ID A0A0Q0YJ68_9CORY Unreviewed; 375 AA.
AC A0A0Q0YJ68;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phosphoserine phosphatase 1 {ECO:0000313|EMBL:KQB86828.1};
DE EC=3.1.3.3 {ECO:0000313|EMBL:KQB86828.1};
GN Name=pspA {ECO:0000313|EMBL:KQB86828.1};
GN ORFNames=Clow_01036 {ECO:0000313|EMBL:KQB86828.1};
OS Corynebacterium lowii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB86828.1, ECO:0000313|Proteomes:UP000050488};
RN [1] {ECO:0000313|EMBL:KQB86828.1, ECO:0000313|Proteomes:UP000050488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130206 {ECO:0000313|EMBL:KQB86828.1,
RC ECO:0000313|Proteomes:UP000050488};
RA Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT human clinical disease and and emended description of Corynebacterium
RT mastiditis.";
RL Submitted (OCT-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:KQB86828.1}.
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DR EMBL; LKEV01000002; KQB86828.1; -; Genomic_DNA.
DR RefSeq; WP_055177187.1; NZ_LKEV01000002.1.
DR AlphaFoldDB; A0A0Q0YJ68; -.
DR STRING; 1544413.Clow_01036; -.
DR PATRIC; fig|1544413.3.peg.1044; -.
DR OrthoDB; 5296884at2; -.
DR Proteomes; UP000050488; Unassembled WGS sequence.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
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:SF34; BROAD-SPECIFICITY PHOSPHATASE YOR283W; 1.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-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 Hydrolase {ECO:0000313|EMBL:KQB86828.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050488}.
FT DOMAIN 1..139
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT ACT_SITE 184
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 260
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 375 AA; 40044 MW; BFE8CFB1F4CE309E CRC64;
MKVCIEADGG SRGNPGIAGS GSVLYDATRT TILREQAYVV GTSATNNVAE YYGLITGLEA
ARDYGATEVA VYMDSKLVVE QMTGRWKIKH PDMQKLALRA RDIMASFDSV TFQWVPREKN
KKADELSNVA MDAAAAGAKP GLVKDTSGSA EVAAAETVGE ASFSPTRVLN PEGAPVTRLI
LVRHGQTEHT VRGCYSGHSD PDLTSIGTAQ AERAAQLVQG LVSSREAVVL SSPLRRARHT
AQAVAQSIGA AVKVEADLIE LNFGDWDGKE FSQVRDAYPA EHAAWLEDTA VAPPGGESLD
ELHRRVSALR ERLVKDHEGA TLVLVSHVNP IKSLLRQALG GGPECFRGIF LDIASVSVVE
FMGERGVVRG INIGQ
//
