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Database: UniProt
Entry: A0A1Q7W7V4_9ACTN
LinkDB: A0A1Q7W7V4_9ACTN
Original site: A0A1Q7W7V4_9ACTN 
ID   A0A1Q7W7V4_9ACTN        Unreviewed;       444 AA.
AC   A0A1Q7W7V4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=ATP-binding protein {ECO:0000313|EMBL:OLE26831.1};
GN   ORFNames=AUG49_07175 {ECO:0000313|EMBL:OLE26831.1};
OS   Catenulispora sp. 13_1_20CM_3_70_7.
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=1805055 {ECO:0000313|EMBL:OLE26831.1, ECO:0000313|Proteomes:UP000186605};
RN   [1] {ECO:0000313|EMBL:OLE26831.1, ECO:0000313|Proteomes:UP000186605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLE26831.1}.
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DR   EMBL; MNJN01000108; OLE26831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7W7V4; -.
DR   Proteomes; UP000186605; 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   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; PINC 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:OLE26831.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000313|EMBL:OLE26831.1};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT   DOMAIN          16..143
FT                   /note="PIN"
FT                   /evidence="ECO:0000259|SMART:SM00670"
SQ   SEQUENCE   444 AA;  47994 MW;  DC96BABC0D03F754 CRC64;
     MAATPRRRAS TKARRRTHVL DTSVLLADPS ALTRFAEHEV VVPIVVVTEL EAKRHHPELG
     YFARNALRIL DELRIQHGRL DAPIPVGSTG GTLRVELNHT DPSGLPPGFR LGDNDSRILA
     VACNLQAEGF DVVLVSKDLP MRVKASAVGL AAEEYRAEIA LEATSGWTGM AELEIPATAV
     DDLFSSGLAD IAEAAEFPCH TGLVLLSERG KALGRVTADK KVRLVRGDRD IFGLHGRSAE
     QRVALDLLLD PDIGIVSLGG RAGTGKSALA LCAGLESVME RRLHRKVVVF RPLYAVGGQE
     LGYLPGTENE KMSPWGQAVF DTLSALTSQA VIDEVVDRGM LEVLPLTHIR GRSLHDSFVI
     VDEAQSLERN VLLTVLSRIG TGSRVVLTHD VAQRGNLRVG RYDGIVSVVE KLKGHPLFAH
     VTLTRSERSP IAALVTELLE ELAV
//
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