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Database: UniProt
Entry: A0A016WAQ1_9BILA
LinkDB: A0A016WAQ1_9BILA
Original site: A0A016WAQ1_9BILA 
ID   A0A016WAQ1_9BILA        Unreviewed;       738 AA.
AC   A0A016WAQ1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   Name=Acey_s0843.g2641 {ECO:0000313|EMBL:EYC36919.1};
GN   Synonyms=Acey-Y66D12A.15 {ECO:0000313|EMBL:EYC36919.1};
GN   ORFNames=Y032_0843g2641 {ECO:0000313|EMBL:EYC36919.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC36919.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYC36919.1}.
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DR   EMBL; JARK01000443; EYC36919.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016WAQ1; -.
DR   Proteomes; UP000024635; 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:UP000024635}.
FT   DOMAIN          299..466
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          520..672
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          188..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   738 AA;  84250 MW;  10A657CF3B55966E CRC64;
     MIMHRRRGAA QQTGDGCRSQ VFFGTIVDVS LLFPIEPADL PADTTAVADH ASRPLWVAPD
     GHIFLESFSP VYKHARDFLI AISEPVCRPE HIHEYQLTAY SLYAAVSVGL QTNDIIEYLE
     RLSKSALPRG IVEFIKMCTL SYGKVKLVLK HNRYFVESRH SDVIQKLLKD KVIQSCILEE
     EKPVEETQTQ IEKINFPQEQ TKEEEKKPEG EDVPEDIGEL YGKMDGDDEE DAEIRSLQLL
     TFEIKQESIE TVQKRCIELE YPLLAEYDFR NDTMNPNLGI DLKPSTTLRP YQEKSLRKMF
     GNSRARSGVI VLPCGAGKTL VGVTAVTTVN KRCLCLANSN VSVEQWRAQF KLWSTITDKQ
     IVRFTREAKD TVPHGPDASK PVVCISTYSM VAYAGKRTYA AEEAMKFIES QEWGLLLLDE
     VHTIPAKMFR RVLTIVQAHC KLGLTATLVR EDDKITDLNF LIGPKIYEAN WMELQKAGHI
     AKVQCAEVWC PMTSEFYAYY LRAQIARRLL LAVMNPNKFR ICQFLIKFHE RRNDKIIVFS
     DNVFALKKYA IEMNKPFLYG ETSQNERMKI LQNFQYNPRV NTIFVSKVAD TSFDLPEANV
     LIQVSAHGGS RRQEAQRLGR ILRAKKHSTD QFNAFFYSLV SQDTVEMGYS RKRQRFLVNQ
     GYAYKESQLQ LLQQVLAASD ADAEEEDVKE EMADGTIRVS RREATMASVS GGSSVSYSNK
     SKQALADRHP LFKRFREK
//
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