618
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24662247 635 EANVLIQISshggsrR-----QEAQRLGRILRakkgaIAEEYNAFFYTLVSQDT-----MEMsYSRKRQRF 695
Cdd:COG0553 619 AADHVIHYD------LwwnpaVEEQAIDRAHR-----IGQTRDVQVYKLVAEGTieekiLEL-LEEKRALA 677
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
332-492 8.13e-11

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: 61.04  E-value: 8.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 332 LRPYQEKSLRKM---FGNGRARSGViVLPCGAGKSLVGVTAC-----CTVRKRALVLCNSGVSVEQWKQQFKmwsTA--D 401
Cdd:cd18032   1 PRYYQQEAIEALeeaREKGQRRALL-VMATGTGKTYTAAFLIkrlleANRKKRILFLAHREELLEQAERSFK---EVlpD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 402 DSMIcrFTSEAKDKPMGCGILVTTYsmithtqkrsweaeQTM--RWLQEQ----EWGIMVLDEVHTIPAKMFRRVLTIVQ 475
Cdd:cd18032  77 GSFG--NLKGGKKKPDDARVVFATV--------------QTLnkRKRLEKfppdYFDLIIIDEAHHAIASSYRKILEYFE 140
                       170
                ....*....|....*..
gi 24662247 476 SHCKLGLTATLLREDDK 492
Cdd:cd18032 141 PAFLLGLTATPERTDGL 157
HELICc smart00490
helicase superfamily c-terminal domain;
595-663 3.52e-10

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 56.84  E-value: 3.52e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24662247    595 FIYGPTSQNERIQILQNFKfNSKVNTIFVSKVADTSFDLPEANVLIQISSHgGSRRQEAQRLGRILRAK 663
Cdd:smart00490  16 RLHGGLSQEEREEILDKFN-NGKIKVLVATDVAERGLDLPGVDLVIIYDLP-WSPASYIQRIGRAGRAG 82
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
332-487 4.16e-06

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: 48.83  E-value: 4.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 332 LRPYQEKSLRKM----FGNGRARS---GVIVLPC-GAGKSLVGVT------ACCTVRKRALVLCNSGVsVEQWKQQFKMW 397
Cdd:cd18007   1 LKPHQVEGVRFLwsnlVGTDVGSDeggGCILAHTmGLGKTLQVITflhtylAAAPRRSRPLVLCPAST-LYNWEDEFKKW 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 398 --STADDSMICRFTSEAKdKPMGC-----------GILVTTYSM----ITHTQKRSWEAEQTMRWLQEQEWGIMVLDEVH 460
Cdd:cd18007  80 lpPDLRPLLVLVSLSASK-RADARlrkinkwhkegGVLLIGYELfrnlASNATTDPRLKQEFIAALLDPGPDLLVLDEGH 158
                       170       180
                ....*....|....*....|....*....
gi 24662247 461 TI--PAKMFRRVLTIVQSHCKLGLTATLL 487
Cdd:cd18007 159 RLknEKSQLSKALSKVKTKRRILLTGTPL 187
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
371-490 1.48e-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: 47.37  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 371 CTVRKRALVLCNSGVsVEQWKQQFKMW----------STADDSMICRFtseakdKPMGCGILVTTYSMIthtqKRSWEAe 440
Cdd:cd18005  67 SSAKKPVLIVAPLSV-LYNWKDELDTWghfevgvyhgSRKDDELEGRL------KAGRLEVVVTTYDTL----RRCIDS- 134
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 24662247 441 qtmrwLQEQEWGIMVLDEVHTI--PAKMFRRVLTIVQSHCKLGLTATLLRED 490
Cdd:cd18005 135 -----LNSINWSAVIADEAHRIknPKSKLTQAMKELKCKVRIGLTGTLLQNN 181
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
352-485 2.44e-05

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: 45.09  E-value: 2.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 352 GVIVLPCGAGKSLVG----VTACCTVRKRALVLCNSGVSVEQWKQQFKMWST--ADDSMICRFTSEAKDKPMGCG---IL 422
Cdd:cd00046   4 VLITAPTGSGKTLAAllaaLLLLLKKGKKVLVLVPTKALALQTAERLRELFGpgIRVAVLVGGSSAEEREKNKLGdadII 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24662247 423 VTTYSMIThtqkRSWEAEqtmRWLQEQEWGIMVLDEVHTIPAKMfRRVLTIVQSHCKL--------GLTAT 485
Cdd:cd00046  84 IATPDMLL----NLLLRE---DRLFLKDLKLIIVDEAHALLIDS-RGALILDLAVRKAglknaqviLLSAT 146
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
555-661 3.79e-04

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: 41.31  E-value: 3.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 555 SKFRSCQFLIKYHEQRGDKTIVFS---DNVFALKHYAIKMNKPF--IYGPTSQNERIQILQNFKFNSKVNTIFVS-KVAD 628
Cdd:cd18793  11 GKLEALLELLEELREPGEKVLIFSqftDTLDILEEALRERGIKYlrLDGSTSSKERQKLVDRFNEDPDIRVFLLStKAGG 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 24662247 629 TSFDLPEANVLI--------QIsshggsrrqEAQRLGRILR 661
Cdd:cd18793  91 VGLNLTAANRVIlydpwwnpAV---------EEQAIDRAHR 122
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
334-462 6.31e-04

