ID A0A099ZPT3_TINGU Unreviewed; 868 AA.
AC A0A099ZPT3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
DE Flags: Fragment;
GN ORFNames=N309_09107 {ECO:0000313|EMBL:KGL82795.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL82795.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL82795.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL82795.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC Pro nor hydroxyproline.; EC=3.4.14.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001257};
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000256|ARBA:ARBA00010036}.
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DR EMBL; KL895600; KGL82795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099ZPT3; -.
DR STRING; 94827.A0A099ZPT3; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR045785; Dpp_8/9_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF109; DIPEPTIDYL PEPTIDASE 9; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF19520; Dpp_8_9_N; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053641}.
FT DOMAIN 37..163
FT /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19520"
FT DOMAIN 174..599
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 697..868
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT NON_TER 868
FT /evidence="ECO:0000313|EMBL:KGL82795.1"
SQ SEQUENCE 868 AA; 99051 MW; DD6F7D204BD8718F CRC64;
MQKIKRVRLE NETAGSWRSF LTSSEGDERM TAVDTLSDSS EVVEMEDVPS QFQVQKHSWD
GLRDIIHSSR KYSGMIVNKA PHDFQFVRKT EESSPHSHRL YYLGMPYGSR ENSLLYSEIP
KKVRKEALLL LSWKQMLDHF QATPHHGMYS REEELLRERK RLGVFGITSY DFHSESGLFL
FQASNSLFHC RDGGKNGFMV SPMKPLEIKT QCTGPRMDPK ICPADPAFFS FINNNDLWVA
NIETGEERRM TYCHKGLSNV LDDPKSAGVA TFVIQEEFDR FTGYWWCPTA STEGSEDLKT
LRILYEEVDE SEVEIIHVPS PALEERKTDS YRYPRTGSKN PKITLKLAEF RTDSKGKIVC
AQDKELVQPF AALFPTVEYI ARAGWTRDGK YAWAMFLDRP QQRLQLILLP PALFIPVPES
EEQRAEFAKT VPENVQPLVI YEETTDVWIN VHDIFYPFIQ REGEEEELCF IRANECKTGF
CHLYRVTAVL KQGSYDWVQP YVHSEDDFKC PIKEEVALTG GEWEVLARHG SKIWVNEATK
LVYFQGTKDT PLEHHLYVVS YESPGEIVRL TTPGFSHSCS MSQNFDMFIS HYSSVSTPPC
VHVYKLSGSD DDPLHKQPKF WASMMPQVKA AGPGCPPDYV PPEIFHFHTQ SDVELYGMVY
KPHDVQAGKK HPTVLFVYGG PQVQLVNNSF KGIKYLRLNT LASLGYAVVV IDGRGSCQRG
LKFEGALKNQ MGQVEIEDQV EGLHYVAEKY GFIDLTRVAI HGWSYGGFLS LMGLICKPNV
FKIAIAGAPV TVWMAYDTGY TERYMDVPEN NQQGYEAGSV ALHVEKLPNE PNRLLILHGF
LDENVHFFHT NFLVSQLIRA GKPYQLQV
//
