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Database: UniProt
Entry: A0A150V913_9PEZI
LinkDB: A0A150V913_9PEZI
Original site: A0A150V913_9PEZI 
ID   A0A150V913_9PEZI        Unreviewed;       660 AA.
AC   A0A150V913;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYG47017.1};
GN   ORFNames=M433DRAFT_105241 {ECO:0000313|EMBL:KYG47017.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG47017.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG47017.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG47017.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG47017.1}.
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DR   EMBL; JPDO01000093; KYG47017.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150V913; -.
DR   STRING; 766039.A0A150V913; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR   CDD; cd18799; SF2_C_EcoAI-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR   PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
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   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   DOMAIN          54..218
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          272..443
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   660 AA;  73736 MW;  C9A5551B8BE08C58 CRC64;
     MVVPFTRSLP HQLFIPRIST QSQCCSRLLG PQRQASTFLK LRPYQQECIE AVLDYVSKGE
     RRLGISLATG SGKTVIFSHL IDQIPAPTKN ATQTLIIAHR RELVEQAAKH CRALYPEKNV
     EVEMGSSSAS GVADITVASV ASLVSGERLL KFDPDRFKLV LVDEAHHIVA PSYLEILRHF
     NLIQDIQKAR TVLVGVSATF SREDGLSLGK AIDHIVYHKD YLDFIQDDWL SNLIFTTVKT
     GADLSKVRSS RGDFQTGSLS KAVNTQENNA LIVRSWLAKA SQRKSTLVFC VDLAHVASLT
     AMFRHHGIDA QFITGDTDAK VRAERLEAFK AGKHPVLINC GIFTEGTDIP NIDCVVLARP
     TKSRNLLVQM IGRGLRKYEN KENCHVLDFV ASLKTGITTT PTLFGLDPDE LVEDADATTL
     RNLKERRESE RVRELASKPQ NLPIGQFSDS SKLVGNVIFT DYDDVNELIE DTSGERHIRA
     ISPHAWVQVG DGVYIVSATG GDYMTIKHTG TSFEVIFTRK LNLKTESSKY PYARPRLLAT
     VQRFGEAVRA ADKFAKEKMP FFAISKNASW RRTPASDTQI AFINKIRDES EKLEKGSITK
     GQAADWITKI KHGARGRFNK ITIAKRKAER ITMKKDKFQE MQRKAQVKVG PVAKEEDMEL
//
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