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Database: UniProt
Entry: A0A0S9Q936_9ACTN
LinkDB: A0A0S9Q936_9ACTN
Original site: A0A0S9Q936_9ACTN 
ID   A0A0S9Q936_9ACTN        Unreviewed;       459 AA.
AC   A0A0S9Q936;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KQP66436.1};
GN   ORFNames=ASF47_01120 {ECO:0000313|EMBL:KQP66436.1};
OS   Nocardioides sp. Leaf285.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP66436.1, ECO:0000313|Proteomes:UP000051495};
RN   [1] {ECO:0000313|EMBL:KQP66436.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP66436.1,
RC   ECO:0000313|Proteomes:UP000051495};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP66436.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP66436.1,
RC   ECO:0000313|Proteomes:UP000051495};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQP66436.1}.
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DR   EMBL; LMNH01000001; KQP66436.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S9Q936; -.
DR   Proteomes; UP000051495; 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:KQP66436.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000313|EMBL:KQP66436.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051495};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT   DOMAIN          31..158
FT                   /note="PIN"
FT                   /evidence="ECO:0000259|SMART:SM00670"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   459 AA;  49459 MW;  DD95D18463AE624F CRC64;
     MPSQAQQSQQ SPGSTRTRRK APARAAAPAV RTYVLDTSVL LADPGALKRF AEHEVVLPVV
     VITELEGKRH HPELGYFART ALRTLDELRI LHGRLDEPVP VGEEGGTLRV ELNHTDASSL
     PSGFRLGDND TRILAVAHNL STEGLAVTLV SKDLPLRIKA SAVGLDAQEY RAEAISDSDT
     GYSGMAELEV AASDLDELYD DGVVDLDAAR DLPCHQGLVL LSDRGSALGR VGPDKQVHLV
     RGDREAFGVH GRSAEQRIAL EMLLDPEVGI VSLGGRAGTG KSAMALCAGL EAVLERGQHK
     KVVVFRPLFA VGGQELGYLP GSESEKMSPW GQAVFDTLGA MTSRDVIDEI LDRGMLEVLP
     LTHIRGRSLH DAFVIVDEAQ SLERNVLLTV LSRIGANSKV VLTHDVAQRD NLRVGRHDGV
     VAVIEKLKGH PLFAHVTLTR SERSPIAALV TEMLENVTL
//
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