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Conserved domains on  [gi|15834617|ref|NP_000391|]
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general transcription and DNA repair factor IIH helicase subunit XPD isoform 1 [Homo sapiens]

Protein Classification

DEAD/DEAH box DNA helicase( domain architecture ID 11489423)

DEAD/DEAH box containing ATP-dependent DNA helicase, similar to Homo sapiens general transcription and DNA repair factor IIH helicase subunit XPD, an ATP-dependent 5'-3' DNA helicase that is a component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
7-708 0e+00

DNA repair helicase (rad3); All proteins in this family for which funcitons are known are DNA-DNA helicases that funciton in the initiation of transcription and nucleotide excision repair 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: 273169 [Multi-domain]  Cd Length: 705  Bit Score: 983.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617     7 GLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPlEVTKLIYCSRTVPEIEKVIEE 86
Cdd:TIGR00604   1 ELLVYFPYEKIYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKP-EVRKIIYASRTHSQLEQATEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617    87 LRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDA-HG 165
Cdd:TIGR00604  80 LRKLMSYRTPRIGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGKCIKLTVSKIKEQRTEKPNVESCEFYENFDElRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   166 REVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELArKAVVVFDEAHNIDNVCID 245
Cdd:TIGR00604 160 VEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSIELK-DSIVIFDEAHNLDNVCIS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   246 SMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRT 325
Cdd:TIGR00604 239 SLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDARKLLDELQKLVEGLKQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   326 AEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRkPLRFCAERLRSLLHTLEITDLADFSPLTLLANFAT 405
Cdd:TIGR00604 319 AEIFLHKLSRYLEYLKDALKVLGVVSELPDAFLEHLKEKTFIDR-PLRFCSERLSNLLRELEITHPEDFSALVLLFTFAT 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   406 LVSTYAKGFTIIIEPFDDrtPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTL 485
Cdd:TIGR00604 398 LVLTYTNGFLEGIEPYEN--KTVPNPILKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHIL 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   486 ARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNK 565
Cdd:TIGR00604 476 KRENLLTLIVTRGSDQVPLSSTFEIRNDPSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   566 LLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQ 645
Cdd:TIGR00604 556 LIFVETKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFLRDQYP 635
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15834617   646 IREN-DFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARGDKRGKLPRWIQEHLTDANLNL 708
Cdd:TIGR00604 636 IRENqDFYEFDAMRAVNQAIGRVIRHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDLNG 699
 
Name Accession Description Interval E-value
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
7-708 0e+00

DNA repair helicase (rad3); All proteins in this family for which funcitons are known are DNA-DNA helicases that funciton in the initiation of transcription and nucleotide excision repair 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: 273169 [Multi-domain]  Cd Length: 705  Bit Score: 983.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617     7 GLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPlEVTKLIYCSRTVPEIEKVIEE 86
Cdd:TIGR00604   1 ELLVYFPYEKIYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKP-EVRKIIYASRTHSQLEQATEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617    87 LRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDA-HG 165
Cdd:TIGR00604  80 LRKLMSYRTPRIGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGKCIKLTVSKIKEQRTEKPNVESCEFYENFDElRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   166 REVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELArKAVVVFDEAHNIDNVCID 245
Cdd:TIGR00604 160 VEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSIELK-DSIVIFDEAHNLDNVCIS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   246 SMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRT 325
Cdd:TIGR00604 239 SLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDARKLLDELQKLVEGLKQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   326 AEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRkPLRFCAERLRSLLHTLEITDLADFSPLTLLANFAT 405
Cdd:TIGR00604 319 AEIFLHKLSRYLEYLKDALKVLGVVSELPDAFLEHLKEKTFIDR-PLRFCSERLSNLLRELEITHPEDFSALVLLFTFAT 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   406 LVSTYAKGFTIIIEPFDDrtPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTL 485
Cdd:TIGR00604 398 LVLTYTNGFLEGIEPYEN--KTVPNPILKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHIL 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   486 ARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNK 565
Cdd:TIGR00604 476 KRENLLTLIVTRGSDQVPLSSTFEIRNDPSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   566 LLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQ 645
Cdd:TIGR00604 556 LIFVETKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFLRDQYP 635
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15834617   646 IREN-DFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARGDKRGKLPRWIQEHLTDANLNL 708
Cdd:TIGR00604 636 IRENqDFYEFDAMRAVNQAIGRVIRHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDLNG 699
DEXDc2 smart00488
DEAD-like helicases superfamily;
8-280 2.58e-123

