ID   D9Y214_9ACTN            Unreviewed;       415 AA.
AC   D9Y214;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Prolyl aminopeptidase {ECO:0000313|EMBL:EFL43007.1};
GN   ORFNames=SSRG_05811 {ECO:0000313|EMBL:EFL43007.1};
OS   Streptomyces griseoflavus Tu4000.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL43007.1, ECO:0000313|Proteomes:UP000002968};
RN   [1] {ECO:0000313|EMBL:EFL43007.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu4000 {ECO:0000313|EMBL:EFL43007.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; GG657758; EFL43007.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9Y214; -.
DR   STRING; 467200.SSRG_05811; -.
DR   ESTHER; 9acto-d9y214; Proline_iminopeptidase.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_024518_2_0_11; -.
DR   Proteomes; UP000002968; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF2; PROLYL AMINOPEPTIDASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:EFL43007.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000313|EMBL:EFL43007.1}.
FT   DOMAIN          31..203
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   415 AA;  45526 MW;  3A5432F3BD041CCD CRC64;
     MPLDHDTPSG ETIDLYAREA VASDKAGQDL PWLLYLQGGP GFGANRFIRK EAWLGRALEE
     YRVLLLDQRG TGHSTPANRQ TLPLRGGPAE QADYLSHFRA DSIVRDCEAI RPQVTGGAPW
     TVLGQSFGGF CAVAYLSTAP EGLDTALVTG GLPSLDAHAD DVYRAAYPRV ARKVAAHYAR
     YPQDVERARR IADHLLTHEV VLPNGYRFTV EAFQSLGLML GGGDGSHRLH HLLEDAFVRT
     PGGPALSDAF QEQAQALLSF AGHPLYALVH EAIYGQDARP TAWSAERVRN EFPGFDAAKT
     LAGDEPLLFT GETIHPWMFD CDPALRPLRE TAELLAARTD WTPLYDPARL AANEVPVAAA
     VYHDDMYVHT AHSLETARAI RGLRTWVTDE FEHDGVRAGG PRVLDRLIAL ARDEV
//