ID A0A2V1AUC1_9ASCO Unreviewed; 1835 AA.
AC A0A2V1AUC1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 08-OCT-2025, 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};
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase {ECO:0000256|ARBA:ARBA00031935};
GN ORFNames=CXQ85_000351 {ECO:0000313|EMBL:PVH21374.1};
OS Candidozyma haemuli.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC Metschnikowiaceae; Candidozyma.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH21374.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH21374.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH21374.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-2017) 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) + UDP + H(+); 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:ARBA00047777};
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:PVH21374.1}.
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DR EMBL; PKFO01000005; PVH21374.1; -; Genomic_DNA.
DR RefSeq; XP_025342314.1; XM_025484099.1.
DR STRING; 45357.A0A2V1AUC1; -.
DR GeneID; 37005684; -.
DR VEuPathDB; FungiDB:CXQ85_000351; -.
DR OrthoDB; 19159at2759; -.
DR Proteomes; UP000244309; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
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 GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IEA:TreeGrafter.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR056261; FKS1-like_dom2.
DR InterPro; IPR003440; Glyco_trans_48_dom.
DR PANTHER; PTHR12741:SF48; 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; PF23605; FKS1_dom2; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
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:UP000244309};
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 963..982
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1088
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1108..1131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1151..1169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 163..275
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1605..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1411
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1835 AA; 211224 MW; A171E3C46CAA48E6 CRC64;
MKHDLSDKVT SPESLPASAS MVSPYPSWHK NNGAPMDVDS VKSVFDDLQA MFGFQKASSV
NMFQYLMSLL ESRSSRMPCN LALVSIHADY IGGDNANYKK WYFAAAYDLD HGYTDKKSIR
AKWKELPQYL QGKHVPNGSK TDANGWWAME TSWRQRMRAY TEEDYLKQLA LYLLIWGEAN
NVRFMPECLC FIYRCASDYM YSFQDEAPPG LPEFYFLDNI ITPIYNYIRD QQFDAIDGKF
FRKLGKDHSH TVGYDDVNSF FWFDQNLKKI SLEDGTNLID HPSETHYTLL HSVDWNNVFF
KSYYETRSWF HLIVNFSRIW IIHLSMFWYF FTINTPVLYT KNYMPHLDNR PAPQVQLFFS
AVLSYSSGTS TLKPWKTTFD RLPTLFLSKV HFPLCSSQKD NFAISKLWNC IVISLYRDHL
VSVEQANRLV YQHDPTETPW RAPTIATPPN FFGSQDDGVA SDAESVFSQS KESARRISFF
ARSLTCQWPE SYSIEGLPSF TVLIPHYSET MVIGQKALLK ERPGCKISLL DYLKKMHKKE
WRSFVREAKL MDAVLSSSIP NTADSALGKD LVSPGSLPES AALEGKFVDE CIDDIPYNSV
GYKNSFPEFA KRTRIWASLR CQTLYRTITG FMNYQTALKA LYFSETYSFE SEHLADQAEL
ELELDRFVSR KFRLLVSMQR YLDFDLEEQE SVEMLRSCNP NLKICYIEKS GEFYYSVLLG
SRNGSEEGTP LRIRLSGNPI IGDGKSDNQN HAVIFQRGEY LQTIDANQDN YIEECLKIKA
VLAEFEEIQV DPSSTYEADI VNAVRPAPIA FLGAREFIFS EKTGVLGDIA AGKEQTFGTL
FARTLSKVDA KLHYGHPDFI NTIFMFTRGG ISKAQKGLHL NEDIYSGMNA ISRGGRIKHC
DYYQCGKGRD MGFGSIVNFT TKIGAGMGEQ SLSRELFNLG TTLPIDRFLS FYYAHAGFHI
NNVFIILSVE LFLLIFLTIG ALKFETISCE DIPGSLPTDP KFALREFILD YKHFLHWIFS
EQTKANSSWS LFRKRHRSRF TGVKKKLLNV QGKHLVELNS PSRWSRLHLD VLYPAVEFCL
YLVPYLFITA QSGVKNPTPV NPIMRVLILS LLPVVLNFIF LIVTFPVNFV LGNTLGLCCG
KYPKMSRGLT FVWSLVNFAF SIQVVIHLHE YSIARTLCAF VCITKFQTWL RNVIYTLCLT
KELDTSSVSS SWWSGKWSLK TLSWLVVTQP SRELFVKTTE LTIGEEFDFE TDGIPTLRPS
QNDDLFGLEE DFGTLRLSPQ KQSSNRPPAR QLNHKPSLSP GFMMQFVESE EDHLSFDKDF
NENDLFNPGD VLRQNGSLVT PKAKFSPGTA SNPSPLRRRS LSDYSEGTDT AMTSEMDDDD
FEEEIDDIFG KEESGIYSSG GRSNSNPNGS RAGQILSNKK EQLQRQAEKE EAEMYERYKQ
SRHSEGAINT LKLKDLNQAM SNNQINQDPL ENERTVNYEY TRDDNEAFED GFDLEQPLDL
EISKFHRPSL KKKSLAREMS MPNFPKSLES SRPTKYKSSM DLAAFTRKDH PVFNSSNEII
KRLNRMPSFH NQTGRSEPKN DDEINRDMEL RKKELLEKYM EITEKQKKLN TSPQRNKTAS
REPTNKRKGV GLVKFLNNQD NAPAVNPNNK MKYNPMHKLW EGNEHDLMRF EEPESDHPGR
KPGLIRKQDF QQRTEKIQGN MRYDAENLRW VNTEDDDKEN EKIFEDVPDL EPNDIPQYTR
PDLNFDIHGR GVSTFTQRTV STTSSDRSSA LGRQNVGNEF QLSTKNLSRF EKEEAKIKRK
THNWFAPKEQ YRLNKERTFS GDYFWEIRKM VCEEN
//
