ID A0A167YK06_CORDF Unreviewed; 1838 AA.
AC A0A167YK06;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 03-MAY-2023, entry version 21.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase {ECO:0000256|ARBA:ARBA00031935};
GN ORFNames=LEL_10502 {ECO:0000313|EMBL:OAA66403.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA66403.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA66403.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA66403.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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}.
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:OAA66403.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZHF01000013; OAA66403.1; -; Genomic_DNA.
DR STRING; 1081108.A0A167YK06; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000076881; 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:UP000076881};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAA66403.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 424..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1274..1294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1325..1346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1421..1439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1445..1461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1534..1553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1573..1600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1612..1635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1647..1669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1702..1723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1769..1793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 278..390
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1838 AA; 210370 MW; 6FE5D7F6175DC6C5 CRC64;
MTENAESNNL HRNNGHANYY GNSTPDNNPY YQDSYAHDDY QVNGEYDESG YYDESGYYEA
RPENPYYNDG GYYDGESQYA DEYGYHYTDE GLDQSDLGRA SFDGFSMPMA ASQRSVPESL
VDYADENTAS ISEPYPAWSG EAQVPVSKEE IEEIFMELTN KLGFQRDSMR NMYDHLMVML
DSRASRMTPN QALLSLHADY IGGHNANYRK WYFAACFDFD HKSKASGRKE RSGSKKKKWK
GSTGTEVNAK DIIEESEPLT LRTAEDQWRT RMSRMSQLQR VRQISLYLLC WGEANQVRFM
PEALCFIFKC ADDFVNAPIS QTASEGAEEV TYLNTIITPL YRYIRDELYE ISDGVYVRRE
RDHKDTIGYD DCNQLFWYPE GISRIVLQDG GKIMDFSPEE RYLKLRDVKW QKCFFKTYKE
TRSWLHMLIN FNRIWIIHVT MFWFYTSHNA PTLLVKDYEQ TLDQQPTPAK QFSIVGFGGC
IATLIQILAT FAEWVYVPRK WPGASHLTSR LFILIGILIL NAAPGVKVFL FPTQKKDKLY
RIDLALGIVQ FVIAVLTYIY FSIVPLESLF GKFWKKNRNR PLANQVFTDN FPDLSFNDRA
TSVGLWMVVF GIKFGVSYKF LTLSYRDVIR YLDIAKVTCA GDNIFGKVTD VLCKHHNVIL
IVLTGCTDVI FFFLDTYLWY VLVNTAFSIA RAFYLGSSIL TPWRNVFTRL PKRIYSKVLA
TPDMDVKYQP KILISQIWNA VVISMYREHL LALEHVQKLL YYQVSSEETG KRTLRAPTFF
VSQDDNSFKS EFFPANSEAS RRISFFAQSL SMPLPEPAPV DGMPTFTVMI PHYSEKILLT
LREIIREEDP HSRVTVLEYL KQLHPHEWEC FVEDTKILAD GTAGVEPDED KKKVDDLPFY
CIGFKSSSPE YTLRTRIWSS LRSQTLYRTV SGFMNYARAI KLLYRVENPG EVQAFGRQAH
RLDQELERMS RRKFKILVSM QRFTKFSKDE MENTEFMLRA FPDLQIAYLD EQAPEVDGEE
PRIFSTLIDG HSEIMENGQR KPKFRVQLSG NPILGDGKSD NQNQALIFYR GEYIQLVDAN
QDNYLEECLK IRNVLAEFEE MTASKLSPYS PNFRTKSPVA IVGAREYIFS ESMGVLGDIA
AGKEQTFGTL FARTLSQIGA KLHYGHPDFL NGIFMTTRGG VSKAQKGLHL NEDIFAGMTA
ITRGGRIKHS EYYQCGKGRD LGFGSVLNFT TKIGTGMGEQ LLCREYYYIG TQLPLDRFLS
FYYAHPGFHV NNMFIMFSIQ LFMICLLNIG VFSYETIPCD YNPDKPITDL LLPVGCVNTN
ALRDWIWRCI LSIFVVFFIS FIPLVAHEVI DRGVLRAVTR FLKQLFSLSI FFEIFACQIY
ANAIEQDISY GGARYIGTGR GFATSRIPFG VLYSRFAGNS IYLGFRLLVI LLFTSVTIWQ
AGLTYFWISV LALTISPFLF NPHQFAWGDF FIDYREFIRW LSRGNSRTHA SSWISFCRFS
RTRIIGYKRK VLGEKSHVSD VARPPKLNLF LSEILAPFLL AVVTVIPYLF INAQTGVIPE
NNDDTKTVPT DSLIRVLIIA IGPIALNLAV LAVMFAMACC MGPVLSMCCK RFGSVLAAIA
HGLAVVFMLV SFEAMFVFES FNFARTLAGL VAVISIQRFI IKLIVTLALT REFKTDQSNL
AFWTGKWYSM GWHSISQPAR ELLCKLVELS MFAADFIIGH WILILMFPLL LIPRIDTLHS
MLLFWLLPSR QIRPPIYSLK QSKLRKTRVA RYAALYLCLL VVFVGMVAGP IAYSNAGEPA
SLLSKIPKIG DFVLLQPNHQ NNNNTSGDVK NLTTTAST
//
