ID U5DJS3_9CHRO Unreviewed; 1008 AA.
AC U5DJS3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Nuclease SbcCD subunit C {ECO:0000256|RuleBase:RU363070};
GN Name=sbcC {ECO:0000256|RuleBase:RU363070};
GN ORFNames=KR51_00024110 {ECO:0000313|EMBL:ERN41147.1};
OS Rubidibacter lacunae KORDI 51-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rubidibacter.
OX NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN41147.1, ECO:0000313|Proteomes:UP000016960};
RN [1] {ECO:0000313|EMBL:ERN41147.1, ECO:0000313|Proteomes:UP000016960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN41147.1,
RC ECO:0000313|Proteomes:UP000016960};
RA Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: SbcCD cleaves DNA hairpin structures. These structures can
CC inhibit DNA replication and are intermediates in certain DNA
CC recombination reactions. The complex acts as a 3'->5' double strand
CC exonuclease that can open hairpins. It also has a 5' single-strand
CC endonuclease activity. {ECO:0000256|RuleBase:RU363070}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000256|RuleBase:RU363070}.
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|RuleBase:RU363070}.
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:ERN41147.1}.
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DR EMBL; ASSJ01000055; ERN41147.1; -; Genomic_DNA.
DR RefSeq; WP_022607609.1; NZ_ASSJ01000055.1.
DR AlphaFoldDB; U5DJS3; -.
DR STRING; 582515.KR51_00024110; -.
DR PATRIC; fig|582515.4.peg.2720; -.
DR eggNOG; COG0419; Bacteria.
DR InParanoid; U5DJS3; -.
DR OrthoDB; 9795626at2; -.
DR Proteomes; UP000016960; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; 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; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|RuleBase:RU363070};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA recombination {ECO:0000256|RuleBase:RU363070};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|RuleBase:RU363070};
KW Endonuclease {ECO:0000256|RuleBase:RU363070};
KW Exonuclease {ECO:0000256|RuleBase:RU363070, ECO:0000313|EMBL:ERN41147.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363070};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|RuleBase:RU363070};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016960}.
FT DOMAIN 6..202
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT DOMAIN 483..522
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|Pfam:PF04423"
FT REGION 651..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..236
FT /evidence="ECO:0000256|RuleBase:RU363070"
FT COILED 457..495
FT /evidence="ECO:0000256|RuleBase:RU363070"
FT COILED 726..774
FT /evidence="ECO:0000256|RuleBase:RU363070"
FT COILED 802..836
FT /evidence="ECO:0000256|RuleBase:RU363070"
FT COMPBIAS 651..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 115157 MW; ED285942FD934037 CRC64;
MIPVHLKLKN FLSYREASLD FRGLHTACIC GPNGSGKSSL LEAITWALWG QSRAAADDDI
INAAAEEVRV DFVFVRDRNT YRAIRSKRRG HTATLDLQVQ TAPDRFRTLS GRGIRPTQQR
IDAAIGIDYD TFVNSAYLRQ GRADEFMLRR PSERKQVLAD LLKLDRYEAL AERAKDFTRQ
LKAQVEQLER QANDLSAQLQ DRQTIDRESV LNAEQLQELQ VAQERDRCQL QMLQAREHQR
LALEQRVSWH QQQLTIAERD CQRLGRDRAA TQQELARLQQ LLTREGDVTA GYRRCLELQR
EEAALSQRFQ AYQGAEQQLL HLQRQQSDRL NKLQLQAQAV ATQLTALEAR ECEVRDVLAR
SPDVATALAD LHAARSHLEC LEALHQQAVP LLQRRQHVQA DIDRSRARLV ARLEQLHATS
AQLSTRVAQA PKMRSQAIVV ETELKELETK QLYRQRVQEK GQERRNFQER LQESQRNYQK
LLAELERKLE LLEQQGAVCP LCDRPLDALH KQHVVAKTQA QRQEAQDRFW VLREQLATCE
RELQVLRGEY KKLSQDLAPF DELLQQRGQL AVRLETTTDV CERLKELTAE RAGVEQSLSV
GSFAPELHTE LAAIDAELAE LDYSEEARVL ARSDVERQRR AEFEQAKIED ARRQQARIDR
EKPPLQQESR DLQKAVKQLA TDSDLAREIA TCQQQLVRLD YDRDRHNNAI AALRESQPWL
LRHQQLQQAR QQFPLVQDRL EQLTTNLQTR VGETEQLRAE LAAATEQLAA AADDRAAIAS
AECRVRDRRQ HLDELLARQG RLDQALAHLD TVSIQHERAQ RELSVARRQN RVYRELAQAF
GKNGIQACAI ETLLPQLEAQ TNHILARLTG NQLHVQFLTQ KASKGRSKKQ PAKTIETLEI
RIADARGTRP YETYSGGEGF RINFAIRLAL AKLLAQQSGT TLQMLIVDEG FGTQDAEGCD
RLIAAIDAIA PDFACILAVT HMPQFKEAFQ NRIEVRKTDS GSQLGIFG
//