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: 41.48  E-value: 6.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 334 PYQEKSLRKMFGNGRarSGVIVLPCGAGKSLVG----VTACCTVRKRALVLCNSGVSVEQ----WKQQFKMwSTADDSMI 405
Cdd:cd17921   4 PIQREALRALYLSGD--SVLVSAPTSSGKTLIAelaiLRALATSGGKAVYIAPTRALVNQkeadLRERFGP-LGKNVGLL 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24662247 406 CRFTSEAKDKPMGCGILVTTYsMITHTQKRSWEAeqtmRWLQEQewGIMVLDEVHTI 462
Cdd:cd17921  81 TGDPSVNKLLLAEADILVATP-EKLDLLLRNGGE----RLIQDV--RLVVVDEAHLI 130
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
331-500 2.02e-03

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: 40.45  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 331 VLRPYQEKS---LRKMFGNGRarSGVIVLPCGAGKSLVGVTACCTVRKRAL----VLCNSGVSVEQWKQQFKMWSTADDS 403
Cdd:cd18009   3 VMRPYQLEGmewLRMLWENGI--NGILADEMGLGKTIQTIALLAHLRERGVwgpfLVIAPLSTLPNWVNEFARFTPSVPV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 404 MICRFTSEAKDK-----------PMGCGILVTTYSMITHTQKRsweaeqtmrwLQEQEWGIMVLDEVHTIPAKMFR--RV 470
Cdd:cd18009  81 LLYHGTKEERERlrkkimkregtLQDFPVVVTSYEIAMRDRKA----------LQHYAWKYLIVDEGHRLKNLNCRliQE 150
                       170       180       190
                ....*....|....*....|....*....|..
gi 24662247 471 LTIVQSHCKLGLTATLLREDDK--IADLNFLI 500
Cdd:cd18009 151 LKTFNSDNRLLLTGTPLQNNLSelWSLLNFLL 182
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
374-521 2.08e-03

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: 40.35  E-value: 2.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 374 RKRALVLCNSGVsVEQWKQQfkMWS-------TADDSMICRFTSEAKDKPMGCGILVTTYSMIthtqkRSWEAEQtmRWL 446
Cdd:cd18011  47 AKRVLILCPASL-VEQWQDE--LQDkfglpflILDRETAAQLRRLIGNPFEEFPIVIVSLDLL-----KRSEERR--GLL 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247 447 QEQEWGIMVLDEVH-------TIPAKMFRRVLTIVQ-SHCKLGLTAT--LLREDDkIADLNFLIGPKLYEANWLELQKKG 516
Cdd:cd18011 117 LSEEWDLVVVDEAHklrnsggGKETKRYKLGRLLAKrARHVLLLTATphNGKEED-FRALLSLLDPGRFAVLGRFLRLDG 195

                ....*
gi 24662247 517 YIARV 521
Cdd:cd18011 196 LREVL 200
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
621-677 2.74e-03

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 37.30  E-value: 2.74e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24662247 621 IFVSKVADTSFDLPEANVLIQISSHGgSRRQEAQRLGRILRAKKgaiaEEYNAFFYT 677
Cdd:cd18785  26 LVATNVLGEGIDVPSLDTVIFFDPPS-SAASYIQRVGRAGRGGK----DEGEVILFV 77
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
333-486 3.81e-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: 38.76  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   333 RPYQEKSLRKMFGNgraRSGVIVLPCGAGKSLV-GVTACCTVRK-----RALVLCNSGVSVEQWKQQFKMWSTADDSMIC 406
Cdd:pfam00270   1 TPIQAEAIPAILEG---RDVLVQAPTGSGKTLAfLLPALEALDKldngpQALVLAPTRELAEQIYEELKKLGKGLGLKVA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247   407 RFTSEAKDKPM-----GCGILVTTYSMI-THTQKRsweaeqtmRWLQEQEWgiMVLDEVHTIPAKMFRRVLTIVQSHCK- 479
Cdd:pfam00270  78 SLLGGDSRKEQleklkGPDILVGTPGRLlDLLQER--------KLLKNLKL--LVLDEAHRLLDMGFGPDLEEILRRLPk 147
                         170
                  ....*....|.
gi 24662247   480 ----LGLTATL 486
Cdd:pfam00270 148 krqiLLLSATL 158
uvsW PHA02558
UvsW helicase; Provisional
333-570 7.68e-03

UvsW helicase; Provisional


Pssm-ID: 222875 [Multi-domain]  Cd Length: 501  Bit Score: 39.61  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247  333 RPYQEKSLRKMFGNGRarsGVIVLPCGAGKSLVgvtACCTVR-------KRALVLCNSGVSVEQWKQQFKMWSTADDS-- 403
Cdd:PHA02558 116 HWYQYDAVYEGLKNNR---RLLNLPTSAGKSLI---QYLLSRyylenyeGKVLIIVPTTSLVTQMIDDFVDYRLFPREam 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247  404 -MICRFTSEAKDKPmgcgILVTTYSMItHTQKRSWeaeqtmrwlqEQEWGIMVLDEVHTIPAKMFRRVLTIVqSHC--KL 480
Cdd:PHA02558 190 hKIYSGTAKDTDAP----IVVSTWQSA-VKQPKEW----------FDQFGMVIVDECHLFTGKSLTSIITKL-DNCkfKF 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662247  481 GLTATLlrEDDKIADLNF--LIGP--KLYEANwlELQKKGYIARVQCAEVWCPMSPEFyreylttktSKKMllyvmnpsK 556
Cdd:PHA02558 254 GLTGSL--RDGKANILQYvgLFGDifKPVTTS--QLMEEGQVTDLKINSIFLRYPDED---------RVKL--------K 312
                        250
                 ....*....|....*..
gi 24662247  557 FRSCQFLIKY---HEQR 570
Cdd:PHA02558 313 GEDYQEEIKYitsHTKR 329
 
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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