ID   Q9HG19_CANDU            Unreviewed;       550 AA.
AC   Q9HG19;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   04-NOV-2026, entry version 79.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   Name=PHR1 {ECO:0000313|EMBL:AAG16995.1};
OS   Candida dubliniensis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Candida.
OX   NCBI_TaxID=42374 {ECO:0000313|EMBL:AAG16995.1};
RN   [1] {ECO:0000313|EMBL:AAG16995.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 7987 {ECO:0000313|EMBL:AAG16995.1};
RX   PubMed=10959725;
RA   Heinz W.J., Kurzai O., Brakhage A.A., Fonzi W.A., Korting H.C., Frosch M.,
RA   Muhlschlegel F.A.;
RT   "Molecular responses to changes in the environmental pH are conserved
RT   between the fungal pathogens Candida dubliniensis and Candida albicans.";
RL   Int. J. Med. Microbiol. 290:231-238(2000).
CC   -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC       the newly generated reducing end (the donor) to the non-reducing end of
CC       another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC       linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC       cell wall. {ECO:0000256|RuleBase:RU361209}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU361209};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU361209}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC       {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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DR   EMBL; AF184907; AAG16995.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HG19; -.
DR   VEuPathDB; FungiDB:CD36_44230; -.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-ARBA.
DR   GO; GO:1903561; C:extracellular vesicle; IEA:UniProtKB-ARBA.
DR   GO; GO:0030446; C:hyphal cell wall; IEA:UniProtKB-ARBA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030445; C:yeast-form cell wall; IEA:UniProtKB-ARBA.
DR   GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IEA:TreeGrafter.
DR   GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:UniProtKB-ARBA.
DR   FunFam; 3.20.20.80:FF:000038; 1,3-beta-glucanosyltransferase; 1.
DR   Gene3D; 1.20.58.1040; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR004886; Glucanosyltransferase.
DR   InterPro; IPR012946; X8.
DR   PANTHER; PTHR31468; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR   PANTHER; PTHR31468:SF2; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR   Pfam; PF03198; Glyco_hydro_72; 1.
DR   Pfam; PF07983; X8; 1.
DR   SMART; SM00768; X8; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622, ECO:0000256|RuleBase:RU361209};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU361209};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361209};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361209};
KW   Transferase {ECO:0000256|RuleBase:RU361209}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT   CHAIN           21..550
FT                   /note="1,3-beta-glucanosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT                   /id="PRO_5005144812"
FT   DOMAIN          388..476
FT                   /note="X8"
FT                   /evidence="ECO:0000259|SMART:SM00768"
FT   REGION          483..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..520
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  59655 MW;  EF863599FBE51EAD CRC64;
     MYSLIKSLAT FVTLFSLTLA KFESSTPPIE VIGNKFYFSN NGSQFLIRGI AYQQDAAGSV
     SSGYDADPNR KYTDPLADAD ACKRDVKYFK ESNTNALRVY AIDPEKDHEE CMKIFSDAGI
     YIVADLSEPT VSINRNSPEW NLDLYERYTK VVDNMQEYSN VLGFFAGNEV TNNRSNTDAS
     PFVKAAIRDM KKYLKDSNYG EIPVGYSSND DEEIRVAIAD YFSCGSLDDR ADFFGINMYE
     WCGKSTFESS GYKDRTEEIK NLTIPAFFSE YGCNANRPRL FQEIGTLFSD KMTDVWSGGI
     VYMYYEEANK YGLVSVDGDS VKTLSDYNNY KSEMNKISPS LAHTSTLSSS EASKTLECPG
     TAASTWKAAT KLPPTPDKDY CDCVSKSFEC VVADSVEKED YGDLFAQVCG YIDCSAISAD
     GNKGDYGVAS FCSDKDRLSY VLNEYYIDQD KKSSACDFKG SASINSKASS SGSCKAVSGV
     ATGKDSASGG SSKSGSGSAS SSASGSSSSS TSSGSSSSSG NKSTQQMSMV KLVSITTIVT
     AFVGGMSIIF
//