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 370.56  E-value: 2.58e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617      8 LLVYFPYDYiYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEV--TKLIYCSRTVPEIEKVIE 85
Cdd:smart00488   1 LLFYFPYEP-YPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSFPERIqkIKLIYLSRTVSEIEKRLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617     86 ELRKLL---------------NFYEKQEGEKLPFLGLALSSRKNLCIHPEV-TPLRFGKDVDGKCHSLTASYVRAQYQHD 149
Cdd:smart00488  80 ELRKLMqkveyesdeesekqaQLLHELGREKPKVLGLSLTSRKNLCLNPEVrTLKQNGLVVDEVCRSLTASKARKYRYEN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617    150 TSLPHCRFYEEFDAHGREVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELArKA 229
Cdd:smart00488 160 PKVERCPFYENTEFLLVRDLLPAEVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIRQALSIELK-DS 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 15834617    230 VVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQR 280
Cdd:smart00488 239 IVIFDEAHNLDNVCISALSSELSRRSLERAHKNIKKYFERIEKIRENDAKR 289
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
489-684 2.39e-80

C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases belonging to superfamily (SF)2. This family includes DDX11 (also called ChlR1), a protein involved in maintaining chromosome transmission fidelity and genome stability, the TFIIH basal transcription factor complex XPD subunit, and FANCJ (also known as BRIP1), a DNA helicase required for the maintenance of chromosomal stability. 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: 350175 [Multi-domain]  Cd Length: 159  Bit Score: 253.68  E-value: 2.39e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 489 CLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVAswyeqgileniqrnkllf 568
Cdd:cd18788   2 QVCPGIVGRGPDQQALNSKFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERVVS------------------ 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 569 ietqdgaetsvalekyqeacengRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKAR---LEYLRDQFQ 645
Cdd:cd18788  64 -----------------------RGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKmddLEYLRDKGL 120
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15834617 646 IRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRF 684
Cdd:cd18788 121 LTGEDWYTFQAMRAVNQAIGRAIRHKNDYGAIVLLDKRF 159
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
72-256 2.46e-55

DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases that are seemingly ubiquitous - members include proteins of eukaryotic, bacterial and archaeal origin. RAD3 is involved in nucleotide excision repair, and forms part of the transcription factor TFIIH in yeast.


Pssm-ID: 399602 [Multi-domain]  Cd Length: 168  Bit Score: 187.47  E-value: 2.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617    72 YCSRTVPEIEKVIEELRKLLNFYekqegeklPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQyqhdts 151
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYYK--------KIRGLILGSRKNLCINPEVLKLKKGNLVNERCRELVKSKARGS------ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   152 lphCRFY---EEFDAHGREvpLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELaRK 228
Cdd:pfam06733  67 ---CPFYnnlEDLLKLRDL--LGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINL-KN 140
                         170       180
                  ....*....|....*....|....*...
gi 15834617   229 AVVVFDEAHNIDNVCIDSMSVNLTRRTL 256
Cdd:pfam06733 141 SIVIFDEAHNIEDVCIESASFSISRSQL 168
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
11-686 3.67e-41

