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GEL4_ASPFU
ID   GEL4_ASPFU              Reviewed;         548 AA.
AC   P0C956; Q4WHH9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=1,3-beta-glucanosyltransferase gel4;
DE            EC=2.4.1.-;
DE   AltName: Full=Glucan elongating glucanosyltransferase 4;
DE   Flags: Precursor;
GN   Name=gel4; ORFNames=AFUA_2G05340;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
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 / Af293 / CBS 101355 / FGSC A1100;
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:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
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; AAHF01000008; EAL87626.1; -; Genomic_DNA.
DR   RefSeq; XP_749664.1; XM_744571.1.
DR   AlphaFoldDB; P0C956; -.
DR   SMR; P0C956; -.
DR   STRING; 746128.CADAFUBP00002184; -.
DR   CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR   CAZy; GH72; Glycoside Hydrolase Family 72.
DR   PRIDE; P0C956; -.
DR   EnsemblFungi; EAL87626; EAL87626; AFUA_2G05340.
DR   GeneID; 3506753; -.
DR   KEGG; afm:AFUA_2G05340; -.
DR   eggNOG; ENOG502QPST; Eukaryota.
DR   HOGENOM; CLU_021855_2_1_1; -.
DR   InParanoid; P0C956; -.
DR   OMA; CATQMSA; -.
DR   OrthoDB; 728071at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR004886; Glucanosyltransferase.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR012946; X8.
DR   PANTHER; PTHR31468; PTHR31468; 1.
DR   Pfam; PF03198; Glyco_hydro_72; 1.
DR   Pfam; PF07983; X8; 1.
DR   SMART; SM00768; X8; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Reference proteome; Signal; Transferase.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..519
FT                   /note="1,3-beta-glucanosyltransferase gel4"
FT                   /id="PRO_0000245553"
FT   PROPEP          520..548
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000245554"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        277
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
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         133..141
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         174
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         175
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         217
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         222
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         309
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           519
FT                   /note="GPI-like-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        425
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        88..117
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        231..364
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        249..280
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        386..437
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        395..461
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        414..419
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
SQ   SEQUENCE   548 AA;  58873 MW;  191DA9A1D29778FE CRC64;
     MKFVYAAAGA SLVGSALATL PVIEAKVLKA CCWTIALDAN SYGNKFFYSN NGTEFFIRGV
     AYQQEYQANG TSTENSDYTD PLANVDNCKR DIPYLKQLRT NVIRTYAVDP TKDHDECMKL
     LDDAGIYLIT DLSAPSESIN RADPAWNTDL YKRYTSVIDA FAKYSNVIGF FAGNEVANDN
     NNTNSIAYVK AAVRDMKSYI KSKDYRSSLL VGYATDDDAH IRADLADYLV CGDKESSIDM
     FGYNIYEWCG DSSFEKSGYK DRTEEFSKYP VPAFFSEYGC IDPKPRKFTD VAALYGPQMN
     DVWSGGIVYM YFQEANDYGL VSVSGDNVKT KEDFSYLSVQ MQKVTATGVN SASYTASNTA
     VPTCPSVGAK WEASNKLPPS PNSELCDCMV ETLSCTVKDS VDEKEYGDLF DYLCAAGVCG
     GINSNSTSGD YGAYSVCSAK QKLSFVMNQY YKKNNKAATA CDFDGKAQTK KGADASGSCA
     SLISQAGTAG TGSVTAGATG SSGSGSASET SKGAAGVAAS PMAVKVGNWQ FGAYIATALF
     AGVGMLVL
 
 
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