ID A0A0L0RUY2_ALLM3 Unreviewed; 1700 AA.
AC A0A0L0RUY2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN ORFNames=AMAG_00083 {ECO:0000313|EMBL:KNE54083.1};
OS Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS macrogynus).
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces.
OX NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE54083.1, ECO:0000313|Proteomes:UP000054350};
RN [1] {ECO:0000313|EMBL:KNE54083.1, ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE54083.1,
RC ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Allomyces macrogynus ATCC 38327.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA Lander E., Nusbaum C.;
RT "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000192};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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DR EMBL; GG745328; KNE54083.1; -; Genomic_DNA.
DR STRING; 578462.A0A0L0RUY2; -.
DR EnsemblFungi; KNE54083; KNE54083; AMAG_00083.
DR VEuPathDB; FungiDB:AMAG_00083; -.
DR eggNOG; KOG0916; Eukaryota.
DR OMA; FTFEALW; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000054350; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF29; 1,3-BETA-GLUCAN SYNTHASE COMPONENT FKS1-RELATED; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054350};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 541..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 569..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1161..1181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1217..1236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1302..1324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1330..1347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1409..1426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1446..1475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1487..1510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1586..1604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1657..1682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..245
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1700 AA; 184837 MW; 240F5581073E6E4C CRC64;
MSRAPAPATT ASLGVDDPPP GAPWATLLWT ECERLKHAFS FQPDSARNQF HLLHRLIASR
ASRLPTPNDA ICSVHADYVS GDHANYVRWL RAPGMTKALF PVQAAEGTDE EPQPTLSGPD
AWISSLRAAP DDATGLARLL ADVALWLLIW GEASNLRYCP EYLCLVFHLA LRRDCAPSPP
VSDAPAEAPF LDVVIRPAYT LLANAAKKPS GQFRQRDHTK IVGYDDWNEL FWDAEWLGSL
RTKSGQQLLL SQPPHAQFEL LAQIDWPKFA RKTFYESRTF THLVVNFARV WALHLGTFIT
LVPPVIYDGF FPPHLGNAPS PVLGPAPPTE TRLFLTGLGG ASVALLLLSV AAIEPCYLPT
SRQVVKRATA KVAWSLLFLV ANMVLPAAYV VYLLLSRPIE GGLGARSGGG PMRYVFGGGA
GRQLVALTQL AISLTTVAAT VARPVFPVHG ESLNNANPAF TARYPRESVL HGSTPRTSRP
GSQGTRRASV LLWTTILALK LITGYFFLLL PLGEPVRIVL QHACHTPVPT PTAGMAIPAP
LALCQVYGWV VTALLVVLTY TFFHLDTYMW YTIATAITGF ALSVVDGASI FRPWQGVFVR
LPDRIRAKIL TTTRALGTTA ATAARVPMTH VAVLWNAIVE SFYTGHQISR PARTSMLYTR
TATELVRPDF FDRQEDASAA VASDAAIQRL RFFGQSLSMR QLPAPLPVKS VPALTVLVPH
YAEATLVSLR ELVRDGDRGS MLQLAYLQAL FPDDWARYVA ANGDVEDLEV GDVDGGGAGD
MPLQMLGFRA PTNAAVLRTR MWASARTQTL YRTILGMMQY RAALMMLAQL EDPKTADRVV
DAWVPTDAEV ERVGEVPTSR AATQLVDEKL TLLVAMQRYA VMTDSERADV DAVRTQFPHC
TLWIAYVEHV DDKWFACLLV HPNDAEVPAH DRDLAEGATA ASHLLYRIEL PGAPTLGDGK
ADNQNTALMF QRGEVLQLID ANQDHYLEEA VKVRSVLAEF ARGDPMLAMV GGREFIFSES
IGLLGNVAAG KEYTFGTLTQ RVMSYLRSRL FYGHADAFNF TFMATRGGVS KGQRGLHLNE
DIYAGMNAQM RGGQIVHTEY MQCGKGRDLG FASILQFTTK IGSGMAEQLI AREHYYLGTQ
LPWDQLLTFY FAHPGFHLTN VLSLVAIRLF LLVTFLLTWY FPSQVGAACT APVPSSMCES
TNPHDRSIVL DWMRQSLLAF VVYFISYLPF ALQLVVEHGL VHALRRLLHQ VVSLAPVFET
MVTQMYAHAL CAGMHAKQAK YAATGRRVAT ARASFSSLYA QYAHVSIQLG LGLTALLAVT
GMSLPSLPPL AFVAFITVSI AIAPFVFNPH QLHRRLLARD YAATLRWLLV PSSGWASQAH
RVKRAAMTGM RGQFAVRLRR KLTRVRDNWL LLAALLWPLT AVPLPTPQLA AKAMASSVAH
GANLRLPLAV VAVACVPLAV SAAIHVAVAP LVAMLGLARV RTDALGAVAR GACVVSVLVS
WLAACILANF DPPVALLSIL ATAQVKQAVT VTAYAFFSRE PDTDAGAAWW GYGTAAKFSP
LGCLSTVVIR ETVAKVLEGW DLGVDFWLVH VLYLGVLVPA AMLPNGDHVH TYHMLLWSCP
ETVAPTHAAA AVGDGTEVGV VLPLRMKRVH GAKDDRVPWG AMVFLGSVVV LVVGVAVVAG
LAPGLVAGVG ARALAIVPVG
//
