ID A0A0A0BR85_9CELL Unreviewed; 440 AA.
AC A0A0A0BR85;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KGM10983.1};
GN ORFNames=N869_04055 {ECO:0000313|EMBL:KGM10983.1};
OS Cellulomonas bogoriensis 69B4 = DSM 16987.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM10983.1, ECO:0000313|Proteomes:UP000054314};
RN [1] {ECO:0000313|EMBL:KGM10983.1, ECO:0000313|Proteomes:UP000054314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69B4 {ECO:0000313|EMBL:KGM10983.1,
RC ECO:0000313|Proteomes:UP000054314};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL Submitted (AUG-2013) 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:KGM10983.1}.
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DR EMBL; AXCZ01000127; KGM10983.1; -; Genomic_DNA.
DR RefSeq; WP_035061489.1; NZ_AXCZ01000127.1.
DR AlphaFoldDB; A0A0A0BR85; -.
DR OrthoDB; 9766527at2; -.
DR Proteomes; UP000054314; 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:KGM10983.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000313|EMBL:KGM10983.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054314};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 7..134
FT /note="PIN"
FT /evidence="ECO:0000259|SMART:SM00670"
SQ SEQUENCE 440 AA; 47910 MW; 21FE562E5C8AE4B6 CRC64;
MATSGTRTYV LDTSVLLSDP RAVHRFDEHD VVLPVVVITE LEAKRHHAEL GYFARSALRL
LDDLRLLHGR LDHPVPVGDQ GGTLRVELNH VDPTVLPTGF RLGDNDTRIL TVARSLADEG
ADVTLVSKDL PLRIKAAAVG LDAAEYRAEL AVDSGWTGTT TLQVSEQHMA QLWESDRLDL
TELDLTGQEP GPLICHTGVV LHSPRGSALA RVTADKHLRL IRGDQEVFGV HGRSAEQRIA
IDLLLDEEVG IVSMGGRAGT GKSALALCAG LEAVLERRRH RKVLVFRPLY AVGGQELGYL
PGTEAEKMNP WAQAVFDTLG ALVPGDVMDE VVARDLLEVL PLTHIRGRSL HDAFVIVDEA
QSLERNVLLT VLSRIGQGSR VVLTHDVAQR DNLRVGRHDG VAAVIETLKG HPLFAHVTLT
RSERSPVAAL VTDLLERAEI
//
