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Database: UniProt
Entry: A0A1J5G2Q6_9BACT
LinkDB: A0A1J5G2Q6_9BACT
Original site: A0A1J5G2Q6_9BACT 
ID   A0A1J5G2Q6_9BACT        Unreviewed;       862 AA.
AC   A0A1J5G2Q6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Zinc-hook domain-containing protein {ECO:0000259|PROSITE:PS51131};
GN   ORFNames=AUK42_07545 {ECO:0000313|EMBL:OIP66869.1};
OS   Candidatus Atribacteria bacterium CG2_30_33_13.
OC   Bacteria; Atribacterota.
OX   NCBI_TaxID=1805029 {ECO:0000313|EMBL:OIP66869.1, ECO:0000313|Proteomes:UP000182763};
RN   [1] {ECO:0000313|EMBL:OIP66869.1, ECO:0000313|Proteomes:UP000182763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_33_13 {ECO:0000313|EMBL:OIP66869.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009439}.
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:OIP66869.1}.
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DR   EMBL; MNYY01000148; OIP66869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5G2Q6; -.
DR   STRING; 1805029.AUK42_07545; -.
DR   Proteomes; UP000182763; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   Gene3D; 1.10.287.510; Helix hairpin bin; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   InterPro; IPR013134; Zn_hook_RAD50.
DR   PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR   PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR   Pfam; PF13476; AAA_23; 1.
DR   Pfam; PF13558; SbcC_Walker_B; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR   PROSITE; PS51131; ZN_HOOK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00471}.
FT   DOMAIN          389..487
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000259|PROSITE:PS51131"
FT   COILED          213..271
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          375..475
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          577..625
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          660..694
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT   BINDING         438
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ   SEQUENCE   862 AA;  101560 MW;  34314DC4BBD7D411 CRC64;
     MIPVKLALKN FLSYGENVPP LDFTQFHLAC LSGNNGQGKS ALLDALTWAV WGEGRKSSQE
     KKADHSLLRI GQKDMQVEFI FDLEGDRYRI IRNYSMLQKS SRSSLEFQIY NPKDDKYISL
     TASSIRKTQE RITKTLRIDY RTFINSAFIL QGRIDEFSRK NARERKEILS EILSLSHYDE
     LANLAKSHLK EINNIMMTKE SRLEYIYQEM TNIDAYKQKI KELSDSYEDI SQKVKKNEDQ
     LNQLKEDINL LKHKKEQFEE LKDRTEQQRQ EIGRGQKQIE LKNKEIADSK KIISQKEIIL
     SNFINYQKFN TENNELTLKL QKIRKIEEER ILTERKIESG KTDLTVEIRN KRDRFRDLQL
     KAERELKSKT EVLEAEKKMR EIKFFEEESE EIRKKGSEFN IAINTIKGQL ERLEKDHRDN
     EEKLRLLREN PEGECPLCEA KLNAERKKKI ETNLSREINL NLKEIERLKK EEERLGKPRE
     ELVKKWREIN QKLKDKDRWQ QKLSKAGLEY DESKQAAKLM VGLQGEIKEI EKIIIEKKYA
     LEEQISLKAF EVQIKNIGYE EEKHRQLNGK IEELGNAPLE KAKLEEAEKK IDSLRDLLSE
     LKENYQQKEL NWKDLEKKKE KIKIELKDLP WWKEKLIQEE QFLKQNQILK DKILEERGGY
     QSKFEQCLKL EKEKKEIKKE LEESKREQNI YEKLMLALGK NGIQALIIEN VLPEIEEEAN
     NLLAKLTNNS TQITIESLRD LKSGKIKETL DLKISDELGI RDYELYSGGE SFRIDFSLRI
     ALSKLLTRRA GTKLRTLVMD EGFGTQDEEG LDNLVQAIQS ISDDFDKILV ITHLESLKDA
     FPVRIEVTKH PETGSRYEII KN
//
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