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Database: UniProt
Entry: A0A151T7C1_CAJCA
LinkDB: A0A151T7C1_CAJCA
Original site: A0A151T7C1_CAJCA 
ID   A0A151T7C1_CAJCA        Unreviewed;      1526 AA.
AC   A0A151T7C1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=KK1_017481 {ECO:0000313|EMBL:KYP62921.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP62921.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP62921.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(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: 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; CM003610; KYP62921.1; -; Genomic_DNA.
DR   STRING; 3821.A0A151T7C1; -.
DR   OMA; DMNQDNH; -.
DR   Proteomes; UP000075243; Chromosome 8.
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   InterPro; IPR026899; FKS1-like_dom1.
DR   InterPro; IPR003440; Glyco_trans_48.
DR   PANTHER; PTHR12741:SF102; CALLOSE SYNTHASE 11; 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   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:UP000075243};
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        311..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        385..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        484..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1096..1118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1264..1287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1338..1359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1371..1392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1404..1425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1432..1455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1475..1494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          87..203
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
SQ   SEQUENCE   1526 AA;  177034 MW;  8EF2412EEF9D5C5B CRC64;
     MDLLDWLRLL FGFQNDNARN QREHLVLHLA NSQMRLDPPP TLADALDAGV LRRFRRKLLH
     NYSAWCSFLG LKSNVLLSRR RDPTDLRREL LYVALYLLVW GEAGNLRFTP ECLCYIYHFM
     AKELNYVIDE HIDPDTGRPY MPTVSGELGF LKSVIMPIYN TIKVEVDSSR NGKAPHSAWR
     NYDDINEYFW SRRCLKRLGW PLSFECNFFG TTPKEKRVGK TGFVEQRSFW NVYKSFDRLW
     VMLILFLQAA VIVSWEGTTY PWQALERRDV QVKMLTLFIT WSVLRLLQSV LDAGTQYSLV
     TRETTWLGVR MALKSMVAIT WTVLFSVFYG LIWLEKGSST IWSDDANQRI YTFLKTALVF
     LIPELLSLVL FVVPWLRNII EGSDWSIVYL LTWWFHTRIF VGRGVRQALI DNIKYTVFWV
     LVLASKFSFS YFVQIKPLVA PTKALLNLRG IHYKWHEFFS NTNRIAVALL WFPVVLVYFM
     DLQIWYSIFS AFYGATIGLF SHLGEIRNVA QLRLRFQFFA SAMQFNLMPE EKQLSQQATL
     LKKLREAIHR LKLRYGLGQP FKKLESNQVD ATRFALIWNE IIITFREEDI ISDRELELLK
     LPPNCWNIRV IRWPCTLLCN ELLLALSQAK ELENESDRSL WLKICKNEYG RCAVIEAYDS
     IKYFVLTPYY DEEVMYSKEA LRKENEDGIT TLFYLQKIYE DEWKNFMERM RREGLKDEDD
     IWTTEKVRDL RLWVSHRGQT LSRTVRGMMY YYRALKMLAF LDLANEMDVK QGSEHIVSHG
     STNQNSSLNG LPSDRHVNLR PADSSVSMLF KGHEYGSALM KFSYVVACQM YGRHKADKNP
     RADEILYLMQ NNEALRVAYV DEVSLGSEGT EYYSVLVKYD QQLQTEVEIY RIRLPGPLKL
     GEGKPENQNH AIIFTRGDAV QTIDMNQDNY FEEAIKMRNL LEEFNIHYGV KRPTILGVRE
     NIFTGSVSSL AWFMSAQETS FVTLGQRVLA NPLKVRMHYG HPDVFDRFWF LGRGGVSKAS
     RVINISEDIF AGFNCTLRGG NVTHHEYIQV GKGRDVGLNQ ISMFEAKVSS GNGEQVLSRD
     VYRLGHRLDF FRMLSVFYTT IGFYFNSMVI VLMVYAFLWG RLYMALSGIE DEAINNASNN
     KALGAVLNQQ FAIQVGIFTA LPMVVENTLE LGFLPAVWDF LTMQLQLASL FYTFSLGTRT
     HFFGRTILHG GAKYRATGRG FVVAHKSFAE NYRLYARSHF VKGIELGVIL IVYASHSPLA
     KNTFVYIAMT ISSWFLVVSW IMSPFVFNPS GFDWLKTVYD FEDFMNWIWY PGGPFKKAEY
     SWETWWNEEQ DHLKTTGIWG KLLEIILDLR FFFFQYGIVY QLSIAGGNTS IAVYLLSWIV
     MVVIVGLYII IAYAQDKYAT KEHIYYRLVQ LLVIVVTVLV VVLLLQFAHL KFIDLLSSLL
     AFVPTGWGMI LIAQVLRPFL QTTKVWETVV SLARLYDLLF GVIVMAPVAI LSWLPGFQSM
     QTRILFNEAF SRGLQISRIV SGKKSV
//
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