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Conserved domains on  [gi|1231988176|gb|OYT49580|]
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hypothetical protein B6U79_01510 [Candidatus Bathyarchaeota archaeon ex4484_231]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1003081)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to human ATP-dependent DNA helicase DDX11

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rad3 super family cl36704
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
59-651 2.71e-109

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]


The actual alignment was detected with superfamily member TIGR00604:

Pssm-ID: 273169 [Multi-domain]  Cd Length: 705  Bit Score: 345.55  E-value: 2.71e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  59 LRLFPYEP-YPQQLKFMKDAETVLDKGGVLVAEACNGFGKTVCALSSALATGRR------IIYATRTHEQVRQVLREIEQ 131
Cdd:TIGR00604   3 LVYFPYEKiYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEkpevrkIIYASRTHSQLEQATEELRK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 132 INK------KAGTDFSAVALASRQNLCLNQICRSLPQTEAVEA-CRVLRNS------------RRCPY------KSQFSF 186
Cdd:TIGR00604  83 LMSyrtpriGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGkCIKLTVSkikeqrtekpnvESCEFyenfdeLREVED 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 187 LGSSLPPvlSTRRLLNYGRTKGICPYYLSRKISQDCTVVVAPYQYIFNESIRATVGLDINGKVLVFDEAHNADKIGQEVL 266
Cdd:TIGR00604 163 LLLSEIM--DIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSIELKDSIVIFDEAHNLDNVCISSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 267 SDTLSERGLDNAVRELE---------------------------------------------------------LVGVPS 289
Cdd:TIGR00604 241 SSNLSVRSLKRCSKEIAeyfekieerkevdarklldelqklveglkqedlltdediflanpvlpkevlpeavpgNIRIAE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 290 VFIGKLTDYLEKT---------VREEPvvKPGSQLFKDLTEVLGEdLSFIVESFKpmvDEIREKRISRGEVPVCYLNGLL 360
Cdd:TIGR00604 321 IFLHKLSRYLEYLkdalkvlgvVSELP--DAFLEHLKEKTFIDRP-LRFCSERLS---NLLRELEITHPEDFSALVLLFT 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 361 NFLLLVDSSEKESYVAIYRKSASGLNLV-EYRCLDPSLAIKPVIEEAHAALIMSGTLSPLDLFTEVLGLSEAETRTYSAI 439
Cdd:TIGR00604 395 FATLVLTYTNGFLEGIEPYENKTVPNPIlKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHI 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 440 AKPENVRTYV------DISVTTKFQERSA-DMLKLYGERISKLAKNVPNGVLIFFPQRRLMNEAVAIWRRNGFIRRRGRr 512
Cdd:TIGR00604 475 LKRENLLTLIvtrgsdQVPLSSTFEIRNDpSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEK- 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 513 lflgKKIVFVEGTRATENARIVDEYKKAARTDQGAVLFAVFRGRNAEGSNFPYEEARGVFNVGLPYADYHDPLVKAQIGF 592
Cdd:TIGR00604 554 ----KKLIFVETKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEF 629
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231988176 593 FNRKKS-RLGELWYLMDAFRAANQAMGRGIRHRDDWCRFYLMDRRYATHWK--FISKWAVEN 651
Cdd:TIGR00604 630 LRDQYPiRENQDFYEFDAMRAVNQAIGRVIRHKDDYGSIVLLDKRYARSNKrkKLPKWIQDT 691
 
Name Accession Description Interval E-value
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
59-651 2.71e-109

