ID A0A2N3NCU9_9PEZI Unreviewed; 837 AA.
AC A0A2N3NCU9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=jhhlp_001932 {ECO:0000313|EMBL:PKS10182.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS10182.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS10182.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS10182.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(2017).
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:PKS10182.1}.
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DR EMBL; NLAX01000008; PKS10182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3NCU9; -.
DR STRING; 41688.A0A2N3NCU9; -.
DR VEuPathDB; FungiDB:jhhlp_001932; -.
DR InParanoid; A0A2N3NCU9; -.
DR OrthoDB; 1360679at2759; -.
DR Proteomes; UP000233524; 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};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233524}.
FT DOMAIN 363..526
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 580..734
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 93969 MW; 97694807F4995898 CRC64;
MPPKRKASGA ITGATKAGKT SQVSTPGVGT PKSIDSSDEY SDTADEVEDA VDAETEEKIE
NVVDKFSTNV LERRVQQEQT RAKKSNHELL THIFGSRDYS YLKMKPDHKN RPLWIDPAKG
RIIMESFNPL AAQAQDFLVT IAEPLSRPSF IHEYALTMHS LYAAVSVGLS PDDIINTLDR
FLKIPLPDAI RQFIKGCTQS YGKVKLVLKN TKYYVESPDP EVLQKLLKDE VIGPLRVQGS
DTITSSAPKM AGLVIPGTQN AAGVNQAAGS LQQPQVQSKD PEVPDDSVLY ANLNDEDEDE
EVTHSFEIPD SAVETVQKRC LELEYPVLEE YDFRRDEVNS NLEIDLRPGT SIRPYQEKSL
SKMFGNGRAK SGIIVLPCGA GKTLVGITAA VTIKKGVIVL CTSSMSVVQW RNEFLKWSNI
SPDDIVAFTA DSKNNMFTGN TGIIVTTYSM VTQTRERSHE AKKMMDFLTG REWGLMLLDE
VHVVPANIFR RVTSSIKSHS KLGLTATLLR EDDKISDLNF LIGPKLFEAN WMELSEQGHI
AKVQCAEVWC SMPTEFFDQY LRAPAREKGL LYIMNPNKFQ ACQYLIQYHE KRGDKIIVFS
DNVYALKAYA LKLKKAFIYG GTGQAERLQV LENFQHNPEV NTLFLSKIGD TSLDLPEATC
LIQISSHYGS RRQEAQRLGR ILRAKRRNDE GFNAFFYSLV SKDTEEMHYS HKRQAFLVDQ
GYAFKVITQL ANIEKTPDLA FATAAERREL LQKIMIENET TNEKEEVDNM WHGKGAGKRK
GAVRRAAGSL MELSGGQDMA YVEQNKNVNR GLKKKKKPQS AFFKKLEREK ERARAGT
//
