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Database: UniProt
Entry: D8SPY8_SELML
LinkDB: D8SPY8_SELML
Original site: D8SPY8_SELML 
ID   D8SPY8_SELML            Unreviewed;      1915 AA.
AC   D8SPY8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
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=SELMODRAFT_157296 {ECO:0000313|EMBL:EFJ13500.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ13500.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
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}.
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DR   EMBL; GL377632; EFJ13500.1; -; Genomic_DNA.
DR   RefSeq; XP_002985370.1; XM_002985324.1.
DR   STRING; 88036.D8SPY8; -.
DR   EnsemblPlants; EFJ13500; EFJ13500; SELMODRAFT_157296.
DR   Gramene; EFJ13500; EFJ13500; SELMODRAFT_157296.
DR   KEGG; smo:SELMODRAFT_157296; -.
DR   eggNOG; KOG0916; Eukaryota.
DR   HOGENOM; CLU_000742_1_1_1; -.
DR   InParanoid; D8SPY8; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
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; 1.
DR   Pfam; PF04652; Vta1; 1.
DR   SMART; SM01205; FKS1_dom1; 1.
PE   3: Inferred from homology;
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:UP000001514};
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        467..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        504..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        538..560
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        580..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        642..663
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        716..735
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1484..1507
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1527..1549
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1561..1581
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1648..1667
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1756..1776
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1796..1814
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1820..1840
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1861..1881
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          299..416
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
SQ   SEQUENCE   1915 AA;  221071 MW;  01F1DCAD55CFD5DE CRC64;
     MTTRLPRTFT TGTFPTEFDS EVVPSSLGPI AAILRVANEV ELDSQRVAYL CRFYAFERAH
     YDDPSSSGRG VRQFKTALLQ RLEKDEEPSR LARRARSDAR EMQQFYQNYY DKYVKALEAD
     HQDRASLAKA YQTAGILFDV LTSVTRQDGA EVDSEMQAMN TDVTKKKKDI KHYNILPLDA
     AGASQAIMKL EEVRAAHDAI ANVRGLPKRK EAPSDILEWL QVMFGFQKDN VANQREHLIL
     LLANVHVSLD PEPSPLYKLD QRATEIVMKR MFKNYRTWCK FLGRSDKLEL PEIQLEVQQR
     MILYMALYLL IWGEAANVRF MPECLCYIFH HMASELSGML SGRVSYVTGE NIKPAYGSED
     EAFLKKVVTP IYNVIFKKES NRNESGGKPH SSWRNYDDLN EYFWSKTCFR LGWPMRKDDE
     FFVGAAEEAH SRSSKLARFL PRKPSCLKTN FVEARSFWHL FRTFDRMWTF FILWLQAMII
     IAWNGSGSLG ALFEGSVFKK VLSVFITAAV LRFFQALLDI IFSFKALHSL GYVGSIRLVL
     KVLVSAFWIV ILSTSYVHSW EHPTGLTRTI KNWLGHNGGP SVYLVAVILY LVPNAIAAIF
     FLLPCVRRVA EESDAIPVRI LLWWSQPPCY IGRGMHEEPL HLFSYTFFWI VLITCKLLFS
     YYVEIKPLVE PTKFILDFTN VRFAWHEFFP HARGNIGVLI ALWTPVILVY FMDIQIWYSI
     MSTIWGGIVG AFMRLGEIRT LSMLRSRFRA LPTTFNWNLI PLESSVKRKY QILRKFKAFE
     HNKLEEARFA HLWNAVVESL REEDFIDDKE KELMLLPYSA DPYPNNNIIQ WPPFLLASMA
     PMAIEMAKEY AEVQGENVED ARLWNKIKEN EYMRCAVEEC YEFLKNILLR VVTGETEKRL
     IHDLLKELGN RKAEGKLLEN FRMNDLPLLA GHFVRFLEFL PDPSDTARDK VVLLLQDMLE
     VFMHDMMVDD TREKFESSHG LNMKPTENQS VMGGKGKIQF FAGKDSILYP LPEDHAWSEQ
     IKRVLLLLTE TESAMDVPKN LDARRRITFF TNSLFMKMPP APRVRKMIPF SVLTPFYEEE
     VLYSKNVIEE PNEDGVSILF YLQNVYPDEW NKFLERVNCT TEEEVEEAAL RDWTSYRGQT
     LSRTVRGMMY YRTALELQAF LDLAPDEDVY TGFKEVSKRR KEEKGQDSFW AKLDAIVDMK
     FTFVATCQKF GQQKHSKDLK EASKAQDIQK LMTKYPSLRV AYVLEEEPSK GKPQKSYYSV
     LSKAVDGRDE EIYKIRLPGP VNIGEGKPEN QNHAIIFTRG LGLQTIDMNQ ENYLEEAFKV
     RNLLEEFKSR HGARFPTILG VREHIFTGSV SSLAWFMSNQ ETSFVTIGQR VLATPLKVRF
     HYGHPDVFDR IFHITRGGVS KASKGINLSE DIFAGFNSTL RRGLVTHHEY IQVGKGRDVG
     LNQISIFEAK VANGNGEQTL SRDVYRLGHR FDFFRMLSFY ITTVGYYFST MIVILTVYVF
     LYGRLYLALS GLERSFVRAA QQNTDSALQS ALASQSLIQL GLLMALPMVM EIGLERGFRM
     ALSDLIVMQL QLASVFFTFT LGSKVHYYGR TIFHGGAKYR ATGRGFVVRH EKFPDNYRLY
     SRSHFVKGFE LMILLIIYDV YGSQTRNAVS YVLITFSMWF LVGTWLFSPF LFNPSGFEWQ
     KIVEDWNDWN KWISSKGRIG VPANKSWESW WEEEQDHLQN TGFRGRVFEV ILALRFVLYQ
     YGIVYQLNIM RGNKSLSMYG LSWVVICVVL FTLKAVSLGR KKFKANFQLV FRMLKGVIFV
     AVLSVIAVLF RFAHLTVGDL FASILAFVPT GWGLLQIFQA CRPVIVTYGM WDSVQALART
     YEYVMGLLLF APVAILAWFP FVSEFQTRLL FNQAFSRGLQ ISRILAGKRK KVADD
//
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