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Database: UniProt
Entry: A0A1B6QKS0_SORBI
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Original site: A0A1B6QKS0_SORBI 
ID   A0A1B6QKS0_SORBI        Unreviewed;       825 AA.
AC   A0A1B6QKS0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00012917};
DE            EC=3.4.19.1 {ECO:0000256|ARBA:ARBA00012917};
GN   ORFNames=SORBI_3001G248300 {ECO:0000313|EMBL:KXG38530.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG38530.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:KXG38530.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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   EMBL; CM000760; KXG38530.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6QKS0; -.
DR   STRING; 4558.A0A1B6QKS0; -.
DR   EnsemblPlants; KXG38530; KXG38530; SORBI_3001G248300.
DR   Gramene; KXG38530; KXG38530; SORBI_3001G248300.
DR   eggNOG; KOG2100; Eukaryota.
DR   InParanoid; A0A1B6QKS0; -.
DR   OrthoDB; 2877590at2759; -.
DR   Proteomes; UP000000768; Chromosome 1.
DR   ExpressionAtlas; A0A1B6QKS0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR045550; AARE_N.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF30; ACYLAMINO-ACID-RELEASING ENZYME 1; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF19283; APEH_N; 1.
DR   Pfam; PF07676; PD40; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT   DOMAIN          76..348
FT                   /note="Acylamino-acid-releasing enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19283"
FT   DOMAIN          607..824
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   825 AA;  90371 MW;  5F582C64B159E7FA CRC64;
     MVVLVKVLVT CAKFCCPAAS LLLSASTSRA RALPGGPLLR RRTSKVSLRS IAMATTQASD
     AAADKGLPLA VDATMADEYA SQSKLLQEFV KIPTIGKAWI FNSKDDDMSK AVVSIGQTDL
     LANKRRQFLL NSHISKSPKS VDFKWSPFPT EISGASAVIP SPSGEKLLLV RNSEDDSPTK
     LEIWGPCQLE NEIHIAKSVH GSLYTDEWFG GISWNQEETF IAYVAEEPPQ PKPVFNDYGF
     KKEGSSEKDC KSWKGQGDWE ETWGETYSKK RIPALFVVNI SSGEVRPVKQ IPRSLSVGQV
     IWAPSSSYSL VFVAWSSDNG FQETPRKLGI KYCYNRPCAL YAAPDPFREE AEKSSTEGNK
     SETTTMIKLT GDLISAFFPR FSPDGKYLVF ISAKSAVDSG AHNATNSMHR IEWPADGNLD
     GSLGIADVVA VVMCPKDNCF PGLYCFGLLR DPWLTDGQTM IISSVWGSRE VILSVNVVSC
     EVSRVSPQDS DYSWNVLAVD KNNILAVSSS LITLPQMYYA IKVPQTESNW EWQEVSTPFP
     KPSDKISSIL AEHKFSILKI PISNPSDKLA NGAKLPFEAI FVSHKDSASN PTIVVLHGGP
     HSVYPSSYSK SLAFLFSQGY NLLVVNYRGS LGFGEEALQS LPGNIGSQDV NDVLTALDLV
     IKRGLIDPSR VAVVGGSHGG FLTTHLIGQA PDTFVAAAAR NPVCNLSLMV GTSDIPDWCF
     VEIYGKEGKK YFSESPSVDD ICQFHQKSPI SHISEVKTPT LFLLGAQDLR VPVSNGLQYA
     RALKERGIES KTIIFPEDIH GIDKPQSDFE SFLNIGVWFK KHMSK
//
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