ID   C3ZTU2_BRAFL            Unreviewed;       395 AA.
AC   C3ZTU2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   ORFNames=BRAFLDRAFT_83080 {ECO:0000313|EMBL:EEN44090.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN44090.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN44090.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN44090.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|PIRNR:PIRNR037226}.
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DR   EMBL; GG666679; EEN44090.1; -; Genomic_DNA.
DR   RefSeq; XP_002588079.1; XM_002588033.1.
DR   AlphaFoldDB; C3ZTU2; -.
DR   eggNOG; ENOG502QQPD; Eukaryota.
DR   InParanoid; C3ZTU2; -.
DR   GO; GO:0016805; F:dipeptidase activity; IBA:GO_Central.
DR   CDD; cd05672; M20_ACY1L2-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR017144; Xaa-Arg_dipeptidase.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR   PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          170..265
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   395 AA;  43364 MW;  36FCC4300DC35B85 CRC64;
     MSVDDLKAKS IAAVLACASD LYDLSQEIWK NPELAFKEHH AHKVLTDFLE KQGFRVDRHY
     KLETAFRAVY GKDGGVHVCV ICEYDALPGI GHGCGHNLIA EVGVAAGIAI KTAIQDLKQP
     VKLTVMGTPA EEWGSGKIFL IKDGCFKDVD FAMMAHPFTF NVSRWRCLAI VTGEVIYKGV
     ASHPAYQTWE GTNALDAAVL CYSNISVLRQ QMRPHHQVHG IIQNGGTHPD IIPSETKLIF
     YLRAHSETEL KKLEKRVVGC VEAAALATGC QVEYNFKTDA SNLIQNNTLA SLYERNAEAL
     GWTNCPDKSV TGAISGSTDM GNVTHVVPGI HPMFALPTDA SIHSRHFTEE AGKREAQPYA
     LNQAKALAMT AIDVICQSQL MDTIREEFKQ DLAND
//