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Database: UniProt
Entry: A0A366R9C3_9HYPO
LinkDB: A0A366R9C3_9HYPO
Original site: A0A366R9C3_9HYPO 
ID   A0A366R9C3_9HYPO        Unreviewed;      1928 AA.
AC   A0A366R9C3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN   ORFNames=FIESC28_08334 {ECO:0000313|EMBL:RBR13148.1};
OS   Fusarium coffeatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR13148.1, ECO:0000313|Proteomes:UP000253153};
RN   [1] {ECO:0000313|EMBL:RBR13148.1, ECO:0000313|Proteomes:UP000253153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR13148.1,
RC   ECO:0000313|Proteomes:UP000253153};
RA   Gardiner D.M.;
RT   "Fusarium incarnatum-equiseti species complex species 28.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the initiation of assembly of the COPII coat
CC       required for the formation of transport vesicles from the endoplasmic
CC       reticulum (ER) and the selection of cargo molecules. Also involved in
CC       autophagy. {ECO:0000256|ARBA:ARBA00024687,
CC       ECO:0000256|RuleBase:RU364101}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. 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 SEC16 family.
CC       {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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:RBR13148.1}.
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DR   EMBL; QKXC01000188; RBR13148.1; -; Genomic_DNA.
DR   OrthoDB; 1361743at2759; -.
DR   Proteomes; UP000253153; Unassembled WGS sequence.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:UniProt.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd09233; ACE1-Sec16-like; 1.
DR   Gene3D; 1.25.40.1030; -; 1.
DR   InterPro; IPR024298; ACE1_Sec16_Sec31.
DR   InterPro; IPR024880; Sec16.
DR   InterPro; IPR024340; Sec16_CCD.
DR   InterPro; IPR024468; Sec16_N.
DR   PANTHER; PTHR13402; RGPR-RELATED; 1.
DR   PANTHER; PTHR13402:SF6; SECRETORY 16, ISOFORM I; 1.
DR   Pfam; PF12932; Sec16; 1.
DR   Pfam; PF12931; Sec16_C; 1.
DR   Pfam; PF12935; Sec16_N; 1.
PE   3: Inferred from homology;
KW   Autophagy {ECO:0000256|RuleBase:RU364101};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU364101};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|RuleBase:RU364101}; Membrane {ECO:0000256|RuleBase:RU364101};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU364101};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364101}.
FT   DOMAIN          269..477
FT                   /note="Sec16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12935"
FT   DOMAIN          974..1092
FT                   /note="Sec16 central conserved"
FT                   /evidence="ECO:0000259|Pfam:PF12932"
FT   DOMAIN          1152..1455
FT                   /note="Ancestral coatomer element 1 Sec16/Sec31"
FT                   /evidence="ECO:0000259|Pfam:PF12931"
FT   REGION          1..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1454..1928
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..130
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..376
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..481
