ID A0A167D272_9HYPO Unreviewed; 2036 AA.
AC A0A167D272;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=BBO_05218 {ECO:0000313|EMBL:OAA41859.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA41859.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA41859.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA41859.1,
RC ECO:0000313|Proteomes:UP000076863};
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 -!- 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}.
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:OAA41859.1}.
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DR EMBL; AZHA01000015; OAA41859.1; -; Genomic_DNA.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000076863; 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 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.
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}; Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1049..1167
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1221..1524
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1906..2036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..329
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..543
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..776
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..846
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1723..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1942
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2036 AA; 218317 MW; 92183EDF4E8C6013 CRC64;
MAEEASNSSW HPAKMPNSLE QRAALPKIDA ATEFHTRAAS EMAEEASNSS WHPAKMPNSL
EQSAALPKAD AAPDVDGHDL ATRSTMPDAT QSHDLDDAWM ADGGEEAVGD AWLMSEEPAT
QSLDLDAPQA APKQYTLENS PFAPENEAQK SQGPEDAHEA NSAAIDPFNT NEDEHEDADS
WFAEKPAQEQ LHTEAAPPPV TDNIELANAE EVKPMAEHQP AAEIQVAPES TELQTQEVEP
QSYIRPETEA AKQPDAELQE TQPLRKSLSQ HSSSMSFART VSHEISFNDD DDSDWTLSRS
NTDQFKFMPP TDRTNSFPPV PPAQSAEPLA PSKPLPSSQA LDVVEEVEKS SFTHDDSEES
KMFWENDSPA DNTHETFQTI GGDIGDAATE ASQSRFEEGL PLIPAAEEVE DGKPSKTTPF
DSFAEDDAGD DFFSTVRREE DSADLMQPIQ RKSTMQVIEN TFSREPSVQQ TAFDTLDEHS
EDFSEEDRHA RALANAFGAA ANDENQLDAA EPPADLSAKW QEAFGTGDDD DDFLLDDTGN
EDETIDTAGF LGSDDEGLLL DDEDDAPAAI ATNAPTTNPY MPTQAQTRPQ PVSAPTSSYG
YAAQPPQQTP YGSAFGYAPA APLRTDTPKA ESFADKAKGG YASPYDLPTD LVSMNIKPRK
RPSLPNPAQE TAPPSMSAPP RTANAYALPP GPVASAPPPA SGAAAQAPPA RSASRQESFF
EDLPVVAKPR PGSRQSLRAS SPSKQYGSPN SSSSTGPPPP AMHQQYQPPP MERPAAPENS
MPDLVAPPKV NPYAALQAGS APPSAPANNA TRYSPAPAQH QKGSSAPPPA APNRFSPVPP
LPRQNSSPPQ TTNASASQTY LPHLPRTSSP LAQFEVHHDK IAAGIDAVHL DRRASYNHEP
RLNRVSSLPP TREVDEEEES PARNQLGALQ QAPAVTARYN PAPQQTPVVP SSHLSSPQKR
QTSNYLPQAA LHQSNFAPPI RSQTQSPGAT RITHQHARPA SAHTNVAPTF GQTAQPTHAM
PVRTRGASLT MVSPTDGREN DPLQRWQGVP IISWGVGGAM VTSFPKSTPR YTMNQSAPTM
LRTPGEVKVK SMKDIEPLPE QLAKFPGPLR GKSKKKDALA WLSSGITALE RELPDLSSNP
QLSLEAKRSI ERLLLWKILR VFIEHDGHLE GSPAVEKAVR EVLSSQEAAD ASLSSGPRFG
QTAPSTGMKA DDVDSVSMES IKESLLQGDR ESAVWAAVDK RLWGHAMLIA HTTSPELYSR
VAQEFVRKEV NYPGHSNQSL GAFYKVLSGN FEDCVDELVP VHARAGLQLM STDSGLGTTQ
DVLSGLEKWK ETVSMVLSNR SENDIRGLNA LGKLLSDYGR AEAAQICFIF SRTISVFGGV
DDPNADFVLV GADHRKQPDQ FAKETEALQL SEVYEYGLTL SGAANLAAGA PHLAGYKLQH
ATVLAEHGYR DKALQYCDAI FTSMSAQTRR SPYHHPLLEA SVDDFMRRLK QAPKDDGSSW
MSKPSMNKVS DSMWNRFNKF VSGDEEGNGK AGADGEHGPF ARIASTPNIS RSPSVSNLET
YGTSPSYGVS ALPPQPTAAT SRYAPAMTPA ATTTQNPYEF VAQQPAPVPQ QASGRTSNEY
TPSPYEPAYP STNTGDSGYP GFNQSAPELS HQPSQPGAST YQPQVPSAAA QPYGLQPSPS
ITAEPNPNAN YGYQGYQPAG GYEPGKPAEA DAPKADCAVE SGYQPAPTQS YGLEPPSMQS
YGYEPPSTQF QSYESPSAQS QGYEPPSSQF QGYEPPQTQS YGYEPPSYQP DVSNDADNNT
LKPKKKSFMD DDDVPTPHVA DNKNKTDLDR ENEEMFKKVA EEEAKRATEA AAAKKSGGWG
FGGWFGASKK AELGSGEAQP QKAIKAKLGE SNSFVYDPDL KRWINKKAGA EQTEALKAAP
PPPRGSAPRS VSGTPPPSAM GPPMAAMARS ASTSNLKAGT MPPSGLGIST PPPMMRTDSI
ASAGGAPTPP SGPPSRPPTS ISNASSIDDL LGAAGPRKAS GKKPRKAGRY VDVMAK
//
