ID A0A1D6HFC4_MAIZE Unreviewed; 1244 AA.
AC A0A1D6HFC4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN ORFNames=ZEAMMB73_Zm00001d017522 {ECO:0000313|EMBL:AQK73344.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK73344.1};
RN [1] {ECO:0000313|EMBL:AQK73344.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK73344.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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}.
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DR EMBL; CM000781; AQK73344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6HFC4; -.
DR PaxDb; 4577-AC211737-3_FGP012; -.
DR ExpressionAtlas; A0A1D6HFC4; baseline and differential.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR Gene3D; 1.25.40.710; -; 1.
DR Gene3D; 2.20.25.690; -; 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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034051; TPP_II_domain.
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; 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; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 115..609
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 637..750
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 769..853
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 894..1080
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 377
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 563
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1244 AA; 135710 MW; D2E763349D45C091 CRC64;
MWATLHKPVA HANLRLLLTV SAFSGPLHLG TASAVAAAVT TRRSSSSRGV AATAMPSSSP
PPLPPAEETT ASAAALAPEG GFSLTEPSFL ESLMPKKEIG VDRFLAAHPE YDGRSALIAI
FDSGVDPAAA GLQTTSDGKP KILDVLDCTG SGDVDTSKVV KADADGAIVG ASGARLVINP
SWKNPSQEWH VGCKLIYELF TDTLTSRLKV NFIFSAYTPK FYIELDILTR VYPPTLQKER
KKKWDEENQE SISDALKQLN EFEKKHPKPD DTMLKKAHED MQSRLDYLRK QAEGYDDKGP
VIDIVTWNDG DVWRVAVDTQ TLEGNNDGGK LADFVPLTNY RLERKYAIFS KLDACSFVAN
VYNDGNLVSI VTDCSPHATH VAGIAAAFHP DEPLLNGVAP GAQLISCKIG DTRLGSMETG
TGLVRALIAA VEHKCDLINM SYGEPTLLPD YGRFIDLSNE VVDKHRIIFI SSAGNNGPAL
NTVGAPGGTS TSIIGVGAYV SPAMAAGAHC VVQPPAKGME YTWSSRGPTA DGDLGVSISA
PGGAVAPVPT WTLQSRMLMN GTSMSSPSAC GGVALLVSGM KAEGIPLSPY SVRKAIENTA
ASISNAPEEK LTTGNGLLQV DRAFEYAQQA KKLPLHVCLA VPKLRGIYLR GGNACCQTSE
WTVQLDPKFH EGASNLEQLV PFEECLQLHS TDTSVVQIPE YILVTNNGRS FNIVVNPANI
SSGLHYFEVY GIDYKAPWRG PIFRVPITVI KPIALLGEPP LLSISNLRFQ SGHIERRFIN
VPFGASWAEV TMRTSAFDTP RRFFLDTVQI CPLKRPVKWE AVVTFSSPSS KNFSFPVEGG
LTLELSIAQF WSSGIASHEP TCVDFEIVLH GISIDQKVST LDGESPLLIV ARSLLASEKL
VPVGTLNKIR IPYRPVECNL SSLPTDRDKL PSGKQIIALT LTYKFKLEDN AEIKPHVPLL
NNRIYDNKFE SQFYRISDSN KRIYSSGDVY PSYVRLSKGE YTLQLYIRHE NVQFLEKLKE
LVLFIERKLD KKDFVPLMFY SQPDGPIVGS GTFKSTVLVP GEPEAFYVGP PSSEKLPKNA
PPGAVLVGSI TYGTVSTFNK KDEQNHRAPV SYSISYTILP SKVSSIECAV SLLSTFVVMM
ILVLVLDHQF RITIRVDDKE KGVLVGTKSI PEQLDEEVRD TKIKFLSSVK QLTEEDKSAW
SELVVSLKSE YPKYTPLLSK ILQCVLQKGT DGDKISHEKE VNVD
//