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Conserved domains on  [gi|820948158|ref|NP_957220|]
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general transcription and DNA repair factor IIH helicase subunit XPD [Danio rerio]

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: 1022.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158    7 GLLVYFPYDYIYPEQYSYMLELKRTLDAKGHGVLEMPSGTGKTISLLSLIVAYQKTYPlEVTKLVYCSRTVPEIEKVVEE 86
Cdd:TIGR00604   1 ELLVYFPYEKIYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKP-EVRKIIYASRTHSQLEQATEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158   87 LRKLMDYYSKQTGVKNDFLALALSSRKNLCIHPEVSSLRFGKEVDGKCHSLTASYIRAQHQSNPNQPVCQFYEEFDNV-G 165
Cdd:TIGR00604  80 LRKLMSYRTPRIGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGKCIKLTVSKIKEQRTEKPNVESCEFYENFDELrE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  166 RQVPIPPGIYNLDDLKDFGRRKGWCPYFLARYALLHANIVVYSYHYLLDPKIADLVSKELaKKSVVVFDEAHNIDNVCID 245
Cdd:TIGR00604 160 VEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSIEL-KDSIVIFDEAHNLDNVCIS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  246 SMSVNITRRTLDRCQTNVETLQNTISRIKETDAAKLREEYRRLVEGLKEANVARETDIYLSNPVLPDEILQEAVPGSIRT 325
Cdd:TIGR00604 239 SLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDARKLLDELQKLVEGLKQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  326 AEHFVGFMKRFLEYLKARLRIHHVVQESAPQFLKDIFEKVCIDRkPLRFCAERLRSLLRTLEIADIADFSPITLISHFAT 405
Cdd:TIGR00604 319 AEIFLHKLSRYLEYLKDALKVLGVVSELPDAFLEHLKEKTFIDR-PLRFCSERLSNLLRELEITHPEDFSALVLLFTFAT 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  406 LVSTYSKGFTIIIEPFEDKTptIANPVLHFSCMDPSIAIKPVFGRFQTVIITSGTLSPLDIYPRILDFRPVTMASFTMTL 485
Cdd:TIGR00604 398 LVLTYTNGFLEGIEPYENKT--VPNPILKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHIL 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  486 ARTCLCPLIVGRGNDQVAMTSKFETREDFAVIRNYGNLLLEMSAIVPDGIVAFFTSYMYMENIVASWYEQGILENIQRNK 565
Cdd:TIGR00604 476 KRENLLTLIVTRGSDQVPLSSTFEIRNDPSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  566 LIFIETQDAAETSMALEKYQEACENGRGAILLSVARGKVSEGIDFVHHFGRAVIMFGVPYVYTQSRILKARLEYLRDQFQ 645
Cdd:TIGR00604 556 LIFVETKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFLRDQYP 635
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820948158  646 IREN-DFLTFDAMRHAAQCVGRAIRGKTDYGLMIFADKRYARADKRGKLPRWIQEHLTDGSLNL 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: 1022.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158    7 GLLVYFPYDYIYPEQYSYMLELKRTLDAKGHGVLEMPSGTGKTISLLSLIVAYQKTYPlEVTKLVYCSRTVPEIEKVVEE 86
Cdd:TIGR00604   1 ELLVYFPYEKIYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKP-EVRKIIYASRTHSQLEQATEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158   87 LRKLMDYYSKQTGVKNDFLALALSSRKNLCIHPEVSSLRFGKEVDGKCHSLTASYIRAQHQSNPNQPVCQFYEEFDNV-G 165
Cdd:TIGR00604  80 LRKLMSYRTPRIGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGKCIKLTVSKIKEQRTEKPNVESCEFYENFDELrE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  166 RQVPIPPGIYNLDDLKDFGRRKGWCPYFLARYALLHANIVVYSYHYLLDPKIADLVSKELaKKSVVVFDEAHNIDNVCID 245
Cdd:TIGR00604 160 VEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSIEL-KDSIVIFDEAHNLDNVCIS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  246 SMSVNITRRTLDRCQTNVETLQNTISRIKETDAAKLREEYRRLVEGLKEANVARETDIYLSNPVLPDEILQEAVPGSIRT 325
Cdd:TIGR00604 239 SLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDARKLLDELQKLVEGLKQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  326 AEHFVGFMKRFLEYLKARLRIHHVVQESAPQFLKDIFEKVCIDRkPLRFCAERLRSLLRTLEIADIADFSPITLISHFAT 405
Cdd:TIGR00604 319 AEIFLHKLSRYLEYLKDALKVLGVVSELPDAFLEHLKEKTFIDR-PLRFCSERLSNLLRELEITHPEDFSALVLLFTFAT 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  406 LVSTYSKGFTIIIEPFEDKTptIANPVLHFSCMDPSIAIKPVFGRFQTVIITSGTLSPLDIYPRILDFRPVTMASFTMTL 485
Cdd:TIGR00604 398 LVLTYTNGFLEGIEPYENKT--VPNPILKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHIL 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  486 ARTCLCPLIVGRGNDQVAMTSKFETREDFAVIRNYGNLLLEMSAIVPDGIVAFFTSYMYMENIVASWYEQGILENIQRNK 565
Cdd:TIGR00604 476 KRENLLTLIVTRGSDQVPLSSTFEIRNDPSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  566 LIFIETQDAAETSMALEKYQEACENGRGAILLSVARGKVSEGIDFVHHFGRAVIMFGVPYVYTQSRILKARLEYLRDQFQ 645
Cdd:TIGR00604 556 LIFVETKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFLRDQYP 635
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820948158  646 IREN-DFLTFDAMRHAAQCVGRAIRGKTDYGLMIFADKRYARADKRGKLPRWIQEHLTDGSLNL 708
Cdd:TIGR00604 636 IRENqDFYEFDAMRAVNQAIGRVIRHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDLNG 699
DEXDc2 smart00488
DEAD-like helicases superfamily;
8-278 2.36e-115

