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PLB2_ASPFU
ID   PLB2_ASPFU              Reviewed;         588 AA.
AC   Q9P8P4; Q4WE07;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Lysophospholipase 2;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B 2;
GN   Name=plb2; ORFNames=AFUA_5G01340;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 393-573, AND VARIANTS ASN-398 AND
RP   VAL-573.
RC   STRAIN=ATCC 90240 / AF-10;
RX   PubMed=15451105; DOI=10.1016/j.femsle.2004.08.019;
RA   Shen D.-K., Noodeh A.D., Kazemi A., Grillot R., Robson G.D., Brugere J.-F.;
RT   "Characterisation and expression of phospholipases B from the opportunistic
RT   fungus Aspergillus fumigatus.";
RL   FEMS Microbiol. Lett. 239:87-93(2004).
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR   EMBL; AAHF01000011; EAL86170.1; -; Genomic_DNA.
DR   EMBL; AF223005; AAF64039.1; -; Genomic_DNA.
DR   RefSeq; XP_748208.1; XM_743115.1.
DR   AlphaFoldDB; Q9P8P4; -.
DR   SMR; Q9P8P4; -.
DR   STRING; 746128.CADAFUBP00004876; -.
DR   EnsemblFungi; EAL86170; EAL86170; AFUA_5G01340.
DR   GeneID; 3505495; -.
DR   KEGG; afm:AFUA_5G01340; -.
DR   VEuPathDB; FungiDB:Afu5g01340; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   InParanoid; Q9P8P4; -.
DR   OMA; FYRYASQ; -.
DR   OrthoDB; 564952at2759; -.
DR   BRENDA; 3.1.1.5; 508.
DR   Proteomes; UP000002530; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..588
FT                   /note="Lysophospholipase 2"
FT                   /id="PRO_0000245557"
FT   DOMAIN          31..574
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   REGION          15..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        529
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        570
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         398
FT                   /note="L -> N (in strain: ATCC 90240 / AF-10)"
FT                   /evidence="ECO:0000269|PubMed:15451105"
FT   VARIANT         573
FT                   /note="I -> V (in strain: ATCC 90240 / AF-10)"
FT                   /evidence="ECO:0000269|PubMed:15451105"
SQ   SEQUENCE   588 AA;  63239 MW;  D268F56BC6EABDD5 CRC64;
     MYKNRVELTT TAPVNRALPN APDGYTPQGE TCPSKRPSIR NATALSSAET SWLKARRNNT
     KDALKAFLSR VDLGSFNGSD YIANHSANAS ALPNIGIAVS GGGYRALMNG GGALQAFDNR
     TTNSTHSGQL GGILQSATYL SGLSGGSWLV GSIYMNNFSD VSSLQDNGSV WQFQDSIFSG
     PTQSTTWDIG TVEYYSQLLG AVDGKSNAGY EVSITDYWGR SLSYQLINAS EGGVGYTWSS
     IALSKDFQAG TMPMPLVIAD GRAPGEILVP ANTTVFEFNP WEFGSWDKSL SAFVSLEFLG
     SNFSKGTLAT GEKCVRGFDN AGFIMGTSSS LFNQAFLQMN NTDAPSVVKD AISAILGKIG
     SENNDIAVYK PNPFYRYASQ SKYTSSPSLT LVDGGEDLQN IPLDPLLQPQ RHVDVILAVD
     SSADTTTRWP NGTSLVATYE RNVDSSQRNS SLPFPSVPDQ NTFVNLGLNN RPTFFGCNSS
     NATGAPLVVY IPNAPYIYPS NVSTFDLQYN TSERNAIIEN GYDVATLGNG TVDSNWPACL
     ACAILSRSFE RTNTTVPKTC STCFKTYCWN GTINATTPGD YYPTLKLH
 
 
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