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: 345.55  E-value: 2.71e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  59 LRLFPYEP-YPQQLKFMKDAETVLDKGGVLVAEACNGFGKTVCALSSALATGRR------IIYATRTHEQVRQVLREIEQ 131
Cdd:TIGR00604   3 LVYFPYEKiYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEkpevrkIIYASRTHSQLEQATEELRK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 132 INK------KAGTDFSAVALASRQNLCLNQICRSLPQTEAVEA-CRVLRNS------------RRCPY------KSQFSF 186
Cdd:TIGR00604  83 LMSyrtpriGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGkCIKLTVSkikeqrtekpnvESCEFyenfdeLREVED 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 187 LGSSLPPvlSTRRLLNYGRTKGICPYYLSRKISQDCTVVVAPYQYIFNESIRATVGLDINGKVLVFDEAHNADKIGQEVL 266
Cdd:TIGR00604 163 LLLSEIM--DIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSIELKDSIVIFDEAHNLDNVCISSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 267 SDTLSERGLDNAVRELE---------------------------------------------------------LVGVPS 289
Cdd:TIGR00604 241 SSNLSVRSLKRCSKEIAeyfekieerkevdarklldelqklveglkqedlltdediflanpvlpkevlpeavpgNIRIAE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 290 VFIGKLTDYLEKT---------VREEPvvKPGSQLFKDLTEVLGEdLSFIVESFKpmvDEIREKRISRGEVPVCYLNGLL 360
Cdd:TIGR00604 321 IFLHKLSRYLEYLkdalkvlgvVSELP--DAFLEHLKEKTFIDRP-LRFCSERLS---NLLRELEITHPEDFSALVLLFT 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 361 NFLLLVDSSEKESYVAIYRKSASGLNLV-EYRCLDPSLAIKPVIEEAHAALIMSGTLSPLDLFTEVLGLSEAETRTYSAI 439
Cdd:TIGR00604 395 FATLVLTYTNGFLEGIEPYENKTVPNPIlKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHI 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 440 AKPENVRTYV------DISVTTKFQERSA-DMLKLYGERISKLAKNVPNGVLIFFPQRRLMNEAVAIWRRNGFIRRRGRr 512
Cdd:TIGR00604 475 LKRENLLTLIvtrgsdQVPLSSTFEIRNDpSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEK- 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 513 lflgKKIVFVEGTRATENARIVDEYKKAARTDQGAVLFAVFRGRNAEGSNFPYEEARGVFNVGLPYADYHDPLVKAQIGF 592
Cdd:TIGR00604 554 ----KKLIFVETKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEF 629
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231988176 593 FNRKKS-RLGELWYLMDAFRAANQAMGRGIRHRDDWCRFYLMDRRYATHWK--FISKWAVEN 651
Cdd:TIGR00604 630 LRDQYPiRENQDFYEFDAMRAVNQAIGRVIRHKDDYGSIVLLDKRYARSNKrkKLPKWIQDT 691
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
54-639 4.81e-64

