ID   A0A0C2Q6X0_9CYAN        Unreviewed;      1008 AA.
AC   A0A0C2Q6X0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Exonuclease SbcC {ECO:0000313|EMBL:KIJ79549.1};
GN   ORFNames=SD81_01080 {ECO:0000313|EMBL:KIJ79549.1};
OS   Tolypothrix campylonemoides VB511288.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ79549.1};
RN   [1] {ECO:0000313|EMBL:KIJ79549.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB511288 {ECO:0000313|EMBL:KIJ79549.1};
RA   Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT   "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT   VB511288.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KIJ79549.1}.
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DR   EMBL; JXCB01000002; KIJ79549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2Q6X0; -.
DR   OrthoDB; 9795626at2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
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; IPR004592; SbcC_gammaproteobac_type.
DR   InterPro; IPR013134; Zn_hook_RAD50.
DR   NCBIfam; TIGR00618; sbcc; 1.
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   Exonuclease {ECO:0000313|EMBL:KIJ79549.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00471}; Nuclease {ECO:0000313|EMBL:KIJ79549.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00471}.
FT   DOMAIN          446..557
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000259|PROSITE:PS51131"
FT   COILED          159..204
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          232..487
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          535..562
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          784..835
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         498
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT   BINDING         501
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ   SEQUENCE   1008 AA;  116443 MW;  EB2062C7D31F0F6E CRC64;
     MIPIQLTLKN FLSYRDATLD FRGLHTACIC GSNGAGKSSL LEAITWAIWG ESRASSEDDV
     IQTGAKEVRV DFIFEANQQT YRVIRTRVRG GSGALEFQIQ IPTGFRALTG KGVRATQDLI
     LEHIKLDYET FINSAYLRQG RADEFMLKRP SERKEILAEL LKLNQYDQLE ERAKELSRQF
     KARTEELERV LDSLKSQLQQ GEAIAQKQGD LEAEINQLQQ VQAFENIQLQ SLQVVQHQRQ
     NWEQQLNFVR QQYQNLTQDC DRLQQEQSAI DSQFSSLEEL LNQAAEIEAG YNEYQVLQSQ
     EEAMGAQFEE YTHAQQARQQ KQQQLTKQIN EIERQLQHAE AQLAAVQQQE QELQQTLTKS
     DEVEAALAQL AAARNRVTQM DQLQLQVAPL LQQRATLQSQ LDRAHAGLVA RLEQLEATAN
     QLQRQHRRQP QLQQAVMEVA IQIEELEKKR VYLQRVQEKG QERRHLIERL QAHQRDFEKL
     LGELQQKLQM LQNPNAICPL CERPLEEHYW NRVVDKTKIE YKDAQDELWI VRERMAVSDR
     EIQVLRQEYR EISQELSHYD ALREQRGQLA AQLQATSDVE QQLQEIVAEK HQLERWLQMG
     NYAHETQAEL QELQQYLQQL NYNEQDHALA RNEVERWRWS EIRLSQIKDA AKRQAQIEAR
     KPEIQAQIAQ LQTRIQQEAT QSECARQIAA LERHIAEIGY VSEEHNNLRM AVRKAQSWQL
     RYQQLVGAQQ QYPQLKTRLQ ELEVSLQARL TERQRLAIQI ESIVQQLEES ANPSAQIPAL
     EQQLASRRRQ LDEQIAQLGR LQQQAHQLET LQLQYEQQQQ QLQEARRQHR IYQELSQAFG
     KNGIQALMIE NVLPQLEIET NQLLSRLSAN QLHVQFVTQR AGKSSKASKK NAKLIDTLDI
     LIADARGTRA YETYSGGEAF RINFAIRLAL AKLLAQRAGA ALQLLIVDEG FGTQDAEGCD
     RLIAAINAIA SDFACILTVT HMPHLKEAFQ ARIEVSKTQS GSQVRLLI
//