ID A0A0F7GD69_9CHLR Unreviewed; 357 AA.
AC A0A0F7GD69;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Aminopeptidase YpdF {ECO:0000313|EMBL:AKG53488.1};
GN Name=ypdF {ECO:0000313|EMBL:AKG53488.1};
GN ORFNames=DGWBC_0819 {ECO:0000313|EMBL:AKG53488.1};
OS Dehalogenimonas sp. WBC-2.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=943347 {ECO:0000313|EMBL:AKG53488.1, ECO:0000313|Proteomes:UP000034106};
RN [1] {ECO:0000313|EMBL:AKG53488.1, ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|EMBL:AKG53488.1,
RC ECO:0000313|Proteomes:UP000034106};
RX PubMed=26452554; DOI=10.1128/AEM.02017-15;
RA Molenda O., Quaile A.T., Edwards E.A.;
RT "Dehalogenimonas sp. Strain WBC-2 Genome and Identification of Its trans-
RT Dichloroethene Reductive Dehalogenase, TdrA.";
RL Appl. Environ. Microbiol. 82:40-50(2015).
RN [2] {ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|Proteomes:UP000034106};
RA Molenda O., Edwards E.A.;
RT "Identification of trans-1,2-dichloroethene reductive dehalogenase (TdrA)
RT in Dehalogenimonas sp. WBC-2.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
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DR EMBL; CP011392; AKG53488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7GD69; -.
DR STRING; 943347.DGWBC_0819; -.
DR KEGG; dew:DGWBC_0819; -.
DR PATRIC; fig|943347.4.peg.858; -.
DR Proteomes; UP000034106; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01092; APP-like; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF8; CYTOPLASMIC PEPTIDASE PEPQ-RELATED; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:AKG53488.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}; Protease {ECO:0000313|EMBL:AKG53488.1}.
FT DOMAIN 7..136
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 144..343
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 357 AA; 38774 MW; F63DDFAD32336F61 CRC64;
MSIYAIRLQN LKNKLQALDV DAILVAQPDN RRYLSGFSGS SGYVLVTMET AVLATDFRYV
EQAAFQAKEC EVLRIDGPVT EWFPALLSGS NIKSLGLEAG FFTIADHDNF EAAISSAGLA
VDLVPIIDAV ETLRAVKDEQ EIQAISAAAN LTDKAFSYVT EHFIKPGVTE LQVAWELEKF
IRETGGELSF PIIVAGGEAS ARPHAQPTCR PLQKNEPLVI DMGAKLDGYC ADLTRTLWLG
AEDTRFRELY NIVLQAQNTA IKGIRSGMTG IEADKLSRDV ITQAGYGKLF GHSLGHGIGL
EVHELPRLSA RATGPLSDGM VFTIEPGIYI PGWGGIRIED DAVLECGKIK LLTASYK
//