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 223.26  E-value: 4.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  54 PQKGFLRLFP-YEPYPQQLKFMKDAETVLDKGGVLVAEACNGFGKT----VCALSSALATGRRIIYATRTHEQVRQVL-R 127
Cdd:COG1199     2 DDGLLALAFPgFEPRPGQREMAEAVARALAEGRHLLIEAGTGTGKTlaylVPALLAARETGKKVVISTATKALQEQLVeK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 128 EIEQINKKAGTDFSAVALASRQN-LCLNQICRSLPQTEAVEACRVLRNSRRCPYKSQFSFLGSSLPPVLSTR--RLLNYG 204
Cdd:COG1199    82 DLPLLRKALGLPLRVALLKGRSNyLCLRRLEQALQEGDDLDDEELLLARILAWASETWTGDRDELPLPEDDElwRQVTSD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 205 RTK---------GICPYYLSRKISQDCTVVVAPYQYIFNESIRATVGLDiNGKVLVFDEAHNADKIGQEVLSDTLSERGL 275
Cdd:COG1199   162 ADNclgrrcpyyGVCPYELARRLAREADVVVVNHHLLFADLALGEELLP-EDDVLIIDEAHNLPDRARDMFSAELSSRSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 276 DNAVRELELVGVPS------VFIGKLTDYLE---KTVREEPVVKPGSQLFKDLTEVLGEDLSFIVESFKPMVDEIREKRI 346
Cdd:COG1199   241 LRLLRELRKLGLRPglkkllDLLERLREALDdlfLALEEEEELRLALGELPDEPEELLEALDALRDALEALAEALEEELE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 347 SRGEVPVCYLNGLLNFLLL---VDSSEKESYVAIYRKSASGLNLvEYRCLDPSLAIKPVI-EEAHAALIMSGTLS---PL 419
Cdd:COG1199   321 RLAELDALLERLEELLFALarfLRIAEDEGYVRWLEREGGDVRL-HAAPLDPADLLRELLfSRARSVVLTSATLSvggPF 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 420 DLFTEVLGLS-EAETRTYSAIAKPENVRTYVDISVTTKFQERsADMLKLYGERISKLAKNVPNGVLIFFPQRRLMNEAVA 498
Cdd:COG1199   400 DYFARRLGLDeDARTLSLPSPFDYENQALLYVPRDLPRPSDR-DGYLEAIAEAIAELLEASGGNTLVLFTSYRALEQVAE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 499 IWRRNGFIRrrgrrlflgkkiVFVEGTRATEnaRIVDEYKKaartDQGAVLFAVfrGRNAEGSNFPYEEARGVFNVGLPY 578
Cdd:COG1199   479 LLRERLDIP------------VLVQGDGSRE--ALLERFRE----GGNSVLVGT--GSFWEGVDLPGDALSLVIIVKLPF 538
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231988176 579 ADYHDPLVKAQIGFFnrkKSRLGELW---YLMDAFRAANQAMGRGIRHRDDWCRFYLMDRRYAT 639
Cdd:COG1199   539 PPPDDPVLEARREAL---EARGGNGFmyaYLPPAVIKLKQGAGRLIRSEEDRGVVVLLDRRLLT 599
DEXDc2 smart00488
DEAD-like helicases superfamily;
61-282 2.20e-48

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 171.41  E-value: 2.20e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176   61 LFPYEPYPQQLKFMKDAETVLDKGGVLVAEACNGFGKTVCALSSALATGRR---------IIYATRTHEQVRQVLREIEQ 131
Cdd:smart00488   4 YFPYEPYPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSfperiqkikLIYLSRTVSEIEKRLEELRK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  132 INK---------------------KAGTDFSAVALASRQNLCLNQICRSLPQTEAV--EACRVLRNSR------------ 176
Cdd:smart00488  84 LMQkveyesdeesekqaqllhelgREKPKVLGLSLTSRKNLCLNPEVRTLKQNGLVvdEVCRSLTASKarkyryenpkve 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  177 RCPYKSQFSFLG--SSLPP-VLSTRRLLNYGRTKGICPYYLSRKISQDCTVVVAPYQYIFNESIRATVGLDINGKVLVFD 253
Cdd:smart00488 164 RCPFYENTEFLLvrDLLPAeVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIRQALSIELKDSIVIFD 243
                          250       260
                   ....*....|....*....|....*....
gi 1231988176  254 EAHNADKIGQEVLSDTLSERGLDNAVREL 282
Cdd:smart00488 244 EAHNLDNVCISALSSELSRRSLERAHKNI 272
Helicase_C_2 pfam13307
Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases.
473-647 3.68e-45

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: 158.49  E-value: 3.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 473 SKLAKNVPNGVLIFFPQRRLMNEAVAIWRRNGFIRrrgrrlflgKKIVFVEGTRAtENARIVDEYKKAARtdqGAVLFAV 552
Cdd:pfam13307   1 LRLLKVIPGGVLVFFPSYSYLEKVAERLKESGLEK---------GIEIFVQPGEG-SREKLLEEFKKKGK---GAVLFGV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 553 FRGRNAEGSNFPYEEARGVFNVGLPYADYHDPLVKAQIGFFNRKKSRLGELWYLMDAFRAANQAMGRGIRHRDDWCRFYL 632
Cdd:pfam13307  68 CGGSFSEGIDFPGDLLRAVIIVGLPFPNPDDPVVEAKREYLDSKGGNPFNEWYLPQAVRAVNQAIGRLIRHENDYGAIVL 147
                         170
                  ....*....|....*..
gi 1231988176 633 MDRRYAT--HWKFISKW 647
Cdd:pfam13307 148 LDSRFLTkrYGKLLPKW 164
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
451-637 3.95e-30

