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Database: UniProt
Entry: A0A0G4E9F0_VITBC
LinkDB: A0A0G4E9F0_VITBC
Original site: A0A0G4E9F0_VITBC 
ID   A0A0G4E9F0_VITBC        Unreviewed;      2688 AA.
AC   A0A0G4E9F0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   28-JUN-2023, entry version 25.
DE   RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE            EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN   ORFNames=Vbra_4667 {ECO:0000313|EMBL:CEL92502.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEL92502.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEL92502.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC       {ECO:0000256|ARBA:ARBA00009040}.
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DR   EMBL; CDMY01000086; CEL92502.1; -; Genomic_DNA.
DR   STRING; 1169540.A0A0G4E9F0; -.
DR   VEuPathDB; CryptoDB:Vbra_4667; -.
DR   InParanoid; A0A0G4E9F0; -.
DR   OrthoDB; 211713at2759; -.
DR   PhylomeDB; A0A0G4E9F0; -.
DR   Proteomes; UP000041254; 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   InterPro; IPR026899; FKS1-like_dom1.
DR   InterPro; IPR003440; Glyco_trans_48.
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; 1.
DR   SMART; SM01205; FKS1_dom1; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        388..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        463..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        501..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        557..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        612..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        640..660
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1910..1933
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1939..1958
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1970..1988
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2053..2074
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2086..2103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2208..2226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2255..2276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2288..2313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2325..2347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          240..335
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
FT   REGION          195..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1243..1339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2382..2421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2453..2555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2608..2636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2669..2688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..870
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1283..1314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2391..2417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2479..2499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2688 AA;  303937 MW;  5B040933710D80A8 CRC64;
     MAQKKVVQQV PPGSWLTWPE SETTKRNVID LFDGHLLSEG LPLVLKNDPK ATRTQLNEYE
     TIIRNILRLF RTGGPGSDGP SRGTVGEKEC GPVSYGGRVG GFTSGTTVFD EIVHKYRLQE
