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Database: UniProt
Entry: A0A3M7MCR6_9PLEO
LinkDB: A0A3M7MCR6_9PLEO
Original site: A0A3M7MCR6_9PLEO 
ID   A0A3M7MCR6_9PLEO        Unreviewed;       991 AA.
AC   A0A3M7MCR6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Coatomer subunit gamma {ECO:0000256|PIRNR:PIRNR037093};
GN   ORFNames=GMOD_00007327 {ECO:0000313|EMBL:RMZ72306.1};
OS   Pyrenophora seminiperda CCB06.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=1302712 {ECO:0000313|EMBL:RMZ72306.1, ECO:0000313|Proteomes:UP000265663};
RN   [1] {ECO:0000313|EMBL:RMZ72306.1, ECO:0000313|Proteomes:UP000265663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB06 {ECO:0000313|EMBL:RMZ72306.1,
RC   ECO:0000313|Proteomes:UP000265663};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:RMZ72306.1};
RX   PubMed=24475219; DOI=10.1371/journal.pone.0087045;
RA   Soliai M.M., Meyer S.E., Udall J.A., Elzinga D.E., Hermansen R.A.,
RA   Bodily P.M., Hart A.A., Coleman C.E.;
RT   "De novo Genome Assembly of the Fungal Plant Pathogen Pyrenophora
RT   semeniperda.";
RL   PLoS ONE 9:E87045-E87045(2014).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC       dilysine motifs and reversibly associates with Golgi non-clathrin-
CC       coated vesicles, which further mediate biosynthetic protein transport
CC       from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC       complex is required for budding from Golgi membranes, and is essential
CC       for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
CC       {ECO:0000256|PIRNR:PIRNR037093}.
CC   -!- SUBUNIT: Oligomeric complex. {ECO:0000256|PIRNR:PIRNR037093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037093}. Golgi
CC       apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR037093};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255,
CC       ECO:0000256|PIRNR:PIRNR037093}. Cytoplasmic vesicle, COPI-coated
CC       vesicle membrane {ECO:0000256|PIRNR:PIRNR037093}; Peripheral membrane
CC       protein {ECO:0000256|PIRNR:PIRNR037093}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR037093}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the COPG family. {ECO:0000256|ARBA:ARBA00010720,
CC       ECO:0000256|PIRNR:PIRNR037093}.
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DR   EMBL; KE747829; RMZ72306.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M7MCR6; -.
DR   Proteomes; UP000265663; Unassembled WGS sequence.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1480; Coatomer, gamma subunit, appendage domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   Gene3D; 3.30.310.10; TATA-Binding Protein; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR   InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR   InterPro; IPR032154; Coatomer_g_Cpla.
DR   InterPro; IPR017106; Coatomer_gsu.
DR   InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR   InterPro; IPR037067; Coatomer_gsu_app_sf.
DR   InterPro; IPR012295; TBP_dom_sf.
DR   PANTHER; PTHR10261; COATOMER SUBUNIT GAMMA; 1.
DR   PANTHER; PTHR10261:SF0; COATOMER SUBUNIT GAMMA-2; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF16381; Coatomer_g_Cpla; 1.
DR   Pfam; PF08752; COP-gamma_platf; 1.
DR   PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR   SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR037093};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|PIRNR:PIRNR037093};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|PIRNR:PIRNR037093};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|PIRNR:PIRNR037093};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037093};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|PIRNR:PIRNR037093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265663};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037093}.
FT   DOMAIN          93..630
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   DOMAIN          724..876
FT                   /note="Coatomer gamma subunit appendage Ig-like subdomain"
FT                   /evidence="ECO:0000259|Pfam:PF08752"
FT   DOMAIN          878..990
FT                   /note="Coatomer subunit gamma C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16381"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   991 AA;  108118 MW;  FB3609B83BD610C8 CRC64;
     MSRASDSDGT VPYRSGRQSL EYPHHMQLEF PGAKTWDHAR AAHTATSDMP AGWHPDTFTA
     HAVAKGHHAV LHPNTMDKKH EDAGGVAQID KTSVFQEARV FNQSPISPRK CRVILTKLAL
     LLFTGESWGR QEATTLFFGI SKLFQNKDAS LRQMVYLVIK ELAGSADDVI MVTSSIMKDT
     SVGSDVVYRP NAIRALCRVI DASTVQAIER LVKTCIVDKN PSVASAALVS SYHLLPVAKD
     VVRRWQSEAA EAASGSKSGG GFLGGFGGGS HTTLQASTNY MTQYHAIGLL YQMRSGDRMS
     LVKMVQQYSA AGVVKSPAAT VLLVRLAAKL AEDDPNLRKP MMQLLDGWLR HKSEMVNFEA
     AKAITDMRDV TDAELVQAVH VLQLFLTSPR AVTKFAALRI LSQMASFKPD AVRSCNQDIE
     SLITNSNRSI ATFAITTLLK TGNESSVDRL MKQITGFMAE ITDEFKVTIV EAVRTLALKF
     KAKQSGFLAF LSGILRDEGG YEFKRAVVEA IMDLIRFVPE AKEDALATLC EFIEDCEFTK
     LAVRILFVLG REGPSTPHPT KYIRYIYNRV VLENAIVRAA ATSALAKFGV GQKDPEIKKS
     VHVLLTRCLD DVDDEVRDRA ALNLRLMDQG DDDMAISFIR NDSMFSLPVL EHQLAMYVSS
     DSRDTFETAF DITKIPTVSR EQADAADLTK KTEGATPTLK APSAAKAPSK AGADAAASAA
     NNAQKYAAEL QKIPELAAHG GVLKSSNPVE LTESETEYVV TAIKHIFKDH IVLQYDIKNT
     LDDAVLIDVE MVVTPEDDGD VQLEEEFVIP APKLTTNEPG TVYVSFKRLE TESQFISASF
     TNVLKFTSKE IDPSTNEPEE GDGYPDEYAV EDLYLTGADY VVPAYAGSFD NVWDQSNGDS
     ATETLQLGNM KSIADATEQL TKTLSFQPLE GTDVALSAST HTLKLYGKTI TGGKVAAMVR
     MAFSAKTGVT MKIDVRSEEE GVAALVVSSV S
//
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