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: 116.16  E-value: 3.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 451 ISVTTKFQER-SADMLKLYGERISKLAKNVPNGVLIFFPQRRLMNEAVAiwrrngfirrrgrrlflgkkivfvegtrate 529
Cdd:cd18788    15 QALNSKFQTReDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERVVS------------------------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 530 narivdeykkaartdQGAVLFAVFRGRNAEGSNFPYEEARGVFNVGLPYADYHDPLVKAQIGF--FNRKKSRL-GELWYL 606
Cdd:cd18788    64 ---------------RGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKMDDleYLRDKGLLtGEDWYT 128
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1231988176 607 MDAFRAANQAMGRGIRHRDDWCRFYLMDRRY 637
Cdd:cd18788   129 FQAMRAVNQAIGRAIRHKNDYGAIVLLDKRF 159
 
Name Accession Description Interval E-value
rad3 TIGR00604
DNA repair helicase (rad3); All proteins in this family for which funcitons are known are ...
59-651 2.71e-109

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: 345.55  E-value: 2.71e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  59 LRLFPYEP-YPQQLKFMKDAETVLDKGGVLVAEACNGFGKTVCALSSALATGRR------IIYATRTHEQVRQVLREIEQ 131
Cdd:TIGR00604   3 LVYFPYEKiYPEQRSYMRDLKRSLDRGDEAILEMPSGTGKTISLLSLILAYQQEkpevrkIIYASRTHSQLEQATEELRK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 132 INK------KAGTDFSAVALASRQNLCLNQICRSLPQTEAVEA-CRVLRNS------------RRCPY------KSQFSF 186
Cdd:TIGR00604  83 LMSyrtpriGEESPVSGLSLASRKNLCLHPEVSKERQGKVVNGkCIKLTVSkikeqrtekpnvESCEFyenfdeLREVED 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 187 LGSSLPPvlSTRRLLNYGRTKGICPYYLSRKISQDCTVVVAPYQYIFNESIRATVGLDINGKVLVFDEAHNADKIGQEVL 266
Cdd:TIGR00604 163 LLLSEIM--DIEDLVEYGELLGLCPYFATRKMLPFANIVLLPYQYLLDPKIRSAVSIELKDSIVIFDEAHNLDNVCISSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 267 SDTLSERGLDNAVRELE---------------------------------------------------------LVGVPS 289
Cdd:TIGR00604 241 SSNLSVRSLKRCSKEIAeyfekieerkevdarklldelqklveglkqedlltdediflanpvlpkevlpeavpgNIRIAE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 290 VFIGKLTDYLEKT---------VREEPvvKPGSQLFKDLTEVLGEdLSFIVESFKpmvDEIREKRISRGEVPVCYLNGLL 360
Cdd:TIGR00604 321 IFLHKLSRYLEYLkdalkvlgvVSELP--DAFLEHLKEKTFIDRP-LRFCSERLS---NLLRELEITHPEDFSALVLLFT 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 361 NFLLLVDSSEKESYVAIYRKSASGLNLV-EYRCLDPSLAIKPVIEEAHAALIMSGTLSPLDLFTEVLGLSEAETRTYSAI 439
Cdd:TIGR00604 395 FATLVLTYTNGFLEGIEPYENKTVPNPIlKFMCLDPSIALKPLFERVRSVILASGTLSPLDAFPRNLGFNPVSQDSPTHI 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 440 AKPENVRTYV------DISVTTKFQERSA-DMLKLYGERISKLAKNVPNGVLIFFPQRRLMNEAVAIWRRNGFIRRRGRr 512
Cdd:TIGR00604 475 LKRENLLTLIvtrgsdQVPLSSTFEIRNDpSLVRNLGELLVEFSKIIPDGIVVFFPSYSYLENIVSTWKEMGILENIEK- 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 513 lflgKKIVFVEGTRATENARIVDEYKKAARTDQGAVLFAVFRGRNAEGSNFPYEEARGVFNVGLPYADYHDPLVKAQIGF 592
Cdd:TIGR00604 554 ----KKLIFVETKDAQETSDALERYKQAVSEGRGAVLLSVAGGKVSEGIDFCDDLGRAVIMVGIPYEYTESRILLARLEF 629
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1231988176 593 FNRKKS-RLGELWYLMDAFRAANQAMGRGIRHRDDWCRFYLMDRRYATHWK--FISKWAVEN 651
Cdd:TIGR00604 630 LRDQYPiRENQDFYEFDAMRAVNQAIGRVIRHKDDYGSIVLLDKRYARSNKrkKLPKWIQDT 691
DinG COG1199
Rad3-related DNA helicase DinG [Replication, recombination and repair];
54-639 4.81e-64

