CBPS1_DICDI
ID CBPS1_DICDI Reviewed; 485 AA.
AC Q55DL1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Probable carboxypeptidase S-like 1;
DE EC=3.4.17.-;
DE Flags: Precursor;
GN ORFNames=DDB_G0270582;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72641.1; -; Genomic_DNA.
DR RefSeq; XP_646120.1; XM_641028.1.
DR AlphaFoldDB; Q55DL1; -.
DR SMR; Q55DL1; -.
DR STRING; 44689.DDB0305000; -.
DR PaxDb; Q55DL1; -.
DR EnsemblProtists; EAL72641; EAL72641; DDB_G0270582.
DR GeneID; 8617069; -.
DR KEGG; ddi:DDB_G0270582; -.
DR dictyBase; DDB_G0270582; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_11_0_1; -.
DR InParanoid; Q55DL1; -.
DR OMA; CKNQLIA; -.
DR PhylomeDB; Q55DL1; -.
DR Reactome; R-DDI-9673163; Oleoyl-phe metabolism.
DR PRO; PR:Q55DL1; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Protease; Reference proteome; Secreted; Signal;
KW Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..485
FT /note="Probable carboxypeptidase S-like 1"
FT /id="PRO_0000327533"
FT ACT_SITE 113
FT /evidence="ECO:0000250"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 485 AA; 55597 MW; C6AA353FF6EF3FD1 CRC64;
MIFKFFFIFF LIILVIKISE SVDSTVNVHL IKSRTELAYS FKESLSFKTI SFDDESNKID
YDEFLKFHNF LQNKFPIIHR VLKRTVINKY SLLFEWTGSD KTLKPLLLNS HYDVVPVTES
EWTFNPWGEI RNDNIYGRGS IDNKVIVMAT MESIEAILAN NYTQPIRTIY LCFGHDEELG
GLNGHRMIAR HFRENLVRAE AIFDEGCPFL ASNFVPGFHD IIAGVGVFEK GYLFYKLTSK
VNSFTHSAIP PKESAIGILS KALAKIESNP FAPIENIEKK NQLLQLFNGE TIKSNPFLDA
MTKTTTALSM IHAGTKPNII PTTASAWVSH RIINGNSIEY VKSRILDLIN DTRITMEIEG
FLEPSPISSP FTTAYQILKQ TIYQQFGGYN VKVVPTQLMA NTDTRHYWDI TDNIYRFMPI
VGNFMDFVSI HGSNEKISID DYIKTIHFYK KLILNFQPFS NSSNSNYINK NLKINDYCPN
SIYSK
