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Database: UniProt
Entry: A0A072PN86_9EURO
LinkDB: A0A072PN86_9EURO
Original site: A0A072PN86_9EURO 
ID   A0A072PN86_9EURO        Unreviewed;      2491 AA.
AC   A0A072PN86;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE            EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN   ORFNames=A1O9_02777 {ECO:0000313|EMBL:KEF61212.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF61212.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF61212.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF61212.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF61212.1}.
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DR   EMBL; AMGV01000002; KEF61212.1; -; Genomic_DNA.
DR   RefSeq; XP_013263802.1; XM_013408348.1.
DR   STRING; 1182545.A0A072PN86; -.
DR   GeneID; 25277718; -.
DR   VEuPathDB; FungiDB:A1O9_02777; -.
DR   HOGENOM; CLU_000488_0_0_1; -.
DR   OrthoDB; 141134at2759; -.
DR   Proteomes; UP000027920; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11323; AmyAc_AGS; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
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:SF2; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1; 1.
DR   PANTHER; PTHR47182; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1-RELATED; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027920};
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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..2491
FT                   /note="alpha-1,3-glucan synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001681725"
FT   TRANSMEM        1080..1102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2024..2044
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2056..2075
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2082..2105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2117..2137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2149..2169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2194..2219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2239..2256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2276..2298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2305..2324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2348..2369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2376..2396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2421..2445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..520
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1708..1760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1778..1801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1841..1865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1712..1728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1848..1865
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2491 AA;  278792 MW;  82049DE657500F74 CRC64;
     MSALLLFLYA LFFTISSAFR YDEAYVQYNL NENKTATDPL DYWGEWTGHT YTPSPENWRF
