ID   DPEH1_SCHPO             Reviewed;         409 AA.
AC   O14124;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Uncharacterized dipeptidase C3A11.10c;
DE            EC=3.4.13.19 {ECO:0000255|PROSITE-ProRule:PRU10073};
DE   Flags: Precursor;
GN   ORFNames=SPAC3A11.10c;
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   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DIL1.
RX   PubMed=20404563; DOI=10.4161/cc.9.9.11526;
RA   Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A.,
RA   Kovacikova I., Miadokova E., Ammerer G., Gregan J.;
RT   "High-throughput knockout screen in Schizosaccharomyces pombe identifies a
RT   novel gene required for efficient homolog disjunction during meiosis I.";
RL   Cell Cycle 9:1802-1808(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC         Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC         ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10073};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10073};
CC   -!- SUBUNIT: Interacts with dil1. {ECO:0000269|PubMed:20404563}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Peptidase M19 family. {ECO:0000255|PROSITE-ProRule:PRU10073}.
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DR   EMBL; CU329670; CAB16385.1; -; Genomic_DNA.
DR   PIR; T11632; T11632.
DR   RefSeq; NP_594193.1; NM_001019617.2.
DR   AlphaFoldDB; O14124; -.
DR   SMR; O14124; -.
DR   BioGRID; 279513; 29.
DR   STRING; 284812.O14124; -.
DR   iPTMnet; O14124; -.
DR   MaxQB; O14124; -.
DR   PaxDb; 4896-SPAC3A11-10c-1; -.
DR   EnsemblFungi; SPAC3A11.10c.1; SPAC3A11.10c.1:pep; SPAC3A11.10c.
DR   GeneID; 2543080; -.
DR   KEGG; spo:SPAC3A11.10c; -.
DR   PomBase; SPAC3A11.10c; -.
DR   VEuPathDB; FungiDB:SPAC3A11.10c; -.
DR   eggNOG; KOG4127; Eukaryota.
DR   HOGENOM; CLU_031404_4_2_1; -.
DR   InParanoid; O14124; -.
DR   OMA; CDHPRNI; -.
DR   PhylomeDB; O14124; -.
DR   Reactome; R-SPO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   Reactome; R-SPO-5423646; Aflatoxin activation and detoxification.
DR   PRO; PR:O14124; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; ISS:PomBase.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01301; rDP_like; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR008257; Pept_M19.
DR   PANTHER; PTHR10443:SF12; DIPEPTIDASE; 1.
DR   PANTHER; PTHR10443; MICROSOMAL DIPEPTIDASE; 1.
DR   Pfam; PF01244; Peptidase_M19; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Dipeptidase; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..409
FT                   /note="Uncharacterized dipeptidase C3A11.10c"
FT                   /id="PRO_0000314654"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10073"
SQ   SEQUENCE   409 AA;  46048 MW;  860A95056C6B1CF1 CRC64;
     MVSDSKLELP LPVNQQKPRR RRILKVHLLI AALILSAVGY LGKGKWIWTP ERKAHFVLTH
     FPLIDGHNDL PIYLRENYDN RLLNISLEHL PGQTDIFRLR QGHVGGQFWS VFVECPSLDS
     NSSLSWNRTG EYEAVTQTLQ QIDVVKRMAL YYPKTFSLTD HSGKVKFDFL RNHISSMMGI
     EGLHQIAGSP SILRQFYDLG VRYATLAHNC DNVFADAAVD GKRTNKGLSP AGRDIVREMN
     RLGMIVDLSH TTPETMHQAL DVSVAPAFFS HSSAKGVYDH PRNVPDDVLI RVKETDGVVM
     VNFYPAFISP HPENATIDTV VEHIMHIANV TGSYRHIGLG GDFDGIDMVP KGLEDVSKYP
     DLFVKLAERG LSITELADIA GRNVLRVWKT TEDLGHSIHE PPLEWEDDF
//