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Database: UniProt
Entry: A0A094CIH0_9PEZI
LinkDB: A0A094CIH0_9PEZI
Original site: A0A094CIH0_9PEZI 
ID   A0A094CIH0_9PEZI        Unreviewed;      2470 AA.
AC   A0A094CIH0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE            EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN   ORFNames=V497_08274 {ECO:0000313|EMBL:KFY53764.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY53764.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY53764.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY53764.1}.
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DR   EMBL; JPJZ01001227; KFY53764.1; -; Genomic_DNA.
DR   STRING; 1420910.A0A094CIH0; -.
DR   HOGENOM; CLU_000488_0_0_1; -.
DR   OrthoDB; 141134at2759; -.
DR   Proteomes; UP000029268; 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   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; 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   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:UP000029268};
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..2470
FT                   /note="alpha-1,3-glucan synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001893975"
FT   TRANSMEM        1155..1181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2043..2063
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2075..2093
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2100..2120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2132..2155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2167..2188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2214..2236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2257..2273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2293..2316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2328..2356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2368..2388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2395..2414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2443..2462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          63..523
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          710..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1725..1792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1804..1879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1959..2005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1746..1792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1852..1867
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2470 AA;  273058 MW;  EE7D8EB061DCC792 CRC64;
     MASLLRIALW GLYALGSNAL RFEQEYVGYN LNEDDPNLGA VNNKWAGHTY HPSPTNWRFP
     FYTLFLDKFV NGDPANDNIN GTLFEHDTMQ TLLRHGGDIQ GLIDSLDYIA GMGVKGLYIA
     GTPWLNFPWG ADSYSPLDFT LLDQHYGDIT KYREMVDEIH RRGMYIIVDT TMSTMGDLHG
     FEGHLNDSAP FKPTEYKVIL RDKTRQYHDF HPQTEDIYNE TCAYPTFWDE TGHEVGEDVL
     SQLGGCFDSE FDQAGDIPGV GFFPDWQNQL GKYQSVQDRL REWMPSVREK LENFACLTIQ
     KLDIDGYRFD KGTQITLDAL ADINLSIREC AREVGKDNFF ITGEISGGNT FGSLYLGRGR
     TPEQYGNITL DEAVKLNNAS NATLFMRDED HGAYDAAAFH YSVYRSLTRF LGMQGFDSSF
     FDVPADWVET WNVLLRSNDL VNPNTNKLDP RHMYGTANQD VFRWPAIQDG VEKQLLGSFI
     TTIHMPGIPL MYYGEEQGLY VLDNTADNYL FGRQAMSASV AWQAHGCYNL SSSQYRDFGD
     VNAQKACEDN SVSLDHRDPS HPIRNIIKGM HQMRTNYPVL NDGLFLQSLS NKTKQVPIDK
     DTREVGLWSA LRSELPKLQD LSTAGGQGKQ EVWLLYHNDN HTGNYEFDCA DEELALVAPF
     PPGTVVRNLF SPYDEVTLLD GIVVPGFGSL DFTAAAVEAR QVLPADPVET AADTAAETAA
     ETAAKTAAEP AATDVPTGTD KVKSSTETGT GKKASTTGKP KSTKTSAKPK ATTSAPPPKF
     TSGCLKKVSL KPYEFRAYVP STKWVAPNPM ITRFVPGHDA RLKSTVPLGQ QENIDIALYF
     SNEMSCTSVT KGITITSTTE DATTASILEG SIKCATVPAQ VELNVPGNIP STWKFSATLT
     GVGHGVHSIT VKDVAAEAGD TSTGSTDKFI FRTGAEDNPI TFPRSANYSS SLLKRRDNGT
     LYISHKAAGA DLWRYTLDWT HYSQWFTYEG GEANLPPKNW TGTAKQKWKG EHVIVEYYNK
     DSGSSDYVQH GDLDSPPRRF PNLFALGTFN GFGADSGILN TFRLDKDGWW TYDLISEWPG
     QLQLNQWGIN PDGLPDQTAV YGDIDNDQVL DRTPPPSLRL ASFDLKDAPP MPHLGYRLSV
     NDGTLAYTIL PTGNMWFQIV VFVVSTVAPV LTGLFAVWGF MGAFYSVKFN KVGVKVKGMG
     AFVPAFIGKR FAGKEKSRAL IPGSAAASRL SLVPGAAGAA AGALADRRTI LIATMEYDIE
     DWAIKIKIGG LGVMAQLMGK NLGHQDLIWV VPCVGGVEYP EAERAEPMSV TILGSTYEVE
     VQYHILRNIT YVLLDAPVFR KQTKTDPYPA RMDDLESAVY YSTWNQCIAL AIARFPIDLY
     HINDYHGAAA PLYMLPDRTI PVCLSLHNAE FQGLWPLRNS KEFNEVCSVF NLPAEIVERY
     VQFGDVFNLL HAGASYIRLH QKGFGAVGVS AKYGARSHAR YPIFWGLKKI GQLPNPDPTD
     LGEWTGKQDD SKVVIDETFE SARPGLKGQA QEWAGLNQDP DAELFVFVGR WSMQKGIDLI
     ADVFPAVLES NPKVQLLTVG PVIDLYGKFA ALKLDVMMKK YPGRVYSKPE FTALPPFIFS
     GAEFALIPSR DEPFGLVAVE FGRKGALGVG ARVGGLGQMP GWWFTVESTT TAHMLSQFKG
     SIKEALASKL ETRRKMRARS AKQRFPVAAW VDQLEKLQSS AINTHVKEVE RGGPRSGLSL
     PLPGRRSRGN SGTYSRPVSG MYSRTMSENA TPSGGNSPPL HPVYFNSDNS MPSTAAASQI
     TLNQSDFDRR RSPLDMGDDD NDLGDGLDRE SLISDPSKPV SLLSRDIPTP PEAEDGPSRE
     GDDLLGNQAR GRDGLGIHYQ SRSRPVSMLS LNTVVGDKKD FLLQKVDPDF TDSKGEYYKA
     FEGKLANLSA GNSEDALCIE DYLVKSEREW YSDFKNAKLG RSSDRSRSGS RSRSRSRSRS
     RGRSDSGSSV LTKKNRASPT PVLYDGEHEA YNMGDDDDEW LLGQDYKPPT GVRYLMQRRI
     GDWPVYSFVL AFGQIMAANS YQVTLLSGTA SSASIVYATG AIYIAFSVVW WILFRKAPSV
     YVLSVPFIFY GSAFFLLGLV PVANSSKVAQ LWIENVATGL YAAASPSGSI FFALNFGDEG
     GSPIKSWVFR ACIIQGTQQI YVVALWAWGN YQNNITGTGA ALSDSMITTT SLKFTAIMVP
     IACLIWAIGA LCYFGLPSYY RQAPGHVPSF YKAIMRRNIV IWFFIVIIIQ NYFLSASTGR
     NWQYLWSSQA AQIYQIALLA IFFFIIVWAL LLLLFAKLSQ AHSWILPLFA IGLIAPRWAQ
     ILWATSNIGI LLPWTGSPLA SALVSRSLWL WLGVLDAFQG VGFGMILLQT LTRLHIAYTL
     VGAQIFGSVA TMIARATSPN RDGQGDLFPD FSVGPLPGLS KPWFWVGLAF QLIITLGFLR
     FFRKEQLSKP
//
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