ID   A0A0M3D5B4_9MICO        Unreviewed;       460 AA.
AC   A0A0M3D5B4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KKX96571.1};
GN   ORFNames=AAY78_17880 {ECO:0000313|EMBL:KKX96571.1};
OS   Microbacterium sp. Ag1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1643443 {ECO:0000313|EMBL:KKX96571.1, ECO:0000313|Proteomes:UP000034223};
RN   [1] {ECO:0000313|EMBL:KKX96571.1, ECO:0000313|Proteomes:UP000034223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKX96571.1,
RC   ECO:0000313|Proteomes:UP000034223};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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:KKX96571.1}.
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DR   EMBL; LBCR01000034; KKX96571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M3D5B4; -.
DR   OrthoDB; 9766527at2; -.
DR   Proteomes; UP000034223; 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:KKX96571.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000313|EMBL:KKX96571.1};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT   DOMAIN          34..160
FT                   /note="PIN"
FT                   /evidence="ECO:0000259|SMART:SM00670"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  49882 MW;  1457FDAFAB565614 CRC64;
     MTTRTAQQAT STAQQSTRKT TRRASSADPD QDLRTYVLDT SVLLSDPQAF FRFAEHSVVL
     PVVVITELEG KRHDPEIGYF ARQALRHLDD LRIEHGRLDF PVEVGEGGTL RVELANTDSS
     VLPAGIRLSD NDTRILSVAM HLAQDGQDVT IVSKDLPMRV KAASLGLRAE EYLAEQAVDS
     GWTGISTLDL SGDDISDLYE SEVGISEQAR GLPVNTGLII HSERGSALGR VTGDGEYRLV
     RGDRDIFGMH GRSAEQRIAI DLLLDQEVGI VSLGGRAGTG KSALALCAGL EAVLERQQQK
     KIIVFRPLFA VGGQELGYLP GDQGEKMGPW GQAVFDTLGS VVSGNVIEEV VERGLLEVLP
     LTHIRGRSLH DAFVIVDEAQ SLERNVLLTV LSRMGQNSRV ILTHDVGQRD NLRVGRHDGI
     ASVIETLKGH DLFGHVTLTR SERSAIAALV TELLEGGELS
//