     DNCLNQYEDI VYSLMAIALR DYPPTNETTR AMKERGFSRL EEYALYRFHW KLFKNYRRWC
     QYVDVRPFPW GESKATTAKP ATKGAATGTQ QGASGGASGS MAAYLKEKEK MRKNPKTSLM
     LMAREVALWK LMWGESANLR HCPELLLFVF HWMMKSWDDV DPTKMPTYVE TITPVINEFW
     EEMRRASGDH PVKMNYEDFN EIFHKAPVVH RWLGGVGERG RGGTWRGNFM EMIKAETTSH
     QFLSLQPPKG RKKTYIEQRS YLHFFRTWWR YYQFNLVTLF ISLAYGAQNR GWDATGWWGM
     VTVCAATGSA VREMFDLFFY WLAPIPLLQR CYDAMEGMKR LNWWARQIMA GIRWALFLAA
     VYVSRSSPLG CSDPALQPSG YVGGACFMFY VLHGLSYFLI RVRKTLPCWQ NGPPTWNTHA
     TFQGNATMLS DEYKHMFGYA LFWMPVLCFK WWIGYHVFVR AFLDLLLPMN QSGSDPIRYD
     FLGYEINDRV KVTLYVFWIS PCMVLYFYDI MFYFSVFQSF VSWCIGWFRG IGFITDLSVI
     QKVFPLLPLQ YDRVLSTDAG GTVRKLKLAT TSSPKTLGWD WLVSVITCNM CCGVFQRKIR
     RKVKPTSYYM SHSRPHYALP LRAPSRTCSR QSKASCTSKK RGPLTKKATY SSLASDGTDS
     LTTVLLRHVP VSPRASHLMR TTANGSSTAP RRGLSLLHGQ ASNEGDSSVS PKASTADKTP
     PSDAGGGDGT VPLLQKSSTS SKSPGAVEQG QGSGVFSPGG ARLSKGGGSS GSDKGKGKRG
     FFLMDGSGSG WVSWWIREIS AVYDHVIPPA TVENQIRRFG FLWNEVLESW REEDLIDNTE
     RCKLQFNELP AIHFKDLSDL NMAFSDCEGS SLRVSWDASD IRHPVWVYCD VLKSFTRECE
     AHQTRVNEIW ENLRDHHRFS KESHHYLHEV LKLPPPTSTP SRLRWPGPTV NHKAKASLHQ
     VGHDFVKKLF GNTRAAVGDP RSDSHQLLLR MALLEIYEAL CLYLTRFFPD GHTLTLRLSA
     VMQRVASHPF CLCLLNLAAV KDLQATLATT FAAAQGDNAA AIEENGVRLL KALQKMALPA
     LFHTPGSSVL ASKGMKQHFP ELVDFLEALS ETTAARQSLK SMVASPLLSS RPPDRDNSSK
     ADTPAVSSTH PHSDPASPPC FTTPHGTPSF GSSRHTTMCE DDTPASSIQS IRDPRVSGPS
     AAAHRRQRPP LPPGGVGGGP GTMWMRMDLA AEVAYCDKLW RLEELQEGVC SNDQLTVSEA
     LKPFFRRSNR ILTAKGHVLK TALAQARLKY FSSSLFMEMP EAPSVQRMVS MCTFTPTYTE
     DAMLDASMLN EKTMEGVRQF DFLRTMYCQE WANFLERMDP QGVRYDWYQH SLAHKNVLSK
     STNIMAAKFE KDIEEWASER TQTLWRTLKS VMYYEQACRM LAWMELQEQR GETAHLCHDR
     NMLSFEQNDR LNWTLVPVQP DSPKKLQVFL RYWERCRERR KVLDNRPYDN DPVAKALATL
     RFQYVLTAQT LGDDLKAPSS NRVATLRVRC VTEMCKRYPS MRVAAIESCD IRLPGSNKPK
     SVKCSVLYKW DVGQQKLVRV YRVVLGLLEG ACGARNPIVG EGKSENQNHA IIFTRGETIQ
     AIDMNQEMYL EEALKLRNLL QEFAKDTKMA IMGFREHAFL PGAVTPSYLS NVQQTCFTAF
     DARAFHMPMR IRFHYGHPDV LDRYLVKTMG GMSRGSAIIN VTEDVYCGMN YVQRGYSSAQ
     VDYIMCSKGW PNDLDQVVAF MRKIATGSAE AQAASRDAYR MAYGMDFFRL LSLFVAFPGW
     NILNPLVFLS IWLFMYGRIV LSAFSSAIPV LLQPFLVSEE LNAVTIMDRV WLLLFAISYL
     KFGAMVALEE GLAGGIRHMW HHIRALSPLH YTFTIGTWLG SFDETVLFGR AKYQSAGRGF
     NINHKTFVHL WKAYFYSHFQ LAMELLLLLF YLRFLQDLQP MVAIRCWWFI LVPVSFLYVP
     HLYNPMGLAW SRLTSDFTGW SRWLRSNNNH DVEESWYAWW KQQMEFRNGA SPLNKIIILT
     RELRFLLLGL CIAKAANWHW YHLVTSPGGA GWSWAWESIR DLVERSPLLA PAVFTALVVL
     VMGLSTHNQD YHPSLHTRRG QIGFMSGLSN AGSRFFTLLT RIGAFALIVL FLYNLITDTT
     YRLSFGTIVG GMVACLLAFL SITTVLAECF GFVEWSPVVE THRLWHFLLG ALQLAPLIAL
     AALKYVFNTS ELQTYYLLNS YGVARSQLHM GHVRKMLQKI RMEQKHHSKP QQHQQQQPGT
     PVNNASNNNN TPVQTPKSDA GREMAMDGVC DDQQSESRMQ TPIAIRYQYS SSSPVPTAIT
     CDSEAVPDVP DDPQVRTPLP DTDTPQNNVS GQDDTPQTAA GEPQLAPDEP ETYVDQPQPR
     SPEAAVDAPV DAPPEADPDV ETQAAPAPPA EGGGMVVEDM SLVIADRGEA DGACVDDHDL
     DRHSVASSIT SDGDLMSSKQ SDMFGDLFEE EDEDEDEETL HDPAVPPNDG LARESPEALV
     AGMIGRERER RAAERARQEE AIERVMREAR ERREREGPES DEERHWFT
//
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