ID B5RTJ4_DEBHA Unreviewed; 1343 AA.
AC B5RTJ4;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=DEHA2D16720p {ECO:0000313|EMBL:CAR65679.1};
GN OrderedLocusNames=DEHA2D16720g {ECO:0000313|EMBL:CAR65679.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAR65679.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAR65679.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SIMILARITY: Belongs to the SEC3 family.
CC {ECO:0000256|ARBA:ARBA00006518}.
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DR EMBL; CR382136; CAR65679.1; -; Genomic_DNA.
DR RefSeq; XP_002770325.1; XM_002770279.1.
DR STRING; 284592.B5RTJ4; -.
DR GeneID; 8998540; -.
DR KEGG; dha:DEHA2D16720g; -.
DR VEuPathDB; FungiDB:DEHA2D16720g; -.
DR eggNOG; ENOG502QSCI; Eukaryota.
DR HOGENOM; CLU_002075_1_0_1; -.
DR InParanoid; B5RTJ4; -.
DR OMA; SFMRVFP; -.
DR OrthoDB; 1547052at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0000145; C:exocyst; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.90; -; 1.
DR InterPro; IPR028258; Sec3-PIP2_bind.
DR InterPro; IPR048628; Sec3_C.
DR InterPro; IPR019160; Sec3_CC.
DR PANTHER; PTHR16092:SF14; EXOCYST COMPLEX COMPONENT 1 ISOFORM X1; 1.
DR PANTHER; PTHR16092; SEC3/SYNTAXIN-RELATED; 1.
DR Pfam; PF15277; Sec3-PIP2_bind; 1.
DR Pfam; PF20654; Sec3_C-term; 1.
DR Pfam; PF09763; Sec3_CC; 1.
DR SMART; SM01313; Sec3-PIP2_bind; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 115..201
FT /note="Exocyst complex component Sec3 PIP2-binding N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01313"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1343 AA; 154792 MW; 1AE8965A152B602D CRC64;
MYPRGPNQNQ RPPESQRPAP SNQRPVAQSQ RAPFQQQRNQ FPPRNQASTS SHNGLEQQRR
SVADKLIADC YSKRIIDRSG KPCVETSYQT HVSIKEYSSF PSRPPPDNLP PNQIGTVKDR
VLVLCIKYSG RVLIQKGKYN ENKDVYQIGR TWDMDELKTI TKCGNDGIIL TLNKDYYWSI
EGGMERTWKF ARFLTNAYGG FMGRYPTLNG FSIEDFKLSS SPQKKHLGNS SPSMGANDSG
NDIVVNEPQP HPQLLKTKSL KRKNLPKPVL PPQPLPQQTY PDQGKQNDFY KDMDFTANGK
LPSKPMKVMQ VDRPSTSSLD QVENQNASTN RFNQSRELQE TNEEFVDNYV TVDDNEPSNV
PTTPKRDSKH PYQVNSPRRS ADTTQDSQNF VFHADNTYSP EKLREYVKTN EERSTSPLRN
YKPRRMSTEV EQRKVSEPLE SAAALGIQLE EQLDGVTNKD ISTDSAHSFQ IPARNVSPDY
SIEEVENDSD EEQETQHRAS MSERKQVPID QEESINQHQP PNAHVDNTIN SSIQDIENYM
DSQLYFAPGD ESVDNSKQIS QNQTLESDIS QREISEGNII PDLSQGNDSE FRSDQLEDET
TSMQEYTEQS EVGLNIDNKD SEFQREKDAE LEEIMDDVNW SISDNSDSLI RKLTKELNNV
KFRNVKDLVT LDFGKDSVSN DVTTSISEIE NLTHIFKKME IDFKFLGPEV NLIENNSKGL
QVKSVNKKLL YNDLSNILNK VSMHSDDLRA IESFKEFDRL NKLEAIEVKL IGLFNALETI
TLDYNENTDN LSSMRALRQY QSNYERVTSS FIRHFSRFIK DQFRLFSQQM MQNMDNIYPQ
AMFRELNNLL IYSGFLYFVK GVSLSDFQDI NGNFNLMMSD LLERMITHKL KNLKFSSSSV
SAHLSQSLDN DMPLKKSRTL RLSTRREKHI SKANQEEFQG LKQNKDSNEI DDPKAVVDII
NSTRDVIFVL QYVTGRLFHY DSNIIDFNEY CQNKPYQERR IALDNPSLDI EDDMNYSNDS
ISNLNAVFGG YINIFMKKVT PTELNIPLLL CYLQNLLDEN KKSNQEFLCF NFLKKASDKF
KIIWSKFIKS QLNLLNKSAI IAHCGILPAI KNVNQVLLIT ESSLDQPGRL FGSLDQSQVR
AMLAESYKEI SEATIHLFMR DDPLLKNHDF DDKEREHRNV SIIQNIFYLT EQLAVFSSPG
ITKMRTQLNS VFNKVLDSYF NKLLHKNIGK LVEFVDNYEA LVKMNNGKPK KYNKKYVKSL
LTGYTSKDVS VKAAEIHKKL EKHFITGGDM FEKDLFDKLW TDMEYQFIDY FSRLNNILKN
DFDREIDYAI TKQDIHSVFV SIH
//
