DPEH1_SCHPO
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 03-AUG-2022, entry version 129.
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;
CC Evidence={ECO:0000255|PROSITE-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; 28.
DR STRING; 4896.SPAC3A11.10c.1; -.
DR iPTMnet; O14124; -.
DR MaxQB; O14124; -.
DR PaxDb; O14124; -.
DR PRIDE; O14124; -.
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 InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR008257; Pept_M19.
DR PANTHER; PTHR10443; PTHR10443; 1.
DR Pfam; PF01244; Peptidase_M19; 1.
DR SUPFAM; SSF51556; SSF51556; 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