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 160.09  E-value: 3.67e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  11 YFP-YDYiYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLL--ALIMAYQRAyplevTKLIYCSRTVPEIEKVIE-E 86
Cdd:COG1199   9 AFPgFEP-RPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAYLvpALLAARETG-----KKVVISTATKALQEQLVEkD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  87 LRKLlnfyekQEGEKLPFLGLALSSRKN-LCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHG 165
Cdd:COG1199  83 LPLL------RKALGLPLRVALLKGRSNyLCLRRLEQALQEGDDLDDEELLLARILAWASETWTGDRDELPLPEDDELWR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 166 RevplpagiYNLDDLKALGRRQGW---CPYFLARYSILHANVVVYSYHYLLdpkiADLVSKE--LARKAVVVFDEAHNID 240
Cdd:COG1199 157 Q--------VTSDADNCLGRRCPYygvCPYELARRLAREADVVVVNHHLLF----ADLALGEelLPEDDVLIIDEAHNLP 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 241 NVCIDSMSVNLTRRTLDRCQGNLETLQKTvLRIKETDE--QRLRDEYRRLVEGLREASAARETDAHLANPvlpDEVLQEA 318
Cdd:COG1199 225 DRARDMFSAELSSRSLLRLLRELRKLGLR-PGLKKLLDllERLREALDDLFLALEEEEELRLALGELPDE---PEELLEA 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 319 VpgsirtaEHFLGFLRRLLEYvkwrlrvqhvvqesppafLSGLAQRvciqRKPLRFCAERLRSLLHTLE-ITDLADFspl 397
Cdd:COG1199 301 L-------DALRDALEALAEA------------------LEEELER----LAELDALLERLEELLFALArFLRIAED--- 348
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 398 tllANFATLVSTYAKGFTiiiepfddrtptianpiLHFSCMDASLAIKP-VFERFQSVIITSGTLS---PLDIYPKI--L 471
Cdd:COG1199 349 ---EGYVRWLEREGGDVR-----------------LHAAPLDPADLLRElLFSRARSVVLTSATLSvggPFDYFARRlgL 408
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 472 DFHPVTMA---TFTM-TLARVCLCPMIigrgndqVAISSKFETREDIAvirnygNLLLEMSAVVPDGIVAFFTSYQYMES 547
Cdd:COG1199 409 DEDARTLSlpsPFDYeNQALLYVPRDL-------PRPSDRDGYLEAIA------EAIAELLEASGGNTLVLFTSYRALEQ 475
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 548 TVAswyeqgILENIQRNKLLFietQDGAETSVALEKYQEacenGRGAILlsVARGKVSEGIDFVHHYGRAVIMFGVPYVY 627
Cdd:COG1199 476 VAE------LLRERLDIPVLV---QGDGSREALLERFRE----GGNSVL--VGTGSFWEGVDLPGDALSLVIIVKLPFPP 540
                       650       660       670       680       690
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15834617 628 TQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFAR 686
Cdd:COG1199 541 PDDPVLEARREALEARGGNGFMYAYLPPAVIKLKQGAGRLIRSEEDRGVVVLLDRRLLT 599
dinG PRK11747
ATP-dependent DNA helicase DinG; Provisional
190-683 2.22e-10

ATP-dependent DNA helicase DinG; Provisional


Pssm-ID: 236966 [Multi-domain]  Cd Length: 697  Bit Score: 64.08  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  190 CPYFLARYSILHANVVVYSyHYLLdpkIADLvskEL--------ARKAVVVFDEAHNIDNVCID----SMSVNLTRRTLD 257
Cdd:PRK11747 208 CPFFKARREIDEADVVVAN-HDLV---LADL---ELgggvvlpdPENLLYVLDEGHHLPDVARDhfaaSAELKGTADWLE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  258 RCQGNLETLQKTVLRIKETDEQRLRDeyrrLVEGLREA--SAARETDAHL-----------ANPVLPDEVLQEAvpgsIR 324
Cdd:PRK11747 281 KLLKLLTKLVALIMEPPLALPERLNA----HCEELRELlaSLNQILNLFLpaggeearyrfEMGELPEELLELA----ER 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  325 TAEHFLGfLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRV--CIQRkplrfcAERLRSLLHTLEITDLADFSPLtllan 402
Cdd:PRK11747 353 LAKLTEK-LLGLLEKLLNDLSEAMKTGKIDIVRLERLLLELgrALGR------LEALSKLWRLAAKEDQESGAPM----- 420
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  403 fatlvstyAKGFTiiIEPFDDRTPTIAN--PILHFSCMDASLaikpvFERFQSVIITSGTL------------------- 461
Cdd:PRK11747 421 --------ARWIT--REERDGQGDYLFHasPIRVGDQLERLL-----WSRAPGAVLTSATLrslnsfdrfqeqsglpekd 485
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  462 --------SPLD-------IYPKiLDFHPVTMATFTMTLARvclcpmiigrgndqvaisskfETREDIAVirNYGNLLLe 526
Cdd:PRK11747 486 gdrflalpSPFDypnqgklVIPK-MRAEPDNEEAHTAEMAE---------------------FLPELLEK--HKGSLVL- 540
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  527 msavvpdgivafFTSYQYMEsTVASwyeqgILENIQRNKLLfieTQDGAETSVALEKYQEACENGRGAILLSVarGKVSE 606
Cdd:PRK11747 541 ------------FASRRQMQ-KVAD-----LLPRDLRLMLL---VQGDQPRQRLLEKHKKRVDEGEGSVLFGL--QSFAE 597
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  607 GIDFVHHYGRAVIM----FGVPyvytQSRILKARLEYLRDQfqiRENDFLTF---DAMRHAAQCVGRAIRGKTDYGLMVF 679
Cdd:PRK11747 598 GLDLPGDYLTQVIItkipFAVP----DSPVEATLAEWLKSR---GGNPFMEIsvpDASFKLIQAVGRLIRSEQDRGRVTI 670

