ID A0A0J1D6X8_9BURK Unreviewed; 511 AA.
AC A0A0J1D6X8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Metal-chelation protein CHAD {ECO:0008006|Google:ProtNLM};
GN ORFNames=AB595_20775 {ECO:0000313|EMBL:KLU34877.1};
OS Massilia sp. WF1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU34877.1, ECO:0000313|Proteomes:UP000036336};
RN [1] {ECO:0000313|Proteomes:UP000036336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA Lou J., Gu H., Wang H., Xu J.;
RT "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT contaminated soil.";
RL Submitted (JUN-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:KLU34877.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LELH02000033; KLU34877.1; -; Genomic_DNA.
DR RefSeq; WP_047826866.1; NZ_LELH02000033.1.
DR AlphaFoldDB; A0A0J1D6X8; -.
DR PATRIC; fig|1406431.3.peg.3864; -.
DR Proteomes; UP000036336; Unassembled WGS sequence.
DR GO; GO:0050355; F:inorganic triphosphate phosphatase activity; IEA:InterPro.
DR CDD; cd07756; CYTH-like_Pase_CHAD; 1.
DR Gene3D; 1.40.20.10; CHAD domain; 1.
DR Gene3D; 2.40.320.10; Hypothetical Protein Pfu-838710-001; 1.
DR InterPro; IPR007899; CHAD_dom.
DR InterPro; IPR038186; CHAD_dom_sf.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR039013; YgiF.
DR PANTHER; PTHR39569; INORGANIC TRIPHOSPHATASE; 1.
DR PANTHER; PTHR39569:SF1; INORGANIC TRIPHOSPHATASE; 1.
DR Pfam; PF05235; CHAD; 1.
DR Pfam; PF01928; CYTH; 1.
DR SMART; SM00880; CHAD; 1.
DR SMART; SM01118; CYTH; 1.
DR SUPFAM; SSF55154; CYTH-like phosphatases; 1.
DR PROSITE; PS51708; CHAD; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000036336}.
FT DOMAIN 1..207
FT /note="CYTH"
FT /evidence="ECO:0000259|PROSITE:PS51707"
FT DOMAIN 222..503
FT /note="CHAD"
FT /evidence="ECO:0000259|PROSITE:PS51708"
SQ SEQUENCE 511 AA; 56315 MW; DFED6631EAD3271E CRC64;
MECEIKLGLD GASASQVKKI PLLRPPGGAK PEEHEHVDRY FDTADFTLWQ HGYALRVRSE
GMRHVQTLKG GGTVVAGLHR RVELEADIAS DEPDRALFAR QLREVLPALA KQFERHAAPL
EPVFVNKSKR SAWMLELDGG AQVECALDTG ELQRGDRTVP VRELELEMKD GDPARLYELA
RQVHAAVPVR IENVSKAERG YALAGAVAPR AVKATAVSLR RKASMGEALA GILRNCLEQM
QANEQGVLSG EVESLHQMRV GLRRLRAAMA MVKGMVQLPA PLADEVEWLA GELGDARNWD
VFIESLLPGL PVPDEHKPAL ARVAVAAREE AERHRARVRA AVGSPRYTGL MLGLGAWIAG
QGWKQADSIP QDAPADALEQ KVLKAAPRLV QHAAARVRKR ARGFDLKQPE SLHKVRIAAK
KERYAREFFE ALSHGKKEAR RHDLLTGMQD ELGLLNDSVV ARGLVAQLRE RVPQEQALLG
FIEGVLAVRA LDALPRAGKH VRRKLRARAA F
//