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 350.14  E-value: 2.36e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158     8 LLVYFPYDYiYPEQYSYMLELKRTLDAKGHGVLEMPSGTGKTISLLSLIVAYQKTYPLEV--TKLVYCSRTVPEIEKVVE 85
Cdd:smart00488   1 LLFYFPYEP-YPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSFPERIqkIKLIYLSRTVSEIEKRLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158    86 ELRKLMDY---------------YSKQTGVKNDFLALALSSRKNLCIHPEVSSL-RFGKEVDGKCHSLTASYIRAQHQSN 149
Cdd:smart00488  80 ELRKLMQKveyesdeesekqaqlLHELGREKPKVLGLSLTSRKNLCLNPEVRTLkQNGLVVDEVCRSLTASKARKYRYEN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158   150 PNQPVCQFYEEFDNVGRQVPIPPGIYNLDDLKDFGRRKGWCPYFLARYALLHANIVVYSYHYLLDPKIADLVSKELaKKS 229
Cdd:smart00488 160 PKVERCPFYENTEFLLVRDLLPAEVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIRQALSIEL-KDS 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 820948158   230 VVVFDEAHNIDNVCIDSMSVNITRRTLDRCQTNVETLQNTISRIKETDA 278
Cdd:smart00488 239 IVIFDEAHNLDNVCISALSSELSRRSLERAHKNIKKYFERIEKIRENDA 287
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
489-684 1.50e-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: 254.45  E-value: 1.50e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 489 CLCPLIVGRGNDQVAMTSKFETREDFAVIRNYGNLLLEMSAIVPDGIVAFFTSYMYMENIVAswyeqgileniqrnklif 568
Cdd:cd18788    2 QVCPGIVGRGPDQQALNSKFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERVVS------------------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 569 ietqdaaetsmalekyqeacengRGAILLSVARGKVSEGIDFVHHFGRAVIMFGVPYVYTQSRILKAR---LEYLRDQFQ 645
Cdd:cd18788   64 -----------------------RGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKmddLEYLRDKGL 120
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 820948158 646 IRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMIFADKRY 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 2.65e-59

