ID A0A090MZQ4_STRRB Unreviewed; 745 AA.
AC A0A090MZQ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=SRAE_2000398900 {ECO:0000313|EMBL:CEF69339.1,
GN ECO:0000313|WBParaSite:SRAE_2000398900.1,
GN ECO:0000313|WormBase:SRAE_2000398900};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF69339.1};
RN [1] {ECO:0000313|EMBL:CEF69339.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000398900.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF69339.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000398900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR EMBL; LN609529; CEF69339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090MZQ4; -.
DR EnsemblMetazoa; SRAE_2000398900.1; SRAE_2000398900.1; WBGene00264216.
DR WBParaSite; SRAE_2000398900.1; SRAE_2000398900.1; WBGene00264216.
DR WormBase; SRAE_2000398900; SRP04248; WBGene00264216; -.
DR OMA; KPTKMRI; -.
DR OrthoDB; 7264at2759; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 36..448
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 518..740
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 745 AA; 85184 MW; 27E6CBF71DC7834D CRC64;
MLLNQLSNIC GTSSFSKISN LLRYASTIKI NTSEYPLIRK DKNVVETLHG IQIADPYRYL
EDPLNEETTN FIKKLNDISS KVFEKSNIRG IIKERLREYI NYEKHDVLFK HGDYYYYSHN
TGLQNHNTIC RKKTLDDKEE IFLDVNKLSK DGLISCSSMK FSNDGSIMAY GLSINGSDWN
TIKFKTSDNK DVDDILEKVK HSNSDFLFNN TGFIYSTYPN RKESDTGRTV TKNEYHSLYY
HKMGTSQKDD VLIVDYPQDK EVFTFGSISN DEKYLFVYFN KGTDPKNMIY YYDLSKNMDK
TFKGKIKLEP LFDKGDASYE IIDSNENEVI VKTDKNAPLG KIIKVKFSEA HKGESAWTVL
IDELKERKIS DVTVVGKDYL LLNCLENVRS SLYMYNKHTG EMIQKFDIDI GIVYQVSGDD
KSNEFFFGFL NQITPGIIYR GYLDNSESNN KFKIEKIIEN NSKNLNSKDF SVKQVFYKSK
DNKDISMFIF HRKDMKLDGN NPVLLEGYGG FSISMTPSFS VSKSMFVKHF NGISCIANIR
GGGEYGEEWH IDGMLHKKQN CFDDFIGAAE YLVSNKYTNP SKLAIRGGSN GGLLMAAVSQ
QRPDLFGAVI NSVGVLDMLR FHKFTAGGAW IAEYGNPEIK EDFDYLLKYS PLHNLEMPPE
PIQWPNTLLK TADHDDRVVP SHTLKYIATL YEVLQTGSKY QTNPVIAKIE KSSGHGSGKP
LSKALDEIVD DYSFLQQVLD INWKN
//