ID A0A120E7K6_9BASI Unreviewed; 1149 AA.
AC A0A120E7K6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN ORFNames=RHOSPDRAFT_18297 {ECO:0000313|EMBL:KWU44239.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44239.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU44239.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU44239.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ954481; KWU44239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A120E7K6; -.
DR STRING; 1305733.A0A120E7K6; -.
DR OrthoDB; 1429550at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd15849; SNARE_Sso1; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040525; UGGT_TRXL_4.
DR PANTHER; PTHR11226; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11226:SF0; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18403; Thioredoxin_15; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT DOMAIN 281..343
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 127355 MW; B44EA9BB24C44FF2 CRC64;
MSRDRLREAR VRPPSRSPRP LSPQQQGAYG AQQGYGQPQD GYGGGAGGGG YAPQQAQQYG
NQGGYGGYNP PPQQYAPPPP QQPQQQNQYS AIPVSYGNAA NDSYAMQTVN GNGNGTQSLI
GSDLGPFFAE VESIQDQIKQ LHQNINHVSE LHARRLASTD DMTQSTTGQQ LTQLTTQTTG
LTNSIRNRIT VLNDANRKSP QGDQGFNTRK LQIANLQNSF KRALEEYNLV EKRSREKYRD
RMARQIKIVK PDATDDEIRA AWDDSQGGAQ IFSQAGARAA FAEVQSRNQD LRKIEETITQ
LAQMMQDMAT LVLEQDESVR MIETQAVQVN SDVENGYVRT VHLLKPSIFY EFVHHLTEYK
IRPKLTFSNP IFSTGPRGEG GHSEPSRYAD HNPIFTRHCP ANDTNSVLEL SLWRSMLFRE
TGMWPSLRLA VAGNLAQDQV EEMYAFHDQR EAEVDKPENT VTNCTTWIDV GSTKVCDMKQ
FWTTIGNVQS RGRFPPPPSF LLTRTPSLLT FFLPDISAQP KVEAFDRLLP AVRNDSLPLV
VLYAAPTDEA FPKLFERLYA LASGTAPRLQ LAARWRPDPE NQIEGYRSSF RAEAMIKEGV
KVPEIQDARV FSDRAIAFVR GAKDKFAALT QVATQLPPVA EQILETPVRR SLPTTTTLTE
KFLVNGRAIA PEDLTYRGLL DIFSHDLRNL MGAQAATHGF WPNAAKQVIF RANTTLESPR
KSATSLAVPT VDRPLRFVFP TEAFKDTGYN FTRSSFIEGA TPETDASDEE GDPPALATFW
VVADLDSASG RKLVKNALRF ADQTTQVRFS FVHNPSESSP APHKFSLSRI IPELIANNMS
IAEVFPSELI AFLEYDATPE TPPRRALDDI WTSESPLTPY ITEGATNEAL AQEYWSLATP
FARNIGLQPG EAAVVLNGRT DRRPVDLQVI ELKGSEFAPG SFSALHQYEM KRRIKPVVDV
ANQNLPYKVK DDRKAKADLY AWSTAIVSAS VGERRWPSPE QVKGLATFTH GNSTNSLFDV
VAIVNPVSPF ARQVAPVLES LKAHQFVHQR IYLIPATESK LELTKLHARS FPLEINMDVD
QSERPPSAIF RGLPEGAVLD VKAFTLDGEE IAGPGGLGGE SVRAPGKVRF GIVGSGEVPE
SHEHVRDEL
//