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: 198.26  E-value: 2.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158   72 YCSRTVPEIEKVVEELRKLMDYYskqtgvknDFLALALSSRKNLCIHPEVSSLRFGKEVDGKCHSLTASYIRAQhqsnpn 151
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYYK--------KIRGLILGSRKNLCINPEVLKLKKGNLVNERCRELVKSKARGS------ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  152 qpvCQFYEEFDNVGRQVP-IPPGIYNLDDLKDFGRRKGWCPYFLARYALLHANIVVYSYHYLLDPKIADLVSKELaKKSV 230
Cdd:pfam06733  67 ---CPFYNNLEDLLKLRDlLGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINL-KNSI 142
                         170       180
                  ....*....|....*....|....*.
gi 820948158  231 VVFDEAHNIDNVCIDSMSVNITRRTL 256
Cdd:pfam06733 143 VIFDEAHNIEDVCIESASFSISRSQL 168
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
11-687 3.50e-40

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 157.01  E-value: 3.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  11 YFP-YDYiYPEQYSYMLELKRTLDAKGHGVLEMPSGTGKTIS-LLSLIVAYQKTYplevTKLVYCSRTVPEIEKVVE-EL 87
Cdd:COG1199    9 AFPgFEP-RPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAyLVPALLAARETG----KKVVISTATKALQEQLVEkDL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  88 RKLmdyySKQTGVknDFLALALSSRKN-LCIHPEVSSLRFGKEVDGKCHSLTASYIRAQHQSNPNQPVCQFYEEfDNVGR 166
Cdd:COG1199   84 PLL----RKALGL--PLRVALLKGRSNyLCLRRLEQALQEGDDLDDEELLLARILAWASETWTGDRDELPLPED-DELWR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 167 QVPIPPGIYNLDDLKDFGRrkgwCPYFLARYALLHANIVVYSYHYLLdpkiADLVSKE--LAKKSVVVFDEAHNIDNVCI 244
Cdd:COG1199  157 QVTSDADNCLGRRCPYYGV----CPYELARRLAREADVVVVNHHLLF----ADLALGEelLPEDDVLIIDEAHNLPDRAR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 245 DSMSVNITRRTLDRCQTNVETLQNTISRIKETDAA-KLREEYRRLVEGLKEANVARETDIYLsnPVLPDEILQEavpgsi 323
Cdd:COG1199  229 DMFSAELSSRSLLRLLRELRKLGLRPGLKKLLDLLeRLREALDDLFLALEEEEELRLALGEL--PDEPEELLEA------ 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 324 rtaehfvgfMKRFLEYLKArlrihhvvqesapqfLKDIFEKVCIDRKPLRFCAERLRSLLRTLE-IADIADfspitlISH 402
Cdd:COG1199  301 ---------LDALRDALEA---------------LAEALEEELERLAELDALLERLEELLFALArFLRIAE------DEG 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 403 FATLVSTYSKGFTiiiepfedktptianpvLHFSCMDPSIAIKP-VFGRFQTVIITSGTLS---PLDIYPRI--LDFRPV 476
Cdd:COG1199  351 YVRWLEREGGDVR-----------------LHAAPLDPADLLRElLFSRARSVVLTSATLSvggPFDYFARRlgLDEDAR 413
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 477 TMA---SFTM-TLARtclcpLIVGRgndqvaMTSKFETREDFavIRNYGNLLLEMSAIVPDGIVAFFTSYMYMENIVAsw 552
Cdd:COG1199  414 TLSlpsPFDYeNQAL-----LYVPR------DLPRPSDRDGY--LEAIAEAIAELLEASGGNTLVLFTSYRALEQVAE-- 478
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 553 yeqgILENIQRNKLIFietQDAAETSMALEKYQEacenGRGAILlsVARGKVSEGIDFVHHFGRAVIMFGVPYVYTQSRI 632
Cdd:COG1199  479 ----LLRERLDIPVLV---QGDGSREALLERFRE----GGNSVL--VGTGSFWEGVDLPGDALSLVIIVKLPFPPPDDPV 545
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 820948158 633 LKARLEYLRDQFQireNDFLTF---DAMRHAAQCVGRAIRGKTDYGLMIFADKRYARA 687
Cdd:COG1199  546 LEARREALEARGG---NGFMYAylpPAVIKLKQGAGRLIRSEEDRGVVVLLDRRLLTK 600
dinG PRK11747
ATP-dependent DNA helicase DinG; Provisional
190-345 9.74e-08