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


Pssm-ID: 440812 [Multi-domain]  Cd Length: 629  Bit Score: 223.26  E-value: 4.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  54 PQKGFLRLFP-YEPYPQQLKFMKDAETVLDKGGVLVAEACNGFGKT----VCALSSALATGRRIIYATRTHEQVRQVL-R 127
Cdd:COG1199     2 DDGLLALAFPgFEPRPGQREMAEAVARALAEGRHLLIEAGTGTGKTlaylVPALLAARETGKKVVISTATKALQEQLVeK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 128 EIEQINKKAGTDFSAVALASRQN-LCLNQICRSLPQTEAVEACRVLRNSRRCPYKSQFSFLGSSLPPVLSTR--RLLNYG 204
Cdd:COG1199    82 DLPLLRKALGLPLRVALLKGRSNyLCLRRLEQALQEGDDLDDEELLLARILAWASETWTGDRDELPLPEDDElwRQVTSD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 205 RTK---------GICPYYLSRKISQDCTVVVAPYQYIFNESIRATVGLDiNGKVLVFDEAHNADKIGQEVLSDTLSERGL 275
Cdd:COG1199   162 ADNclgrrcpyyGVCPYELARRLAREADVVVVNHHLLFADLALGEELLP-EDDVLIIDEAHNLPDRARDMFSAELSSRSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 276 DNAVRELELVGVPS------VFIGKLTDYLE---KTVREEPVVKPGSQLFKDLTEVLGEDLSFIVESFKPMVDEIREKRI 346
Cdd:COG1199   241 LRLLRELRKLGLRPglkkllDLLERLREALDdlfLALEEEEELRLALGELPDEPEELLEALDALRDALEALAEALEEELE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 347 SRGEVPVCYLNGLLNFLLL---VDSSEKESYVAIYRKSASGLNLvEYRCLDPSLAIKPVI-EEAHAALIMSGTLS---PL 419
Cdd:COG1199   321 RLAELDALLERLEELLFALarfLRIAEDEGYVRWLEREGGDVRL-HAAPLDPADLLRELLfSRARSVVLTSATLSvggPF 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 420 DLFTEVLGLS-EAETRTYSAIAKPENVRTYVDISVTTKFQERsADMLKLYGERISKLAKNVPNGVLIFFPQRRLMNEAVA 498
Cdd:COG1199   400 DYFARRLGLDeDARTLSLPSPFDYENQALLYVPRDLPRPSDR-DGYLEAIAEAIAELLEASGGNTLVLFTSYRALEQVAE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 499 IWRRNGFIRrrgrrlflgkkiVFVEGTRATEnaRIVDEYKKaartDQGAVLFAVfrGRNAEGSNFPYEEARGVFNVGLPY 578
Cdd:COG1199   479 LLRERLDIP------------VLVQGDGSRE--ALLERFRE----GGNSVLVGT--GSFWEGVDLPGDALSLVIIVKLPF 538
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1231988176 579 ADYHDPLVKAQIGFFnrkKSRLGELW---YLMDAFRAANQAMGRGIRHRDDWCRFYLMDRRYAT 639
Cdd:COG1199   539 PPPDDPVLEARREAL---EARGGNGFmyaYLPPAVIKLKQGAGRLIRSEEDRGVVVLLDRRLLT 599
DEXDc2 smart00488
DEAD-like helicases superfamily;
61-282 2.20e-48

