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Database: UniProt
Entry: A0A150VC74_9PEZI
LinkDB: A0A150VC74_9PEZI
Original site: A0A150VC74_9PEZI 
ID   A0A150VC74_9PEZI        Unreviewed;       501 AA.
AC   A0A150VC74;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=Zinc finger ZPR1-type domain-containing protein {ECO:0000259|SMART:SM00709};
GN   ORFNames=M433DRAFT_2354 {ECO:0000313|EMBL:KYG48051.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48051.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG48051.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG48051.1,
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   -!- SIMILARITY: Belongs to the ZPR1 family.
CC       {ECO:0000256|ARBA:ARBA00008354}.
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:KYG48051.1}.
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DR   EMBL; JPDO01000059; KYG48051.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150VC74; -.
DR   STRING; 766039.A0A150VC74; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 2.60.120.1040; ZPR1, A/B domain; 2.
DR   Gene3D; 2.20.25.420; ZPR1, zinc finger domain; 2.
DR   InterPro; IPR004457; Znf_ZPR1.
DR   InterPro; IPR040141; ZPR1.
DR   InterPro; IPR042451; ZPR1_A/B_dom.
DR   InterPro; IPR042452; ZPR1_Znf1/2.
DR   NCBIfam; TIGR00310; ZPR1_znf; 2.
DR   PANTHER; PTHR10876; ZINC FINGER PROTEIN ZPR1; 1.
DR   PANTHER; PTHR10876:SF0; ZINC FINGER PROTEIN ZPR1; 1.
DR   Pfam; PF03367; zf-ZPR1; 2.
DR   SMART; SM00709; Zpr1; 2.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          49..206
FT                   /note="Zinc finger ZPR1-type"
FT                   /evidence="ECO:0000259|SMART:SM00709"
FT   DOMAIN          290..460
FT                   /note="Zinc finger ZPR1-type"
FT                   /evidence="ECO:0000259|SMART:SM00709"
FT   REGION          224..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  55294 MW;  C7ECB631B00D35C7 CRC64;
     MAEQQKTNIK KPHGASLAQD LFKDMGLQVN EMSGGTEDQD ERVVEEIDSL CMNCHADGTT
     RLLLTKIPFF REIIVMSFSC PKCGFQNNEI QSAGQIQPKG AKYALRVERD VDLQRSVVKS
     DTCVFRIEDI DLEIPAGKGQ YTNVEGIIAG VKQDLESHQV ERMEQMPEVG EKVAGVIRTL
     ADMLEGQRYP FMVSVDDPSG NSWIEPKPGD AMGKWAKSEY NRTPAQNGLL GLGDDVPPPG
     HETHDHATSG PGRQPEYRPS GMVPQMPPDA TPANVDTEEI VENQVYSFPA SCPGCTRPCV
     TNMKMVNIPH FKQVVLMSTV CDHCGYRSNE VKTGGEVPER GRRITLEVKT QEDLARDILK
     SESAALACPE LQLRVEPGTM GGRFTTVEGI LTNIKRDLRA QAFGLDDGDA PLPEGAGDSM
     TQESKKSWDE FFESLTQAIK GEKPFSLVLE DPMASSYVQS LTAPDPDPQI KLEDYDRTDE
     EEEHLGLKDM KTEGYEEGAA H
//
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