ATP-dependent DNA helicase DinG; Provisional


Pssm-ID: 236966 [Multi-domain]  Cd Length: 697  Bit Score: 55.60  E-value: 9.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 190 CPYFLARYALLHANIVVYSyHYLLdpkIADLvskEL--------AKKSVVVFDEAHNIDNVCID----SMSVNITRRTLD 257
Cdd:PRK11747 208 CPFFKARREIDEADVVVAN-HDLV---LADL---ELgggvvlpdPENLLYVLDEGHHLPDVARDhfaaSAELKGTADWLE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 258 RCQTNVETLQNTISRIKE---TDAAKLREEYRRLVEGLKE-----ANVARETDIYL-SNPVLPDEILQEAvpgsIRTAEH 328
Cdd:PRK11747 281 KLLKLLTKLVALIMEPPLalpERLNAHCEELRELLASLNQilnlfLPAGGEEARYRfEMGELPEELLELA----ERLAKL 356
                        170
                 ....*....|....*..
gi 820948158 329 FVGFMKRFlEYLKARLR 345
Cdd:PRK11747 357 TEKLLGLL-EKLLNDLS 372
 
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: 1022.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158    7 GLLVYFPYDYIYPEQYSYMLELKRTLDAKGHGVLEMPSGTGKTISLLSLIVAYQKTYPlEVTKLVYCSRTVPEIEKVVEE 86
Cdd:TIGR00604   1 ELLVYFPYEKIYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEKP-EVRKIIYASRTHSQLEQATEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158   87 LRKLMDYYSKQTGVKNDFLALALSSRKNLCIHPEVSSLRFGKEVDGKCHSLTASYIRAQHQSNPNQPVCQFYEEFDNV-G 165
Cdd:TIGR00604  80 LRKLMSYRTPRIGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGKCIKLTVSKIKEQRTEKPNVESCEFYENFDELrE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  166 RQVPIPPGIYNLDDLKDFGRRKGWCPYFLARYALLHANIVVYSYHYLLDPKIADLVSKELaKKSVVVFDEAHNIDNVCID 245
Cdd:TIGR00604 160 VEDLLLSEIMDIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSIEL-KDSIVIFDEAHNLDNVCIS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  246 SMSVNITRRTLDRCQTNVETLQNTISRIKETDAAKLREEYRRLVEGLKEANVARETDIYLSNPVLPDEILQEAVPGSIRT 325
Cdd:TIGR00604 239 SLSSNLSVRSLKRCSKEIAEYFEKIEERKEVDARKLLDELQKLVEGLKQEDLLTDEDIFLANPVLPKEVLPEAVPGNIRI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  326 AEHFVGFMKRFLEYLKARLRIHHVVQESAPQFLKDIFEKVCIDRkPLRFCAERLRSLLRTLEIADIADFSPITLISHFAT 405
Cdd:TIGR00604 319 AEIFLHKLSRYLEYLKDALKVLGVVSELPDAFLEHLKEKTFIDR-PLRFCSERLSNLLRELEITHPEDFSALVLLFTFAT 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  406 LVSTYSKGFTIIIEPFEDKTptIANPVLHFSCMDPSIAIKPVFGRFQTVIITSGTLSPLDIYPRILDFRPVTMASFTMTL 485
Cdd:TIGR00604 398 LVLTYTNGFLEGIEPYENKT--VPNPILKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHIL 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  486 ARTCLCPLIVGRGNDQVAMTSKFETREDFAVIRNYGNLLLEMSAIVPDGIVAFFTSYMYMENIVASWYEQGILENIQRNK 565
Cdd:TIGR00604 476 KRENLLTLIVTRGSDQVPLSSTFEIRNDPSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEKKK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  566 LIFIETQDAAETSMALEKYQEACENGRGAILLSVARGKVSEGIDFVHHFGRAVIMFGVPYVYTQSRILKARLEYLRDQFQ 645
Cdd:TIGR00604 556 LIFVETKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEFLRDQYP 635
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820948158  646 IREN-DFLTFDAMRHAAQCVGRAIRGKTDYGLMIFADKRYARADKRGKLPRWIQEHLTDGSLNL 708
Cdd:TIGR00604 636 IRENqDFYEFDAMRAVNQAIGRVIRHKDDYGSIVLLDKRYARSNKRKKLPKWIQDTIQSSDLNG 699
DEXDc2 smart00488
DEAD-like helicases superfamily;
8-278 2.36e-115

