ID A0A2H9THM0_9FUNG Unreviewed; 1378 AA.
AC A0A2H9THM0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=PSACC_02936 {ECO:0000313|EMBL:PJF17254.1};
OS Paramicrosporidium saccamoebae.
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Paramicrosporidium.
OX NCBI_TaxID=1246581 {ECO:0000313|EMBL:PJF17254.1, ECO:0000313|Proteomes:UP000240830};
RN [1] {ECO:0000313|EMBL:PJF17254.1, ECO:0000313|Proteomes:UP000240830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSL3 {ECO:0000313|EMBL:PJF17254.1,
RC ECO:0000313|Proteomes:UP000240830};
RA Quandt C.A., Beaudet D., Corsaro D., Michel R., Corradi N., James T.;
RT "The genome of Paramicrosporidium saccamoebae is the missing link in
RT understanding Cryptomycota and Microsporidia evolution.";
RL Submitted (OCT-2016) 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|RuleBase:RU364101}.
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:PJF17254.1}.
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DR EMBL; MTSL01000182; PJF17254.1; -; Genomic_DNA.
DR STRING; 1246581.A0A2H9THM0; -.
DR Proteomes; UP000240830; 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; 1.20.58.940; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000240830};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 327..409
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 481..529
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT DOMAIN 534..689
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 731..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 149840 MW; 5B693AB6EB3E35C0 CRC64;
MVASEPPAPH YPPAMPTRRE ELQPAVGQFF GAPESVPDGK TIRVAPQASA TRQTVHAADA
PGWFGAESGT DVFASIAASQ PPVTQNPSVQ PVQQPSLQFS MPAQNSHASR GSFSSPNVPK
IQSSVEAVPY SGFKYEETNF IGDETFEQLS ISGSISAFGD IPPGSVACHR CNRPNDQSST
FCTRCGFQLV KPSGGFFTQS AYAQPPNTQP PMGGQFSNPP PIAPYSGDVV PLTRTGTLDS
MVSGRFSQAP SSFTVQPSVG MASSASFGRA APPSAPLVSH AFPPPQMIPP TSFRSFSPPQ
PAQMPFVLQP VAVEEPVKSQ KEQRVYPVFC FGFGGQVFAT FPMKQMRFMA NSSTGTAHYR
PSVMYRTAVH TLPFIQEKLV QPILDSLNGL PMSEKYVKTK DVIKYIKDTW IDGASPSRDY
REVFYKLVDL MLSNKGGLSD AGEEALRKIL LPDSLAEKSE VSSPTTMSAA PVSPAVVNEL
TKLLIKGDRG NAVLLAVTNQ MWTHALLIAS HVDRDTYCSV VSEFAKQTLP MGTADDYIAI
TGLGDALLSA GEVFAAHICY LLSDDASLIS GVDSPQSRMV YAGCAHGNKM ETFYRDWSAL
RRTELLELAF TLASNGQYCM HHLQAYKLLY SRYLSDLGLN SLALKYCDSV GSIVRTFGST
SPYLHKEFIS QLKQFEERVY RHTGEVPSSP VGDGSWFKMG GLLEAFDRGI TRVMGVSNQD
VDITEVKEER PRRLSVQAET NLGPTVTEAP PIPMFSGTEM TAGELGHQPP VSYYQPPPVT
SQYSQPQQQQ WADPNQQQPF VSNHTHYDNF NPQQSTRQYS APSQNQESYQ QASGDYSNSV
QSQTQRPLEE MMQTHSINDK GHDFSKPPQT QGHDQSVSFA SPPQSHLGVQ SHPVTHQHEQ
ERELVPVIPV QKFSSPTEPH SQGKASTMRA DFDSTFSAPP VGAPAQPLYA APTNFPAPET
FAVAPPTMPA MTETRPSGEA SFLPPVPMMP NMPAEAPYSH QAPPMHTVPA VDTTRTQFKP
SSPPADVAQT QFKSSDPAVD VTRTQFKPSD PAGGATFAHQ PPTVPVSGAL HQAPSVTAAP
SFPPAFAEAQ PMIFAGPQKS PPHPMMSASQ DYSTHPPSFS QPPVQSHQLD DDLGFGNTTK
LSPNKPEGQQ PAIQDEDQQQ DKKGMLGFIS GWFGRKTPTD QPGGPKQASL GEPSSFKYDE
TLKRWIDTKD PGSTAAAVAP PPPPAMAAAP SMNPMSSDGP VSFRRGATRS AKSRYIDPFN
ADDGEAPPVI PTVPLPGSIA PLATETAPPQ QQWTDPNQQQ QWADPNQQQQ QEWTNPNQQQ
QWVDPNQQTQ WAQTHDAHSQ QQWVDPNQQA QWSQAHEAHS QQQWAHPPQQ QSYGQGAF
//
