ID A0A1F8A0H5_9EURO Unreviewed; 812 AA.
AC A0A1F8A0H5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=ABOM_006158 {ECO:0000313|EMBL:OGM44818.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM44818.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM44818.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM44818.1}.
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DR EMBL; LYCR01000050; OGM44818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8A0H5; -.
DR STRING; 109264.A0A1F8A0H5; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000179179; 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:UniProtKB-KW.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OGM44818.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OGM44818.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW ECO:0000313|EMBL:OGM44818.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT DOMAIN 331..493
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 547..701
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 91621 MW; 77BAD14F2BDC0A16 CRC64;
MPVKRKATDS GRSSRASKRA TPVPDIQDVG SSDEFSEYDP KEDSLKEVVD KFSLESFSNK
KSSAVQKQDP NFGYKDFSSL PLKPDHANRP LWIDPLKGTI TLESFSPLAP QAQDFLTTIA
EPLSRPTHLH EYRLTGNSLY AAVSVGLQPQ DIINFLDRLS KTPLPDTIKS FIIDFTKPTE
RSSTDPAMLQ MLLQDEVIGA QRVQGGSAGI IQQAAPKMGG LVIPGTKDAA GVKQSTDQQQ
PSEENQGEKR QEDDLLLAIR DEDDDEEQAQ VHSFEIPNEA VEPVKARCQA MGCPALEEYD
FRNDEINPTL EIDLKPQARI RSYQEKSLSK MFGNGRAKSG IIVLPCGAGK TLVGITAACT
IKKGTIILCT SSMSVVQWRN EFLRWSNIDP GDIAVFTSDN KEKFRRSTGI IVSTYSMVSQ
TRARSHDAQK MMDWIQSREW GLMILDEVHV VPASMFRKVT SAIATQSKLG LTATLLREDD
KIKDLNFLIG PKLYEANWME LAEQGHIAKV QCAEVWCPMT TEFYSEYMRE KSRKAALLYI
MNPRKFQACQ FLIDYHEKRG DKVIVFSDNV YALERYALKL NKAYIYGGTP QNERMRILEN
FQHNEQVNTI FLSKIGDTSL DLPEATCLIQ ISSHYGSRRQ EAQRLGRILR AKRRNDEGFN
AFFYSLVSKD TDEMFYSSKR QAFLVDQGYA FKVITHLQGI ENLDGLAYAT PGERRELLQE
VMLQNETSAE VEAVTDDLFS ERSGGPRAKK GAVKRSAATL SGLAGGEDMA YIEYNKSRNK
QLKDKVGHHP LFRKIERERQ KRKKEMEEFG MH
//
