ID A0A1R3GGE8_COCAP Unreviewed; 1931 AA.
AC A0A1R3GGE8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE AltName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00032165};
GN ORFNames=CCACVL1_25939 {ECO:0000313|EMBL:OMO57178.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO57178.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO57178.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO57178.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000192};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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:OMO57178.1}.
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DR EMBL; AWWV01014411; OMO57178.1; -; Genomic_DNA.
DR STRING; 210143.A0A1R3GGE8; -.
DR EnsemblPlants; OMO57178; OMO57178; CCACVL1_25939.
DR Gramene; OMO57178; OMO57178; CCACVL1_25939.
DR OMA; ENEPMHQ; -.
DR OrthoDB; 211713at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 1.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF29; 1,3-BETA-GLUCAN SYNTHASE COMPONENT FKS1-RELATED; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
DR Pfam; PF04652; Vta1; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OMO57178.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 487..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1498..1521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1665..1686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1737..1755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1775..1795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1815..1833
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1839..1860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1880..1900
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..442
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1931 AA; 221263 MW; 0FE8307E51CF763C CRC64;
MTNPESAGHS SSGPPGLTRR PSRSAATTTF SMEVFDNEVV PSSLSSIAPI LRIAKEIEHE
RPRVAYLCRF YAFEKAHRLD PSSSGRGVRQ FKTGLLQRLE RDNASSLASR VKKTDAREIE
SYYQQYYEHY VRALDQGDQA DRAQLGKAYQ TAGVLFEVLC AVNKTEKVEE VAPEIIAAAR
DVQEKKEIYT PYNILPLDAA GASQSIMQLE EVKAAVGALG NNRGLNWPAA FEPQRQKSGD
LDILDWLRAM FGFQRDNVRN MREHLILLLA NNHIRLHPKP EPLNKLDERA IDAVMSKLFK
NYKTWCKFLG RKHSLRLPQG SQEIQQRKIL YMGLYLLIWG EAANVRFLPE CLCYIFHNMA
YELHGLLAGN VSIVTGENIK PSYGGDDEAF LRKVITPLYG VIAKEAEKCQ NGKASHSEWC
NYDDLNEYFW SPECFSLGWP MRDDGDFFKS TIDKGKKTSQ RKSGSTGKSN FVEIRSFWHL
FRSFDRLWTF YVLALQVLII LAWTEASIKE IFQKKTLYYV SSIFITAAIL RFLQSVLDLV
LNFPGYHRWK FTDVLRNILK IIVSLAWAII LPLFYVHALS FAPDKLKDVL SFLHQVKGIS
PLYILAVALY LLPNLLAAAL FIFPMLRRWI ENSDWLIIRF LLWWSQPRIY VGRGMHDSQF
ALIKYTLFWI LLLCAKFAFS YFVQIKPLVK PTKAIMGIRH ITYAWHEFFP NAEHNYGAVI
TLWAPVITIY FMDTQIWYSI FSTICGGISG AFDRLGEIRT LGMLRSRFQS LPGAFNACLV
PSDKSRKRGF SLSKRFAEVT ASRRSEAAKF AQLWNEVISS FREEDLISDR EMDLLLVPYT
SDPSLKIIQW PPFLLASKIP IALDMAVQFR SKDADLWKRI CADEYMKCAV IECYESFKMV
LNTLVVGENE KRTIGIIIKE IESNIAKNTL LANFRMVSLP VLCKKFVDFV GILKDGDPSK
QNAVVFLLQD MLEVVTRDMM VTEIRELVEL GQSNKESGRQ LFAGTGEKPA IVFPPVLRAQ
WEEQVYIIIN LIIYIDKNPN FKESATDVPT NLEARRRIAF FANSLFMDMP RAPRVRNMLS
FSVLTPYYSE ETVYAKSDLE MENEDGVSIL YYLQKIYPDE WNNFMERINC EKDDEIWDKD
EDILQLRHWV SLRGQTLCRT VRGMMYYRRA LKVQAFLDMA TEKEILAGYK SICTPSDEDK
KSQRSLYAQL EAVADLKFTY VATCQNYGNQ KRSGDRHATN ILNLLVNNPS LRVAYIDEVE
EREGGRSQKV YYSVLVKGVD HLDQEIYRIK LPGTAKLGEG KPENQNHAIV FTRGEALQTI
DMNQDNYLEE AFKMRNLLEE FNEDHGVRPP TILGVREHIF TGSVSSLAWF MSNQETSFVT
IGQRVLARPL KVRFHYGHPD VFDRIFHITR GGISKASRGI NLSEDIFAGF NSTLRRGNIT
HHEYIQVGKG RDVGLNQISL FEAKVACGNG EQILSRDIYR LGHRFDFFRM LSCYFTTVGF
YVSSMMVVIT VYLFLYGRLY LSLSGLEESI VKFASSKGET ALKSAMASQT VVQLGLLTAL
PMVMEIGLER GFRTALGDII IMQLQLAAVF FTFSLGTRTH YFGRTVLHGG AKYRATGRGF
VVRHEKFAEN YRMYSRSHFT KALEILILLI CYRIYGSAAT DNVSFALLSF SMWFLVVSWL
FAPFLLNPSG FEWQKIVEDW DDWAKWISSR GGIGVPSNKS WESWWNEEQE HLQHTGLMGR
LVEILLSLRF FIYQYGIVYH LNMTEKSRPG LRHSLVVYGL SWLVIVAVMV VLKIVSMGRK
TFSADFQLMF RILKLFLFIG FVVLIAMLFY FLDFTVGDIF QSLLAFMPTG WALLQISQAI
QPIVKGIGMW GSVKALARGY EYMMGAILFG PIAILAWFPF VSEFQSRLLF NQAFSRGLQI
QRILAGTKKN T
//