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 350.14  E-value: 2.36e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158     8 LLVYFPYDYiYPEQYSYMLELKRTLDAKGHGVLEMPSGTGKTISLLSLIVAYQKTYPLEV--TKLVYCSRTVPEIEKVVE 85
Cdd:smart00488   1 LLFYFPYEP-YPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSFPERIqkIKLIYLSRTVSEIEKRLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158    86 ELRKLMDY---------------YSKQTGVKNDFLALALSSRKNLCIHPEVSSL-RFGKEVDGKCHSLTASYIRAQHQSN 149
Cdd:smart00488  80 ELRKLMQKveyesdeesekqaqlLHELGREKPKVLGLSLTSRKNLCLNPEVRTLkQNGLVVDEVCRSLTASKARKYRYEN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158   150 PNQPVCQFYEEFDNVGRQVPIPPGIYNLDDLKDFGRRKGWCPYFLARYALLHANIVVYSYHYLLDPKIADLVSKELaKKS 229
Cdd:smart00488 160 PKVERCPFYENTEFLLVRDLLPAEVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIRQALSIEL-KDS 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 820948158   230 VVVFDEAHNIDNVCIDSMSVNITRRTLDRCQTNVETLQNTISRIKETDA 278
Cdd:smart00488 239 IVIFDEAHNLDNVCISALSSELSRRSLERAHKNIKKYFERIEKIRENDA 287
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
489-684 1.50e-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: 254.45  E-value: 1.50e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 489 CLCPLIVGRGNDQVAMTSKFETREDFAVIRNYGNLLLEMSAIVPDGIVAFFTSYMYMENIVAswyeqgileniqrnklif 568
Cdd:cd18788    2 QVCPGIVGRGPDQQALNSKFQTREDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERVVS------------------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 569 ietqdaaetsmalekyqeacengRGAILLSVARGKVSEGIDFVHHFGRAVIMFGVPYVYTQSRILKAR---LEYLRDQFQ 645
Cdd:cd18788   64 -----------------------RGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKmddLEYLRDKGL 120
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 820948158 646 IRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMIFADKRY 684
Cdd:cd18788  121 LTGEDWYTFQAMRAVNQAIGRAIRHKNDYGAIVLLDKRF 159
DEAHc_XPD cd17969
DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; ...
26-256 1.62e-70

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: 227.70  E-value: 1.62e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  26 LELKRTLDAKGHGVLEMPSGTGKTISLLSLIVAYQKTYPLEVTKLVYCSRTVPEIEKVVEELRKLMDYYSKQTGVKNDFL 105
Cdd:cd17969    1 LELKRTLDAKGHCVLEMPSGTGKTVSLLSLIVAYQKAYPLEVTKLIYCSRTVPEIEKVVEELRKLMDYYEKQTGEKPNFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 106 ALALSSRknlcihpevsslrfgkevdgkchsltasyiraqhqsnpnqpvcqfyeefdnvgrqvpippgiynlddlkdfgr 185
Cdd:cd17969   81 GLALSSR------------------------------------------------------------------------- 87
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820948158 186 rkgwcpyflaryallHANIVVYSYHYLLDPKIADLVSKELAKKSVVVFDEAHNidnvcIDSMSVNITRRTL 256
Cdd:cd17969   88 ---------------HANVVVYSYHYLLDPKIAELVSKELSKKSVVVFDEAHN-----IDFQSVVITSGTL 138
HELICc2 smart00491
helicase superfamily c-terminal domain;
542-686 1.79e-60

