ID   GEL2_ASPFU              Reviewed;         475 AA.
AC   P0C954; Q4WM30; Q9P8U4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   04-NOV-2026, entry version 87.
DE   RecName: Full=1,3-beta-glucanosyltransferase gel2;
DE            EC=2.4.1.-;
DE   AltName: Full=Glucan elongating glucanosyltransferase 2;
DE   Flags: Precursor;
GN   Name=gel2; ORFNames=AFUA_6G11390;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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. Involved in cell wall morphogenesis (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR   EMBL; AAHF01000006; EAL88984.1; -; Genomic_DNA.
DR   RefSeq; XP_751022.1; XM_745929.2.
DR   AlphaFoldDB; P0C954; -.
DR   SMR; P0C954; -.
DR   FunCoup; P0C954; 62.
DR   STRING; 330879.P0C954; -.
DR   Allergome; 8986; Asp f GT.
DR   CAZy; GH72; Glycoside Hydrolase Family 72.
DR   GlyCosmos; P0C954; 4 sites, No reported glycans.
DR   EnsemblFungi; Afu6g11390-T; Afu6g11390-T-p1; Afu6g11390.
DR   GeneID; 3508327; -.
DR   KEGG; afm:AFUA_6G11390; -.
DR   VEuPathDB; FungiDB:Afu6g11390; -.
DR   eggNOG; ENOG502QRZZ; Eukaryota.
DR   HOGENOM; CLU_021855_1_2_1; -.
DR   InParanoid; P0C954; -.
DR   OMA; AAGMYMM; -.
DR   OrthoDB; 421038at2759; -.
DR   PHI-base; PHI:434; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:AspGD.
DR   GO; GO:0042123; F:glucanosyltransferase activity; IDA:AspGD.
DR   GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:AspGD.
DR   FunFam; 3.20.20.80:FF:000032; 1,3-beta-glucanosyltransferase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR004886; Glucanosyltransferase.
DR   PANTHER; PTHR31468; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR   PANTHER; PTHR31468:SF4; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS3-RELATED; 1.
DR   Pfam; PF03198; Glyco_hydro_72; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Reference proteome; Signal; Transferase.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..451
FT                   /note="1,3-beta-glucanosyltransferase gel2"
FT                   /id="PRO_0000245549"
FT   PROPEP          452..475
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000245550"
FT   REGION          420..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..446
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="1"
FT                   /ligand_note="donor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         159
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="1"
FT                   /ligand_note="donor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         160
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="2"
FT                   /ligand_note="acceptor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         201
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="2"
FT                   /ligand_note="acceptor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         294
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="1"
FT                   /ligand_note="donor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   LIPID           451
FT                   /note="GPI-like-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        69..98
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        215..350
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        234..265
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
SQ   SEQUENCE   475 AA;  51718 MW;  AD974DE49CDF0A91 CRC64;
     MLPTYVRLFT AVCALATTAS AVVPIEVKGK DFVNSKTGDR FQILGVDYQP GGSSGFTKDK
     DPLSDPDACL RDAALMQRLG VNTIRIYNLS PSLNHDECAS IFNAAGIYMI LDVNSPLYGG
     YLDRTDPEST YNDVYFKQVF GVIEAFKNFP NTLAFFAGNE VINEQSVKNV PTYVRAIQRD
     MKDYIAKNLD RSIPVGYSAA DIRPILMDTL NYFMCADDAN SQSDFFGLNS YSWCGNSSYT
     KSGYDVLTKD FADASIPVFF SEYGCNEVQP RYFSEVQALY GQEMTQSFSG GLVYEYTQEE
     NDYGLVQIND NGTVTLLVDY DNLMAQYSKL DMSRIQASNT TQTSAKPPKC ESSLITNSTF
     TDSFDLPKRP SKVQTMIDKG LSDANTGKLV EVKNTDIKQK IYNANGEEIT GIKLSILASG
     ESNTPGAHSS GSTSGSSSSG GSSSSSSDKE SAAGTISVPF VGLLSAASFM AFFML
//