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Database: UniProt
Entry: A0A1V2QML7_9PSEU
LinkDB: A0A1V2QML7_9PSEU
Original site: A0A1V2QML7_9PSEU 
ID   A0A1V2QML7_9PSEU        Unreviewed;       686 AA.
AC   A0A1V2QML7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=S9 family peptidase {ECO:0000313|EMBL:ONI89497.1};
GN   ORFNames=ALI22I_15940 {ECO:0000313|EMBL:ONI89497.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI89497.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI89497.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI89497.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI89497.1}.
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DR   EMBL; MTQP01000056; ONI89497.1; -; Genomic_DNA.
DR   RefSeq; WP_077006267.1; NZ_MTQP01000056.1.
DR   AlphaFoldDB; A0A1V2QML7; -.
DR   STRING; 1933778.ALI22I_15940; -.
DR   OrthoDB; 9812921at2; -.
DR   Proteomes; UP000188617; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF193; DIPEPTIDYL-PEPTIDASE 9; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000188617}.
FT   DOMAIN          108..394
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          488..685
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          66..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   686 AA;  73555 MW;  B482F878F0916E1B CRC64;
     MGNEISFPRQ HARTQRFTLG APRTFTAAPD GAKVYFLRTA TATSRANGLW AFDTATRTET
     LLADPSTLLT DPEDLSPEER ARRERTRESA AGIVGYSTDS DVRQAAFALS GRLFVVELAG
     GAVRELPVTG AVIDPRLDPT GRKVGYVADG ALHVVDLETG ADRVVASPDG PDVTWGLAEF
     IAAEEMSRFR GYWFSPDGEH VLAARVDNAP VPRWHIADPA NPGTPAAEIA YPAAGEANAV
     VGVAVFGAGR VDVAWDHDAF PYLSAVSWSS HGKPLLQVQS RDQRRVQVLA VDVETGAADV
     VADDTDPHWL EIVPGTPAWT PDGELLRVLP IGDANRLVVG DRAWTPDGFQ VRSVVDVAED
     GVLVTASTDD PTQTHVFLVT GDNITRLSTE DGVHGATRAG GVLVLARSSM DHFGPKVTVS
     TGGEIGTFAE TPVLTPEVRL MTVGDRDLRA ALLFPRDHVP GVKLPVLLDP YGGPHAQRVI
     SARNAYLTSQ WLADQGFAVL VVDGRGTPGR GPAWEREIAF DFAGATLDDQ VDALHAVAAQ
     EPDLDLTRVG IRGWSYGGYL AALAVLRRPD VFHAGIAGAP VTDWRLYDTH YTERYLGHPA
     DQPDVYDSNS LIADAPKLER PLMIVHGLAD DNVVAAHTLR LSSALLAAGR PHTVLPLSGV
     THMTPQEQVA ENLLLLQVDF LHRALA
//
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