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Database: UniProt
Entry: A0A162KJ31_CORDF
LinkDB: A0A162KJ31_CORDF
Original site: A0A162KJ31_CORDF 
ID   A0A162KJ31_CORDF        Unreviewed;       210 AA.
AC   A0A162KJ31;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Erp2,4 {ECO:0000313|EMBL:OAA75658.1};
GN   ORFNames=LEL_07646 {ECO:0000313|EMBL:OAA75658.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA75658.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA75658.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA75658.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(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:OAA75658.1}.
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DR   EMBL; AZHF01000005; OAA75658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162KJ31; -.
DR   STRING; 1081108.A0A162KJ31; -.
DR   OrthoDB; 601480at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR015720; Emp24-like.
DR   InterPro; IPR009038; GOLD_dom.
DR   InterPro; IPR036598; GOLD_dom_sf.
DR   PANTHER; PTHR22811:SF50; RE49489P; 1.
DR   PANTHER; PTHR22811; TRANSMEMBRANE EMP24 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01105; EMP24_GP25L; 1.
DR   SMART; SM01190; EMP24_GP25L; 1.
DR   SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 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:UP000076881};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..210
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007836580"
FT   TRANSMEM        181..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..115
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
SQ   SEQUENCE   210 AA;  23558 MW;  3DEBA23C58BD0D1D CRC64;
     MKFSTLLTGA VALFSSEVIA TSLTYRVEAH ERACFYANTK NANEKIAFYF AVQSGGSFDI
     DYEVTSPTSK VIMSGEKERQ GDFAFTAQTA GDYAFCFSNQ MSTFAEKFVD IEISVENEAR
     AELPSKQGSS PEQTNVLEES VYKISGQLST ISRNQKYFRT RENRNFATVM STENRIVNFS
     MIQSFLVVCM GGLQVFVVRF FFQGARKGYV
//
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