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1,3-beta-glucanosyltransferase gel1 (EC 2.4.1.-) (Glucan elongating glucanosyltransferase 1)

 GEL1_ASPFU              Reviewed;         452 AA.
P0C7S9; O74687; Q4WIP0;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 1.
20-JUN-2018, entry version 59.
RecName: Full=1,3-beta-glucanosyltransferase gel1;
EC=2.4.1.-;
AltName: Full=Glucan elongating glucanosyltransferase 1;
Flags: Precursor;
Name=gel1; Synonyms=bgt2; ORFNames=AFUA_2G01170;
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
A1100) (Aspergillus fumigatus).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=330879;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
PubMed=16372009; DOI=10.1038/nature04332;
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
Machida M., Hall N., Barrell B.G., Denning D.W.;
"Genomic sequence of the pathogenic and allergenic filamentous fungus
Aspergillus fumigatus.";
Nature 438:1151-1156(2005).
-!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and
transfers the newly generated reducing end (the donor) to the non-
reducing end of another 1,3-beta-glucan molecule (the acceptor)
forming a 1,3-beta linkage, resulting in the elongation of 1,3-
beta-glucan chains in the cell wall. Involved in cell wall
morphogenesis (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}.
-!- PTM: The GPI-like anchor contains a phosphoceramide lipid group.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
{ECO:0000305}.
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EMBL; AAHF01000008; EAL87215.1; -; Genomic_DNA.
RefSeq; XP_749253.1; XM_744160.1.
ProteinModelPortal; P0C7S9; -.
SMR; P0C7S9; -.
CAZy; GH72; Glycoside Hydrolase Family 72.
PRIDE; P0C7S9; -.
EnsemblFungi; EAL87215; EAL87215; AFUA_2G01170.
GeneID; 3506970; -.
KEGG; afm:AFUA_2G01170; -.
EuPathDB; FungiDB:Afu2g01170; -.
HOGENOM; HOG000164982; -.
InParanoid; P0C7S9; -.
OMA; AQYMNCG; -.
OrthoDB; EOG092C1TYR; -.
Proteomes; UP000002530; Chromosome 2.
Proteomes; UP000002530; Unassembled WGS sequence.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009277; C:fungal-type cell wall; IDA:AspGD.
GO; GO:0005886; C:plasma membrane; IDA:AspGD.
GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:AspGD.
GO; GO:0042123; F:glucanosyltransferase activity; IDA:AspGD.
GO; GO:0031505; P:fungal-type cell wall organization; ISA:AspGD.
InterPro; IPR004886; Glucanosyltransferase.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR31468; PTHR31468; 1.
Pfam; PF03198; Glyco_hydro_72; 1.
SUPFAM; SSF51445; SSF51445; 1.
3: Inferred from homology;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal;
Transferase.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 419 1,3-beta-glucanosyltransferase gel1.
/FTId=PRO_0000245547.
PROPEP 420 452 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000245548.
ACT_SITE 160 160 Proton donor. {ECO:0000250}.
ACT_SITE 261 261 Nucleophile. {ECO:0000250}.
BINDING 89 89 Donor substrate; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q06135}.
BINDING 159 159 Donor substrate.
{ECO:0000250|UniProtKB:Q06135}.
BINDING 160 160 Acceptor substrate.
{ECO:0000250|UniProtKB:Q06135}.
BINDING 201 201 Acceptor substrate; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q06135}.
BINDING 206 206 Acceptor substrate.
{ECO:0000250|UniProtKB:Q06135}.
BINDING 292 292 Donor substrate.
{ECO:0000250|UniProtKB:Q06135}.
LIPID 419 419 GPI-like-anchor amidated alanine.
{ECO:0000255}.
CARBOHYD 249 249 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 71 100 {ECO:0000250|UniProtKB:Q06135}.
DISULFID 215 345 {ECO:0000250|UniProtKB:Q06135}.
DISULFID 233 264 {ECO:0000250|UniProtKB:Q06135}.
SEQUENCE 452 AA; 48077 MW; 017169E2BCDCB66E CRC64;
MKASAVTAAL AVGASTVLAA PSIKARDDVT PITVKGNAFF KGAERFYIRG VDYQPGGSSD
LADPIADADG CKRDIAKFKE LGLNTIRVYS VDNSKNHDEC MNALADAGIY LVLDVNTPKY
SINRAKPKES YNDVYLQYIF ATVDAFAGYK NTLAFFSGNE VINDGPSSSA APYVKAVTRD
LRQYIRSRKY REIPVGYSAA DIDTNRLQMA QYMNCGSDDE RSDFFAFNDY SWCDPSSFKT
SGWDQKVKNF TGYGLPLFLS EYGCNTNKRQ FQEVSSLYST DMTGVYSGGL VYEYSQEASN
YGLVEISGNN VKELPDFDAL KTAFEKTSNP SGDGNYNKTG GANPCPAKDA PNWDVDNDAL
PAIPEPAKKY MTEGAGKGPG FAGPGSQDRG TQSTATAEPG SGSATGSSSS GTSTSSKGAA
AGLTVPSLTM APVVVGAVTL LSTVFGAGLV LL


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