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Database: UniProt
Entry: A0A3D8S878_9HELO
LinkDB: A0A3D8S878_9HELO
Original site: A0A3D8S878_9HELO 
ID   A0A3D8S878_9HELO        Unreviewed;      2469 AA.
AC   A0A3D8S878;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE            EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN   ORFNames=BP6252_03659 {ECO:0000313|EMBL:RDW82547.1};
OS   Coleophoma cylindrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Coleophoma.
OX   NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW82547.1, ECO:0000313|Proteomes:UP000256645};
RN   [1] {ECO:0000313|EMBL:RDW82547.1, ECO:0000313|Proteomes:UP000256645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP6252 {ECO:0000313|EMBL:RDW82547.1,
RC   ECO:0000313|Proteomes:UP000256645};
RX   PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA   Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA   Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA   De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA   Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA   Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA   Xiong C., Yue Q., Zhang X.;
RT   "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT   Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT   basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT   Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT   and Morchella septimelata.";
RL   IMA Fungus 9:199-223(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDW82547.1}.
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DR   EMBL; PDLM01000003; RDW82547.1; -; Genomic_DNA.
DR   STRING; 1849047.A0A3D8S878; -.
DR   Proteomes; UP000256645; Unassembled WGS sequence.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   CDD; cd06174; MFS; 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   Hydrolase {ECO:0000313|EMBL:RDW82547.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256645};
KW   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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..2469
FT                   /note="alpha-1,3-glucan synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017761209"
FT   TRANSMEM        1093..1114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2045..2067
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2079..2096
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2103..2126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2138..2158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2170..2191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2211..2235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2258..2275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2295..2316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2323..2343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2367..2387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2394..2417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2441..2461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          69..526
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1660..1679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1703..1724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1738..1766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1794..1893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1703..1719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1820..1847
