ID B3SBM8_TRIAD Unreviewed; 1185 AA.
AC B3SBM8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 79.
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};
GN ORFNames=TRIADDRAFT_61672 {ECO:0000313|EMBL:EDV19912.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV19912.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV19912.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV19912.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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; DS985265; EDV19912.1; -; Genomic_DNA.
DR RefSeq; XP_002117654.1; XM_002117618.1.
DR AlphaFoldDB; B3SBM8; -.
DR STRING; 10228.B3SBM8; -.
DR EnsemblMetazoa; TriadT61672; TriadP61672; TriadG61672.
DR GeneID; 6758845; -.
DR KEGG; tad:TRIADDRAFT_61672; -.
DR CTD; 6758845; -.
DR eggNOG; KOG1114; Eukaryota.
DR HOGENOM; CLU_003084_1_0_1; -.
DR InParanoid; B3SBM8; -.
DR OMA; SLRDFQC; -.
DR OrthoDB; 2441948at2759; -.
DR PhylomeDB; B3SBM8; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; -; 2.
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; 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; 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:UP000009022};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 76..563
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 585..701
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 722..805
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 796..964
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT DOMAIN 978..1037
FT /note="Tripeptidyl peptidase II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12583"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1102..1129
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 327
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 512
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1185 AA; 132072 MW; 5912A20A883F756E CRC64;
MAKEDWPRGK REANKTPRWD NRAGVRPDNR PSTKEGSYPV REAMASPSSQ FPLQDLLPKQ
ETAADRFLRQ YPDYDGRGTI IAIFDTGVDP GADGLQMTSD GRRKIIDCID CTGSGDVDTS
TVSSIDDDGC VTGLTGRKLQ IPAEWENPTG KFHLGIKHAT ELFPSPLCDR LKKEYRKKKW
APSHSKCTAD AIRELQQSES KGQKQTFLDE LMREELQQRT EQLKNLDKIG DESLPIFDCV
VFHNGSVWRY RYNILAMRFI RTKIFTPFSR AVIDTTETGN LSKCTVLPEF RLQPVYGTFG
EDDLLNYTIS VYDDGNRLSI VTNAGSHGTH VACITSGYFE STPEKNGIAP GAQILSVKIG
DTRLDSMETG PGIVRGLIAS KNYGCDLINM SYGEACQKPN EGRIMELCNE FVDEHDIIMV
SSAGNNGPAM STVGSPGGTC SSVISVGAHV TPKMMAAQYS LLERVQSMQY TWTSRGPCID
GALGVSISAP GGAIASVPKW TLSSSQLMNG TSMSSPNACG GIALILSGLK ACQIPFSPSS
VRRAVENTAS SITGEDHFSM GYGLLQVDKA FEYIRNSVDK LNNNVHFEIT CGSSYDKRGI
YLREPQETSS ISYLPVRVRP CYKSELDLKL KANLEYRISL VPTATWIDAP KYFMLNNSAR
SFDIKVDTSD LRPGAHYSEI CGYDSACIEL GPLFRIPITV TKPISIRDPL TPISESLTLD
KGQIKRMFIA TPPKATWVEI ALTSLEESGK FTMVLDVSHL HKDKSFKYQF SNNRVALGCG
ETKNITFKVE GEKTLELCLT SWWSTRESKK IKYAITFHSL LPNERNVAME NSCEVRPNVS
LLSDLLYEAL YESQLWMIFD KNKQHIASGD AFPHQYKVKL DKGDYILKLQ VRHDKRDLLE
RLKNIPVLLE HKLANSVSLD VYSSQLKALS GGSKISNNYW LNKNNTAVLY FAPLDDDKLP
KGAKPGMYLT GTISYSSSGK SANNDFEAAH KKFMLSWLTR MDFEHGDKLY KDLEQKYEDD
LSLKVERMKM LDVAANKHGS VEAFENVIKA AQCIIDLIDT NALLNFYGMI SDLSENAAKK
KSEMDEKKKY LTESLICKGK NMGLLAKQLE CLEEESARYQ ATVSAMNDVY CELSKWIDLK
NHRALAFILV HAITLKQYAR AIDVGETELA SHCKLLQASD IEEIS
//
