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Database: UniProt
Entry: A0A1Q7MAE3_9CREN
LinkDB: A0A1Q7MAE3_9CREN
Original site: A0A1Q7MAE3_9CREN 
ID   A0A1Q7MAE3_9CREN        Unreviewed;       601 AA.
AC   A0A1Q7MAE3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Acyl-peptide hydrolase {ECO:0000256|ARBA:ARBA00032596};
DE   AltName: Full=Acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00032284};
GN   ORFNames=AUI95_00390 {ECO:0000313|EMBL:OLD09639.1};
OS   Crenarchaeota archaeon 13_1_40CM_3_52_4.
OC   Archaea; Thermoproteota.
OX   NCBI_TaxID=1805097 {ECO:0000313|EMBL:OLD09639.1, ECO:0000313|Proteomes:UP000186346};
RN   [1] {ECO:0000313|EMBL:OLD09639.1, ECO:0000313|Proteomes:UP000186346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLD09639.1}.
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DR   EMBL; MNGM01000006; OLD09639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7MAE3; -.
DR   Proteomes; UP000186346; Unassembled WGS sequence.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   PANTHER; PTHR42776:SF27; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 6; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF07676; PD40; 2.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   4: Predicted;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          391..596
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   601 AA;  67444 MW;  817CF10F5AE7F9DC CRC64;
     MDIDKLYYTR GILSVQWSVD GEHLYFDTNI TGRYNIWAVP SNRGWPVQLT VSDERTLLQD
     PSPDGRYLLY TQDVQGDEKP NLYLLDLTEF TISNITVTEK IGYRDTRWSP DGRSLVFAGE
     RQGPGTYPVF QFDPDKGTIK KIIGHEAGDC ESLEFSPDGH KLALTRTRNY QYTGASVYDL
     ETGNETMLAP IDDKSTTITG GWTRDGKRVY VTSNANDRGI DAVALLELKQ GPEFQWLTLQ
     DWDSQLVDVS PTEDRFAYVV NEGGNVRLLL RDLNGQEEEI PPTQGVVRAA KFSRDGKRLA
     IIHASGDSPH DIWVYDLKAR SLKQITDSLV GGLHRENFVN PQLVVYPSFD QTPIAGFLYV
     PANIKADHSH PAIVYSHGGP QWEHFNSWFP SLQYYTSHGY LVIAPNFRGS TGFGRGFTES
     LRKDAGGGDL KDLVAAVDYL KSTGYVDPSR IAITGGSWGG YLTLMALTKY PDLWAAGVSI
     VPLANWFTAH ENEDPVLQKN DEWLMGDPVE DHDLWQDRSP LFFANRIRAP LLLLAGRNDI
     RCPVKETEQM AEAARKNGVT VEVKIYENEG HGFVRRENEI DAIKRAASFL ETHVGQRSTR
     G
//
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