helicase superfamily c-terminal domain;


Pssm-ID: 214694 [Multi-domain]  Cd Length: 142  Bit Score: 200.20  E-value: 1.79e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158   542 YMYMENIVASWYEQGILEniqRNKLIFIETQDAAETSMALEKYQEACENGrGAILLSVARGKVSEGIDFVHHFGRAVIMF 621
Cdd:smart00491   1 YRYLEQVVEYWKENGILE---INKPVFIEGKDSGETEELLEKYSAACEAR-GALLLAVARGKVSEGIDFPDDLGRAVIIV 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820948158   622 GVPYVYTQSRILKARLEYLRDQFQIRENDF-LTFDAMRHAAQCVGRAIRGKTDYGLMIFADKRYAR 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 2.65e-59

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: 198.26  E-value: 2.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158   72 YCSRTVPEIEKVVEELRKLMDYYskqtgvknDFLALALSSRKNLCIHPEVSSLRFGKEVDGKCHSLTASYIRAQhqsnpn 151
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYYK--------KIRGLILGSRKNLCINPEVLKLKKGNLVNERCRELVKSKARGS------ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  152 qpvCQFYEEFDNVGRQVP-IPPGIYNLDDLKDFGRRKGWCPYFLARYALLHANIVVYSYHYLLDPKIADLVSKELaKKSV 230
Cdd:pfam06733  67 ---CPFYNNLEDLLKLRDlLGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINL-KNSI 142
                         170       180
                  ....*....|....*....|....*.
gi 820948158  231 VVFDEAHNIDNVCIDSMSVNITRRTL 256
Cdd:pfam06733 143 VIFDEAHNIEDVCIESASFSISRSQL 168
HBB pfam06777
Helical and beta-bridge domain; HBB is the domain on DEAD-box eukaryotic DNA repair helicases ...
270-413 1.33e-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: 172.56  E-value: 1.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  270 ISRIKETDAAKLREEYRRLVEGLKEANVARETDIYLSN-PVLPDEILQEAVPGSIRTAEHFVGFMKRFLEYLKARLRIHH 348
Cdd:pfam06777   2 IDEAKEYDEPKLQDEYSRLVEGLREAYEARLEDYVLSEvPVLPDEILEEAVPGNIRSAEHFLAFLKRLVEYGKARREVKI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  349 VVQESAPQFLKDI--------------------------FEKVCID-RKPLRFCAERLRSLLRTLEIADIADFSPIT--- 398
Cdd:pfam06777  82 VKSESPRSFLSHLgefllawlssdsedyvflvsreegpsLEAVCIDpSKPLRFLAERLSSLLMSGTLTPLEDYSDLMgle 161
                         170       180
                  ....*....|....*....|....*....
gi 820948158  399 --------------LISHFATLVSTYSKG 413
Cdd:pfam06777 162 aklkkfpspfpkenLIVLFATLVSTYYKG 190
Helicase_C_2 pfam13307
Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases.
525-700 1.29e-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: 155.03  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  525 LEMSAIVPDGIVAFFTSYMYMENIVASWYEQGILENIQrnklIFIEtQDAAETSMALEKYQEAcenGRGAILLSVARGKV 604
Cdd:pfam13307   1 LRLLKVIPGGVLVFFPSYSYLEKVAERLKESGLEKGIE----IFVQ-PGEGSREKLLEEFKKK---GKGAVLFGVCGGSF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  605 SEGIDFVHHFGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMIFADKRY 684
Cdd:pfam13307  73 SEGIDFPGDLLRAVIIVGLPFPNPDDPVVEAKREYLDSKGGNPFNEWYLPQAVRAVNQAIGRLIRHENDYGAIVLLDSRF 152
                         170
                  ....*....|....*.
gi 820948158  685 ARADKRGKLPRWIQEH 700
Cdd:pfam13307 153 LTKRYGKLLPKWLPPG 168
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
11-687 3.50e-40

