ID F4XIS1_9CYAN Unreviewed; 1006 AA.
AC F4XIS1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Nuclease SbcCD subunit C {ECO:0000256|RuleBase:RU363070};
GN Name=sbcC {ECO:0000256|RuleBase:RU363070};
GN ORFNames=LYNGBM3L_03380 {ECO:0000313|EMBL:EGJ35583.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ35583.1, ECO:0000313|Proteomes:UP000003959};
RN [1] {ECO:0000313|Proteomes:UP000003959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA Gerwick W.H., Gerwick L.;
RT "Genomic insights into the physiology and ecology of the marine filamentous
RT cyanobacterium Lyngbya majuscula.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
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}.
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DR EMBL; GL890819; EGJ35583.1; -; Genomic_DNA.
DR RefSeq; WP_008178050.1; NZ_MKZR01000001.1.
DR AlphaFoldDB; F4XIS1; -.
DR eggNOG; COG0419; Bacteria.
DR HOGENOM; CLU_004785_0_2_3; -.
DR OrthoDB; 9795626at2; -.
DR Proteomes; UP000003959; 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; 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|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:EGJ35583.1};
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}.
FT DOMAIN 5..207
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT DOMAIN 482..526
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|Pfam:PF04423"
FT COILED 163..235
FT /evidence="ECO:0000256|RuleBase:RU363070"
FT COILED 297..494
FT /evidence="ECO:0000256|RuleBase:RU363070"
FT COILED 777..835
FT /evidence="ECO:0000256|RuleBase:RU363070"
SQ SEQUENCE 1006 AA; 115743 MW; 316E1A7E9319AB95 CRC64;
MIPIQLTLKN FLSYRDATLD FRGLHTACIC GQNGAGKSSL LEAITWAIWG QSRVASENDI
IHTGAKEVRV DFIFQNNQQT HRIIRTRHRK QGTSLEFQVE TPNGFKSLTQ KGVRATQLLI
IANLKLDYDT FINSSYLRQG RADEFMVRRP SERKQILADL LKLDQYEKLA DQAKDLSKQL
KGQVEQLEQS LQGIKEQLGE RDAIAQETAT LETALHQLQQ DQDQDAQQLK KLQAIGHQRN
SWEQQLNFVR TQYLNLTQDC DRIQQDIATA VAQQQQLSEL LSQDQQITAG YAEYLQLQEL
EESLAAKLQT YQKAQQQRQQ LQQQLDQQIN QLNLQIRDIQ AQLEALGTQE QEIQDTLSRS
GQVATALAQL KQVRERLKQL DNLQLEVSPL LQRRGSIQSE LDRVQARLSA KLEELVSSEK
QLSQQVATTP QLRQAALQLE AELGELEKKR VYLSRLQDKG LERRGFRERL HENQRRYEKL
LGELTQKIQL LQVQNAVCPL CEQPLDAAHS DRVIQKTTAE HKDVQDQFWV VREQLTVCER
ELQVLRHEYS QISKQLSPYE ELLEQRGQLA AQLEATDEVY DRLYEVSEEK KELQQSLSIP
GYGVELHEEL RQLDLRIQQL NYDEQTHALA RGEVDRWRWA EIHSAKLEEA RRRQKKIDAQ
KPQLLRKLDT LQASVHQLQT NSPLKQQLDQ LDRYIAEIGY NLDAHNQVRA SLRQAQSWQL
PYQELQTAQE QQPQVGQRLA SLTQTLQSRR SNLKEVNTQI EDIVKQMEQS PDVTRDLQAL
EQGMKQRRQQ MDKQLSQQGR LQQRLQQLES LQSQYQQQLE KLQQLQRQYR VYQELAIAFG
KNGIQALMIE NILPQLEAQS NQILARLTGN QLHIQIVTQK AGSRSSKKKT KLIDTLDILI
ADATGTRPYE TYSGGEAFRI NFAIRLALAQ LLAQRSGTSL QMLIVDEGFG TQDAEGCERL
IAAINAIASD FACILTVTHM PQFKEAFQTR IEVSKTSLGS QLSLTM
//
