ID A0A0Q0VER5_9SPHI Unreviewed; 777 AA.
AC A0A0Q0VER5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Peptidase S9 {ECO:0000313|EMBL:KQC01551.1};
GN ORFNames=AQF98_07540 {ECO:0000313|EMBL:KQC01551.1};
OS Pedobacter sp. Hv1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQC01551.1, ECO:0000313|Proteomes:UP000050543};
RN [1] {ECO:0000313|EMBL:KQC01551.1, ECO:0000313|Proteomes:UP000050543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hv1 {ECO:0000313|EMBL:KQC01551.1,
RC ECO:0000313|Proteomes:UP000050543};
RA Ott B.M., Beka L., Graf J., Rio R.;
RT "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT Medicinal Leech Mucosal Castings.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KQC01551.1}.
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DR EMBL; LLWP01000003; KQC01551.1; -; Genomic_DNA.
DR RefSeq; WP_055131317.1; NZ_LLWP01000003.1.
DR AlphaFoldDB; A0A0Q0VER5; -.
DR STRING; 1740090.AQF98_07540; -.
DR OrthoDB; 9777457at2; -.
DR Proteomes; UP000050543; 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:SF118; BLR1971 PROTEIN; 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:UP000050543};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..777
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006185256"
FT DOMAIN 126..477
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 565..757
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 143..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 86246 MW; 1B6330697A0C8689 CRC64;
MNKYLLTATA LAFAFVANAQ QGKSLTAKDY ERAEQFMSYN TEKFVDAGTV RPNWLAGDKF
WYLSNSSAKG AEFILVDPVK RTRAAAFDHQ KLATALSAAS GNTYEATKLP FPTISYAADG
KSISFSANGK RWDYDLQTNQ VTPSTGTADA VTGPPTRGRM GGGNNGVTSP DGTKAVFIKD
WNLWVRDVAT KKETQLTTDG VKDYGYATDN AGWTMSDGPI VRWSPDSKKV ATFQQDQRNV
SDMYLVTTNV GAPVLKAWKY PLPGDKVIAT IRRVIIEVEN AKVVSLQIPP DPHRATLSDD
IASSGTFDDI DWKADGSEMA FLSTSRDHKQ EKFRIANAAT GAVREVFEEV VKTQFESGRG
AINWRYLPNT NEILWYSERD NWGHMYLYDA KTGKLKNQIT KGDWLVSRLL KVDEKERVLY
FMGNGREAGN PYFSYLYKIG FDGKGLTLLS PELGNHQITF SPSNNYFIDT YSQPDVPSVT
NFRNIDGKLI GSLEKGDVSR LIATGWKAPT PVNVKAHDGT TDIYGLVFTP TQMDPNKKYP
VIDYIYPGPQ GGSVGSWSFS ASRGDHQALA ELGFIVVMIE GTSNPFRSKS FHDMSYGNMA
ENTLPDQITA IRQLAKTYPI DTNKVGIWGH SGGGFATAAA MFRYPDFFKV GIAESGNHDN
RNYEDDWGER YNGLVENSNY EAQANQNYAK NLKGKLMLAH GMMDNNVPPS NTLLVVDALI
KANKNFDLVL FPNSAHGFGA NSPYMMRKRW DYFVTNLLDA EPPKEFNLRG AIQTSRN
//
