ID A0A3G3GM00_9BACT Unreviewed; 851 AA.
AC A0A3G3GM00;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Serine hydrolase {ECO:0000313|EMBL:AYQ32280.1};
GN ORFNames=DTQ70_08850 {ECO:0000313|EMBL:AYQ32280.1};
OS Runella sp. SP2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae; Runella.
OX NCBI_TaxID=2268026 {ECO:0000313|EMBL:AYQ32280.1, ECO:0000313|Proteomes:UP000270973};
RN [1] {ECO:0000313|EMBL:AYQ32280.1, ECO:0000313|Proteomes:UP000270973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:AYQ32280.1,
RC ECO:0000313|Proteomes:UP000270973};
RA Jin H.M.;
RT "Genome sequence of Runella sp. SP1.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP031030; AYQ32280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G3GM00; -.
DR KEGG; rup:DTQ70_08850; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000270973; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR023100; D-aminoacylase_insert_dom_sf.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR Pfam; PF07969; Amidohydro_3; 2.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AYQ32280.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000270973};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..851
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018333722"
FT DOMAIN 46..351
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT DOMAIN 410..620
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 739..833
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 851 AA; 94382 MW; 0F430B8818E01FB2 CRC64;
MALYSTLHQW TRKAWWLCLA LTALGTAMAQ PNAQKLATLD SSLTLLHQRG MLNGTFLVAK
EGKTVYKKAF GTVAANATQS LTTASAFNLA SVSKQFTSMM VMMLKEEGKL NYDDKLKHHL
PDFPYDTITI RHLLNHTHGL PEYFDLAAQY NTTLDTLTNE GVLKLLKNHR PPLQFQPNSQ
FSYCNTGYIL LACLIEKLTA EPIQRYFERK IVQPLGLKNT YIYTLTMPKS PENRVYGSKR
VNGKYVPNDL IRLDGVWGDG NVYSSVEDLL IWEQALLTEK LIKKATLQDA FKPAKLNDSS
FSWYGFGWGL DKEGLKVSHT GGWVGFQTII ERHLAQKWTF IALTSSEDGT AIRVAQQILE
GKIAKLPTTE LITNAKIVDG TGLASYAGAV RIKNNRIWEV GDLQPYVGEK VTDANGLVLA
PGFIDAHSHH FGGLENRPDA EALVSQGITT IVIGQDGSSY PIDTLQKRMK QQPVAVNVAT
YTGHSTLRAK AMGAKSLFRT AKTDEIEKMK RELKSEMEKG SLGLATGLEY ESAFFSNRDE
VLQLAKVAAK AGGRYMSHIR SEDIGFDEAL DEIIEIGRQT NMPVQISHIK IAKRDQWGRS
REVLGTLQKA RAQGINITAD CYPYDFWNST LRVLFPKRDY TNAESAEFAV NQLFDPSGSV
LVRYAPNAAY VGKTISEIAA IRKETTSKTL MGLIAEAADF DEKNPDFKGS TETIMGKSMS
EEDVANFLAW PFTTICSDGG WGGHPRGYGA FTRVLGNYVR EKKLILLETA IQKMTSLTAE
NLGIRQRGLI QPAFYADLVL FDPNVVNGNA SIQNPTALSS GIERVWVNGE EVYHTQKSTG
KRSGVFIGRG K
//
