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Database: UniProt
Entry: M2RJA5_CERS8
LinkDB: M2RJA5_CERS8
Original site: M2RJA5_CERS8 
ID   M2RJA5_CERS8            Unreviewed;      1643 AA.
AC   M2RJA5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   03-MAY-2023, 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};
GN   ORFNames=CERSUDRAFT_48098 {ECO:0000313|EMBL:EMD38542.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD38542.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD38542.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD38542.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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; KB445795; EMD38542.1; -; Genomic_DNA.
DR   STRING; 914234.M2RJA5; -.
DR   HOGENOM; CLU_000844_0_1_1; -.
DR   OrthoDB; 354539at2759; -.
DR   Proteomes; UP000016930; 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:UP000016930};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMD38542.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        267..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        350..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        440..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        511..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1116..1134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1166..1187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1271..1301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1377..1397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1409..1436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1448..1472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1552..1571
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1605..1629
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          121..233
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
SQ   SEQUENCE   1643 AA;  187834 MW;  D8F93886772EE00F CRC64;
     MSTEEIEDIF LDLAQKFGFQ RDSMRNMFDF LMQLLDSRAS RMTPDQALLT VHADYIGGPH
     ANYRKWYFAA QLNLDDAVGQ SQNPGLQRLR SVKGAVKTAG TKSLDSATNR WRNAMNNMSQ
     YDRLRQVALW LLCWAEAGNV RFTPECLCFI FKCADDYYRS PECQNRVDPV PEGLYLESVI
     KPLYCFMRDQ GYEVVEGKFV RKEKDHDQII GYDDINQLFW YPEGLAKIVL QDNTRLIDIP
     PAQRYTKFSR IAWNRVFFKT FFEKRSIAHL LVNFNRVWIL HVAVYWFYTA FNSPKVYAPT
     PTTDPSPAMT WSATALGGAV ATLIMIFATL AEFSYIPTTW NNASHLTTRL IFLLIVLALT
     GGPTVYIIIV DGPKNKSNIP LIIGIVQFFV SVVATIAFGI IPSGRMFGDR VAGKSRKYMA
     SQTFTASYPK LSGSARTGSV MLWLLIFGCK FVESYFFLTS SFSSPIAVMA RTKVLGCNDR
     YFGSALCSNQ VPFALTIMYV MDLVLFFLDT YLWYIIWIVV FSVTRSFYLG LSIWTPWKEV
     YTRMPKRIYA KLLATAEMEV KYKPKVLVSQ VWNAIIISMY REHLLSIHHV QRLLYHQVDG
     PDGRRTLRAP PFFTHNNGNE SDFFPAGGEA ERRISFFASS LHTALPEPLP VDAMPTFTVL
     VPHYSEKILL SLREIIREED QNTRVTLLEY LKQLHPVEWD NFVKDTKILA EESTAATTTF
     DGTASTNEKG NTRTDDLPFY CIGFKTAAPE YTLRTRIWAS LRAQTLYRTV SGMMNYAKAI
     KLLYRVENPQ IVQRFAGNTD RLERELERMA RRKFKFAVSM QRYAKFNKEE LENAEFLLRA
     YPDLQIAYLD EEPGPKGSDP RLFSILIDGH SEIDETTGKR KPKFRVELPG NPILGDGKSD
     NQNHAIIFYR GEYLQLIDAN QDNYLEECLK IRNILGEFEQ YSISSQSPYA QWGHKEFHKD
     PVAIVGTREY IFSENIGVLG DIAAGKEQTF GTMTPRTLAW IGGKLHYGHP DFLNATFMTT
     RGGVSKAQKG LHLNEDIFAG MTAIGRGGRI KHSEYYQCGK GRDLGFGTIL NFQTKLGTGM
     GEQMLSREYY YLGTQLPLDR FLTFYYGHPG FHINNIMVMY SIQIFMVTLL YIGTLNKELA
     ICKSSSTGDV LPGEHDCYNL NPVFDWIHRC IVSIFLVFFI AFLPLFLQEL LERGTGKALI
     RLGKHFLSLS PIFEVFSTQI YSQSILSNLT FGGARYIATG RGFATTRISF SILYSRFAGP
     SIYMGMRNIL LLLYASLAMW SPFLIYFWVS VLSLCIAPFL FNPHQFSFAD FVVDYREFLR
     WMSRGNSRTK ASSWYGYCRL SRTMITGYKK KKLGHPSEKL SGDVPRAKWR SVIFSEVVWP
     ICHATIFVVA YMFVKSFPID GKMPPSPLIR IAIIAVGPVV WNAAMLLALF FISLFLGPML
     ESWAKFPSVM AAIAHFLALV GLIAFFEFFW FLELWDASHA VLGVISIIAI QRAIQKILIA
     VFLSREFKHD ETNRAWWSGK WYGRGLGTSA LSQPAREFVV KIVEMSLWSS DFLLGHILMI
     ILTPPTLVPF IDKLHSTMMF WLRPSKQIRP PLFSTKQKRQ RRWIVFKYTI VYIIVVAGLA
     ALIVLPALFR DDIKFTCTLC QNI
//
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