ID   A0A928WG17_9CYAN        Unreviewed;      1008 AA.
AC   A0A928WG17;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   02-APR-2025, entry version 10.
DE   RecName: Full=Nuclease SbcCD subunit C {ECO:0000256|ARBA:ARBA00013368};
GN   ORFNames=IQ243_06670 {ECO:0000313|EMBL:MBE9050098.1};
OS   Nostocales cyanobacterium LEGE 11386.
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales.
OX   NCBI_TaxID=1828825 {ECO:0000313|EMBL:MBE9050098.1, ECO:0000313|Proteomes:UP000625354};
RN   [1] {ECO:0000313|EMBL:MBE9050098.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LEGE 11386 {ECO:0000313|EMBL:MBE9050098.1};
RA   Castelo-Branco R., Eusebio N., Adriana R., Vieira A.,
RA   Brugerolle De Fraissinette N., Rezende De Castro R., Schneider M.P.,
RA   Vasconcelos V., Leao P.N.;
RL   Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000256|ARBA:ARBA00011322}.
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009439}.
CC   -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006930}.
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:MBE9050098.1}.
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DR   EMBL; JADEXK010000012; MBE9050098.1; -; Genomic_DNA.
DR   Proteomes; UP000625354; 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; 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; PF04423; Rad50_zn_hook; 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|ARBA:ARBA00023054, 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|PROSITE-ProRule:PRU00471};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000625354};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00471}.
FT   DOMAIN          446..557
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000259|PROSITE:PS51131"
FT   COILED          163..266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          322..435
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          463..490
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          535..596
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          777..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;  116497 MW;  52D03F3F50EFB5B7 CRC64;
     MIPVQLILKN FLSYRDATLD FRGLHTACIC GSNGAGKSSL LEAITWAIWG ESRAGVEDDV
     IHSGAKEVRV DFVFQCNQQK YRVIRTRVRG ASGVLEFQIE TPSGFRAITG KGVRATQDLI
     LEHIKLDYDT FINSAYLRQG RADEFMLKRP TERKEILAEL LKLNQYDELE ERAKESARQF
     KARAEELERS LESSKTQLQQ REVTQAQRVE LETELDQLQQ VQAFENIQLQ SLQVVQHQRQ
     NWQQQLNFVR QQHQNLTQDS DRLQQEQLAV QSQLSDLKAI LNQETEIKNG YAQYQSLQSQ
     EEAFATKFQE YTRSTALRQQ KQQQLTSQIH ELERQLQQLQ GQLAALAQQE QEIQHTLSKS
     GEVEAALAQL TAARRRVTQL DELQMQVSPL LQQRQNLQSQ LDRVHAGLIA RLEQLQATEN
     QLQRSSRRQP QLQQAVMDVG MQIEQMEKDR VYLQRVQEKG QERRHFIERL QAQQREYERL
     LGELEQKLQM LRTPDAICPL CERPLDEHHW NRVVDKTKDE YKDTEGQLWV FREQMAVSDR
     EIQLLRQEYR EISQKLAPYD TLREQRGQLA AQLQSTSDAD QQLQQLATEK QHLERSLQAG
     DYAPDKQAEL RQLEQYLQQL NYNEQDHALA RSEVERWRWA EIKQGQIKDA AKRQAQIAAR
     KPELQATIAQ LQTRIQQEQT DSECAKQISE LERHIADIGY SSEQHNNLRV AVRQAQSWQL
     RYQQLLSAQQ QYPQLQQRWQ DLEASRSARL DERQKLAHQI ESITQELAQS ANPTEQINAL
     EQQIQARRRQ LDEKIANLGR LEQLMLQLEA LQIQYDQQQQ QLQSCKQEQR VYQELAQAFG
     KNGIQALMIE NVLPQLEAET NQLLSRLSAN QLHVQFITQK SGRSGKSKKK NAKLIDTLDI
     LIADSRGTRA YETYSGGEAF RINFAIRLAL AKLLAQRAGA ALQLLIIDEG FGTQDAEGCD
     RLIASINAIA GDFACILTVT HMPHLKEAFQ ARIEVNKTQQ GSQLSLSI
//