ID A0A1I3FZL5_9PLAN Unreviewed; 1264 AA.
AC A0A1I3FZL5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN ORFNames=SAMN05421753_106107 {ECO:0000313|EMBL:SFI16665.1};
OS Planctomicrobium piriforme.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctomicrobium.
OX NCBI_TaxID=1576369 {ECO:0000313|EMBL:SFI16665.1, ECO:0000313|Proteomes:UP000199518};
RN [1] {ECO:0000313|Proteomes:UP000199518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26348 {ECO:0000313|Proteomes:UP000199518};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOQD01000006; SFI16665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3FZL5; -.
DR STRING; 1576369.SAMN05421753_106107; -.
DR Proteomes; UP000199518; Unassembled WGS sequence.
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 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:UP000199518};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 60..505
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 550..656
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 676..763
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 799..983
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT ACT_SITE 69
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 468
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1264 AA; 139159 MW; EB63EC72A4FCDAB6 CRC64;
MCDVWNRAKW GLAIWLLIVP AGYAWEESPV PKPSFPTIDL LPKTETGALR FLKEHPHYDG
RGVIVAIFDT GVDPAATGLQ TTTDGKPKIL DLIDGTGSGD VPLKEAEPVK EGTLVGATGR
TLKIDPRWKN PTGKYRIGLK AGYDLFPPEL VERLTEERRE QFAKGQRKLE AQLRDQLVSI
EEGTDKSLSK DECEARLKCL TEAWEGYADP GPVYDCAVFH DGDVFRAVVD TDEDGDLADE
KVLTDYAREH RYAVFSDASR LSFSVQILDD GHLLSLVTAS GEHGTHVAGI VAAHDSAAPE
RNGLAPGAQI ISINIGDPRI DTMETGAALL RGLNAAVNWK CDLINMSYGE PTTTPNHGAL
VSKFREIVRE KNVIFVAAAG NEGPALSTVG APGGTTSEVI GVGAYVSPAM MKAGYGLAQA
GQGQAYTWAS RGPTTDGDWG VDLFAPGAAI APIPHYSLQQ VRHMNGTSMA SPNACGNIAL
LVSGLKQKQA AFTPTSILRS LQATAERIPG IDLPAQGPGL VQIDQAFVHH VQWGNSPGQN
VPLHVSLLDR NNARGVYLRD PHETDRIFEG DLMIEPKFSR TVEKELPLQF QMPLVLKSTA
DWVTVGEHLL LTKDGEMIPI KVDPTKLEPG LHIAEVLGYV ADAPERGPVL RVPVVVTRPP
QAAGQRWETV VESQSGEITR NFLAVPAGSR TATVRLTRVN GSEDGERIFM LHAVQLVPGW
SFEHRNFKKG AALAPGEKFE ATFPVTAERT LEVCLAQYWS DRGTASLKVE VEFIGLDGPT
TAFELPSDGS AAALTVSSRL AVEKCEPSAS LDHWERIVPP HSAKLHLLKG ARNELWDEQR
LSQLVLTYEL ELSSKGNVTL ACPELQGLLY DSPVSSYRMF VFNADQELVH MEHTDPQPFE
LPKGTYTVKV ELRDLDRSRL EPFEAMVLTS RQRLSSPITV PVDRNRPDAV EEKNEFEKVE
LAPGTAAVLF LKFPHAAELP DDIQTGDRLT GTLHFTKARN ASVPLVHNYV AGSDDSAGES
DGKAASDKSS DKKFDVAGAE LEFWLTTLRA RHWPQDKDVI DQLLAKVLER DPQNLEARVI
KLHLIDNDDR EERLPEVVAA ATEVLALIPV PALKEYFGTR HASKTPEEKA LNKQRETQKK
QLVDALYRKG RALGHMDLPE NLEKHPIADR PAHDKAFAET VAELANWVDL TEKEYVLLQV
RKDRRAGDFG EALKLLDQEI AADPLKKLYQ EKRAEVYEQL GWKEWEQNQQ RWLLRRFPAS
EAAF
//
