ID A0A0T1QHE3_9ACTN Unreviewed; 449 AA.
AC A0A0T1QHE3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Ribonuclease {ECO:0000313|EMBL:KQX16743.1};
GN ORFNames=ASC82_00300 {ECO:0000313|EMBL:KQX16743.1};
OS Streptomyces sp. Root431.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736535 {ECO:0000313|EMBL:KQX16743.1, ECO:0000313|Proteomes:UP000051818};
RN [1] {ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|Proteomes:UP000051818};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX16743.1, ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|EMBL:KQX16743.1,
RC ECO:0000313|Proteomes:UP000051818};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQX16743.1}.
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DR EMBL; LMEI01000001; KQX16743.1; -; Genomic_DNA.
DR RefSeq; WP_056639709.1; NZ_LMEI01000001.1.
DR AlphaFoldDB; A0A0T1QHE3; -.
DR OrthoDB; 5296884at2; -.
DR Proteomes; UP000051818; Unassembled WGS sequence.
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;
FT DOMAIN 5..137
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 329
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 449 AA; 46797 MW; 7E166BA4267A201D CRC64;
MPSPSSREVI VEADGGSRGN PGPAGYGAVV LDPVTGETLA EAAEYIGVAT NNVAEYKGLV
AGLTAARELF PDATVHVRMD SKLVVEQMSG RWKIKHPDMK PLAAEAGRVF PAGRVRYEWI
PRELNKHADR LANEAMDAGK QGRQWEPSGS TAALDTAAAR SAASLPPSGP PGDAAAGAAR
ARAALATRTV EPSEASDQVD DGLFAPDEAV AAQARASLAS AARTEATTQA EKAPQGWTGP
DMGAPATFVL LRHGETALTP EKRFSGSGGT DPELSAAGLR QAEAVAEALA ARGTIQEIVS
SPLTRCRQTA AAVAARLGLD VQVERGLRET DFGAWEGMTF GEVRERYGDD LDAWLASPKA
APTGGGESFA AVARRVAATR DRLTAAHAGR TVLLVTHVTP IKTLVRLALG APPESLFRME
LSAASISAVA YYADGNASVR LLNDTSHLR
//
