ID A0A069JX29_9ACTN Unreviewed; 440 AA.
AC A0A069JX29;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KDQ69231.1};
GN ORFNames=DT87_19200 {ECO:0000313|EMBL:KDQ69231.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69231.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ69231.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69231.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000256|ARBA:ARBA00038093}.
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:KDQ69231.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JJOB01000001; KDQ69231.1; -; Genomic_DNA.
DR RefSeq; WP_030627863.1; NZ_JJOB01000001.1.
DR AlphaFoldDB; A0A069JX29; -.
DR OrthoDB; 9766527at2; -.
DR Proteomes; UP000027475; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR CDD; cd09883; PIN_VapC_PhoHL-ATPase; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003714; PhoH.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR PANTHER; PTHR30473:SF2; PIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR30473; PROTEIN PHOH; 1.
DR Pfam; PF02562; PhoH; 1.
DR Pfam; PF13638; PIN_4; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:KDQ69231.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000313|EMBL:KDQ69231.1};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 13..140
FT /note="PIN"
FT /evidence="ECO:0000259|SMART:SM00670"
SQ SEQUENCE 440 AA; 48144 MW; 4972A7215034B233 CRC64;
MVTSTKRRMS DRRTYVLDTS VLLADPNAMT RFDEHEVVLP IVVVTELEAK RHHPELGYFA
RQALRLLDDF RVRYGRLDAP IPLGDLGGSL RVELNHSDPG VLPAGYRLGD NDSRILAVAR
NLQAEGYDVT VVSKDLPLRI KASSVGLLAE EYRAELAITD SGWTGMAELA LTAEQVDLLF
TEETLYVPEA AAYPVHTGLV LQSERGKALG RVTAEGNVRL VRGDREAFGI HGRSAEQRVA
LDLLLDPDVG IVSMGGRAGT GKSALALCAG LEAVLERRQH QKVMVFRPLY AVGGQELGYL
PGTEAEKMSP WAQAVFDTLS AVAGREVIEE VLGRGMLEIL PLTHIRGRSL HDAFVIVDEA
QSLERNVLLT VLSRIGANSR VVLTHDVAQR DNLRVGRYDG VVAVVEKLKG HPLFAHVTLT
RSERSPIAAL VTEMLEEGHI
//