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2469 AA;  275281 MW;  0B5F84D31692BC08 CRC64;
     MFGFRGAALA WLSLWSSTSR VSALVYDEQY VGYNLNTNKT ATSPHDYWGE WEGHTYMPSP
     TNWRFPFYTL FLDRFVNGDP TNDNANGTAF EQDVMQTQLR HGGDLQGLID SLDYIQGMGI
     KAIYIAGSIM INQPWGSDAY SPLDLTLLDA HFGDISKWRE MTQAVHDRGM YVVLDNTMGT
     MGDLIAFDGY LNSSTPFQLT EHKVQWRDPN RQYLDFAFGE EYNTTCDYPR FWLETGYPVG
     TSVTDLMNGC YNSEFDQYGD TEAFGVFPDW QRQLSKFASV QDRLREWLPS VRTKIDLFTC
     MQIAQLDIDG IRLDKATQIT IDALGDFAHA TRECARALGK ENFFIPGEIT GGNTFGAIYI
     GRGRQPDMQP STISSAVQMT TNSSLEYFIR DADYNALDAG AFHYSIYRSL TRFLGMDGNL
     ASGYDTPVNW VDAWNEMLLT NDFINPNTGV FDPRHMYGTA NQDVFRWPAI KNGTEKLLLG
     LFITTLHMPG IPLLLWGEEQ AFYVLDNTAS NYIFGRQAMS AATAWQTHGC YLLGSSSYYQ
     FPVESATTGC TDDWNMRDHR DPAAPIRNII KHMYQMRENY PSLQDGWFLQ QLSNMTGWIQ
     YPGSGTTKTE TGLWSTMRSG FENIQDLSGT GAGNQSVWLV YQNGNTSKTY SFTCSDNDTA
     LIAPFDSGTT VRNLFYPFDT VTLKASSQKL GIANQTGYNG CLDSLTMSAW EFKAYVPADT
     WVGPGPMITK FSPGHDVSVQ SAVKPGEQES IPIEFHFSQE MNCTALMANM KITSTTEDGK
     VAQLDSNTAT CNVVPTEAVT DYIGSIPTTW KFTANLTNVS NGIHSITLTN VSTNSGNDTT
     KSVDKFLFRV GQTDNPVVFP RLANYTLGLL HQNTDGSLYV SHKAAGADRF RYSLNWESTW
     SNWTTYTGGN TTLETQPWTG TSKQKWDGEH VIMQYFSNLT GSSSYTQHAD LDASQQARRF
     PHLFIEGPFN LYGYDAGLKN EMTKNKITGL WEAYFMTEWP GVFQINVWGM NPDGEPDKTV
     ILGDVDLDGV LDRMPPSSLS TTLVNYTYRA DTGKHLIGDF IYPPAPYLGY KVVLNDGDYA
     YGLVPYGSRA QQMILAFLMI IIPVFTGGLS IWLFMKSFYA VKFNAVGISE PHHFIPLAIR
     RKLKRQEKGE KDMALGVPSP IMMHDNPSNV GLSADAGGGR RRTVLIATME YDIEDWEIKI
     KIGGLGVMAQ LMGKNLGHQD LIWVVPCVGG IDYPVDTPAA SMDVTILGKP YEIQVQYHTL
     RNITYVLLDA PVFRAQSKSE PYPARMDDLD SAVYYSAWNQ CIALAIQRFP IDLYHINDYH
     GSLAPVHLLP RTIPCCLSLH NAEFQGLWPM RTKKERAEVC AVYNLSEEVV TKYVQFGDVF
     NLLHAGASYL RVHQKGFGAV GVSKKYGKRS WARYPIFWGL NKIGNLPNPD PSDTGEWTGE
     QDKEEAVVNQ DFEANRGELK RQAQEWAGLD QNPKADLLVF VGRWSMQKGI DLIADVMPAV
     LEENPNVQLI CVGPVIDLYG KFAALKLDVM MKKYKGRVFS KPEFTALPPF IFSGAEFALI
     PSRDEPFGLV AVEFGRKGAL GIGARVGGLG QMPGWWFTVE STTTTHLLHQ FKMAIKEALS
     SKLETRQMMR ARSAKQRFPV AQWVHDLETL QGKAIKIHLK EEGKSSGRPS SRGNDSRSLF
     ASNRRVSRHM LGMNASESQI DVSTISNSTR PSSPSGTIEP PAANAGLSRK LSLGYRAGPG
     HRVMKRGRAN DSSASLGMGL ANEPITDVDE DTDFEDRTMS IYDEYVLSPE ELEAERQREQ
     QHFHAQSPGL PGHGGLLSPH GNSFSGSPRT SFANSPRVTQ RMLSGQPESD YSLPIAARGS
     AIYSGPPSPS GADSPGADDV LLPPAPFGSD QASHRASMLS LSSVVGDKTD FKLQKVDPFF
     TDTQGEYYEA FARSLDNLNG KNSEQLLCIE DYLVKSEKKW FDKFRDAKLG RGSFVPPTPS
     ALGAGSRRGS VSDSFMNETI VHSRQNSEND GHGGSQEEND QFLLGKDYKP PTGLRLIMQY
     RYSDWPVYSF FLAFGQIIAA NSYQITLLSG TVGQTAEKLY ITAAIYLVSS IFWWMVFIRL
     KSIYVLSCPF FFYGMAFFLL GMAPFVSGTA SRGWIQNVAT GFYSVAASSG SIFFALNFGD
     EGGSPIKSWV YRACLIQGTQ QAYNVVLWWW GDYLNKRSAD GLSATFTTAS TTMSMITIPV
     ACLIWACGVI LFLGLPDYYR QKPGKVPSFY TSLFRRKIVM WFFVTVMIQN FFLSTNYGRN
     WMYLFSSNNA TAWEIILLII LFFGGVWALF LWFFGMLSKD HSWILPIFAI GLGAPRWCQQ
     LWACTPIGQY VPWAGSPLGS ALFSRSLWLW LGVLDALQGA GFGMILLQTL TRLHIAFTLI
     AAQVIGSIFT IIARAWANNN TGPGDVFPDF SLGAYPGITK AWFWIGLLFQ LAICGGFFTF
     FRKEQLSKP
//
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