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ASPG4_SCHPO
ID   ASPG4_SCHPO             Reviewed;         356 AA.
AC   Q8TFF8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Probable L-asparaginase 4;
DE            EC=3.5.1.1;
DE   AltName: Full=L-asparagine amidohydrolase 4;
DE   Flags: Precursor;
GN   ORFNames=SPAP8B6.05c, SPBPB8B6.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC         Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAD27911.1; -; Genomic_DNA.
DR   RefSeq; NP_001018766.1; NM_001020941.2.
DR   AlphaFoldDB; Q8TFF8; -.
DR   SMR; Q8TFF8; -.
DR   STRING; 4896.SPBPB8B6.05c.1; -.
DR   iPTMnet; Q8TFF8; -.
DR   MaxQB; Q8TFF8; -.
DR   PaxDb; Q8TFF8; -.
DR   EnsemblFungi; SPBPB8B6.05c.1; SPBPB8B6.05c.1:pep; SPBPB8B6.05c.
DR   GeneID; 3361187; -.
DR   KEGG; spo:SPBPB8B6.05c; -.
DR   PomBase; SPBPB8B6.05c; -.
DR   VEuPathDB; FungiDB:SPBPB8B6.05c; -.
DR   eggNOG; KOG0503; Eukaryota.
DR   HOGENOM; CLU_019134_1_2_1; -.
DR   InParanoid; Q8TFF8; -.
DR   PhylomeDB; Q8TFF8; -.
DR   PRO; PR:Q8TFF8; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0009986; C:cell surface; NAS:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR   GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR   GO; GO:0006530; P:asparagine catabolic process; IBA:GO_Central.
DR   GO; GO:0006531; P:aspartate metabolic process; NAS:PomBase.
DR   CDD; cd08964; L-asparaginase_II; 1.
DR   Gene3D; 3.40.50.1170; -; 1.
DR   Gene3D; 3.40.50.40; -; 1.
DR   InterPro; IPR004550; AsnASE_II.
DR   InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR040919; Asparaginase_C.
DR   InterPro; IPR027473; L-asparaginase_C.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   InterPro; IPR037152; L-asparaginase_N_sf.
DR   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF17763; Asparaginase_C; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF53774; SSF53774; 1.
DR   TIGRFAMs; TIGR00520; asnASE_II; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   3: Inferred from homology;
KW   Cell wall; Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..356
FT                   /note="Probable L-asparaginase 4"
FT                   /id="PRO_0000002366"
FT   DOMAIN          36..356
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        46
FT                   /note="O-isoaspartyl threonine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         126..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   356 AA;  38057 MW;  E7935A592DB06FDA CRC64;
     MWGFIVTCGI FLVLLCQLRL LSKRKSKSTP YNALLPNVTV FAMGGTIAGC ANSSLEIVNY
     IPGSVGIEKL IEAVPAIKAI ANINGVQVTN MGSENLTPAD VLKLAKLILA EVAKPNVHGI
     VITHGTDSLE ETAMFLDLTI STAKPIVVVG AMRPSTAIGA DGPMNLLNAV AVASSNQSMG
     RGTLVLLNDR IGSAFYTTKT NGNTLDTFKS YEAGSLGIVL NQKPFYFFSP AVPTGKVFFD
     IYNIKQLPRV DILYGYQGLN PKLAESAVHL GAKGLVLAAM GATSWTDDGN EVISSLIREH
     NIPVVYSHRT AEGYSSNSCL GIPSYFLNPQ KARYMLMLAI SSGYSIRDIE GLFSIK
 
 
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