ID A0A0N0MWS0_9ACTN Unreviewed; 859 AA.
AC A0A0N0MWS0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Polynucleotide kinase-phosphatase, bacterial {ECO:0000313|EMBL:KPI10528.1};
DE EC=3.6.1.17 {ECO:0000313|EMBL:KPI10528.1};
GN ORFNames=OK074_0163 {ECO:0000313|EMBL:KPI10528.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI10528.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI10528.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI10528.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-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:KPI10528.1}.
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DR EMBL; LJCV01000221; KPI10528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0MWS0; -.
DR PATRIC; fig|1592327.3.peg.3527; -.
DR OrthoDB; 9807890at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07423; MPP_Prp_like; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041780; MPP_PrpE-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR024028; PNKP_bac.
DR InterPro; IPR032380; PNKP_ligase_dom.
DR NCBIfam; TIGR04075; bacter_Pnkp; 1.
DR PANTHER; PTHR12435:SF2; PROTEIN KTI12 HOMOLOG; 1.
DR PANTHER; PTHR12435; UNCHARACTERIZED; 1.
DR Pfam; PF13671; AAA_33; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16542; PNKP_ligase; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KPI10528.1};
KW Kinase {ECO:0000313|EMBL:KPI10528.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Transferase {ECO:0000313|EMBL:KPI10528.1}.
FT DOMAIN 202..388
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 476..854
FT /note="Polynucleotide kinase-phosphatase ligase"
FT /evidence="ECO:0000259|Pfam:PF16542"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 94443 MW; 91182CED79652851 CRC64;
MTENETETQA QAQTQPRHKK RTLPVTDLSL VVLIGASGSG KSTFARRHFK PTEVISSDFC
RGLVADDEND QSASGDAFDV LHYIAGKRLA AGRRTVVDAT SVQSDSRRQL VELARQYDVL
PIAIVLDVSE EVCAERNAAR ADRAAMPRRV ITRHTRELRR SLRHLEREGF RKVHVLRGVE
EVETASVVTE RRFNDLTHLT GPFDIVGDVH GCAAELETLL GQLGYADGVH PDGRTAVFVG
DLVDRGPDSP GVLRRVMSMV ASGNALCVSG NHENKFGRYL KGRQVQHTHG LAQTIAQMAE
ESDEFRSLVR EFVDGLISHY VLDGGRLVVC HAGLPEKYHG RTSGRVRSHA LYGDTTGETD
EFGLPVRYPW AEDYRGRAAV VYGHTPVPEA TWLNNTICLD TGAVFGGRLT ALRWPEREVV
DVPAERVWYE PARPLRTEAP GGADGRPLDL ADVHGRRVVE TRYAGRVTVR EENAAAALEV
MSRFAVDPRL LPYLPPTMAP TPTSQVEGYL EHPAEAFAQY AADGVARVVC EEKHMGSRAV
ALVCRDAEAA RRRFGVDGPT GALYTRTGRP FLSDAAVTEE LLDRVRKSAD AAGLWDELAT
DWLLLDAELM PWSLKASGLL RAQYAAVGAA SGAVFPGALA ALDRAAARGT DVRDLLARQR
ERAADAAAFT DAYRRYCWPT DGLEGVRLAP FQLLAVQGRS LAALPHAEQL ALLDRLVEHD
GSGLLQTTRR LYVDTGDAES IGAGTDWWLE LTARGGEGMV VKPLDALVRD GRGRLVQPGV
KCRGREYLRI IYGPEYTRPD NLARLRHRSL NHKRSLAIRE YALGTEALDR LAEGEPLWRV
HEAVFAVLAL ESEPVDPRL
//