ID A0A062VQA1_9MICO Unreviewed; 453 AA.
AC A0A062VQA1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KDA06513.1};
GN ORFNames=DC31_08880 {ECO:0000313|EMBL:KDA06513.1};
OS Microbacterium sp. CH12i.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1479651 {ECO:0000313|EMBL:KDA06513.1, ECO:0000313|Proteomes:UP000027096};
RN [1] {ECO:0000313|EMBL:KDA06513.1, ECO:0000313|Proteomes:UP000027096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH12i {ECO:0000313|EMBL:KDA06513.1,
RC ECO:0000313|Proteomes:UP000027096};
RA Ferreras E.R., DeMaayer P., Guerrero L.D., Aislabie J.M., Cowan D.A.;
RT "Draft genome sequence of Microbacterium sp. strain CH12i, isolated from
RT shallow groundwater in Cape Hallet, Antarctica.";
RL Submitted (MAR-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:KDA06513.1}.
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DR EMBL; JHET01000003; KDA06513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A062VQA1; -.
DR STRING; 1479651.DC31_08880; -.
DR Proteomes; UP000027096; 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:KDA06513.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000313|EMBL:KDA06513.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027096};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 27..153
FT /note="PIN"
FT /evidence="ECO:0000259|SMART:SM00670"
FT REGION 1..24
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 453 AA; 49184 MW; 21A98EB1BD8EB01A CRC64;
MTTRTAQQST RQVSRRASSG KPDQDLRTYV LDTSVLLSDP QAFFRFAEHS IVLPVVVITE
LEGKRHDPEI GYFARQALRH LDELRIEHGR LDFPVPVGEG GTLRVELNNT DGSVLPSGIR
LGDNDSRILA VAMHLSQDGQ DVTIVSKDLP MRVKAASLGL IAEEYLAEQA VDSGWTGIAT
LDLSGDEISD LYESEVGLSE DARGFPVNTG LIIHSERGSA LGRMTGEGEY KLVRGDRDLF
GMHGRSAEQR IAIDLLTDPD VGIISLGGRA GTGKSALALC AGLEAVLERQ QQKKIIVFRP
LFAVGGQELG YLPGDQAEKM GPWGQAVFDT LGSVVSGNVV EEVMERGILE VLPLTHIRGR
SLHDAFVIVD EAQSLERNVL LTVLSRMGQN SRVVLTHDVG QRDNLRVGRY DGIASVIETL
KGHDLFGHVT LMRSERSAIA ALVTELLEGG ELS
//
