ID A0A0Q7UC81_9MICO Unreviewed; 457 AA.
AC A0A0Q7UC81;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KQZ05013.1};
GN ORFNames=ASD19_03145 {ECO:0000313|EMBL:KQZ05013.1};
OS Microbacterium sp. Root53.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736553 {ECO:0000313|EMBL:KQZ05013.1, ECO:0000313|Proteomes:UP000051407};
RN [1] {ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|Proteomes:UP000051407};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ05013.1, ECO:0000313|Proteomes:UP000051407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root53 {ECO:0000313|EMBL:KQZ05013.1,
RC ECO:0000313|Proteomes:UP000051407};
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:KQZ05013.1}.
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DR EMBL; LMFR01000012; KQZ05013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7UC81; -.
DR STRING; 1736553.ASD19_03145; -.
DR Proteomes; UP000051407; 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:KQZ05013.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000313|EMBL:KQZ05013.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051407};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 31..157
FT /note="PIN"
FT /evidence="ECO:0000259|SMART:SM00670"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 49248 MW; F1E0F6897529F227 CRC64;
MTISTTQQAS RRGSTAREAA PDDASSEQAL RAYVLDTSVL LSDPRAFFRF AEHSVVIPVV
VIGELEGKRH DPELGYFARQ ALRHLDELRI EHGRLDFPVP VGEGGTLRVE LNNTDATVLP
SGIRLADNDS RILAVAMHLA QDGNDVTVIS KDLPMRVKAA SLGLSAEEYL AEQAVDSGWT
GIASLDLSGD EMADLYETEV ASHDDVRGIP VNTGLVIHSE RGSALGRVTG EGELRLVRGD
RDVFGLHGRS AEQRIAIDLL LDPEVGIVSL GGRAGTGKSA LALCAGLEAV LERQQQKKII
VFRPLFAVGG QELGYLPGDQ AEKMNPWGQA VFDTLGSVVS NNVLEEVIQR GLLEVLPLTH
IRGRSLHDAF VIVDEAQSLE RNVLLTVLSR IGQNSRVVLT HDVAQRDNLR VGRHDGIASV
IETLKGHGLF GHVTLTRSER SAIAALVTDL LEAGELA
//
