ID A0A2C9V296_MANES Unreviewed; 1108 AA.
AC A0A2C9V296;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=V-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50892};
GN ORFNames=MANES_10G011200 {ECO:0000313|EMBL:OAY38396.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY38396.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY38396.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY38396.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL family.
CC {ECO:0000256|ARBA:ARBA00008070}.
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DR EMBL; CM004396; OAY38396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9V296; -.
DR STRING; 3983.A0A2C9V296; -.
DR EnsemblPlants; OAY38396; OAY38396; MANES_10G011200.
DR Gramene; OAY38396; OAY38396; MANES_10G011200.
DR Proteomes; UP000091857; Chromosome lg10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IEA:EnsemblPlants.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblPlants.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IEA:EnsemblPlants.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR CDD; cd15873; R-SNARE_STXBP5_6; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR042855; V_SNARE_CC.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR10241; LETHAL 2 GIANT LARVAE PROTEIN; 1.
DR PANTHER; PTHR10241:SF38; TRANSDUCIN FAMILY PROTEIN _ WD-40 REPEAT FAMILY PROTEIN; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU00290};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857}.
FT DOMAIN 1043..1107
FT /note="V-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50892"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 121788 MW; 46065DFD0DA0255C CRC64;
MLAKLFQKNN PQDPPSPKMV EGSVEKGVLR PQDINPRIDV HFGIPSTASI LAFDPIQSLL
AVGTLDGRIK VIGGDNIEGL LLSPKELPFK NLEFLQNQGF LVSITSENEI QVWDLEQRQL
ASTLKWESNL TALSVIGGSS YMYVGDEYGM VCVLKYDSEE GKLIQLPYYV PSDSIAEASG
MSSPYNHSVV GLLPQPASQG KRILIAYDDG LITIWDVSED KVILIKGNKD LQLKSKTLTD
FQKGMGQELC DDVSEDEHME KEISSLCWVS TDGTVLAVGY IDGDIMLWNL STMASNNKTE
KSSTDVVKLQ LSSVDRRLPV IVLHWSADSS HNNSCGRIFV YGGDAIGSEE VLTILSIDWS
SGIENLKCIG RIDLTLNGSF ADLALLQNDG ISKTRGAFIL TNPGQLHFYD DACFASLMSQ
QQKQNSVSSL EYPAVIPVLE PCMTVGKLGF ICRDEKFSKA FSKEAQTPRS TKWPLTGGIP
SQPLNVENYQ VERLYIAGYQ DGSVRIWDAT HPTFSLLYIL GTGVKGINIA GANASVSALE
FCPFTLSLAI GNELGMISLY KLMGSTDETH LYIVKETERE VHTLNKGDRP HCTAVFSFLN
SPISTLQFAN YGTRLAVGYH CGKVAMLDIS ALSVLFLTDS VSNSRSPVKS LAVTSMSDTI
SSKSNPEHIE SKSNADYVKW ELFATTKDAH FAIIDGNTGS LVCSQSLQPE KELSIISTHT
LDGGNLISRA SSKNDPLNSN QKNETKSEPD QGVTRSGSTP LEVDSETSPR TAYSRQRVEN
ILLLLCCEDA LHLYSMKSLK EGDINPIRKM NLLKPCCWTA TFKKDDKECG LIVLYHTGVV
EIRSLSDLEV VGESSLMSIL KWNYKTNMEK TMCSSDTAQI ILVNGCEFAS VSLLPCENIF
RIPESLPILH DKVLAAAAEA TVSLSPSQKK TQVSPSGILG GFIKGLQAGK GEQNVDLPEV
CNNNLAHLEI IFSSPPFLKP SLDITDNQKV LELNIDDIHI DEPLVVLPSS EMSKKDTKDK
GTERDRLFEG TTSDSKPRLR TAEEIKAKYR KEDASAAAAR ARDKLAERGE KLERLSLQTE
ELESGAQDFA SMAHELAKQM EKRKWWNI
//
