ID K9W2N0_9CYAN Unreviewed; 1014 AA.
AC K9W2N0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Exonuclease SbcC {ECO:0000313|EMBL:AFZ14481.1};
GN ORFNames=Cri9333_3668 {ECO:0000313|EMBL:AFZ14481.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ14481.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ14481.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ14481.1,
RC ECO:0000313|Proteomes:UP000010472};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003620; AFZ14481.1; -; Genomic_DNA.
DR RefSeq; WP_015204584.1; NC_019753.1.
DR AlphaFoldDB; K9W2N0; -.
DR STRING; 1173022.Cri9333_3668; -.
DR KEGG; cep:Cri9333_3668; -.
DR PATRIC; fig|1173022.3.peg.3946; -.
DR eggNOG; COG0419; Bacteria.
DR HOGENOM; CLU_004785_0_2_3; -.
DR OrthoDB; 9795626at2; -.
DR Proteomes; UP000010472; Chromosome.
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; PF04423; Rad50_zn_hook; 1.
DR Pfam; PF13558; SbcC_Walker_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
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:AFZ14481.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nuclease {ECO:0000313|EMBL:AFZ14481.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010472};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 447..558
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 164..415
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 450..488
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 522..563
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 778..829
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1014 AA; 117265 MW; 96446044F47A35FF CRC64;
MIPIQLTLKN FFSYREASLD FRGLHTACIC GANGAGKSSL LEAITWAIWG ESRAATEDDV
INAGALEVRV DFVFQYNQQT YRVIRTRQKG GSGSLEFQIE TSNNNFRSLT EKGVRATQQL
ITGHLKLDYD TFINSAYLRQ GRADEFMLRR PNERKQILAD LLKLDQYEVL AEQAKDSSRQ
FKAKAEQLDL SLQSIQTQLQ QKEAIALQQS EIETQLQQLQ QVQEIDRQQL QQLQSLQHQR
QTWQQQLTWQ RQQYQNLTQD CDRLQQDIAT NQRQQQQLES LIAQESQITT GYTEYLNLQA
TEEALAGKFQ AYQDAQQQKQ QLQQQLTEKI NEINLQIRQK QAKLEALSQQ EAEIQETLNK
SAEITTALEQ LQRSRTRLAQ LDKLQLNVSP LLQRRANLQT EINRAQARLT AKLEEINSSV
SQLYNQSVRQ PQLQSRVVQV DTQIEQLEKK RVYQQRVQEK GQERRNLQER LQENQHTYER
QIAELTQKLE MLKTPDASCP LCDRSLDEHH WNHVVEKTQT QQQEAQQQYW VIREQLAECE
RQREELRQEY RQLSQELAVY ESLREQRGEL AAQLQASSEV QVRLQQITVE KELLERSLTI
GNYAVDLQDE LQELDEYLQE LQYDEKTHAL ARGEAERWRW AEIKQAQLKD AVRRQGLLDA
QKPELLGKIA SLETALIELQ TNSELAQKLA DVQQGIAELN YERSHHNIIL ASLRQAQSWQ
FRYQELNQAK QQYPEVGDRI TLLNQSLQER LTNQQGINHQ IEAMVNQLAE MADPTGEIRS
LEQQIQQRRQ QLDSYIANLG RLQHQKSQIE TLQTQYELQQ EQLQEFKRQF RIYDELSKAF
GKNGIQALMI ENVLPQLEAE TNNILSRLSG NQLHVQFVTQ KAGKSTRSRS AKASVKNAKL
IDTLDILIAD ASGTRPYETY SGGEAFRINF AIRLALARML AQRSGTALQL LIVDEGFGTQ
DQEGCDRLIA AINAIASDFA CILTVTHMPQ FKEAFQTRIE VRKTNNGSQL SLLT
//
