CBPS2_DICDI
ID CBPS2_DICDI Reviewed; 519 AA.
AC Q55FR8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Probable carboxypeptidase S-like 2;
DE EC=3.4.17.-;
GN ORFNames=DDB_G0267984;
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: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73445.1; -; Genomic_DNA.
DR RefSeq; XP_647465.1; XM_642373.1.
DR AlphaFoldDB; Q55FR8; -.
DR SMR; Q55FR8; -.
DR STRING; 44689.DDB0233064; -.
DR PaxDb; Q55FR8; -.
DR EnsemblProtists; EAL73445; EAL73445; DDB_G0267984.
DR GeneID; 8616272; -.
DR KEGG; ddi:DDB_G0267984; -.
DR dictyBase; DDB_G0267984; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_11_1_1; -.
DR InParanoid; Q55FR8; -.
DR OMA; NYGDHSG; -.
DR PhylomeDB; Q55FR8; -.
DR PRO; PR:Q55FR8; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Membrane; Metal-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..519
FT /note="Probable carboxypeptidase S-like 2"
FT /id="PRO_0000327534"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 153
FT /evidence="ECO:0000250"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 519 AA; 58763 MW; DBF0D61A5A818A94 CRC64;
MDKRKQSDYD NGKSKPTNGS KTTKFNLIKI IIRNLLIGIL LMLVLNTIRF TSKQPKVEIL
SPDHIDSFTT LSDIELAQRL AKATTFKTIS FGESDEFDQY EPEFLKFHEF LKITFPKVHK
YLKLNIIANY SLVYNWKGLD ESLKPILLAG HIDVVPTLFL DKWTHPPFSG HIDDTYIWGR
GTMDDKGSVM AILESVEDLL SQGFKPQRSI YFAFGHDEEL GGNNGAFNIN KYFDTNEIGP
FEFILDEGLP ILLPPVFPGL SKPIASVGIT EKGAIDIKLS VTIVGGHSSM PRRESAIGVL
AQAVSKLENN PPSPKLRETR LLFDFVGREC SLPYRFLFSN LWLFEPIISR VLSTKPTLDA
LQRTTTALTI FNAGNKANVI PMEANATINF RVVPGDSTND IIDHVNRVIN DDRVKISKIS
NIIEPAPVSS TTSKSFNLLQ STILQEFPDV VVAPTIMIAN TDTRHYWNLT ENIFRFCPMV
LENSDLQRLH GIDERLTIKN YKQLVDFYYH LIKNTEKYL
