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Database: UniProt
Entry: A0A150VFL6_9PEZI
LinkDB: A0A150VFL6_9PEZI
Original site: A0A150VFL6_9PEZI 
ID   A0A150VFL6_9PEZI        Unreviewed;       417 AA.
AC   A0A150VFL6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN   ORFNames=M433DRAFT_21429 {ECO:0000313|EMBL:KYG49358.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG49358.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG49358.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG49358.1,
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:KYG49358.1}.
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DR   EMBL; JPDO01000025; KYG49358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150VFL6; -.
DR   STRING; 766039.A0A150VFL6; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR46156; CCCH ZINGC FINGER; 1.
DR   PANTHER; PTHR46156:SF1; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF00642; zf-CCCH; 2.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; CCCH zinc finger; 2.
DR   PROSITE; PS50103; ZF_C3H1; 3.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          244..272
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          273..299
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   DOMAIN          300..328
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         244..272
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         273..299
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   ZN_FING         300..328
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ   SEQUENCE   417 AA;  46864 MW;  80E5EFBBF1DFB6D9 CRC64;
     MTEQADLQAK IAELAGRINL HKQQKQQQQY FGNGRWYPYA RSGRGTYTPT HKNRTLVLNG
     TVTPPGNVLT SGGGTHQIMN KDTYDRELRH KLEYIEQQHN AKRRKRNVEE QHRILHHFAA
     PQQASRELVI NGIRFTLTHD GSKLTRMPDA ATAGLETPKK TKVADVEFYR TKHGNLVRAS
     ALNTSARNHI KQAPQCEHFT RHGTDPPFPE VVGFAQAQTL RSHHLKPLAG SCPYGARCHF
     NHDPVKVAIC KDFAKKGQCH RGANCDLSHE MTYHRVPACI YFLRGNCTNA ACRYPHVQVS
     SAAPVCRAFA TLGYCAKGTD CDKRHVVECP DYANRGFCAN LENGRCTLPH PERAAVLRKA
     VERQAKIDSD LGSDLSSDEE DVTNLEDVDS DQEDILMTGM GDDKHELSQQ HDYVAFY
//
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