DEAD-like helicases superfamily;


Pssm-ID: 214693 [Multi-domain]  Cd Length: 289  Bit Score: 171.41  E-value: 2.20e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176   61 LFPYEPYPQQLKFMKDAETVLDKGGVLVAEACNGFGKTVCALSSALATGRR---------IIYATRTHEQVRQVLREIEQ 131
Cdd:smart00488   4 YFPYEPYPIQYEFMEELKRVLDRGKIGILESPTGTGKTLSLLCLTLTWLRSfperiqkikLIYLSRTVSEIEKRLEELRK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  132 INK---------------------KAGTDFSAVALASRQNLCLNQICRSLPQTEAV--EACRVLRNSR------------ 176
Cdd:smart00488  84 LMQkveyesdeesekqaqllhelgREKPKVLGLSLTSRKNLCLNPEVRTLKQNGLVvdEVCRSLTASKarkyryenpkve 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  177 RCPYKSQFSFLG--SSLPP-VLSTRRLLNYGRTKGICPYYLSRKISQDCTVVVAPYQYIFNESIRATVGLDINGKVLVFD 253
Cdd:smart00488 164 RCPFYENTEFLLvrDLLPAeVYDIEDLLELGKRLGGCPYFASRKAIEFANVVVLPYQYLLDPKIRQALSIELKDSIVIFD 243
                          250       260
                   ....*....|....*....|....*....
gi 1231988176  254 EAHNADKIGQEVLSDTLSERGLDNAVREL 282
Cdd:smart00488 244 EAHNLDNVCISALSSELSRRSLERAHKNI 272
Helicase_C_2 pfam13307
Helicase C-terminal domain; This domain is found at the C-terminus of DEAD-box helicases.
473-647 3.68e-45

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: 158.49  E-value: 3.68e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 473 SKLAKNVPNGVLIFFPQRRLMNEAVAIWRRNGFIRrrgrrlflgKKIVFVEGTRAtENARIVDEYKKAARtdqGAVLFAV 552
Cdd:pfam13307   1 LRLLKVIPGGVLVFFPSYSYLEKVAERLKESGLEK---------GIEIFVQPGEG-SREKLLEEFKKKGK---GAVLFGV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 553 FRGRNAEGSNFPYEEARGVFNVGLPYADYHDPLVKAQIGFFNRKKSRLGELWYLMDAFRAANQAMGRGIRHRDDWCRFYL 632
Cdd:pfam13307  68 CGGSFSEGIDFPGDLLRAVIIVGLPFPNPDDPVVEAKREYLDSKGGNPFNEWYLPQAVRAVNQAIGRLIRHENDYGAIVL 147
                         170
                  ....*....|....*..
gi 1231988176 633 MDRRYAT--HWKFISKW 647
Cdd:pfam13307 148 LDSRFLTkrYGKLLPKW 164
DEAD_2 pfam06733
DEAD_2; This represents a conserved region within a number of RAD3-like DNA-binding helicases ...
114-275 8.14e-39

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: 140.86  E-value: 8.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 114 YATRTHEQVRQVLREIEQINKKAgtDFSAVALASRQNLCLNQICRSLPQTEAV-EACRVLRNSR---RCPYKSQFSFLGS 189
Cdd:pfam06733   1 YCSRTHSQLEQVVKELRRLPYYK--KIRGLILGSRKNLCINPEVLKLKKGNLVnERCRELVKSKargSCPFYNNLEDLLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 190 S----LPPVLSTRRLLNYGRTKGICPYYLSRKISQDCTVVVAPYQYIFNESIRATVGLDINGKVLVFDEAHNADKIGQEV 265
Cdd:pfam06733  79 LrdllGDEVMDIEDLVELGEKLGICPYYLSRELIPDADIIILPYNYLLDPKIRESLSINLKNSIVIFDEAHNIEDVCIES 158
                         170
                  ....*....|
gi 1231988176 266 LSDTLSERGL 275
Cdd:pfam06733 159 ASFSISRSQL 168
HELICc2 smart00491
helicase superfamily c-terminal domain;
517-639 2.33e-32

helicase superfamily c-terminal domain;


