ID   A0A3B4GCJ9_9CICH        Unreviewed;       730 AA.
AC   A0A3B4GCJ9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Acylamino-acid-releasing enzyme {ECO:0000256|ARBA:ARBA00018421};
DE            EC=3.4.19.1 {ECO:0000256|ARBA:ARBA00012917};
DE   AltName: Full=Acyl-peptide hydrolase {ECO:0000256|ARBA:ARBA00032596};
DE   AltName: Full=Acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00032284};
GN   Name=LOC102194625 {ECO:0000313|RefSeq:XP_005732521.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000019338.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000019338.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005732521.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-
CC         terminus of a polypeptide.; EC=3.4.19.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000721};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   RefSeq; XP_005732521.1; XM_005732464.1.
DR   AlphaFoldDB; A0A3B4GCJ9; -.
DR   STRING; 303518.ENSPNYP00000019338; -.
DR   Ensembl; ENSPNYT00000019823.1; ENSPNYP00000019338.1; ENSPNYG00000014597.1.
DR   GeneID; 102194625; -.
DR   CTD; 327; -.
DR   GeneTree; ENSGT00940000165736; -.
DR   OrthoDB; 2877590at2759; -.
DR   Proteomes; UP000261460; Unplaced.
DR   Proteomes; UP000695023; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR045550; AARE_N.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF16; ACYLAMINO-ACID-RELEASING ENZYME; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF19283; APEH_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000695023}.
FT   DOMAIN          12..284
FT                   /note="Acylamino-acid-releasing enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19283"
FT   DOMAIN          520..728
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   730 AA;  81218 MW;  070ADF93F24FAF4D CRC64;
     MESQVVTSAK EIAKLYKELS LYPSLTRADV GPVITSQYGG KYSNIYTEWN QRDLERNETV
     KFCRQYIVFH DDKSVVYSGA SGNCTEIKGE VLSKDSPSGE MKAVVRECTV QGKDKQFLEI
     WSKNIKVKSI DLTALKKHGK VYEDDQFGCL VWSHSETHLL YVAERKRPTA ESFFQTESPE
     LSSIGDEDET LRTEKKEAVK GEQFVFHEDW GETLVSKSCP VLCVLDIEGS NVSVLEGVPE
     DISPGQAFWA PGDTGVVFVG WWHEPFRLGL KYCPNRRSSL FYVDLTGGKC EQLSSGTSAV
     CSPRLSPDQC RIVYLECSVY GPHMQCNRLC MYDWYTKKTS VVVDVVKRPG EDGFTGIYSC
     QLSPQCWSAD SQRVIISCPQ RSLKDLLMVD ISTGSITSLT TKSEVGNWCL LNIERDLMVV
     NCSSPNNPPN LMVGFLPSRE SEEDVVWVTL EDSPTLPEID WKILTFTPPP DQDNSQYPGL
     DFDALLIKPK EVKDGVKLPL IVIPHGGPHS VIVAEWGLSV AVLCKMGFAV LLVNYRGSIG
     YGQDNILSLL GNVGSQDVKD VQFAVESVLK SNDLDVQKVA VCGGSHGGFL ACHLIGQYPE
     FYKACVARNP VINLASMIGS TDIPDWCMVE AGYNYSTDCL PDPAVWEQML NKSPIRHVAQ
     VKTPVLLTIG EDDKRVPNKQ GVEYYKALKA KQVPVRLLWY PGSNHSLSKV DAESDGFMNI
     ALWIIQHLSL
//