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}.
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; 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
//