Pssm-ID: 214694 [Multi-domain]  Cd Length: 142  Bit Score: 122.00  E-value: 2.33e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  517 KKIVFVEGTRATENARIVDEYKKAARTdQGAVLFAVFRGRNAEGSNFPYEEARGVFNVGLPYADYHDPLVKAQIGFFNRK 596
Cdd:smart00491  20 NKPVFIEGKDSGETEELLEKYSAACEA-RGALLLAVARGKVSEGIDFPDDLGRAVIIVGIPFPNPDSPILRARLEYLDEK 98
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1231988176  597 -KSRLGELWYLMDAFRAANQAMGRGIRHRDDWCRFYLMDRRYAT 639
Cdd:smart00491  99 gGIRPFDEVYLFDAMRALAQAIGRAIRHKNDYGVVVLLDKRYAR 142
SF2_C_XPD cd18788
C-terminal helicase domain of xeroderma pigmentosum group D (XPD) family DEAD-like helicases; ...
451-637 3.95e-30

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: 116.16  E-value: 3.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 451 ISVTTKFQER-SADMLKLYGERISKLAKNVPNGVLIFFPQRRLMNEAVAiwrrngfirrrgrrlflgkkivfvegtrate 529
Cdd:cd18788    15 QALNSKFQTReDEAVMDELGNLLLELCAVVPDGVLVFFPSYSYMERVVS------------------------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 530 narivdeykkaartdQGAVLFAVFRGRNAEGSNFPYEEARGVFNVGLPYADYHDPLVKAQIGF--FNRKKSRL-GELWYL 606
Cdd:cd18788    64 ---------------RGALLLAVCRGKVSEGIDFSDDLGRAVIMVGIPYPNTKDPILKLKMDDleYLRDKGLLtGEDWYT 128
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1231988176 607 MDAFRAANQAMGRGIRHRDDWCRFYLMDRRY 637
Cdd:cd18788   129 FQAMRAVNQAIGRAIRHKNDYGAIVLLDKRF 159
DEAHc_FancJ cd17970
DEAH-box helicase domain of Fanconi anemia group J protein and similar proteins; Fanconi ...
90-284 7.89e-21

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: 90.48  E-value: 7.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  90 EACNGFGKTVCALSSALA-----TGR---------------RIIYATRTHEQVRQVLREieqINKKAGTDFSAVALASRQ 149
Cdd:cd17970     7 ESPTGTGKTLSLLCSTLAwrqslKGKatsegsdgggsgkipKIIYASRTHSQLAQVVRE---LKRTAYKRPRMTILGSRD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 150 NLCLNQICRSLPQTEAVEACRVLRNSRrcpyksqfsflgsslppvlstrrllnygrtkgicpyylsrkisQDCTVVVAPY 229
Cdd:cd17970    84 HLCIHPVINKLSNQNANEACMALLSGK-------------------------------------------NEADLVFCPY 120
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1231988176 230 QYIFNESIRATVGLDINGKVLVFDEAHNADKIGQEVLSDTLSErgLDNAVRELEL 284
Cdd:cd17970   121 NYLLDPNIRRSMGLNLKGSVVIFDEAHNIEVRTIILTSGTLSP--LDSFASELGT 173
HBB pfam06777
Helical and beta-bridge domain; HBB is the domain on DEAD-box eukaryotic DNA repair helicases ...
286-459 6.12e-15