     PWYTLFLDRF VNGDPTNDNI NGTTFEHDTN SNQMRHGGDL QGLVDTLDYL QGMGIKGLYI
     AGSPFINSPW GYDQYSPLDL SILDQHFGNI QMWRTAIQEI HARNMYVVLD NTFATLGDLI
     GFDGYLNATT PFRLDEHEVQ WKSGRQYYDF SIGNEYNKTC EYPKFWLETG YPVDEEVTKE
     MVGCYDSDFD QYGDTEAFGV FPDWRRQLSK FASVQDRLRE WHEPVRRKLE NFYCMLIAQL
     DIDGYRYDKA TQSTVDAMGF MNDAMRQCAR RHGKENFFLP GEITGGNVFG SLFIGRGRQP
     DMLPDNLTAA VTMTNNSDDK YFLRAPEHGG LDAGAFHYTV YRTLTRFLGM DGNLEAGYDA
     PPNWVDMWND FLLTNDFVNP NTGKFDPRHM FGVTNQDVFR WPAITNGVRR QLLGHFVTTI
     ELPGAPLLLW GEEQAFYVLD NTASNYIFGR QAMSSATAWQ THGCYSLSST QYYRMPLDAA
     LNGCHDDSVS FDHRDPSHPV RNIIHHMNQL RDQFPVLQDG FFLQQLSNQT QQVQYPGSNK
     VTTETGMWSV LRSIFPEHQD LSGAGAGNLP VWLLYSNTND SRTWEFDCSN NDTALNTTSL
     IAPYDAGTTV KNLFHPYDEH TLIESVHSLG INGSDQPNGC LAKLSMEAYD YRAYVPISQW
     VGPKPMITKF SPGHDARIHS TVAPNGTESV AVELQFSVEM NCESVTNSIM LNSTTETGLS
     PTIDAASVNC TVMSTPETLD YVGAISSTWS WSARLNGVAN GIHAITVRNA TTEGGEQYTN
     AVDKFLFRIG QLDNPIVFTR SANYSSTLFS KNDNGSLILS HSAAGADQWR YSTNWGSSFS
     NWLPYEGGET QIEEQPWSGT NLQNWKGTHV RVEYFSRFAG SSDHIQQADL DSHTPRRFPH
     LFLNGPYNQY GFDAGLDNEM KLTDNSTWEH HFMTEWSLSG TLAQVNVWGI NPDGQPDQTY
     VLGDADGDSV LDRLPPSSLS SVVLNITQPP PKPHLGWRIV INDGTMRFAL QPSGNMYNQM
     ILYILLWIVP VFMAAVAVWA FMQSFYSVKF NEIGISEKAS LIPAIFKKHF KKLADEETGP
     GIVGKFTRKE KFLQPTDTVI NQERRRTVII ATMEYDIEDW QIKIKIGGLG VMAQLMGKNL
     GHQDLIWVVP CVGGVDYPED QTAEPMTVTI LGKPYEVQVQ YHVLRNITYV LLDAPVFRQQ
     TKSEPYPPRM DDLSSAIYYS AWNQCISQAI NRFPVDLYHI NDYHGSVAPL YLLPRTIPAC
     LSLHNAEFQG LWPMRTKRER EEVCSVFNLS SELVQRYVQF GEVFNLLHAG ASYLRVHQQG
     FGAVGVSKKY GKRSYARYPI FWGLKKVGKL PNPDPSDTGE WDKKLPKQED IRIDPVFEAA
     RPELKRQAQE WAGLEQNPRA ELFVFVGRWS MQKGIDLIAD VFPSVLEANP NVQLITIGPV
     IDLYGKFAAM KLDKMMKLYP GRVFSKPVFT ALPPFIFSGA EFALIPSRDE PFGLVAVEFG
     RKGALGVGAR VGGLGQMPGW WYTVESVSTV HLIHQFKQAI EEALSSKSDV RALMRARSSL
     QRFPVASWVE DLEILQSTAV KIHDKVEASK RHLATGEMMR PISGRTTPAM SGAATPSGWQ
     TPVFGQSKAA THAALSSLAA RLKHIGHNRE QSHDNSSNTA TGLSRSASLG SRRGPGHITV
     HDHHEGEESS TPTILPPVPD VEGDDTGLGT AVMRYGEGTD HASDQEDSNF EDDDEDDHIT
     MPTQTRGRYE RVPANGDGPI TPPWDRTFGF SRTPGLELAQ YPKQRPSPYG SPSIPGTPHP
     EPETGLLAPP RALAEGNNRI SASPSMLSIS SIVGEKTDFK LQKVDPFFTD SNGEFSRAFE
     KKLESLNGNN SESTTCIEEF LVKSEKTWFT SFRDAKLGRH QHTPSAQESR FTSAAPSIYG
     GQSEHDSEGQ EHDSNNLADE FLLGKDYVPP SGVRNWMQIR IGDWPVYAFF MAFGQIIAAN
     SYQITLLTGE VGQTASKLYV IASIYLATSI CWWILFRRFS SVLCLSLPFF FYGLAFVLIG
     LAHYASTVSE RGWVQNVGTA FYAVASSSGS IFFALNFGDE GGAQVKAWVF RACVIQGTQQ
     IYVVALWYWG SYLNKSHNDG LLKSSDPITN SWKITAITLP IAGLLWAVGL LMWFGLPTYY
     RQAPGKMPSF YKSLSRRKIV LWFFATVLIQ NFFLSAPYGR NWSFLWSSPH TSTWQVVVLV
     AVFFIGFWAG ILWILGMLSK SHSWILPLFA IGLGAPRWAQ IWWATSNIGL YLPWAGGYTT
     GALLSRALWL WLGTLDALQG VGLGMILLAT LTRVHVAFTL IMAQVLGSVA TIVARACAPN
     NIGPGPISPD ISAGFGSIFQ AWFWVGLIAN LSICVGYFMV SYIALITSCL ESSFADIYGS
     FIAKNSSASL DDRAFEECDD VRWDTDFIDS L
//
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