ID I4EVQ5_9ACTN Unreviewed; 394 AA.
AC I4EVQ5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:CCH87468.1};
GN OrderedLocusNames=MODMU_2033 {ECO:0000313|EMBL:CCH87468.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH87468.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH87468.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH87468.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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DR EMBL; FO203431; CCH87468.1; -; Genomic_DNA.
DR AlphaFoldDB; I4EVQ5; -.
DR STRING; 477641.MODMU_2033; -.
DR KEGG; mmar:MODMU_2033; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_023620_2_2_11; -.
DR OrthoDB; 3514520at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT DOMAIN 57..389
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 394 AA; 41142 MW; 221BD25BA0D3722C CRC64;
MATTVYRGAA LADGTGPELV RDVSVQVEDD RVRWIGPADD EPDPGPDAEV VDCSGAVVVP
GLVDSHSHLT MPGGAHWVDR GFDPPVRLVA VAEDNARLLR SAGVRWARDV GSPTGTDPVD
GRVRGLALGV RDRWAGHREY PYVRAAGTWI SQRGSLPGGL AVEVTDGDAL LAAALAQLDD
GADLVKLYLD GPDADTSPFT VDEVRRVVAA AAERGARVAA HSSSLPGARA GAEAGVASLE
HGFTLDADVA GLMAAHGVAL VSTLSVLESW RTFSRTTTLP RFAGEESEAQ IAERRERAHE
SVRLAARAGV LIASGTDFGG GSTRANQLAW EVECLVEAAL EPWQALAAAT RNGGQLLGEP
EAGVLRVGGP ADLVLVHGDP LSDPAALWRV WQVS
//
