ID A0A150VII5_9PEZI Unreviewed; 222 AA.
AC A0A150VII5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=GOLD domain-containing protein {ECO:0000259|PROSITE:PS50866};
GN ORFNames=M433DRAFT_401 {ECO:0000313|EMBL:KYG50310.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG50310.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG50310.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG50310.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU003827}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003827}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC {ECO:0000256|ARBA:ARBA00007104, ECO:0000256|RuleBase:RU003827}.
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:KYG50310.1}.
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DR EMBL; JPDO01000006; KYG50310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VII5; -.
DR STRING; 766039.A0A150VII5; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR PANTHER; PTHR22811; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22811:SF159; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003827};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..222
FT /note="GOLD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007571635"
FT TRANSMEM 190..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..132
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
SQ SEQUENCE 222 AA; 25244 MW; 1077664E44928A1A CRC64;
MWSLILLAGL ALLTSQARAL YFYIDGPTQK CFFEELPKDT MVVGSYKATQ WNEQSRSYVQ
NHEMGIYITV DETFDNDHRI VAQRGASVGK FTFSAADSGN HRLCFTPTNV PSTSGFLFSG
SQVGGIKFEL DMAIGETSAI ESSDKDKLSE VVQKVRDINA RLQDVRREQI FQREREAEFR
DQSEAVNARV VRWTLVQLFV LGITCAWQLS YLRAFFIKQK LT
//
