ID V7BC29_PHAVU Unreviewed; 1376 AA.
AC V7BC29;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN ORFNames=PHAVU_007G071600g {ECO:0000313|EMBL:ESW15422.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW15422.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002294; ESW15422.1; -; Genomic_DNA.
DR RefSeq; XP_007143428.1; XM_007143366.1.
DR STRING; 3885.V7BC29; -.
DR EnsemblPlants; ESW15422; ESW15422; PHAVU_007G071600g.
DR GeneID; 18625137; -.
DR Gramene; ESW15422; ESW15422; PHAVU_007G071600g.
DR KEGG; pvu:PHAVU_007G071600g; -.
DR eggNOG; KOG1114; Eukaryota.
DR OMA; WENATTF; -.
DR OrthoDB; 2441948at2759; -.
DR Proteomes; UP000000226; Chromosome 7.
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; IPR022398; Peptidase_S8_His-AS.
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; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 110..569
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 620..727
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 746..830
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 872..1057
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT REGION 1099..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 221..267
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1267..1283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 532
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1376 AA; 152739 MW; CD653976157BCBEF CRC64;
MHNQHTLLLR LPSLSSHSLT TILHPTTKTK LNTTRRKHTR SSSFRRSNWV VPNALTMHCT
SRCGGDDNNN RNGASFRNSK LNESTFLASL MPKTEIGADR FLNAHPHYDG RGALIAIFDS
GVDPAAAGLQ VTSDGKPKIL DIIDCTGSGD VDTSKVVKAD ADGCILGASG ASLVINTSWK
NPSGDWHVGY KLVYELFTEN LTSRLKKERK KKWDEKNQEE IAKAVKQLAD FDQEHKKVEE
ANLKRVREDL QNKLDLLKKQ SEIYDDKGPA IDAVVWYDGE VWRVAIDTQS LEDDPDCGKL
ANFVPLTNYR TEKKYGIFSK LDACTYVVNV YNDGNVLSMV TDCSPHGTHV AGIAAAFHPE
EPLLNGVAPG AQLISCKIGD SRLGSMETGT GLTRAMIAAV EHKCDLINMS YGEPTSLPDY
GRFVDLVNEA VNKHRLIFVS SAGNSGPALS TVGAPGGTSS NIIGVGAYVS PAMAAGAHSV
VEPPSDGLEY TWSSRGPTTD GDVGVSVSAP GCAVAPVPTW TLQRRMLMNG TSMASPSACG
GIALLISAMK AEGIPVSPYS VRKALENTSV PIGGSPEDKL STGQGLMQVD KCYEYIKQSQ
NIPSVSYQIM VKKSGKTKPW SRGIYLREAN DCRQPMEWTV QVDPKFHEDA NKLEELAMFE
EFIELHSSDE TVVKAPEYLL LTHNGRTFNI IVDPTNLNDG LHYYELYGID YKAPWRGPIF
RIPITVTKPM AVTDRHPVVS FSNMLFLPGQ VERKYIEVPN GASWIEATMK ASSFDTVRRF
FVHTVQICPL RRPFARRNVI TFFSPATKSF TFRVVGGQTL ELVIAQFWSS GIGSHETTRV
DLEVMFHGIK VNQEEIVLDG SEAPIRIDAE ALLASEKLAP VGILNKIRVP YRPIDAMISS
LSSDRDKLPS GKQILALTLT YKIKLEDGAE IKPQIPFLNN RIYDTKFESQ FYIISDSNKK
VYSSGDAYPN STKLPKGEYN LQLYLRHDNV QILEKMKQLV LFIQRNLEEK DIIPLCFFSE
PDGPVMGDGS FKSSTLVPGI KEGFYLGPPP KDKLPKNSLP GSVLVGSISY GKLSFAAQQN
GKNPEKHPVS HRVSYIIPPN KVDEDKGKSS SLSSKKTVSE RLEQEVRDAK IKVFGGVKQG
TDEECLEWKE LSASLKTEYP KYTPLLAKIL EGLVSRSYIK EKFLHHEEII DAADEVINSI
DKEELVKYFA VKNDPGDEEA EKIKKEMDST RGQLAEALYQ KGLALAEIES LKEVDESLAS
VATEGAKQDV EKTDEQSKDD DVHPDLFKEN FNELKKLVDV KCRKYGILLV TNERRNQRLG
TALKVLNDII QDDAEPAKKK FYELKLSLLE EIGWTHFCTY EREWMLVRFP PSLPPF
//