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 157.01  E-value: 3.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  11 YFP-YDYiYPEQYSYMLELKRTLDAKGHGVLEMPSGTGKTIS-LLSLIVAYQKTYplevTKLVYCSRTVPEIEKVVE-EL 87
Cdd:COG1199    9 AFPgFEP-RPGQREMAEAVARALAEGRHLLIEAGTGTGKTLAyLVPALLAARETG----KKVVISTATKALQEQLVEkDL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  88 RKLmdyySKQTGVknDFLALALSSRKN-LCIHPEVSSLRFGKEVDGKCHSLTASYIRAQHQSNPNQPVCQFYEEfDNVGR 166
Cdd:COG1199   84 PLL----RKALGL--PLRVALLKGRSNyLCLRRLEQALQEGDDLDDEELLLARILAWASETWTGDRDELPLPED-DELWR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 167 QVPIPPGIYNLDDLKDFGRrkgwCPYFLARYALLHANIVVYSYHYLLdpkiADLVSKE--LAKKSVVVFDEAHNIDNVCI 244
Cdd:COG1199  157 QVTSDADNCLGRRCPYYGV----CPYELARRLAREADVVVVNHHLLF----ADLALGEelLPEDDVLIIDEAHNLPDRAR 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 245 DSMSVNITRRTLDRCQTNVETLQNTISRIKETDAA-KLREEYRRLVEGLKEANVARETDIYLsnPVLPDEILQEavpgsi 323
Cdd:COG1199  229 DMFSAELSSRSLLRLLRELRKLGLRPGLKKLLDLLeRLREALDDLFLALEEEEELRLALGEL--PDEPEELLEA------ 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 324 rtaehfvgfMKRFLEYLKArlrihhvvqesapqfLKDIFEKVCIDRKPLRFCAERLRSLLRTLE-IADIADfspitlISH 402
Cdd:COG1199  301 ---------LDALRDALEA---------------LAEALEEELERLAELDALLERLEELLFALArFLRIAE------DEG 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 403 FATLVSTYSKGFTiiiepfedktptianpvLHFSCMDPSIAIKP-VFGRFQTVIITSGTLS---PLDIYPRI--LDFRPV 476
Cdd:COG1199  351 YVRWLEREGGDVR-----------------LHAAPLDPADLLRElLFSRARSVVLTSATLSvggPFDYFARRlgLDEDAR 413
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 477 TMA---SFTM-TLARtclcpLIVGRgndqvaMTSKFETREDFavIRNYGNLLLEMSAIVPDGIVAFFTSYMYMENIVAsw 552
Cdd:COG1199  414 TLSlpsPFDYeNQAL-----LYVPR------DLPRPSDRDGY--LEAIAEAIAELLEASGGNTLVLFTSYRALEQVAE-- 478
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 553 yeqgILENIQRNKLIFietQDAAETSMALEKYQEacenGRGAILlsVARGKVSEGIDFVHHFGRAVIMFGVPYVYTQSRI 632
Cdd:COG1199  479 ----LLRERLDIPVLV---QGDGSREALLERFRE----GGNSVL--VGTGSFWEGVDLPGDALSLVIIVKLPFPPPDDPV 545
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 820948158 633 LKARLEYLRDQFQireNDFLTF---DAMRHAAQCVGRAIRGKTDYGLMIFADKRYARA 687
Cdd:COG1199  546 LEARREALEARGG---NGFMYAylpPAVIKLKQGAGRLIRSEEDRGVVVLLDRRLLTK 600
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
35-257 6.14e-29