                 ....
gi 15834617  680 ADKR 683
Cdd:PRK11747 671 LDRR 674
 
Name Accession Description Interval E-value
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
7-708 0e+00

DNA repair helicase (rad3); All proteins in this family for which funcitons are known are DNA-DNA helicases that funciton in the initiation of transcription and nucleotide excision repair 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: 273169 [Multi-domain]  Cd Length: 705  Bit Score: 983.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617     7 GLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPlEVTKLIYCSRTVPEIEKVIEE 86
Cdd:TIGR00604   1 ELLVYFPYEKIYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKP-EVRKIIYASRTHSQLEQATEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617    87 LRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDA-HG 165
Cdd:TIGR00604  80 LRKLMSYRTPRIGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGKCIKLTVSKIKEQRTEKPNVESCEFYENFDElRE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   166 REVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELArKAVVVFDEAHNIDNVCID 245
Cdd:TIGR00604 160 VEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSIELK-DSIVIFDEAHNLDNVCIS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   246 SMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRT 325
Cdd:TIGR00604 239 SLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDARKLLDELQKLVEGLKQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   326 AEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRkPLRFCAERLRSLLHTLEITDLADFSPLTLLANFAT 405
Cdd:TIGR00604 319 AEIFLHKLSRYLEYLKDALKVLGVVSELPDAFLEHLKEKTFIDR-PLRFCSERLSNLLRELEITHPEDFSALVLLFTFAT 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   406 LVSTYAKGFTIIIEPFDDrtPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTL 485
Cdd:TIGR00604 398 LVLTYTNGFLEGIEPYEN--KTVPNPILKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHIL 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   486 ARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNK 565
Cdd:TIGR00604 476 KRENLLTLIVTRGSDQVPLSSTFEIRNDPSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   566 LLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQ 645
Cdd:TIGR00604 556 LIFVETKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFLRDQYP 635
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15834617   646 IREN-DFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARGDKRGKLPRWIQEHLTDANLNL 708
Cdd:TIGR00604 636 IRENqDFYEFDAMRAVNQAIGRVIRHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDLNG 699
DEXDc2 smart00488
DEAD-like helicases superfamily;
8-280 2.58e-123

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 370.56  E-value: 2.58e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617      8 LLVYFPYDYiYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEV--TKLIYCSRTVPEIEKVIE 85
Cdd:smart00488   1 LLFYFPYEP-YPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSFPERIqkIKLIYLSRTVSEIEKRLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617     86 ELRKLL---------------NFYEKQEGEKLPFLGLALSSRKNLCIHPEV-TPLRFGKDVDGKCHSLTASYVRAQYQHD 149
Cdd:smart00488  80 ELRKLMqkveyesdeesekqaQLLHELGREKPKVLGLSLTSRKNLCLNPEVrTLKQNGLVVDEVCRSLTASKARKYRYEN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617    150 TSLPHCRFYEEFDAHGREVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELArKA 229
Cdd:smart00488 160 PKVERCPFYENTEFLLVRDLLPAEVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIRQALSIELK-DS 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 15834617    230 VVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQR 280
Cdd:smart00488 239 IVIFDEAHNLDNVCISALSSELSRRSLERAHKNIKKYFERIEKIRENDAKR 289
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
489-684 2.39e-80

C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases belonging to superfamily (SF)2. This family includes DDX11 (also called ChlR1), a protein involved in maintaining chromosome transmission fidelity and genome stability, the TFIIH basal transcription factor complex XPD subunit, and FANCJ (also known as BRIP1), a DNA helicase required for the maintenance of chromosomal stability. 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: 350175 [Multi-domain]  Cd Length: 159  Bit Score: 253.68  E-value: 2.39e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 489 CLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVAswyeqgileniqrnkllf 568
Cdd:cd18788   2 QVCPGIVGRGPDQQALNSKFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERVVS------------------ 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 569 ietqdgaetsvalekyqeacengRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKAR---LEYLRDQFQ 645
Cdd:cd18788  64 -----------------------RGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKmddLEYLRDKGL 120
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15834617 646 IRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRF 684
Cdd:cd18788 121 LTGEDWYTFQAMRAVNQAIGRAIRHKNDYGAIVLLDKRF 159
DEAHc_XPD cd17969
DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; ...
26-240 4.79e-69

DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; TFIIH can be resolved biochemically into a seven subunit core complex containing XPD/Rad3, XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and p8/Tfb5 and a three subunit Cdk Activating Kinase (CAK) complex containing CDK7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3. XPD interacts directly with p44, which stimulates XPD helicase activity. XPD/Rad3 also interacts directly with the CAK via its MAT1/Tfb3 subunit inhibiting the helicase activity of XPD. XPD is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350727 [Multi-domain]  Cd Length: 157  Bit Score: 223.85  E-value: 4.79e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  26 RELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLNFYEKQEGEKLPFL 105
Cdd:cd17969   1 LELKRTLDAKGHCVLEMPSGTGKTVSLLSLIVAYQKAYPLEVTKLIYCSRTVPEIEKVVEELRKLMDYYEKQTGEKPNFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 106 GLALSSRknlcihpevtplrfgkdvdgkchsltasyvraqyqhdtslphcrfyeefdahgrevplpagiynlddlkalgr 185
Cdd:cd17969  81 GLALSSR------------------------------------------------------------------------- 87
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15834617 186 rqgwcpyflarysilHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNID 240
Cdd:cd17969  88 ---------------HANVVVYSYHYLLDPKIAELVSKELSKKSVVVFDEAHNID 127
HELICc2 smart00491
helicase superfamily c-terminal domain;
542-686 3.05e-60

helicase superfamily c-terminal domain;


Pssm-ID: 214694 [Multi-domain]  Cd Length: 142  Bit Score: 199.81  E-value: 3.05e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617    542 YQYMESTVASWYEQGILEniqRNKLLFIETQDGAETSVALEKYQEACENGrGAILLSVARGKVSEGIDFVHHYGRAVIMF 621
Cdd:smart00491   1 YRYLEQVVEYWKENGILE---INKPVFIEGKDSGETEELLEKYSAACEAR-GALLLAVARGKVSEGIDFPDDLGRAVIIV 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15834617    622 GVPYVYTQSRILKARLEYLRDQFQIRENDF-LTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFAR 686
Cdd:smart00491  77 GIPFPNPDSPILRARLEYLDEKGGIRPFDEvYLFDAMRALAQAIGRAIRHKNDYGVVVLLDKRYAR 142
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
72-256 2.46e-55

DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases that are seemingly ubiquitous - members include proteins of eukaryotic, bacterial and archaeal origin. RAD3 is involved in nucleotide excision repair, and forms part of the transcription factor TFIIH in yeast.


Pssm-ID: 399602 [Multi-domain]  Cd Length: 168  Bit Score: 187.47  E-value: 2.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617    72 YCSRTVPEIEKVIEELRKLLNFYekqegeklPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQyqhdts 151
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYYK--------KIRGLILGSRKNLCINPEVLKLKKGNLVNERCRELVKSKARGS------ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   152 lphCRFY---EEFDAHGREvpLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELaRK 228
Cdd:pfam06733  67 ---CPFYnnlEDLLKLRDL--LGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINL-KN 140
                         170       180
                  ....*....|....*....|....*...
gi 15834617   229 AVVVFDEAHNIDNVCIDSMSVNLTRRTL 256
Cdd:pfam06733 141 SIVIFDEAHNIEDVCIESASFSISRSQL 168
HBB pfam06777
Helical and beta-bridge domain; HBB is the domain on DEAD-box eukaryotic DNA repair helicases ...
272-413 1.97e-49

Helical and beta-bridge domain; HBB is the domain on DEAD-box eukaryotic DNA repair helicases (EC:3.6.1.-) that appears to be a unique fold. It's conformation is of alpha-helices 12-16 plus a short beta-bridge to the FeS-cluster domain at the N-terminal. The full-length XPD protein verifies the presence of damage to DNA and allows DNA repair to proceed. XPD is an assembly of several domains to form a doughnut-shaped molecule that is able to separate two DNA strands and scan the DNA for damage. HBB helps to form the overall DNA-clamping architecture. This family represents a conserved region within a number of eukaryotic DNA repair helicases (EC:3.6.1.-).


