XPD_SULAC
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 03-AUG-2022, entry version 100.
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; Crenarchaeota; 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}.
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DR EMBL; CP000077; AAY79611.1; -; Genomic_DNA.
DR RefSeq; WP_011277112.1; NC_007181.1.
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 EnsemblBacteria; AAY79611; AAY79611; Saci_0192.
DR GeneID; 3474005; -.
DR KEGG; sai:Saci_0192; -.
DR PATRIC; fig|330779.12.peg.184; -.
DR eggNOG; arCOG00770; Archaea.
DR HOGENOM; CLU_006515_9_0_2; -.
DR OMA; QVNPVNE; -.
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; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR DisProt; DP01941; -.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR010614; DEAD_2.
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 PANTHER; PTHR11472; PTHR11472; 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; SSF52540; 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 BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 105
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 137
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT MUTAGEN 35
FT /note="K->A: Abolishes helicase activity but not iron-
FT 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
