ID A0A1M6M018_9CLOT Unreviewed; 249 AA.
AC A0A1M6M018;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Putative hydrolase {ECO:0000313|EMBL:SHJ76784.1};
GN ORFNames=SAMN02745912_01004 {ECO:0000313|EMBL:SHJ76784.1};
OS Paramaledivibacter caminithermalis DSM 15212.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Paramaledivibacter.
OX NCBI_TaxID=1121301 {ECO:0000313|EMBL:SHJ76784.1, ECO:0000313|Proteomes:UP000184465};
RN [1] {ECO:0000313|EMBL:SHJ76784.1, ECO:0000313|Proteomes:UP000184465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15212 {ECO:0000313|EMBL:SHJ76784.1,
RC ECO:0000313|Proteomes:UP000184465};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01561};
CC Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01561};
CC -!- SIMILARITY: Belongs to the PHP family. {ECO:0000256|HAMAP-
CC Rule:MF_01561}.
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DR EMBL; FRAG01000008; SHJ76784.1; -; Genomic_DNA.
DR RefSeq; WP_073147588.1; NZ_FRAG01000008.1.
DR AlphaFoldDB; A0A1M6M018; -.
DR STRING; 1121301.SAMN02745912_01004; -.
DR OrthoDB; 9808747at2; -.
DR Proteomes; UP000184465; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd07437; PHP_HisPPase_Ycdx_like; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR HAMAP; MF_01561; YcdX_phosphat; 1.
DR InterPro; IPR023710; Phosphatase_YcdX_put.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR PANTHER; PTHR36928; PHOSPHATASE YCDX-RELATED; 1.
DR PANTHER; PTHR36928:SF1; PHOSPHATASE YCDX-RELATED; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01561};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01561}; Reference proteome {ECO:0000313|Proteomes:UP000184465};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01561}.
FT DOMAIN 5..79
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01561"
SQ SEQUENCE 249 AA; 28004 MW; 329102BB3169F41D CRC64;
MKFVLDTHTH TIASGHAYST IHDYIEVAKK KKLELVAFTD HGPAMPGGPN IFYIGNQRVI
PREIDGIEIL RGVEANIMDF EGNIDIPDFY LERLDLVLAS LHDVCIQPGT REENTRAFIK
VMNNRYVDIV AHPGNPRFPI DINEFVLAAK KNNKIIEINN STFTNPGRSG SRDNCIMIAR
KAKEHGVFVV AGSDAHISFD VGSFQKSIEV FKLVEMPEEL IMNTSKEKLK KYLKEKGKKL
EEKAVGPIK
//