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Database: UniProt
Entry: E6R8V6_CRYGW
LinkDB: E6R8V6_CRYGW
Original site: E6R8V6_CRYGW 
ID   E6R8V6_CRYGW            Unreviewed;      2431 AA.
AC   E6R8V6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE            EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN   OrderedLocusNames=CGB_G0300C {ECO:0000313|EMBL:ADV23282.1};
OS   Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS   (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV23282.1, ECO:0000313|Proteomes:UP000007805};
RN   [1] {ECO:0000313|EMBL:ADV23282.1, ECO:0000313|Proteomes:UP000007805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX   PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WM276;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwong-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 0:0-0(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC         alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-
CC         COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC         EC=2.4.1.183; Evidence={ECO:0000256|ARBA:ARBA00000687};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000256|ARBA:ARBA00006122}.
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DR   EMBL; CP000292; ADV23282.1; -; Genomic_DNA.
DR   RefSeq; XP_003195069.1; XM_003195021.1.
DR   GeneID; 10190845; -.
DR   KEGG; cgi:CGB_G0300C; -.
DR   VEuPathDB; FungiDB:CGB_G0300C; -.
DR   eggNOG; ENOG502QSGC; Eukaryota.
DR   HOGENOM; CLU_000488_0_0_1; -.
DR   OrthoDB; 141134at2759; -.
DR   Proteomes; UP000007805; Chromosome G.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047657; F:alpha-1,3-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11323; AmyAc_AGS; 1.
DR   CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   PANTHER; PTHR47182; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1-RELATED; 1.
DR   PANTHER; PTHR47182:SF2; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE MOK13; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..2431
FT                   /note="alpha-1,3-glucan synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003210081"
FT   TRANSMEM        2041..2058
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2065..2084
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2104..2121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2133..2154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2166..2190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2211..2231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2251..2273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2280..2300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2315..2342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2349..2369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2403..2423
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          76..526
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1678..1719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1740..1802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1817..1846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1956..1986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1776..1802
