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Database: UniProt
Entry: F2F9R3_SOLSS
LinkDB: F2F9R3_SOLSS
Original site: F2F9R3_SOLSS 
ID   F2F9R3_SOLSS            Unreviewed;      1017 AA.
AC   F2F9R3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Nuclease SbcCD subunit C {ECO:0000256|ARBA:ARBA00013368};
GN   OrderedLocusNames=SSIL_0610 {ECO:0000313|EMBL:BAK15033.1};
OS   Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX   NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK15033.1, ECO:0000313|Proteomes:UP000006691};
RN   [1] {ECO:0000313|Proteomes:UP000006691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA   Morohoshi T., Someya N., Ikeda T.;
RT   "Genome sequence of Solibacillus silvestris StLB046.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAK15033.1, ECO:0000313|Proteomes:UP000006691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB046 {ECO:0000313|EMBL:BAK15033.1,
RC   ECO:0000313|Proteomes:UP000006691};
RX   PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA   Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT   "Complete genome sequence and characterization of the N-acylhomoserine
RT   lactone-degrading gene of the potato leaf-associated Solibacillus
RT   silvestris.";
RL   J. Biosci. Bioeng. 113:20-25(2012).
CC   -!- SUBUNIT: Heterodimer of SbcC and SbcD. {ECO:0000256|ARBA:ARBA00011322}.
CC   -!- SIMILARITY: Belongs to the SMC family. SbcC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006930}.
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DR   EMBL; AP012157; BAK15033.1; -; Genomic_DNA.
DR   RefSeq; WP_014822687.1; NC_018065.1.
DR   AlphaFoldDB; F2F9R3; -.
DR   STRING; 1002809.SSIL_0610; -.
DR   KEGG; siv:SSIL_0610; -.
DR   PATRIC; fig|1002809.3.peg.616; -.
DR   eggNOG; COG0419; Bacteria.
DR   HOGENOM; CLU_004785_2_1_9; -.
DR   Proteomes; UP000006691; Chromosome.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
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   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; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022839};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006691}.
FT   DOMAIN          5..213
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   COILED          291..358
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          389..437
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          468..502
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          556..610
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          750..837
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1017 AA;  116412 MW;  B82FCCF9BF9B0F9A CRC64;
     MKPIKLSMTA FGPYHQKEVI DFTKLHEHGI FVVSGATGAG KTTIFDAITF ALYDSGSGED
     REKSLFLRSD FADEAVDTEV ELEFEVRGRL YRIWRKFGHD GASAKREFFE ITDGVTVPAV
     EKFQVKLIQS KIEELIGLTQ SQFNQIVMLP QGEFQKLLTS ESKHKEEIFR KIFKTERFTK
     MVELLKEKKN IAEKHYEQAR MQQDNTIHDI RSRLPHRESE LFTALNNDVI NLYQVKTALE
     TEQQFYEEQC AALKGQYAAS KAHLQTLVKS LNEQRLLNER IEKFLIRKAR LDELLQQKDK
     IQAEQQKLVL AKKANQIEPL EREYEKVKRQ LEQAEVSLQK AKADYERAQV QLLQATNHYQ
     EQKQHEPLLD EFTKSISQLE QLVPIYQSIN TQREKVAKLA ENQKNAKQLF DKLQKEAASL
     KEKHQQQQAI INELEDATVT YHETYEAHAV LTRKIEMAKE VAAIQMNIET LVRQLADKKQ
     IADGAQQKLQ NMEQQIRSNQ AAFLAAQLHH GEACPVCGST EHPAIHNSEA FTIDENALEH
     LRQEGDRAMQ SFYQVNSKLD VEKAALEQKR NALELLNVDL SQLHYYEQQL AELTEQLTKQ
     KQQQAQLITE KKTMAQLIES KEVLQGRIEK GQQYVVDIDK QYAQEKGKLE QSEQSLLPQF
     STLDEVTQEL ASQQQKHRHL KSAIQSALEA MQKIQLDGKS CEVNHLHAQN LVTEKQQETL
     SAQKAFDTAL QQESFDLETY KNALLPLNVQ QQIQDEVEAY KQNVHTLSVQ ISEEEPLLEG
     KERADLTASE QQIHELNEQI EAQYSKITLT QSYVEQCEET LEKLDQSAQQ IESYKAKLIQ
     VEHVYNLIRG QNDSKISFER FVQIGYLEKV THAANERLRV LSNGQYFLKS TGRKEGNAQS
     GLSIDVYDSH TGQTRDVKTL SGGEKFNASL SLALGMADVI QSVQGSVHID TMFIDEGFGT
     LDEEALRRAI DILIDLQQTG RLIGVISHVA ELKAAMPAIL QVQKLKEGYS KTEIIIK
//
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