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