ID   A0A026WFU6_OOCBI        Unreviewed;       794 AA.
AC   A0A026WFU6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPB {ECO:0000256|ARBA:ARBA00014343};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=X777_05345 {ECO:0000313|EMBL:EZA54927.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA54927.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA54927.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
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:0000256|ARBA:ARBA00001665};
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006637}.
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DR   EMBL; KK107234; EZA54927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026WFU6; -.
DR   STRING; 2015173.A0A026WFU6; -.
DR   OMA; RCQEIDY; -.
DR   Proteomes; UP000053097; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR   CDD; cd18029; DEXHc_XPB; 1.
DR   CDD; cd18789; SF2_C_XPB; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR032438; ERCC3_RAD25_C.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001161; XPB/Ssl2.
DR   InterPro; IPR032830; XPB/Ssl2_N.
DR   NCBIfam; TIGR00603; rad25; 1.
DR   PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1.
DR   PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR   Pfam; PF16203; ERCC3_RAD25_C; 1.
DR   Pfam; PF13625; Helicase_C_3; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   PRINTS; PR00851; XRODRMPGMNTB.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT   DOMAIN          342..503
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          557..712
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  90935 MW;  47353C719632A509 CRC64;
     MGPPKRFKRD TGKWKKRKDD YDEYNDEDSI DSNEADGVPD AAKNDVEKQD ESAIEDEFGA
     KDYRSQMILK PDCASRPLWV APNGHIFLES FSPVYKHAHD FLIAISEPVC RPEHIHEYKL
     TAYSLYAAVS VGLQTQDIIE YLKRLSKTSI PDGIIEFIKL CTLSYGKVKL VLKHNKYFIE
     SPFPEVLQKL LKDPVIQECR LRKIVEDTEA DDIVTNVQAK IKAPQFGAKA AGNVPAPSKT
     NPETESDQVI TETVAIPEDI TAFYDKIDKE DEDEEEEQEL KTVSFEVNQE KIEVIQKRCI
     ELEHPLLAEY DFRNDTVNAD INIDLKPSAV LRPYQEKSLR KMFGNGRARS GVIVLPCGAG
     KSLVGVTACC TVRKRALILC NSGVSVEQWK QQFKMWSTAD DSMICRFTSE AKDKPMGCGI
     LITTYSMITH TQKRSWEAEQ TMRWLQEQEW GIMVLDEVHT IPAKMFRRVL TIVQSHCKLG
     LTATLLREDD KIADLNFLIG PKLYEANWLE LQKRGFIARV QCAEVWCPMT PEFYREYLGC
     KMSKKLLLYV MNPNKFRCCQ YLIRYHERRG DKTIVFSDNV FALKHYAIKM NKPYIYGPTS
     QNERIQILQN FKFNMKVNTI FVSKVADTSF DLPEANVLIQ ISSHGGSRRQ EAQRLGRILR
     AKKGAIAEEY NAFFYTLVSQ DTMEMNYSRK RQRFLVNQGY AYKVITKLAG MDEEPDLMYT
     SREEQGQLLQ QVLTASDTDA DEERIPGEGA RPIIRKAGTM TSMSGADDAV YYEYKKAASS
     STANKHPLFK KFRT
//