ID A0ZDB3_NODSP Unreviewed; 1008 AA.
AC A0ZDB3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Exonuclease SbcC {ECO:0000313|EMBL:AHJ29423.1};
GN ORFNames=NSP_30960 {ECO:0000313|EMBL:AHJ29423.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ29423.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ29423.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ29423.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
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; CP007203; AHJ29423.1; -; Genomic_DNA.
DR RefSeq; WP_006195518.1; NZ_CP007203.1.
DR AlphaFoldDB; A0ZDB3; -.
DR STRING; 313624.NSP_30960; -.
DR PATRIC; fig|313624.11.peg.3114; -.
DR eggNOG; COG0419; Bacteria.
DR HOGENOM; CLU_004785_0_2_3; -.
DR Proteomes; UP000019325; 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; 2.
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:AHJ29423.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nuclease {ECO:0000313|EMBL:AHJ29423.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 315..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 380..490
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 798..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; 116625 MW; 227BD6CC2C3ADE80 CRC64;
MIPVQLILKN FLSYRDATLD FRGLHTACIC GSNGAGKSSL LEAITWAIWG QSRAGVEDDV
IHSGAKEVRV DYVFQCNQQK YRVIRTRVRG ASGVLEFQIE TASGFRALTG KGVRATQDLI
LQHIKLDYDT FINSAYLRQG RADEFMIKRP SERKEILAEL LKLNQYDQLE ERAKETYRQF
KARAEELERS LESSQIQLQQ QEATQAQKTE LETELNQLQQ VQAFENIQLQ SLQVVQHQRQ
NWEQQLHFVK QQHQNLTQDG DRLQQEQSAV QTQLSDLEAI LNQEAEINTG FTQYQTLQAQ
EEAFATKFQA YTRATALLQQ KQQELTNQIH ALERELQQVE GQLVALEQQE PEIQHTLNKS
AEVEAALTQL TAARRRVTEL DELQMQVSPL LQQRQNLQSQ LDRVHAGLVA RLEQLQATEN
QLQRSSQRQP QLQQAAKDLE IQISQMEKDK VYLQRVQEKG QERRHFMERL QAQQREYERL
LAELEQKLEM LRTPDAMCPL CERPLDEHHW NRVVDKTKDE YQDTEGQLWV FREQKAVSDR
EIQVLRQEYR EILQKVSPYD TLREQRGQLA AQLQSTSDAD QQLQELAAEK QHLERSLQAG
DYAPDKQAEL QQLAEYLQQL NYNEQDHALA RSEVERWRWA EIKQGQIKDA AKRQAQIVAR
KPELQASISQ LQTRIQQDKI DSDCAKEIAQ LERQISEIAY SSEEHHNLRV AVRQAQSWQL
RYQQLLSAQQ QYPQLQQRWQ DLEVSRRERL EERQKLLTQI ESISQELVKS ANPTQEITVL
EQQIQTRRRQ LDDKIANLGR LEQLMLQLET LQNQYEQQQQ QLQSCQQEQR VYQELAQAFG
KNGIQALMIE NVLPQLEAET NQLLSRLSAN QLHVQFITQK SGRSSKAKKK DAKLIDTLDI
LIADSRGTRA YETYSGGEAF RINFAIRLAL AKLLAQRAGA ALQLLIIDEG FGTQDAEGCD
RLIASINAIA CDFACILTVT HMPHLKEAFQ ARIEVNKTQQ GSQVSLSI
//
