YA55_SCHPO
ID YA55_SCHPO Reviewed; 513 AA.
AC Q09735;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative aminopeptidase C13A11.05;
DE EC=3.4.11.-;
GN ORFNames=SPAC13A11.05;
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA90806.1; -; Genomic_DNA.
DR PIR; T37612; T37612.
DR RefSeq; NP_592993.1; NM_001018392.2.
DR AlphaFoldDB; Q09735; -.
DR SMR; Q09735; -.
DR BioGRID; 278606; 3.
DR STRING; 4896.SPAC13A11.05.1; -.
DR MEROPS; M17.009; -.
DR iPTMnet; Q09735; -.
DR MaxQB; Q09735; -.
DR PaxDb; Q09735; -.
DR PRIDE; Q09735; -.
DR EnsemblFungi; SPAC13A11.05.1; SPAC13A11.05.1:pep; SPAC13A11.05.
DR GeneID; 2542130; -.
DR KEGG; spo:SPAC13A11.05; -.
DR PomBase; SPAC13A11.05; -.
DR VEuPathDB; FungiDB:SPAC13A11.05; -.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_0_1_1; -.
DR InParanoid; Q09735; -.
DR OMA; MKNTGPR; -.
DR PhylomeDB; Q09735; -.
DR BRENDA; 3.4.11.1; 5613.
DR PRO; PR:Q09735; -.
DR Proteomes; UP000002485; Chromosome I.
DR ExpressionAtlas; Q09735; differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:PomBase.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; ISO:PomBase.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..513
FT /note="Putative aminopeptidase C13A11.05"
FT /id="PRO_0000165853"
FT ACT_SITE 292
FT /evidence="ECO:0000255"
FT ACT_SITE 366
FT /evidence="ECO:0000255"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 513 AA; 56195 MW; F904CC0607502018 CRC64;
MKGLGLSTRT FNWSSLSSIL LPRIPLATTK ADSLILAVRH DKQVFSEDYR QVVDQYFETS
PKKNDIRLFW NTQGFVRLAI VQLEENVSEK SVRSAAAEAA KILKSNGAKS IAVDGMGFPK
DAALGAALAT YDFSLRRDHL SVYQDEKVVE KENLFTSPAP ERLTFQLLSN TSEKKTATAE
ENAFKVGLIE AAAQNLARSL MECPANYMTS LQFCHFAQEL FQNSSKVKVF VHDEKWIDEQ
KMNGLLTVNA GSDIPPRFLE VQYIGKEKSK DDGWLGLVGK GVTFDSGGIS IKPSQNMKEM
RADMGGAAVM LSSIYALEQL SIPVNAVFVT PLTENLPSGS AAKPGDVIFM RNGLSVEIDN
TDAEGRLILA DAVHYVSSQY KTKAVIEAST LTGAMLVALG NVFTGAFVQG EELWKNLETA
SHDAGDLFWR MPFHEAYLKQ LTSSSNADLC NVSRAGGGCC TAAAFIKCFL AQKDLSFAHL
DIAGVMDKQL NSWDCDGMSG RPVRTIIEVA RKY