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2431 AA;  272388 MW;  1701B2F25910FF59 CRC64;
     MLLRPPREAR ISLFPLVLTL FATSLSVLGL KYNETLDAWN INKNQDATNV LDYTTTRSNR
     TYTKSPDNWR SLPTYTLLLD KWIDGSPQNN DFFGLKYEYD MRETQLRAGG DAKGLMSDRS
     LDYLLSMGYK AIYIAGTNFI NMPWQSDGYS ALDFTLLDPH YGTLQEWVDL VDRIHAKGMH
     IILDFTVGTM GDLIGFEGHL NTSTPFSMDE HVAQWKLPDY APWGFQKYPD FNFTNDYNNS
     CIYPTFWLDD GTIYDPGKVG CYASDFDQYG DIEAFGVFPD WQRQLAKFAS VQDRLREWRP
     DTAAKLKRFS CLAIEALDID GIRIDKATQV TVDFMAEWAN STRECARQFN KDNFFIPGEI
     TGGDTFGALY IGRGRTPTLQ PSNFTQAVEL TQDQGEYFLR GEGIAGLDSA AFHYSIYRSL
     CRFLGMDGNL QVAYDVDVNF VTAWNEMVVS NEFLNSQTND FDPRHMYGTT NQDVFRWPGL
     ANGTERQQLG QFVTVLLMPG IPLGWYGEEQ AFYLLDNTAS NYLYGRQAMV SNPAWKKHGC
     YKVGSSQYYN MPYDKVLTGC DDPWNSLDHY DPTAEPLRGI RNMMYLRTRF PSLQDGFSLT
     TLGNWTHFIQ LPGSNQTQTE LGMWSVTRAP IAQQEGHGSF EANGTISQAV WLIYTNENDT
     VPYSPDCKQE GWISSPFQSG VTVRNLFYPY ENYTLQDSLS SYYADGNPPY RGCLGSITLD
     PFMYKALVPQ DQWIPQLPTV TKFTPGHDYR YQTSGGTTNV DITIEYDTDM DCDSLRRAMT
     LNYTIVGSGS PSLSDGTCQS IAQADWETPS IPSVAPGRWR WTGQLQNAPD GIYEIIISSV
     DSQISGVPTN NTDHLLLRLG QTSNAIVFPE NDYSDSLLTV SDGVYTLNNT ADGADAYRYS
     ADFGQTWSAW MNYETNPTLN ASMFDDDTHW WDGYHVVVQY YSNIAGSANH LIHGDANWAH
     GHRRWPQLLA RGSFNTWGYD LGADSSFALV EDGTWEIPLS SAWPAYIQLN VWAFDDYFYG
     DVDGDGVIDR LAPNAQSANY LNMSIPPAPH LAWNVIVDDA TGEWSVEPIG HQTTTAIAFA
     LLIVIPALTA FAAAAIFRYS FYSIKVNRFG LKPNKASKET SYFPIIGGHS EKKGDVSEKG
     ALALNEKHHK TPAKVIGWPE DQNKRRKVLI ATLEYEIMDW KLKVKIGGLG VMSSLMGKAM
     TDVDLIWVVP KVQDLEYPQG EYAEPIEVII FGEPYLIEVE THKLDNITYV ILDSPVFRAQ
     TKADPYPQRM DDLSSAIFYS TWNQAIAETI RRNPIVDIYH INDYHGALAP LYMLPKVVPV
     CLSLHNAEFQ GLWPLRTKDE MKEVCAAFNI PKEVCSKYVQ FGNTFNLLHA AASFISHHQK
     SVGVAGVSDK YGKRSWARYP ALWTLRNIDS LPNPDPTDIA ALDEQPLAVD KIEVDQEAES
     KRPEQKRQAQ EWAGLKQDPD ADLFVFVGRW SKQKGVDLIA DVMPSLLDKK PKIQLICVGP
     VIDLYGRFAA EKLARLMEMY PDRVYSKPEF TALPPYLFSG ADFALIPSRD EPFGLVAVEF
     GRKGALGVGS RLGGLGLMPG WWFPVESSAT VHMLSQLTKT IKLALKSTPE ERAILRARSA
     VQRFPVVEWR QRLEDFQRRS IIASRQGAGD HAWGYDLVDQ EVGSGFYAQG DNGSFTSLAR
     GEWGRSATPD STAPNSPMPG HSPLAGEGQN FFDPNLPMAS SNSSLGANYH KRFDKNANRQ
     SAESFYDEDP NASPLYYGDK RQSGKPKFFG YDDQDVASSV GSSDQGDTTV VGSTSGQRDP
     SAQTYDNFLA AANRQFAKSS GERNAPDPYF SNRTSQDSTN FAPSRPFTAH SRVSSFDSIS
     SIVDEKGSSP LNKAMETFTD ADGEVAQSFV QKLKDLSASN SKGDLCIEKF LIKSEKAFFD
     EVKKDKIASM SIRSRDSFVQ SRAPSMIDGF RPDSPMSHSM SHSGHGHDEM SQYGGIPGGH
     DMYDEGGHSE PRMTKLQIFM GRQIYRWPLY SIVLSLGQLL SATSFQLSLL GGSNTQTATD
     LYIICSIFAV ATIAWYTLFR MKPSVYCLSL PWVIFTIAFL LIGFPSIHGV FLAPRLTITR
     VATYMYAIAS SAGFLFFGLN FGEEAGAATE IWVTRACIVQ GLQQIWVSAL WYWGYTLNGS
     DPDKYVPSRI IICICWPLAA VSAVFAYVMW FGLPEYYRQI PPYVPNFFKT LFRRKLVIWF
     LIAEILRDYW LSGPYGRSWQ YLWSQAGVPK WAVVIMIAIF FVGIWGLLLG ILIRYSKIHS
     WLLPVFAIGL GCPRWCQMWW GTSGMGLYIP WGGSAGPYIG VCTWLWLGVL DAIQGVGLGM
     VLLQTLSRLH VCVTLALAQF VGSCVVMLAR GTAPDKVGPG KVFPNVAIWD IGGSGKNMPL
     AHYEFWLCLV FQIIIVIGYA IFFRREQLSK P
//
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