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Database: UniProt
Entry: V5GIN7_KALBG
LinkDB: V5GIN7_KALBG
Original site: V5GIN7_KALBG 
ID   V5GIN7_KALBG            Unreviewed;       308 AA.
AC   V5GIN7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=CCCH-type Zn-finger protein {ECO:0000313|EMBL:EST05852.1};
GN   ORFNames=PSEUBRA_SCAF4g05003 {ECO:0000313|EMBL:EST05852.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST05852.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
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DR   EMBL; KI545884; EST05852.1; -; Genomic_DNA.
DR   RefSeq; XP_016290841.1; XM_016438384.1.
DR   AlphaFoldDB; V5GIN7; -.
DR   STRING; 1365824.V5GIN7; -.
DR   GeneID; 27421077; -.
DR   eggNOG; KOG0811; Eukaryota.
DR   HOGENOM; CLU_059257_2_0_1; -.
DR   OMA; KWCLYLL; -.
DR   OrthoDB; 2049889at2759; -.
DR   Proteomes; UP000019377; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd15840; SNARE_Qa; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 1.20.58.70; -; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957:SF38; LD27581P; 1.
DR   PANTHER; PTHR19957; SYNTAXIN; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF14523; Syntaxin_2; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        288..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          215..277
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  33410 MW;  94C141760C90E95C CRC64;
     MSFNDLERGS SSRGGGSGGS GGSRKTPLPL YRDEVSSALP PEFEKLSSKI GIQIFKINSN
     VTAIQKLITL SSSNASGKAG AQDWSKRIND LIETTRELVK DATADIKQLS TFPLGPANGG
     AKLTQGKLQR DFQAAALQFQ RVQKEAVAKT RAKLEQDKQK ERQMLKSRNS QQLLIDTEES
     DRSAAAIGGA EGGLQAESLD LLPEGPTQAD LEYQESLITS REAEIREIES GVQELNEIFR
     DLGNIVQEQG GMIDNIEFNI NSIAENTAGA DRELVVAHEY QRKAGRRCII LLLVVGFVVA
     VVLLAVLN
//
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