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Database: UniProt
Entry: B9Y774_9FIRM
LinkDB: B9Y774_9FIRM
Original site: B9Y774_9FIRM 
ID   B9Y774_9FIRM            Unreviewed;       270 AA.
AC   B9Y774;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=PHP domain protein {ECO:0000313|EMBL:EEF68161.1};
DE            EC=3.1.3.- {ECO:0000313|EMBL:EEF68161.1};
GN   ORFNames=HOLDEFILI_01667 {ECO:0000313|EMBL:EEF68161.1};
OS   Holdemania filiformis DSM 12042.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Holdemania.
OX   NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF68161.1, ECO:0000313|Proteomes:UP000005950};
RN   [1] {ECO:0000313|EMBL:EEF68161.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF68161.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEF68161.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF68161.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL   Submitted (FEB-2009) 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:EEF68161.1}.
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DR   EMBL; ACCF01000093; EEF68161.1; -; Genomic_DNA.
DR   RefSeq; WP_006058859.1; NZ_GG657556.1.
DR   AlphaFoldDB; B9Y774; -.
DR   STRING; 545696.HOLDEFILI_01667; -.
DR   eggNOG; COG0613; Bacteria.
DR   HOGENOM; CLU_067347_1_2_9; -.
DR   Proteomes; UP000005950; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07438; PHP_HisPPase_AMP; 1.
DR   Gene3D; 1.10.150.650; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   PANTHER; PTHR42924; EXONUCLEASE; 1.
DR   PANTHER; PTHR42924:SF3; POLIIIAC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; PHP domain-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EEF68161.1}.
FT   DOMAIN          3..68
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   270 AA;  30545 MW;  7E145DFABD4FFF4F CRC64;
     MYADLHIHSW YSDRTMTVDE IVEQARVRHV SLIAVTDHNQ LAGSRECLQK TRGTGIRCLS
     GVELDAQDFG INFHILGYGV DLENGQFQEF VEANRLRLER VNELLIEKME HAGEPVSLDE
     YRQFSYDRRL GGWKALHYFA AKDLVADFKQ GFLMYARYHH DYCCVGFPPV REVVRQIQAA
     KGKAILAHPG KVIPAAKLSE VLPAVMAEGL DGIECWYPSH DAGTTQICVN YCRERDLMMT
     AGADCHGSFE TTQIGQLKTP IAQLVLKDWI
//
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