YOD1_SCHPO
ID YOD1_SCHPO Reviewed; 451 AA.
AC Q9UUD8; O74403;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Uncharacterized peptidase C18A7.01;
DE EC=3.4.-.-;
GN ORFNames=SPBC18A7.01, SPBC4F6.19c;
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; CU329671; CAA20739.2; -; Genomic_DNA.
DR PIR; T39750; T39750.
DR RefSeq; NP_596119.2; NM_001022036.3.
DR AlphaFoldDB; Q9UUD8; -.
DR SMR; Q9UUD8; -.
DR BioGRID; 277328; 9.
DR STRING; 4896.SPBC18A7.01.1; -.
DR MEROPS; M24.A11; -.
DR MaxQB; Q9UUD8; -.
DR PaxDb; Q9UUD8; -.
DR EnsemblFungi; SPBC18A7.01.1; SPBC18A7.01.1:pep; SPBC18A7.01.
DR GeneID; 2540809; -.
DR KEGG; spo:SPBC18A7.01; -.
DR PomBase; SPBC18A7.01; -.
DR VEuPathDB; FungiDB:SPBC18A7.01; -.
DR eggNOG; ENOG502RYZM; Eukaryota.
DR HOGENOM; CLU_017266_2_1_1; -.
DR InParanoid; Q9UUD8; -.
DR OMA; PYLNGAN; -.
DR PhylomeDB; Q9UUD8; -.
DR PRO; PR:Q9UUD8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0016805; F:dipeptidase activity; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..451
FT /note="Uncharacterized peptidase C18A7.01"
FT /id="PRO_0000185097"
FT BINDING 305
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 316
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 316
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 384
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 414
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 428
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 428
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 451 AA; 50594 MW; 36FDBBEDE05C1766 CRC64;
MVSFESSFER GTDFLNRNFK KCLFACISIF IFALLALSFL SLLQPDTVQR LYQCAVPSMI
YVPPMINEAI SIQHEEFNNR RRRLSAALRE DKLDALIMEP TVSMDYFANI TTGSWGLSER
PFLGIIFSDD EPYPGDVASR IYFLVPKFEL PRAKELVGKN IDAKYITWDE DENPYQVLYD
RLGPLKLMID GTVRNFIAQG LQYAGFTTFG VSPRVASLRE IKSPAEVDIM SRVNIATVAA
IRSVQPCIKP GITEKELAEV INMLFVYGGL PVQESPIVLF GERAAMPHGG PSNRRLKKSE
FVLMDVGTTL FGYHSDCTRT VLPHGQKMTE RMEKLWNLVY DAQTAGIQML SHLSNTSCAE
VDLAARKVIK DAGYGEYFIH RLGHGLGLEE HEQTYLNPAN KGTPVQKGNV FTVEPGIYIP
DEIGIRIEDA VLASDVPILL TNFRAKSPYE P
