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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//