Pssm-ID: 462008  Cd Length: 190  Bit Score: 172.18  E-value: 1.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   272 RIKETDEQRLRDEYRRLVEGLREASAARETDAHLAN-PVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVV 350
Cdd:pfam06777   4 EAKEYDEPKLQDEYSRLVEGLREAYEARLEDYVLSEvPVLPDEILEEAVPGNIRSAEHFLAFLKRLVEYGKARREVKIVK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   351 QESPPAFLSGLA--------------------------QRVCIQ-RKPLRFCAERLRSLLHTLEITDLADFSPLT----- 398
Cdd:pfam06777  84 SESPRSFLSHLGefllawlssdsedyvflvsreegpslEAVCIDpSKPLRFLAERLSSLLMSGTLTPLEDYSDLMgleak 163
                         170       180
                  ....*....|....*....|....*..
gi 15834617   399 ------------LLANFATLVSTYAKG 413
Cdd:pfam06777 164 lkkfpspfpkenLIVLFATLVSTYYKG 190
Helicase_C_2 pfam13307
Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases.
525-700 3.87e-43

Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases.


Pssm-ID: 463840 [Multi-domain]  Cd Length: 168  Bit Score: 153.49  E-value: 3.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   525 LEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQrnklLFIETQDGAETSVaLEKYQEAcenGRGAILLSVARGKV 604
Cdd:pfam13307   1 LRLLKVIPGGVLVFFPSYSYLEKVAERLKESGLEKGIE----IFVQPGEGSREKL-LEEFKKK---GKGAVLFGVCGGSF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617   605 SEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRF 684
Cdd:pfam13307  73 SEGIDFPGDLLRAVIIVGLPFPNPDDPVVEAKREYLDSKGGNPFNEWYLPQAVRAVNQAIGRLIRHENDYGAIVLLDSRF 152
                         170
                  ....*....|....*.
gi 15834617   685 ARGDKRGKLPRWIQEH 700
Cdd:pfam13307 153 LTKRYGKLLPKWLPPG 168
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
11-686 3.67e-41

Rad3-related DNA helicase DinG [Replication, recombination and repair];


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 160.09  E-value: 3.67e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  11 YFP-YDYiYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLL--ALIMAYQRAyplevTKLIYCSRTVPEIEKVIE-E 86
Cdd:COG1199   9 AFPgFEP-RPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAYLvpALLAARETG-----KKVVISTATKALQEQLVEkD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  87 LRKLlnfyekQEGEKLPFLGLALSSRKN-LCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHG 165
Cdd:COG1199  83 LPLL------RKALGLPLRVALLKGRSNyLCLRRLEQALQEGDDLDDEELLLARILAWASETWTGDRDELPLPEDDELWR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 166 RevplpagiYNLDDLKALGRRQGW---CPYFLARYSILHANVVVYSYHYLLdpkiADLVSKE--LARKAVVVFDEAHNID 240
Cdd:COG1199 157 Q--------VTSDADNCLGRRCPYygvCPYELARRLAREADVVVVNHHLLF----ADLALGEelLPEDDVLIIDEAHNLP 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 241 NVCIDSMSVNLTRRTLDRCQGNLETLQKTvLRIKETDE--QRLRDEYRRLVEGLREASAARETDAHLANPvlpDEVLQEA 318
Cdd:COG1199 225 DRARDMFSAELSSRSLLRLLRELRKLGLR-PGLKKLLDllERLREALDDLFLALEEEEELRLALGELPDE---PEELLEA 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 319 VpgsirtaEHFLGFLRRLLEYvkwrlrvqhvvqesppafLSGLAQRvciqRKPLRFCAERLRSLLHTLE-ITDLADFspl 397
Cdd:COG1199 301 L-------DALRDALEALAEA------------------LEEELER----LAELDALLERLEELLFALArFLRIAED--- 348
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 398 tllANFATLVSTYAKGFTiiiepfddrtptianpiLHFSCMDASLAIKP-VFERFQSVIITSGTLS---PLDIYPKI--L 471
Cdd:COG1199 349 ---EGYVRWLEREGGDVR-----------------LHAAPLDPADLLRElLFSRARSVVLTSATLSvggPFDYFARRlgL 408
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 472 DFHPVTMA---TFTM-TLARVCLCPMIigrgndqVAISSKFETREDIAvirnygNLLLEMSAVVPDGIVAFFTSYQYMES 547
Cdd:COG1199 409 DEDARTLSlpsPFDYeNQALLYVPRDL-------PRPSDRDGYLEAIA------EAIAELLEASGGNTLVLFTSYRALEQ 475
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 548 TVAswyeqgILENIQRNKLLFietQDGAETSVALEKYQEacenGRGAILlsVARGKVSEGIDFVHHYGRAVIMFGVPYVY 627
Cdd:COG1199 476 VAE------LLRERLDIPVLV---QGDGSREALLERFRE----GGNSVL--VGTGSFWEGVDLPGDALSLVIIVKLPFPP 540
                       650       660       670       680       690
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15834617 628 TQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFAR 686
Cdd:COG1199 541 PDDPVLEARREALEARGGNGFMYAYLPPAVIKLKQGAGRLIRSEEDRGVVVLLDRRLLT 599
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
35-257 8.31e-33

DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350673 [Multi-domain]  Cd Length: 138  Bit Score: 123.31  E-value: 8.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  35 KGHGVLEMPSGTGKTVSLLALIMAYQRAYPleVTKLIYCSRTVPEIEKVIEELRKLLNFyekqegekLPFLGLALSSRkn 114
Cdd:cd17915   1 GGHVALESPTGSGKTLSLLCSALSYQREFH--KTKVLYCSRTHSQIEQIIRELRKLLEK--------RKIRALALSSR-- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 115 lcihpevtplrfgkdvdgkchsltasyvraqyqhdtslphcrfyeefdahgrevplpagiynlddlkalgrrqgwcpyfl 194
Cdd:cd17915     --------------------------------------------------------------------------------
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15834617 195 arysilHANVVVYSYHYLLDPKIADLvSKELARKAVVVFDEAHNidnvcIDSMSVNLTRRTLD 257
Cdd:cd17915  69 ------DADIVVLPYPYLLDARIREF-IGIDLREQVVIIDEAHN-----LDERSVIITSGTLS 119
DEAHc_FancJ cd17970
DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi ...
35-239 2.47e-17

DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi anemia group J protein (FACJ or FANCJ, also known as BRIP1) is a DNA helicase required for the maintenance of chromosomal stability. It plays a role in the repair of DNA double-strand breaks by homologous recombination dependent on its interaction with BRCA1. FANCJ belongs to the DEAD-box helicase family, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350728 [Multi-domain]  Cd Length: 181  Bit Score: 80.47  E-value: 2.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  35 KGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVT-------------KLIYCSRTVPEIEKVIEELRKllNFYEKqegek 101
Cdd:cd17970   1 GQNALLESPTGTGKTLSLLCSTLAWRQSLKGKATsegsdgggsgkipKIIYASRTHSQLAQVVRELKR--TAYKR----- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617 102 lPFLGLaLSSRKNLCIHPeVTPLRFGKDVDGKCHSLtasyvraqyqhdtslphcrfyeeFDAHGrevplpagiynlddlk 181
Cdd:cd17970  74 -PRMTI-LGSRDHLCIHP-VINKLSNQNANEACMAL-----------------------LSGKN---------------- 111
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15834617 182 algrrqgwcpyflarysilHANVVVYSYHYLLDPKIADLVSKELaRKAVVVFDEAHNI 239
Cdd:cd17970 112 -------------------EADLVFCPYNYLLDPNIRRSMGLNL-KGSVVIFDEAHNI 149
DEAHc_XPD cd17969
DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; ...
451-480 5.82e-14

DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; TFIIH can be resolved biochemically into a seven subunit core complex containing XPD/Rad3, XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and p8/Tfb5 and a three subunit Cdk Activating Kinase (CAK) complex containing CDK7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3. XPD interacts directly with p44, which stimulates XPD helicase activity. XPD/Rad3 also interacts directly with the CAK via its MAT1/Tfb3 subunit inhibiting the helicase activity of XPD. XPD is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350727 [Multi-domain]  Cd Length: 157  Bit Score: 70.15  E-value: 5.82e-14
                        10        20        30
                ....*....|....*....|....*....|
gi 15834617 451 FQSVIITSGTLSPLDIYPKILDFHPVTMAT 480
Cdd:cd17969 128 FQSVVITSGTLSPLDMYPKILDFRPVTMAS 157
dinG PRK11747
ATP-dependent DNA helicase DinG; Provisional
190-683 2.22e-10

