ID S5ZMQ6_9CREN Unreviewed; 209 AA.
AC S5ZMQ6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Pyroglutamyl-peptidase I {ECO:0000256|PROSITE-ProRule:PRU10077};
DE EC=3.4.19.3 {ECO:0000256|PROSITE-ProRule:PRU10077};
GN ORFNames=N186_07690 {ECO:0000313|EMBL:AGT35876.1};
OS Thermofilum adornatum.
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=1365176 {ECO:0000313|EMBL:AGT35876.1, ECO:0000313|Proteomes:UP000015543};
RN [1] {ECO:0000313|EMBL:AGT35876.1, ECO:0000313|Proteomes:UP000015543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1910b {ECO:0000313|Proteomes:UP000015543};
RX PubMed=24029764;
RA Dominova I.N., Kublanov I.V., Podosokorskaya O.A., Derbikova K.S.,
RA Patrushev M.V., Toshchakov S.V.;
RT "Complete Genomic Sequence of 'Thermofilum adornatus' Strain 1910bT, a
RT Hyperthermophilic Anaerobic Organotrophic Crenarchaeon.";
RL Genome Announc. 1:e00726-13(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal pyroglutamyl group from a
CC polypeptide, the second amino acid generally not being Pro.;
CC EC=3.4.19.3; Evidence={ECO:0000256|PROSITE-ProRule:PRU10077};
CC -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641}.
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DR EMBL; CP006646; AGT35876.1; -; Genomic_DNA.
DR RefSeq; WP_020963183.1; NC_022093.1.
DR AlphaFoldDB; S5ZMQ6; -.
DR MEROPS; C15.001; -.
DR GeneID; 25406070; -.
DR KEGG; thb:N186_07690; -.
DR PATRIC; fig|1365176.7.peg.1519; -.
DR eggNOG; arCOG05850; Archaea.
DR HOGENOM; CLU_043960_4_3_2; -.
DR OrthoDB; 39672at2157; -.
DR Proteomes; UP000015543; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00501; Peptidase_C15; 1.
DR Gene3D; 3.40.630.20; Peptidase C15, pyroglutamyl peptidase I-like; 1.
DR InterPro; IPR000816; Peptidase_C15.
DR InterPro; IPR016125; Peptidase_C15-like.
DR InterPro; IPR036440; Peptidase_C15-like_sf.
DR InterPro; IPR029762; PGP-I_bact-type.
DR InterPro; IPR033694; PGPEP1_Cys_AS.
DR NCBIfam; TIGR00504; pyro_pdase; 1.
DR PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR PANTHER; PTHR23402:SF1; RE07960P; 1.
DR Pfam; PF01470; Peptidase_C15; 1.
DR PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR PRINTS; PR00706; PYROGLUPTASE.
DR SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 1.
DR PROSITE; PS01334; PYRASE_CYS; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000015543};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT ACT_SITE 143
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10077"
SQ SEQUENCE 209 AA; 23092 MW; F959E17F7F3A4F17 CRC64;
MKILLSGFGP FGEEDTNPSE IVATRVAEKL REAGHEARHV VLPVAYRRAK AILEQVVGEL
RPDIAIALGL YGGITHVRVE RVALNMMDFS IPDVDGEKPQ DLPIDPEGPT AYLASIPTRR
VVERLKEEGI PASLSYSAGT YLCNYVMYTL LRLSDRTGYP RRAGFIHIPY TIDIASRKKG
LPASLPLDVL VKGVLIAVEE TIKEIEKEK
//
