ID A0A091TZJ6_PHORB Unreviewed; 857 AA.
AC A0A091TZJ6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Tripeptidyl-peptidase 2 {ECO:0000256|ARBA:ARBA00020244};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
DE AltName: Full=Tripeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032232};
DE Flags: Fragment;
GN ORFNames=N337_11168 {ECO:0000313|EMBL:KFQ83641.1};
OS Phoenicopterus ruber ruber.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC Phoenicopterus.
OX NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ83641.1, ECO:0000313|Proteomes:UP000053700};
RN [1] {ECO:0000313|EMBL:KFQ83641.1, ECO:0000313|Proteomes:UP000053700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ83641.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KK409305; KFQ83641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091TZJ6; -.
DR Proteomes; UP000053700; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.710; -; 1.
DR Gene3D; 2.60.40.3170; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR022232; TPPII_C_art.
DR InterPro; IPR046939; TPPII_C_sf.
DR InterPro; IPR048384; TPPII_GBD.
DR InterPro; IPR048383; TPPII_Ig-like-1.
DR InterPro; IPR022229; TPPII_Ig-like-2.
DR InterPro; IPR046940; TPPII_Ig-like_sf.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR Pfam; PF12583; TPPII_C; 1.
DR Pfam; PF21316; TPPII_GBD; 1.
DR Pfam; PF21223; TPPII_Ig-like-1; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053700};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 9..247
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 268..381
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 401..488
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 525..710
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT DOMAIN 757..816
FT /note="Tripeptidyl peptidase II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12583"
FT REGION 744..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ83641.1"
FT NON_TER 857
FT /evidence="ECO:0000313|EMBL:KFQ83641.1"
SQ SEQUENCE 857 AA; 94724 MW; 258E1E2DD38C015D CRC64;
VIQLFICSGA HGTHVASIAA GYFPEEPERN GVAPGAQILA IKIGDTRLST METGTGLIRA
MIEAIKYKCD LVNYSYGEAT HWPNSGRICE VINEAVWKHN VIYVSSAGNN GPCLSTVGCP
GGTTSSVIGV GAYVSPDMMV AEYSLREKLP ANQYTWSSRG PSTDGALGVS ISAPGGAIAS
VPNWTLRGTQ LMNGTSMSSP NACGGIALVL SGLKANDIHY TVHSVRRALE NTAVKAENIE
VFAQGHGIIQ VDKAYDYLIQ NSSFTSNIGF TVTVGSNRGI YLRDPAQIAA PSDHGVGIEP
VFPENTENTE RISLQLHLAL TSNAPWVQCP SHLELMNQCR HINIRVDPRG LREGLHYTEV
CGYDTAMPNA GPLFRVPITV VIPTRVDESS SYDLTYTDVH FKPGQIRRHF IDVPQGATWA
EVTVCSCSAD VTAKFVLHAV QLVKQKAYRS HEFYKFSSLP EKGSVTEAFP VLAGKTIEFC
VARWWASLSD VSINYTISFH GVLCGTPQLN MHASEGIVRF DVQSLLKYED IAPCINLKSW
VQTLRPVSAK IKPLGSRDIL PNNRQLYEMI LTYNFHQPKS GEVTPSCPLL CELLYESEFD
SQLWIIFDQN KRQMGSGDAY PHQYSVKLEK GDYTIRLQIR HEQNSELDRI KDLPFIVSHR
LSSTLSLDIY ENHSLALLGK KKSNSLTLPP KHSQPFFVTS LPDDKIPKGA GPGCYLAGAL
TLSKTELGKK ADVLTVHYHL IPSPSKSKNG GKEKEREQEK EKDVKEEFAE ALRDLKIQWM
TKLDTTDMYN ELKEAFPNHL PLYVARLHQL DSEKERMKRL DEIVEAANTV ISHIDQTALA
VYFAMKTDPR PDATTIK
//
