ID F2RKP2_STRVP Unreviewed; 499 AA.
AC F2RKP2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Phosphoglycerate mutase family {ECO:0000313|EMBL:CCA55281.1};
GN OrderedLocusNames=SVEN_1994 {ECO:0000313|EMBL:CCA55281.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA55281.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA55281.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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DR EMBL; FR845719; CCA55281.1; -; Genomic_DNA.
DR RefSeq; WP_015033199.1; NZ_CP029197.1.
DR AlphaFoldDB; F2RKP2; -.
DR STRING; 953739.SVEN_1994; -.
DR GeneID; 69864152; -.
DR KEGG; sve:SVEN_1994; -.
DR PATRIC; fig|953739.5.peg.4148; -.
DR eggNOG; COG0328; Bacteria.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_035712_0_0_11; -.
DR OrthoDB; 5296884at2; -.
DR Proteomes; UP000006854; 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; 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 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:UP000006854}.
FT DOMAIN 5..137
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 162..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 303
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 379
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 499 AA; 50996 MW; A9360142816E3349 CRC64;
MTASSSREVI VEADGGSRGN PGPAGYGAVV LDPVTGETLA EAAEYIGVAT NNVAEYKGLV
AGLKAARELF PDATVHVRMD SKLVVEQMSG RWKIKHPDMK PLAAEAGRVF PAGRVRYEWI
PRERNKHADR LANEAMDAGK LGRAWEPSAS TAALDSAAAR NAATLPPSGP PGDATAGAAR
ARAALATAGG LEPGGTRTAP GGTHPAPGGG TAPGGGTGTG AWPGAVSRPT TPDVQTGPGT
GAADGLFAAE EAAPPATASG DFEAEAAAAR PAALQPPPAA APRQGWSGGP DMGAPATFVL
LRHGETALTP EKRFSGSGGT DPELSPAGLR QAEAVAEALA ARGTVQEIVS SPLTRCRQTA
AAVAARLGLD VRVEQGLRET DFGAWEGLTF REVRERYAED LDAWLASPKA APTGGGESFA
TVARRVAATR DRLTAAYAGR TVLLVTHVTP IKTLVRLALG APPESLFRME LSAASISAVA
YYADGNASVR LLNDTSHLR
//
