ID A0A0U3PTQ8_9ACTN Unreviewed; 401 AA.
AC A0A0U3PTQ8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acid phosphatase {ECO:0000313|EMBL:ALV36018.1};
GN ORFNames=AS200_31215 {ECO:0000313|EMBL:ALV36018.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV36018.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV36018.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV36018.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013743; ALV36018.1; -; Genomic_DNA.
DR RefSeq; WP_058925620.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PTQ8; -.
DR STRING; 1725411.AS200_31215; -.
DR KEGG; scx:AS200_31215; -.
DR OrthoDB; 5296884at2; -.
DR Proteomes; UP000068029; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd09279; RNase_HI_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR014636; RNaseH/PGlycerate_mutase.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF13456; RVT_3; 1.
DR PIRSF; PIRSF036922; RNaseH_PGAM; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT DOMAIN 1..140
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 132..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 281
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 401 AA; 41998 MW; 3EBCED659ACC69E6 CRC64;
MREFIVEADG GSRGNPGPAG YGSVVLDAAT GETLAEAAEY IGVTTNNVAE YRGLLAGLRA
AHALDPSASV HVRMDSKLVV EQMSGRWKIK HPDLKPLAME AARVFPAERV TYEWIPRERN
KHADRLANEA MDAGARGEQW SAAESTAELD SAAESLGGGA AFAEGAGAGD AGKAAADARA
ATAVASPGWA PADMGAPATF VLLRHGETPL TPQKRFSGSG GTNPALSEVG REQAERVGAA
LARRGTVQAI VASPLARTRE TAAIVARHLG LEVSVEDEIR ETDFGAWEGL TFGEVRERYP
DDLTRWLADP TVAPSGGGES FAATATRIAA ARDKLVAAHA GRTVLLVSHV TPIKTFIQLA
LGAPPQALFR MELSAASLSA VAYYADGNAS VRLFNDTSHL R
//
