ID XPD_SULAC Reviewed; 551 AA. AC Q4JC68; DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=ATP-dependent DNA helicase Saci_0192; DE EC=3.6.4.12; GN OrderedLocusNames=Saci_0192; OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC OS 15157 / NCIMB 11770). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=330779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770; RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005; RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF LYS-35; LYS-84; RP CYS-88; CYS-102; CYS-105; PHE-136 AND CYS-137. RX PubMed=16973432; DOI=10.1016/j.molcel.2006.07.019; RA Rudolf J., Makrantoni V., Ingledew W.J., Stark M.J., White M.F.; RT "The DNA repair helicases XPD and FancJ have essential iron-sulfur RT domains."; RL Mol. Cell 23:801-808(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND IRON-SULFUR CLUSTER. RX PubMed=18510924; DOI=10.1016/j.cell.2008.04.030; RA Fan L., Fuss J.O., Cheng Q.J., Arvai A.S., Hammel M., Roberts V.A., RA Cooper P.K., Tainer J.A.; RT "XPD helicase structures and activities: insights into the cancer and aging RT phenotypes from XPD mutations."; RL Cell 133:789-800(2008). CC -!- FUNCTION: ATP-dependent 5'-3' DNA helicase involved in nucleotide CC excision repair (NER) of DNA. {ECO:0000269|PubMed:16973432}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CC Evidence={ECO:0000269|PubMed:16973432}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:16973432}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:16973432}; CC -!- DOMAIN: 4Fe-4S iron-sulfur-binding is required for protein stability CC and helicase activity. {ECO:0000269|PubMed:18510924}. CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000077; AAY79611.1; -; Genomic_DNA. DR RefSeq; WP_011277112.1; NZ_CP046615.1. DR PDB; 3CRV; X-ray; 2.00 A; A=1-551. DR PDB; 3CRW; X-ray; 4.00 A; 1=1-551. DR PDB; 5H8C; X-ray; 2.29 A; A=3-551. DR PDBsum; 3CRV; -. DR PDBsum; 3CRW; -. DR PDBsum; 5H8C; -. DR AlphaFoldDB; Q4JC68; -. DR SMR; Q4JC68; -. DR STRING; 330779.Saci_0192; -. DR GeneID; 78440544; -. DR KEGG; sai:Saci_0192; -. DR PATRIC; fig|330779.12.peg.184; -. DR eggNOG; arCOG00770; Archaea. DR HOGENOM; CLU_006515_9_0_2; -. DR BRENDA; 3.6.4.12; 6160. DR EvolutionaryTrace; Q4JC68; -. DR Proteomes; UP000001018; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB. DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; EXP:DisProt. DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR CDD; cd17915; DEAHc_XPD-like; 1. DR CDD; cd18788; SF2_C_XPD; 1. DR DisProt; DP01941; -. DR Gene3D; 1.10.275.30; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR006555; ATP-dep_Helicase_C. DR InterPro; IPR045028; DinG/Rad3-like. DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3. DR InterPro; IPR006554; Helicase-like_DEXD_c2. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010614; RAD3-like_helicase_DEAD. DR PANTHER; PTHR11472:SF65; DNA HELICASE REPD; 1. DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1. DR Pfam; PF06733; DEAD_2; 1. DR Pfam; PF13307; Helicase_C_2; 1. DR SMART; SM00488; DEXDc2; 1. DR SMART; SM00491; HELICc2; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; ATP-binding; DNA damage; DNA repair; DNA-binding; KW Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding; KW Reference proteome; Transcription. FT CHAIN 1..551 FT /note="ATP-dependent DNA helicase Saci_0192" FT /id="PRO_0000352309" FT DOMAIN 1..228 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOTIF 180..183 FT /note="DEAH box" FT BINDING 29..36 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT BINDING 88 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:18510924" FT BINDING 102 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:18510924" FT BINDING 105 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:18510924" FT BINDING 137 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:18510924" FT MUTAGEN 35 FT /note="K->A: Abolishes helicase activity but not FT iron-sulfur-binding." FT /evidence="ECO:0000269|PubMed:16973432" FT MUTAGEN 84 FT /note="K->H: Impairs iron-sulfur-binding and helicase FT activity." FT /evidence="ECO:0000269|PubMed:16973432" FT MUTAGEN 88 FT /note="C->S: Abolishes iron-sulfur-binding and helicase FT activity." FT /evidence="ECO:0000269|PubMed:16973432" FT MUTAGEN 102 FT /note="C->S: Does not affect iron-sulfur-binding nor FT helicase activity." FT /evidence="ECO:0000269|PubMed:16973432" FT MUTAGEN 105 FT /note="C->S: Abolishes iron-sulfur-binding and helicase FT activity." FT /evidence="ECO:0000269|PubMed:16973432" FT MUTAGEN 136 FT /note="F->P: Impairs iron-sulfur-binding and helicase FT activity." FT /evidence="ECO:0000269|PubMed:16973432" FT MUTAGEN 137 FT /note="C->S: Abolishes iron-sulfur-binding and helicase FT activity." FT /evidence="ECO:0000269|PubMed:16973432" FT HELIX 6..20 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 24..28 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:5H8C" FT HELIX 35..46 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 48..56 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 60..67 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:3CRV" FT TURN 106..109 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 120..134 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 138..145 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 150..155 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 157..160 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 162..165 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:5H8C" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 182..192 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 198..207 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 211..224 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 245..264 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 272..285 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 296..300 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 305..308 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 317..324 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 328..333 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 341..345 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 346..349 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 357..363 FT /evidence="ECO:0007829|PDB:3CRV" FT TURN 370..372 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 375..391 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 393..401 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 403..410 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 415..419 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 426..432 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 435..438 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 440..446 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 460..470 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 478..486 FT /evidence="ECO:0007829|PDB:3CRV" FT TURN 493..495 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 496..499 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 501..513 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 522..529 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 530..533 FT /evidence="ECO:0007829|PDB:3CRV" FT HELIX 535..540 FT /evidence="ECO:0007829|PDB:3CRV" FT STRAND 547..549 FT /evidence="ECO:0007829|PDB:3CRV" SQ SEQUENCE 551 AA; 64011 MW; BEE17759C4E065DA CRC64; MLKLRDWQEK LKDKVIEGLR NNFLVALNAP TGSGKTLFSL LVSLEVKPKV LFVVRTHNEF YPIYRDLTKI REKRNITFSF LVGKPSSCLY AEKGAESEDI PCKYCELKGS IVEVKTDDSP LSLVKKLKKD GLQDKFCPYY SLLNSLYKAD VIALTYPYFF IDRYREFIDI DLREYMIVID EAHNLDKVNE LEERSLSEIT IQMAIKQSKS EESRRILSKL LNQLREVVLP DEKYIKVENV PKLSKEELEI LADDYEDIRK DSLKQGKVNK IHIGSILRFF SLLSIGSFIP FSYSKRLVIK NPEISYYLNL LNDNELSIIL MSGTLPPREY MEKVWGIKRN MLYLDVEREI QKRVSGSYEC YIGVDVTSKY DMRSDNMWKR YADYLLKIYF QAKANVLVVF PSYEIMDRVM SRISLPKYVE SEDSSVEDLY SAISANNKVL IGSVGKGKLA EGIELRNNDR SLISDVVIVG IPYPPPDDYL KILAQRVSLK MNRENEEFLF KIPALVTIKQ AIGRAIRDVN DKCNVWLLDK RFESLYWKKN LKCLNANKMK L //