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Database: UniProt
Entry: T0KBF5_COLGC
LinkDB: T0KBF5_COLGC
Original site: T0KBF5_COLGC 
ID   T0KBF5_COLGC            Unreviewed;       395 AA.
AC   T0KBF5;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Emp24/gp25L/p24 family/GOLD {ECO:0000313|EMBL:EQB52692.1};
GN   ORFNames=CGLO_07674 {ECO:0000313|EMBL:EQB52692.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB52692.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC       {ECO:0000256|ARBA:ARBA00007104}.
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:EQB52692.1}.
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DR   EMBL; AMYD01001542; EQB52692.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0KBF5; -.
DR   STRING; 1237896.T0KBF5; -.
DR   HOGENOM; CLU_698310_0_0_1; -.
DR   OrthoDB; 601480at2759; -.
DR   Proteomes; UP000015530; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UP000015530};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
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..395
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004565885"
FT   TRANSMEM        180..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..115
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
FT   REGION          233..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   395 AA;  44111 MW;  A57178513F301657 CRC64;
     MRLSAVACGL FACFVSQVAA TALTYKIHAN EKACFYAKTQ KENEKVAFYF AVQSGGSFDI
     DYVVTGPGNK VILDGSKERQ GDFVFTAQQI GDYEFCFNNE MSTFAEKFVD FEIAVENEVR
     AQLPSKQGAS QEQHTTLEET IFKLSGQLST ISRGQKYFRT RENRNFSTVR STESRIINFS
     MIQCALIVLM GALQVFIVRF FFQGARKGYA PSKDVTSKAI FDWKKKQEEA YTQYATGSEE
     PESQREREEG VEDQGASSHS PTVSTLDSSQ PIRPPHRRKR LHSERLAEAH ENSQIEDSEE
     DEPDLSKRHC SEPPSLLSFG SEFDTDAASD ILLEAPSNIF VAIPSKVEFD PTEYLSVSGS
     QGSTSHGSQP ISTQEDEDNQ GLTPKNLNLL PQQSR
//
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