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: 112.52  E-value: 6.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  35 KGHGVLEMPSGTGKTISLLSLIVAYQKTYPleVTKLVYCSRTVPEIEKVVEELRKLMDYyskqtgvkNDFLALALSSRkn 114
Cdd:cd17915    1 GGHVALESPTGSGKTLSLLCSALSYQREFH--KTKVLYCSRTHSQIEQIIRELRKLLEK--------RKIRALALSSR-- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 115 lcihpevsslrfgkevdgkchsltasyiraqhqsnpnqpvcqfyeefdnvgrqvpippgiynlddlkdfgrrkgwcpyfl 194
Cdd:cd17915      --------------------------------------------------------------------------------
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820948158 195 aryallHANIVVYSYHYLLDPKIADLvSKELAKKSVVVFDEAHNidnvcIDSMSVNITRRTLD 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 3.64e-20

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: 88.56  E-value: 3.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158  35 KGHGVLEMPSGTGKTISLLSLIVAYQKTYPLEVT-------------KLVYCSRTVPEIEKVVEELRKLMdYYSKQTGVk 101
Cdd:cd17970    1 GQNALLESPTGTGKTLSLLCSTLAWRQSLKGKATsegsdgggsgkipKIIYASRTHSQLAQVVRELKRTA-YKRPRMTI- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 102 ndflalaLSSRKNLCIHPeVSSLRFGKEVDGKCHSLTAsyiraqhqsnpnqpvcqfyeefdnvGRQvpippgiynlddlk 181
Cdd:cd17970   79 -------LGSRDHLCIHP-VINKLSNQNANEACMALLS-------------------------GKN-------------- 111
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 820948158 182 dfgrrkgwcpyflaryallHANIVVYSYHYLLDPKIADLVSKELaKKSVVVFDEAHNI 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 1.08e-13

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: 69.38  E-value: 1.08e-13
                         10        20        30
                 ....*....|....*....|....*....|
gi 820948158 451 FQTVIITSGTLSPLDIYPRILDFRPVTMAS 480
Cdd:cd17969  128 FQSVVITSGTLSPLDMYPKILDFRPVTMAS 157
dinG PRK11747
ATP-dependent DNA helicase DinG; Provisional
190-345 9.74e-08

ATP-dependent DNA helicase DinG; Provisional


Pssm-ID: 236966 [Multi-domain]  Cd Length: 697  Bit Score: 55.60  E-value: 9.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 190 CPYFLARYALLHANIVVYSyHYLLdpkIADLvskEL--------AKKSVVVFDEAHNIDNVCID----SMSVNITRRTLD 257
Cdd:PRK11747 208 CPFFKARREIDEADVVVAN-HDLV---LADL---ELgggvvlpdPENLLYVLDEGHHLPDVARDhfaaSAELKGTADWLE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820948158 258 RCQTNVETLQNTISRIKE---TDAAKLREEYRRLVEGLKE-----ANVARETDIYL-SNPVLPDEILQEAvpgsIRTAEH 328
Cdd:PRK11747 281 KLLKLLTKLVALIMEPPLalpERLNAHCEELRELLASLNQilnlfLPAGGEEARYRfEMGELPEELLELA----ERLAKL 356
                        170
                 ....*....|....*..
gi 820948158 329 FVGFMKRFlEYLKARLR 345
Cdd:PRK11747 357 TEKLLGLL-EKLLNDLS 372
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
451-475 1.42e-05

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: 45.50  E-value: 1.42e-05
                         10        20
                 ....*....|....*....|....*
gi 820948158 451 FQTVIITSGTLSPLDIYPRILDFRP 475
Cdd:cd17915  108 ERSVIITSGTLSPLDIYSKILGIRN 132
DEAHc_DDX11_starthere cd17968
DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) ...
38-89 1.19e-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: 42.69  E-value: 1.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 820948158  38 GVLEMPSGTGKTISLLSLIVAYqktypleVTKLVYCSRTVPEIEKVVEELRK 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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