ID A0A165GIJ3_9BASI Unreviewed; 877 AA.
AC A0A165GIJ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=CALCODRAFT_554984 {ECO:0000313|EMBL:KZT58114.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT58114.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT58114.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT58114.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(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}.
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DR EMBL; KV423955; KZT58114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GIJ3; -.
DR STRING; 1353952.A0A165GIJ3; -.
DR InParanoid; A0A165GIJ3; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000076842; 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:KZT58114.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KZT58114.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806,
KW ECO:0000313|EMBL:KZT58114.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 398..560
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 614..768
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 97524 MW; E2DC0B3469A15BCC CRC64;
MPPKRPAEGA HPSSALMTTT LKRTVGSAAS TSSKKQKRGL PAQSAGLDNP QYDVPGSDDE
PLEDLDLVSD VGDDASSTDN IAADSLIPRG AKLNLSALAR KARQYERGTR ADLVSHMFGD
QDFAYLQLKG DHVSRPLWID PVDGHIILEG FSPIAEQAQD FLVAISEPVS RPSFIHEYKL
TAYSLYAAVS VGLETEDIIE VLNRLSKVPI PENVISYIRS CTMSYGKVKL VLKHNKYFVE
STHPEILQTL LRDGEIRGAR VVPGAGGAYE AANGANGGQT KKLLHSTETG SGKGSAAGTP
APSGAATPNQ KPGQAEADLF TSVVGVDQDE IEEDDENTVS FQIMDDKIDD VKKRCHDLDF
PVLEEYDFRN DTVNANLDID LKPITVIRPY QEKSLSKMFG NGRARSGIIV LPCGAGKTLV
GITAACTIKK STLVLCTSTV SVMQWKQQFM QWSNITDRQI SVFTAEQKEK FSGAAGIVVS
TYSMVANTRN RSYESQKMMD FLTSREWGFI LLDEVHVVPA QMFRRVVTTI KAHAKLGLTA
TLVREDNKID DLNYMIGPKL YEANWMDLAA KGHIANVQCA EVWCPMTPEF YREYLREKPR
RRMLLYCMNP NKFQACQFLI DYHERRGDKI IVFSDNVFAL EAYAKKLSKP FIHGATAQVE
RMRVLQNFQH NPVVNTIFLS KVGDTSIDLP EATCLIQISS HFGSRRQEAQ RLGRILRAKR
RNDEGFNAFF YSLVSKDTQE MYYSTKRQQF LIDQGYAFKV ITQLEGLHHM PNLVYKTQSE
QIELLQSVLI ANESALDFSG SDLMGLQGAQ GQKARKSAQK YEAKRAVGSL GALSGAQHMS
YIERNKTANR QLARDANASR HKLFKKRDVQ KKQANAG
//
