ID A0A091UC71_PHALP Unreviewed; 499 AA.
AC A0A091UC71;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Beta-Ala-His dipeptidase {ECO:0000313|EMBL:KFQ71633.1};
DE Flags: Fragment;
GN ORFNames=N335_01911 {ECO:0000313|EMBL:KFQ71633.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ71633.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ71633.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ71633.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR037242-3};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR037242-3};
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; KK445869; KFQ71633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UC71; -.
DR MEROPS; M20.006; -.
DR PhylomeDB; A0A091UC71; -.
DR Proteomes; UP000053638; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:InterPro.
DR CDD; cd05676; M20_dipept_like_CNDP; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017153; CNDP/DUG1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF1; BETA-ALA-HIS DIPEPTIDASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645};
KW Manganese {ECO:0000256|PIRSR:PIRSR037242-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037242-3};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Reference proteome {ECO:0000313|Proteomes:UP000053638}.
FT DOMAIN 221..378
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 113
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 144
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 144
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 179
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 207
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 457
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT SITE 240
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ71633.1"
FT NON_TER 499
FT /evidence="ECO:0000313|EMBL:KFQ71633.1"
SQ SEQUENCE 499 AA; 55556 MW; 0EF377B18DFDE7B1 CRC64;
LLFKAGMSAS SSSVLEMDIF QYIDVHQSDF IEDLKEWVAV ESDSVQPDLR KEVIRMMALA
AERLAALGAT VNLVNLGSHQ LPDGQDLPLP PVILGELGKD PQNPTVCFYG HVDVQPAKKE
DGWKTDPYAL TEIDGNLYGR GATDNKGPVL AWINAVDTFR ALNLAMPVNF KFVIEGMEEA
GSLGLEKLLE EEKQCFFSDV DYVVISDNLW LSNKKPALTY GSRGNACFSV EVECGDKDLH
SGTFGGIIHE PLTDLIALLD SLVDPTGRIQ IPGIYDSVAA LTEEEKKLYE SIEFDLEEHK
SNSGVKKFLY GTKEEILLHL WRYPSLSIHG IEGAFHEQGI KTVIPAKVIG KFSIRQVPHM
DLSVMKQQVV EHLESVFSKR NSPNKLKVSM PLGAKPWLAD VNGPLYKAAR RAIKTVFGED
PDFIRDGSTI PVARMFQTIT QKSVMMFPIG AADDREHSQN EKISRHNYIE GTKVFAAFFL
EISNLHRHLH ETSNTETND
//
