ID A0A179U892_BLAGS Unreviewed; 2421 AA.
AC A0A179U892;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=BDBG_00595 {ECO:0000313|EMBL:OAT03943.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT03943.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657448; OAT03943.1; -; Genomic_DNA.
DR STRING; 559298.A0A179U892; -.
DR VEuPathDB; FungiDB:BDBG_00595; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000002038; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002038};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2421
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008107240"
FT TRANSMEM 1072..1094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1997..2017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2029..2048
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2055..2078
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2090..2110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2122..2142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2169..2191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2211..2228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2248..2270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2277..2295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2347..2370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2393..2413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..518
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1639..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1817..1847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1930..1962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2421 AA; 272727 MW; 59AD244B173CB10E CRC64;
MMRRWLVGVS LALLATGATS WPYDPEFEGY NLNENKTATN PADYYGEWEN HEYFPSPENW
RFPFYSLFLD RFVNGDPRND NINGTFFEHD LNSNQMRHGG DISGLVDTLD YLQGMGIKGI
YLAGTILMNA PSGADGYSVL DTTLLDRHYG NIQEFRYAIT EIHKRGMYVL MDNTLATMGD
LIGFKGYLNT TTPFDVNEHE AVWKTNRRYV DFDIGNNYNE TCDYPRFYWE NGYPVGNDVT
DQLKGCYDSD FDQYGDIEAF GVYPDWQRQL AKFASVQDRL REWVPSVRQR LMRHSCLIIR
QLDIDGFRYD KALQATVDAF ADISEHYREC AKSVGKHNFF LPGEITGGNT LGSIYIGRGR
QPNMLPETLE DAVKLTNTSS EKYFIREPGK SALDAGAFHY SIYRSLTRFL GMDGNLAAGY
DTPVNWVDTW YEFLLTNDFV NANGKFDPRH MFGATNQDVF RWPTIREGTE RMLLAFYITT
LHLPGIPLLL WGEEQAFYVL DNTARNYIFG RQAMSPATAW QTHGCYSLGS EQYYQWPIES
GKYACHDETV SYDHRDPSHP VRNVLKTMYQ MREHYPTLND GWFVQHLSNQ TWQVFLPGSN
NTPTETGMWS IHRSRFEAVQ DFGREGNLPV WLVYQNYNKT HKYEFDCSDN DTALISSFDS
GTTVKNLFYP FDELTLKEGP KKLGFDQSAE FNGCLDSLEL KPWDFRAYVP KDRFIRPRPM
VTKFVPGHDA RLQSTVSPDQ DETVPIELYY SEAMSCDGVT RSITFNSTTD NGKKPSIDAS
SVKCTTVTPE PPKYIGEVPH SWKWSANLVG VYNGVHRVTI SNAPSNDGLT NTTSVDHFLF
RIGQPDNPMV FTRAANYSSN LLHKDNKGNL YVTHHAAGAD LYRYSLTWGS SFSDWLPYEG
GNTTLERQHW SGTKLQRWEG EHVSIEYWNR MTGSSSHVQH GDLDWPSSKP RRFPHLFWNG
PYNQYGYDAG LKNHMVQDDD GIWKFIFMTE WPALAQVNVW GINPDGKPDQ TFVFGDIDGD
SVLDRLPPSS LAKTIINITQ PPPAPHLAWL FSLNDGTLRF QLHPVGNHYH QLILYILLWV
IPILTSAIGI YVFMKSFYRV KFNQVGISDK GGFVPLAIRR KFRRQALEES HTMKPLMKLA
NKSKFVQSTS ALVDHSGKRR TTLIATLEYY IPDWKIKIKI GGLGVMAQLM GENLGHQDLI
WVIPCVGGVD YPVDQVAEPM TVTILGNAYE VKVQYHILNN ITYVLLDAPV FRQQSTAEPY
PARMDDLDSA IYYSAWNQCI ALAIRRFPVD LYHINDYHGS AAPLYLLPQT IPACLSLHNA
EFQGLWPMRT QTEKEEVCAV FNLPLDVASR YVQFGEVFNL LHAGASYLRV HQQGFGAVGV
SRKYGKRSYA RYPIFWGLKK VGNLPNPDPS DTGEWNKQLP KDSDITVDPE FEAKRAELKR
QAQEWAGLDQ NPDADLLVFV GRWSMQKGVD LIADVFPAVL EARENVQLIC IGPVIDLYGK
FAALKLEKMM KLYPGRVFSR PEFTALPPYI FSGAEFALIP SRDEPFGLVA VEFGRKGALG
IGARVGGLGQ MPGWWYTVES TTTSHLLNQF KLAIDSALNS KPEVRAMMRA RSATQRFPVA
QWVEDLEILQ STAIRIHNKE SAKSTGQPHT PSGYNTPGIP GSPLGPGSMS PATPGSRNHS
YAAGHRLSAF GPQARNTVIY HQDSSPGPDT DNEIPAGLSR NLSLGVRSGP GHMGGESHVP
RKLRKNNAPV GVPENEPENE PEPVGVAVTA DIDEESDDDT AAHYFGDDDE YTLTREQAEA
GRGNQLGLLS RNFHNADFNE QRTPGTSRPP SPSSADGFLP PSRPLPYSGN FPSSTSVLSL
GSVVGSKKDF KLQKVDPFFT DSNGEFYRAF EKKLEDLNSE NSETDLCIEG YLVKSEKKWF
NRFRNARLGR NTNSDNPPSL FRAKRGSGVS PAPSEYGEDL ESRASDYGKD GDEFLLGNDY
IPPTGLEKWM QLRIGDWPAY SFFLAFGQII AANSYQITLL TGEVGQSATK LYAIATTYLI
TSIIWWFIFR WFKSVIPLSL PFFFYGLAFM FIGVARFAGT ENGVGWIRNI GSGLYATASS
SGSIFFALNF GDESGAPVKD WVFRACVIQG TQQIYVVALW YWGSTLTKNI AEGVIEADPI
ASSWKLTAIA IPIGLFLWTI GLLLFFGLPN YYRQTPGKVP SFYKSLFRRK IVIWFFVTVV
VQNFFLSAPY GRNWAFLWSS KHAKPWHIVL LILLFFIVVW AVLLAVLGYL SKDHSWILPL
FAIGLGAPRW AQIWWGTSGI GQHVPWAGGY ISGALISRSL WLWLGVLDAM QGVGFGMILL
QTLTRLHICF TLLAAQVLGS IATICARTFA PNKIGPGDIH PDISGGISAI ENAWFWICLF
CQLAICAGFY LFFRKEQLSK P
//
