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YJV7_SCHPO
ID   YJV7_SCHPO              Reviewed;         533 AA.
AC   O59805;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Putative amidase C550.07;
DE            EC=3.5.1.4;
GN   ORFNames=SPCC550.07;
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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC         NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA19111.1; -; Genomic_DNA.
DR   PIR; T41382; T41382.
DR   RefSeq; NP_588099.1; NM_001023090.2.
DR   AlphaFoldDB; O59805; -.
DR   SMR; O59805; -.
DR   BioGRID; 276041; 17.
DR   STRING; 4896.SPCC550.07.1; -.
DR   PaxDb; O59805; -.
DR   PRIDE; O59805; -.
DR   EnsemblFungi; SPCC550.07.1; SPCC550.07.1:pep; SPCC550.07.
DR   GeneID; 2539478; -.
DR   KEGG; spo:SPCC550.07; -.
DR   PomBase; SPCC550.07; -.
DR   VEuPathDB; FungiDB:SPCC550.07; -.
DR   eggNOG; KOG1212; Eukaryota.
DR   HOGENOM; CLU_009600_9_2_1; -.
DR   InParanoid; O59805; -.
DR   OMA; TIAHGND; -.
DR   PhylomeDB; O59805; -.
DR   PRO; PR:O59805; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017064; F:fatty acid amide hydrolase activity; ISS:PomBase.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009062; P:fatty acid catabolic process; ISS:PomBase.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT   CHAIN           1..533
FT                   /note="Putative amidase C550.07"
FT                   /id="PRO_0000316202"
FT   ACT_SITE        132
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        207
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        231
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   533 AA;  58705 MW;  7A6449A2E7EE3EB6 CRC64;
     MTIDWRQIAA KYCAHRDGSI PEPFKIKTLP KDTVLNVTKI PSECGLLTPK EIELTEKYDA
     TALAEMIKDR KVTSVELVTA FCKRAAIAQQ LVNCVNELFY EEALARAAEL DEYYAKTGSL
     VGPLHGVPVS VKEHISIKNH TATASFLAKA NIIAEKDSDL VATVRKAGAV FYCRTPQPQA
     IMHLETSSNL TGVTVNPFNR KLTPGGSSGG EGALLGIKAS VLGIGSDIGG SIRSPAANNG
     LFGLRPSTLR LSRKGCQGAV SGQETILGVV GPLGRSVRDM NLFMKACIDS QPWLDDASLL
     PMPWRSVAPP KTLKVGIMRS DNVVNPQPPV ARAMQMAIDQ LSKNPDFDLV DVEPLDHKYS
     WDLISEMYWL DGGKVYYDLF NKVGEPILPL TEWIMHQPNV KPHDITAVWK LTAARDEYRN
     RYLKHLQAYG VDVLLTPVGP SPAPKLGEAK YWTYTSVWNL LDLPAVVFPV TTVDPKLDVK
     DESYIPMNEQ DAANYETYSP EDYLDAPVSL QLVGKRWQDE ELLAALDKIV SML
 
 
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