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Database: UniProt
Entry: A0A1F8M828_9CHLR
LinkDB: A0A1F8M828_9CHLR
Original site: A0A1F8M828_9CHLR 
ID   A0A1F8M828_9CHLR        Unreviewed;       853 AA.
AC   A0A1F8M828;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Zinc-hook domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2Z71_06045 {ECO:0000313|EMBL:OGN94779.1};
OS   Chloroflexi bacterium RBG_13_50_21.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797623 {ECO:0000313|EMBL:OGN94779.1, ECO:0000313|Proteomes:UP000177581};
RN   [1] {ECO:0000313|EMBL:OGN94779.1, ECO:0000313|Proteomes:UP000177581}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(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:OGN94779.1}.
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DR   EMBL; MGMQ01000100; OGN94779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8M828; -.
DR   STRING; 1797623.A2Z71_06045; -.
DR   Proteomes; UP000177581; 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-KW.
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; PF04423; Rad50_zn_hook; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF75712; Rad50 coiled-coil 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          5..256
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   DOMAIN          403..447
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000259|Pfam:PF04423"
FT   COILED          210..275
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          324..420
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          575..609
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          658..688
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   853 AA;  96903 MW;  A61A69B326C6F03A CRC64;
     MIPIKLTITG FLSYRETTVL DFTQFDLACI SGPNGAGKSS LLDAFTWVLF GQARKRDETL
     INLHSNAAEV ALVFEYESNI YRVQRSLAKG KTTVLEFQIR EPSDEKWKPL TGATLRNTQE
     LIEHTLRLDY ETFVNASFFL QGKADQFTQQ KPTDRKRILG SILGLEVWET YRQRVNDRRK
     GIDAEIFNLD GRTAEIKAEL SEEEARTERL ATLQADLKHL SKARKAQEQL LEQARKVDAT
     LAEQRKLINM LGEQLEAAQN RLAELDGRLA ARKQERDEFA HRVANATEIE VAYADWIARR
     AELERWDEVA ARFREHEARR MQPRMEIEAE KARLLQELDQ LQQMEKLVQA QNLSRVELEA
     QAESTRAALE QAEQAISHKV SLDVELQAAR QRQAESKAEN PRLKAEMDQL KARIDQLSQT
     EGAACPLCGR SLETHDRLQL IDEIAAQGRE MGDRYRTNLA YLKEADQKVA EIESRIALLS
     KVDAERLIFT QNMARLNGQI EAIQQKSEDW DRVGVPRMAE VQVILETETY APEQRKKLAE
     IDIELKAIGY DAVAHDTCRN QENAARSADA EFRALETARA ALQPLEREIA EAQVQLETTR
     QEVSNLQKHY DDSSVHLAAA EADAPDLDVA ERIYHELLEQ ENSQRLEVGA AQQKVAVLKD
     LKVRLKDLSA HRESLARLVG QYRQLERAFG KDGVPALLIE QALPEIEMRA NNLLDRLSEG
     NMSVRFATQA QFKDKKREDL KETLDILISD GAGTRDYELY SGGEAFRVNF AIRLALSELL
     AIRAGARLQT LVIDEGFGSQ DAMGRQHLIE AINMVKQDFA KVLVITHIDE LKEAFPNRIE
     VEKSDRGSLV RVV
//
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