ATP-dependent DNA helicase DinG; Provisional


Pssm-ID: 236966 [Multi-domain]  Cd Length: 697  Bit Score: 64.08  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  190 CPYFLARYSILHANVVVYSyHYLLdpkIADLvskEL--------ARKAVVVFDEAHNIDNVCID----SMSVNLTRRTLD 257
Cdd:PRK11747 208 CPFFKARREIDEADVVVAN-HDLV---LADL---ELgggvvlpdPENLLYVLDEGHHLPDVARDhfaaSAELKGTADWLE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  258 RCQGNLETLQKTVLRIKETDEQRLRDeyrrLVEGLREA--SAARETDAHL-----------ANPVLPDEVLQEAvpgsIR 324
Cdd:PRK11747 281 KLLKLLTKLVALIMEPPLALPERLNA----HCEELRELlaSLNQILNLFLpaggeearyrfEMGELPEELLELA----ER 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  325 TAEHFLGfLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRV--CIQRkplrfcAERLRSLLHTLEITDLADFSPLtllan 402
Cdd:PRK11747 353 LAKLTEK-LLGLLEKLLNDLSEAMKTGKIDIVRLERLLLELgrALGR------LEALSKLWRLAAKEDQESGAPM----- 420
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  403 fatlvstyAKGFTiiIEPFDDRTPTIAN--PILHFSCMDASLaikpvFERFQSVIITSGTL------------------- 461
Cdd:PRK11747 421 --------ARWIT--REERDGQGDYLFHasPIRVGDQLERLL-----WSRAPGAVLTSATLrslnsfdrfqeqsglpekd 485
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  462 --------SPLD-------IYPKiLDFHPVTMATFTMTLARvclcpmiigrgndqvaisskfETREDIAVirNYGNLLLe 526
Cdd:PRK11747 486 gdrflalpSPFDypnqgklVIPK-MRAEPDNEEAHTAEMAE---------------------FLPELLEK--HKGSLVL- 540
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  527 msavvpdgivafFTSYQYMEsTVASwyeqgILENIQRNKLLfieTQDGAETSVALEKYQEACENGRGAILLSVarGKVSE 606
Cdd:PRK11747 541 ------------FASRRQMQ-KVAD-----LLPRDLRLMLL---VQGDQPRQRLLEKHKKRVDEGEGSVLFGL--QSFAE 597
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15834617  607 GIDFVHHYGRAVIM----FGVPyvytQSRILKARLEYLRDQfqiRENDFLTF---DAMRHAAQCVGRAIRGKTDYGLMVF 679
Cdd:PRK11747 598 GLDLPGDYLTQVIItkipFAVP----DSPVEATLAEWLKSR---GGNPFMEIsvpDASFKLIQAVGRLIRSEQDRGRVTI 670

                 ....
gi 15834617  680 ADKR 683
Cdd:PRK11747 671 LDRR 674
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
451-480 1.18e-06

DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members are DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350673 [Multi-domain]  Cd Length: 138  Bit Score: 48.58  E-value: 1.18e-06
                        10        20        30
                ....*....|....*....|....*....|.
gi 15834617 451 FQSVIITSGTLSPLDIYPKILD-FHPVTMAT 480
Cdd:cd17915 108 ERSVIITSGTLSPLDIYSKILGiRNMLVLAV 138
DEAHc_DDX11_starthere cd17968
DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) ...
38-89 1.73e-04

DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) encodes a protein of the conserved family of Iron-Sulfur (Fe-S) cluster DNA helicases and is thought to function in maintaining chromosome transmission fidelity and genome stability. Mutations in the Chl1 human homologs ChlR1/DDX11 and BACH1/BRIP1/FANCJ collectively result in Warsaw Breakage Syndrome, Fanconi anemia, cell aneuploidy and breast and ovarian cancers. DDX11 is a member of the DEAD-box helicases, 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. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350726  Cd Length: 134  Bit Score: 42.31  E-value: 1.73e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15834617  38 GVLEMPSGTGKTVSLLALIMAYqraypleVTKLIYCSRTVPEIEKVIEELRK 89
Cdd:cd17968   4 GIFESPTGTGKSLSLICGALTW-------LTKIYYCSRTHSQLAQFVHEVQK 48
 
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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