ID A0A0P7YW76_9SPHN Unreviewed; 742 AA.
AC A0A0P7YW76;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Dipeptidyl-peptidase 4 {ECO:0000313|EMBL:KPP95066.1};
DE EC=3.4.14.5 {ECO:0000313|EMBL:KPP95066.1};
GN ORFNames=HLUCCO15_03190 {ECO:0000313|EMBL:KPP95066.1};
OS Erythrobacteraceae bacterium HL-111.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae.
OX NCBI_TaxID=1666908 {ECO:0000313|EMBL:KPP95066.1, ECO:0000313|Proteomes:UP000050295};
RN [1] {ECO:0000313|EMBL:KPP95066.1, ECO:0000313|Proteomes:UP000050295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-111 {ECO:0000313|EMBL:KPP95066.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPP95066.1}.
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DR EMBL; LJSW01000004; KPP95066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7YW76; -.
DR PATRIC; fig|1666908.3.peg.1978; -.
DR Proteomes; UP000050295; Unassembled WGS sequence.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
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 Hydrolase {ECO:0000313|EMBL:KPP95066.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..742
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006146728"
FT DOMAIN 138..454
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 543..736
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 742 AA; 83041 MW; 997BE8A20C7FDFB4 CRC64;
MRLSILAAAG AAILSSQPVL ADTPMTAEPE LTFERVFASP SLDGPAPRQA KLSPDGKYLT
LLRNRADDLE RYDLWGYDIA TREWRMLVDS EALGTGRELS EDEKMQRERA RVGNLKGIIT
YQWASDGSGV LVPLDGDLYF ANLDGSVTRL TDTEGTELNP KLSGKGGFVS FVRDRQLWVG
PFGEEARPIT PKEGETIRWG EAEFVAQEEM GRLTGYWWSP DDSRLVVQRT DEEPVGVVTR
AAIGATGTRV FDQRYPVAGS DNAIVELYVM DPDGSDRVKV DLGPDTDIYV ARVDWAPDGS
AIYVQRQNRA QTVLDMLRVD PATGESEVWF TERAARPDYW INLSDNYRFL KDGSLLWWSE
RSGYGQFYRF DGDAWTQLTE GESPATSLDG VNEEEGSFFY TRVDGVLTRQ VYRAALDRAA
TPQRLTDPSY TNSASMDRKG RALLVTRSRP DQPPQSYLAG REGQRLAWIE ENALGEDHPY
TPYLMSHVMP EFGTIKAEDG TPLHYMMLKP EMEPGKKYPV FYYHYSGPGP QVVTKGWTGA
LAQAIVDKGY IWFALDNRGS ANRGVDFEQP IYRAMGGVEV RDQKAGAEWL KRQSYVDGDR
IALYGWSYGG YMTLKQLEAD PGLYAAGVSG APVTKWELYD THYTERYMGD PREVPEAYEA
ASAIPQATRI SDPLLIVHGM ADDNVVFENS SEIIAALQEG NVPFEMMLYP GYTHRVSGET
ISPHLWNTIF RFLDSHGVTP PE
//
