ID A0A0R2PSW4_9MICO Unreviewed; 449 AA.
AC A0A0R2PSW4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:KRO40091.1};
GN ORFNames=ABR66_00900 {ECO:0000313|EMBL:KRO40091.1};
OS Microbacteriaceae bacterium BACL25 MAG-120322-bin65.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae.
OX NCBI_TaxID=1655574 {ECO:0000313|EMBL:KRO40091.1, ECO:0000313|Proteomes:UP000053725};
RN [1] {ECO:0000313|EMBL:KRO40091.1, ECO:0000313|Proteomes:UP000053725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL25 MAG-120322-bin65 {ECO:0000313|EMBL:KRO40091.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRO40091.1}.
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DR EMBL; LIAY01000001; KRO40091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2PSW4; -.
DR Proteomes; UP000053725; 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:KRO40091.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000313|EMBL:KRO40091.1};
KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT DOMAIN 22..148
FT /note="PIN"
FT /evidence="ECO:0000259|SMART:SM00670"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 48715 MW; 22E534DDCA03D0B9 CRC64;
MEKSASTATS RSSSRRKETK ERTYVLDTSV LLSDPRALFR FAEHHVVLPV VVISELEKKR
HDPEIGFFAR QALRHLDDLR SEHERLDFPI AVGEGGTLRV ELNHSNQAIL PSGLQLGDND
ARILAVALNL ANDGLAVTVV SKDLPMRVKA ASIGLAAEEY RAELAPESGW TGMAEIAMSA
QDMATLYDAE VISSDAVADM PVNTSLVISS ERGSALGRVS APGKIAVVRG DRELFGLNGR
SAEQRLAIDL LLDPTIGIIS LGGRAGTGKS ALALCAGLEA VLEKQQHRKI MVFRPLYAVG
GQDLGYLPGD AKEKMNPWAE ATFDTLSSVV SHHVVEEVMD RGLLEVLPLT HIRGRSLHDA
FVIVDEAQSL ERNVLLTMLS RIGQNSRVVL THDIAQRDNL RVGRHDGVFS VIEALKGQPL
FGHITLMRSE RSAIAALVTD LLEEGYPAA
//
