ID A0A316YPQ1_9BASI Unreviewed; 1813 AA.
AC A0A316YPQ1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JUN-2023, entry version 14.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN ORFNames=FA10DRAFT_242039 {ECO:0000313|EMBL:PWN91006.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN91006.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN91006.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN91006.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819636; PWN91006.1; -; Genomic_DNA.
DR STRING; 215250.A0A316YPQ1; -.
DR InParanoid; A0A316YPQ1; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000245768; 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:UP000245768};
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 433..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 514..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 642..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 675..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1286..1305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1335..1356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1437..1470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1541..1563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1575..1604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1616..1642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1649..1673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1774..1799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 287..399
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1813 AA; 203183 MW; BA20A74AD681E2EE CRC64;
MASPGGYGGH GPPPSGGHGG GAVPPTNPFA GFHDEAASES SYRRDTFASE GSAADLIPGH
GYNDGDSFEG GYNKEAYAYS QESGGPGGRG GPPPMMAGSQ MSSHGGGSGN GGMGAGGYGA
ASYAPSGISS PYTDYPGQGY RQREPYPAWT AEHQIPLAKE EIEDIFIDLA NKFGFQRDSM
RNMYDHLMIL LDSRSSRMSP TQALLTLHAD YIGGEHANYR KWYFAAQLDL DDAIGKAQNP
GLARAASLGG KKTGAAAAAA AKLNASAKSL ESAATRWREA MNRMSDYDRL RQIALYLLCW
GEGGQVRFVP ECLCFIFKCA DDYYRSPECQ NRMEPVPEGL YLRAVVKPLY RFLRDQVFEV
VDGKFVKKEK DHDKIIGYDD VNQLFWYPEG IGRIVLNDKT RLVDVPANQR FMKFDKIDWN
RVFFKTYKEK RSFAHVLVNF NRIWILHISV FWYYTAFNAP MIYEQTKNPS TAQLLSASAL
GGAVSTVLMI LATIAEFSYI PTTWNNTSHL MRRMIFLLIC LGVTVAPAVY IHGFNKEGTV
ANIVSYCHIG AAGCITALFS LVPSGRMFGD RVAGKARKYL ANQTFTASYA PLQASHRFVS
CLLWCLIFGC KLTESYFFLT LSFRDPLAVM ITMKVQACSD KYFGAGLCAN QPAFALTAMT
IMDLCLFFLD TFLWYVIWNS VFSIAWSFSM GLSIWTPWSD IFQRLPKRIY AKLLATADME
IKYKPKVLVS QVWNAIIISM YREHLLSIDH VQKLLYHQVP SGDEGKRTLR APMFFISQTD
KGVKSEFFPK GSEAERRISF FAQSLTTTLP EPLPIDAMPT FTVLTPHYSE KILLSLREII
REEDQNTRVT LLEYLKQLHP IEWDNFVKDT KILAEETSGL AGSSPFGAGD GSDEKSGTKG
SSTKTDDLPF YCIGFKSAAP EYTLRTRIWS SLRAQTLYRT VSGFMNYAKA IKLLYRVENP
EVVQLFGGNT EKLERELERM SRRKFKFVIS MQRYSKFNKE EHENTEFLLR AYPDLQIAYL
DEEAPRKDGG ESRWFSALVD GHSEILPNGK RRPKFRIELP GNPILGDGKS DNQNHAIVFH
RGEYVQLIDA NQDNYLEECL KIRSVLGEFE SFNVSNQNPY GSGHREHAKS PVAILGAREY
IFSENIGILG DVAAGKEQTF GTLAGRGLAQ IGGKLHYGHP DFLNALFMTT RGGVSKAQKG
LHLNEDIYAG MNAFGRGGRI KHCEYYQCGK GRDLGFGTIL NFTTKLGNGM GEQMLSREYY
YLGTQLPIDR FLTFYYGHPG FNINNILVIM SVQMFMLAMV FIGTLNAELS ICESTNSEYQ
VGTGGCYYLQ PVFEWIKRTI ISIFLVFMIA FLPLFLQELS ERGALSAIVR LSKHFLSLSP
VFEVFSTQIS SHSIISNMTF GGARYIATGR GFATTRQSFA LLYSRFAGPS IYSGMRLLLL
LLYVTLTLWI PHLIYFWVSI LALCIAPFLF NPHQFSISDF IIDYREFLRW MSRGNSRSHA
NSWIGYCRLS RTKVTGYKKK RLGHPSEKLA GDVPRASWRT IIFAECLGPF IMAVIFVVAY
AFVKSFHNRG DPPMGAIARI AIIALGPIVW NAAVLLILFM ISMFLGPALN NCCAKFGSVM
AAIAHILAVV GIIVAFEFLW FLELWNASHA VLGIIAVVAI QRAIFKILIS LVLSRELKHD
ETNRAWWTGR WYGRGLGGHA FSQPAREFVV KIIEASLFSA DFVQAHILLF GLSLPLLIPF
MNKIHSMMLF WLRPSRQIHA PIYSLRARKQ RRSIVIRYGL LFVLAFAIFV CLIAVPAILG
STINVDCEFC KTL
//