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: 73.57  E-value: 6.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 286 GVPSVFIGKLTDYLektVREEPVvkPGSQLFKDLTEVLGEDLSFIVESFKPMV---DEIREKRISRGEVPVCYLNGLLNF 362
Cdd:pfam06777  23 GLREAYEARLEDYV---LSEVPV--LPDEILEEAVPGNIRSAEHFLAFLKRLVeygKARREVKIVKSESPRSFLSHLGEF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 363 LLLVDSSEKESYVAIYRKSaSGLNLVEYrCLDPSLAIKPViEEAHAALIMSGTLSPLDLFTEVLGLsEAETRTYSAIAKP 442
Cdd:pfam06777  98 LLAWLSSDSEDYVFLVSRE-EGPSLEAV-CIDPSKPLRFL-AERLSSLLMSGTLTPLEDYSDLMGL-EAKLKKFPSPFPK 173
                         170
                  ....*....|....*..
gi 1231988176 443 ENVRTYVDISVTTKFQE 459
Cdd:pfam06777 174 ENLIVLFATLVSTYYKG 190
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
84-273 2.71e-11

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: 61.68  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  84 GGVLVAEACNGFGKTVCALSSALATGR-----RIIYATRTHEQVRQVLREIEQInkKAGTDFSAVALASRqnlclnqicr 158
Cdd:cd17915     1 GGHVALESPTGSGKTLSLLCSALSYQRefhktKVLYCSRTHSQIEQIIRELRKL--LEKRKIRALALSSR---------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 159 slpqteaveacrvlrnsrrcpyksqfsflgsslppvlstrrllnygrtkgicpyylsrkisqDCTVVVAPYQYIFNESIR 238
Cdd:cd17915    69 --------------------------------------------------------------DADIVVLPYPYLLDARIR 86
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1231988176 239 ATVGLDINGKVLVFDEAHNADKIGQEVLSDTLSER 273
Cdd:cd17915    87 EFIGIDLREQVVIIDEAHNLDERSVIITSGTLSPL 121
DEAHc_DDX11_starthere cd17968
DEAH-box helicase domain of ATP-dependent DNA helicase DDX11; DDX11 (also called ChlR1) ...
84-257 5.55e-05

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: 43.46  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176  84 GGVLVAEACNGFGKTVCALSSALATGRRIIYATRTHEQVRQVLREIEQinKKAGTDFSAVALASRQnlclnqicrslPQT 163
Cdd:cd17968     1 GKVGIFESPTGTGKSLSLICGALTWLTKIYYCSRTHSQLAQFVHEVQK--SPFGKDVRLVSLGSRQ-----------PAA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 164 EaveacrvlrnsrrcpyksqfsflgsslppvlstrrllnygrtkgicpyylsrkisqdctVVVAPYQYIFNESIRATVGL 243
Cdd:cd17968    68 Q-----------------------------------------------------------VVVLPYQMLLHAATRKASGI 88
                         170
                  ....*....|....
gi 1231988176 244 DINGKVLVFDEAHN 257
Cdd:cd17968    89 KLKDQVVIIDEAHN 102
DEAHc_XPD cd17969
DEAH-box helicase domain of TFIIH basal transcription factor complex helicase XPD subunit; ...
198-271 7.78e-04

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: 40.49  E-value: 7.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1231988176 198 RRLLNY-----GRTKGICPYYLSrkiSQDCTVVVAPYQYIFNESIRATVGLDINGK-VLVFDEAHNADKIGQEVLSDTLS 271
Cdd:cd17969    63 RKLMDYyekqtGEKPNFLGLALS---SRHANVVVYSYHYLLDPKIAELVSKELSKKsVVVFDEAHNIDFQSVVITSGTLS 139
DEAHc_XPD-like cd17915
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ...
402-431 2.42e-03

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: 38.57  E-value: 2.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1231988176 402 VIEEAH-----AALIMSGTLSPLDLFTEVLGLSEA 431
Cdd:cd17915    99 IIDEAHnlderSVIITSGTLSPLDIYSKILGIRNM 133
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
224-273 3.68e-03

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 38.54  E-value: 3.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1231988176 224 VVVAPYQYIFNESIRATVGLDINGKVLVFDEAHNADKIGQEVLSDTLSER 273
Cdd:cd00046    82 IIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVR 131
 
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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