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Database: UniProt
Entry: J0D9A1_AURST
LinkDB: J0D9A1_AURST
Original site: J0D9A1_AURST 
ID   J0D9A1_AURST            Unreviewed;       684 AA.
AC   J0D9A1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=AURDEDRAFT_147223 {ECO:0000313|EMBL:EJD36361.1};
OS   Auricularia subglabra (strain TFB-10046 / SS5) (White-rot fungus)
OS   (Auricularia delicata (strain TFB10046)).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Auriculariaceae; Auricularia.
OX   NCBI_TaxID=717982 {ECO:0000313|EMBL:EJD36361.1, ECO:0000313|Proteomes:UP000006514};
RN   [1] {ECO:0000313|Proteomes:UP000006514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFB10046 {ECO:0000313|Proteomes:UP000006514};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; JH687863; EJD36361.1; -; Genomic_DNA.
DR   RefSeq; XP_007355525.1; XM_007355463.1.
DR   AlphaFoldDB; J0D9A1; -.
DR   KEGG; adl:AURDEDRAFT_147223; -.
DR   eggNOG; KOG1123; Eukaryota.
DR   InParanoid; J0D9A1; -.
DR   OrthoDB; 1360679at2759; -.
DR   Proteomes; UP000006514; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EJD36361.1};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EJD36361.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW   ECO:0000313|EMBL:EJD36361.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006514}.
FT   DOMAIN          273..435
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          489..643
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          168..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  77419 MW;  6DCA38FE2D206957 CRC64;
     MDSACGSPGF AAVRRGEASR VHRAIIERCL NSLPLKAGHD SRPLWVCENH SIVFERFSPF
     AEQVQDFLIA IAEPVSRPEF IHEYQLTTSS LYAAASVGLK TAEIIDVLSR FSKTPLPPST
     IEFIRDCTVS YGKVQLVLKN SKYFIESKHA EIIQRLLKDP VVGTARATAD GADAGSRSET
     PARPKMSGVA PLPANRLEER LNTEYNDDED ERSYGFQIDL NKIDEVKKRC NDLGFPMLQE
     YDFRKDVINR NLNIRLTTSG FVRPYQETSL RKMFGNGRAR SGIIVLPCGA GKTLVGVMAA
     GTINKSCLVL CTSAVSAGQW RHQFKLWAQI KDSQISLFTS EEQKEFQAPS GVLISTYSMI
     ANTRKRSRDA ERKMEFVSSR EWGLVILDEV HVVPANTFRL VFGSIKAHAK LGLTATLVRE
     DDKIVDLDHL IGPKLYEANW KDLAAQGHIA NVLCAEVQCP MSPEFYHQYL RATSLKKTLL
     HCMNPTKLQA CQYLMDYHER RGDKIIVFSD NVFALEYYAR KLKRLFIHGK VSQVERELIL
     ERFKEDPDIK TIFLSKVGDT SLDIPEATCL IQISSHFGSR RQEAQRLGRI LRAKRRSEEG
     FNAYFYSLVS KDTDEMVFST KRQQFLVDQG YAFKVITRLD GIERFPGLAF RTIDERWALL
     REVYHAQEKD GETGNDVAVT LEVA
//
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