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..700
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..796
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..839
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..855
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1475..1499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1520..1545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1554..1580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1682..1737
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1804..1849
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1873..1901
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1928 AA;  205104 MW;  97082531C0AFFAF4 CRC64;
     MSNDSDDSNS STEVPAPATS STTDTLAQHS QPTTQEDTPD APSQPDQETT EQSGAANAWL
     SQEAEDDDGN DWLASDDAVH KPTQQEETQS EATPEQAEPA QASTQPTDTE PVETEPVDTE
     QVDTEQVDPA PEDTEAVSQP KGPVSQHSSS RSFARTVSHE ISFGDDDEGE WNLSRTDTDP
     FKFMPPSDRT NSFPPVPPAH STTDAEDQQP LPTNQAMDVL EETEKEAEAE EELYQHEEAS
     EGLEAPKRRG HSSSISIGGD LKSPEGQDSD ERYEEGIPLI PQSAEETNEA TAVQENHPTA
     DPFDKEEGED GADFFSQIQG SEPVGEEQPV PTLERKSTMQ VLDSMNAGSV PKKSTLEGTP
     EEEEEDDSDS DDSEDKSEDE KAAQAESTPA ASEPAPAKQE DLASKWEQAF ADDEDDDDFL
     LDDNAGGDKQ VDPAAFFGSD DEGFLEDEEP AADSTPAPAP ASFPASHQPP APNPYMPQAP
     VIQQAPSPYA PVSQVPGVAV PPTPMYNSPA PGTAPFGSTP QYGQPPPVRP DMSKAQSFAD
     KSKGGYHSPY DLPTDLVTNV VKPRKRASMQ QLSQPNHPHA PVQAPPRSAS VGMPAPPTKL
     TPPSSSHGLP AQQAGPPNPT TSGAQHKENF FEELPMTSRP RPSSRTSQRA ASPARNAPPM
     ARTSHVPSPL APSFPNQMPP PSIPVMAPPP SEPYSEPPTQ APVPGAGLVA PERVSPYAAL
     TTSANHMPPP TSTSASRYSP APGTSHTAPP APVASRYSPA PPATKTHGSY GAVATSGPAP
     MLPHQPRTSS PLTHSETAHF EPRLSRVSSL PPTREVDEED DQQTQTRSVS ATLSPPPQES
     RYNPTSPPPP SYAGQLTLSP PKQSGPYAPH AAPTAHHGFV PPPRAQTQSP SAALGHRQAQ
     GSSDSTRRPS SAHSHSHPSP LAAKPAPSPY APAAPAAPAA GVSTVRTRGQ SITMNMIAPT
     DGREHDELQR WKGVPIISWG VGGTIVTSFP KSVPRYGMNQ AVPMIVRTPG EVKVQSVKDI
     EPLHEHVAKF PGPLRGKSKK KETISWLNAG IELLEKDLPD VSFHSQLSLE AKRAVERLLL
     WKIMRIFVEN DGALEGTPAV EAAVRDVLSP GENPSTTGDD AVFPAAGNFA AGIASVTSMQ
     ADGVDVSTMD QVRHHLLRGD RDKAVWALVD KRLWGHAMLI SHTVEGDLYK RVAQEFVRKE
     VNYPGHANES MAALYKILSG NFEDCVDELV PVHARAGLQL MSTDAGPGPT KDTLDGLDKW
     RETLSLVLSN RSTDDIQGLN ALGSLLSSYG RAEAAHICFI FGRHSSIFGG LDDPNANFVL
     IGADHRQQSD QFAKETEALQ LSEVYEYGLS LAGGALAAAG TPHLAAYKLE HAMTLAEYGH
     RDKAMQYCDA ILTAMSSQTK RSPYHHHVLE TAVEDFMSRL KSAPKEESGS WISKPSMNKV
     SDSMWNRFNK FVAGDDNEDN AGGAGEAGPF TRPSGEFSRS PSVSNFDIYG QQSPGFGMTP
     AQPPANAAAS KYAPATMTPA ANLNPYSPTS QYTPGRSSME QTPAEFGSNP YEPGYPGATS
     TSQGDSFTPS IPQPESNNPG VGGSIGLAPP AQITQSYSPA GYQPYGMPAS TPMGGDENPA
     DSSAQGFQPL SYGYEPPQMP SNPPEQESEK NNGEAHSGGY EPPSFQPHGY EPPSYEPQSI
     ADNDDEAPKP KKKSIMDDDD DDFPSMKSSE KSKADKDREN EEMFRKAAEE DAKRAAAQQS
     SKKGWGFGGW FGGSKKAALE PSSSGESSPG KPIRAKLGEA SSFVYDPDLK RWVNKKPGAE
     NTPAKTATPP PPKAGPRSVS GTPPPPTGTP PPPLITSNSA PPPLLPPKVR AGTPELMKQA
     STESLGLAPP AMARSVSNTS NASAPPSRPT TSMSNASSID DLLSAAPRKA SDKKKARKGG
     RYVDVMAK
//
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