ID A0A0B5HK88_ARCG5 Unreviewed; 687 AA.
AC A0A0B5HK88;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Exonuclease SbcC {ECO:0000313|EMBL:AJF60666.1};
GN ORFNames=QT03_C0001G1185 {ECO:0000313|EMBL:AJF60666.1};
OS Archaeon GW2011_AR10.
OC Archaea.
OX NCBI_TaxID=1579370 {ECO:0000313|EMBL:AJF60666.1, ECO:0000313|Proteomes:UP000031777};
RN [1] {ECO:0000313|Proteomes:UP000031777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25702576; DOI=10.1016/j.cub.2015.01.014;
RA Castelle C.J., Wrighton K.C., Thomas B.C., Hug L.A., Brown C.T.,
RA Wilkins M.J., Frischkorn K.R., Tringe S.G., Singh A., Markillie L.M.,
RA Taylor R.C., Williams K.H., Banfield J.F.;
RT "Genomic expansion of domain archaea highlights roles for organisms from
RT new phyla in anaerobic carbon cycling.";
RL Curr. Biol. 25:690-701(2015).
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DR EMBL; CP010424; AJF60666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5HK88; -.
DR STRING; 1579370.QT03_C0001G1185; -.
DR KEGG; agw:QT03_C0001G1185; -.
DR HOGENOM; CLU_400443_0_0_2; -.
DR Proteomes; UP000031777; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Exonuclease {ECO:0000313|EMBL:AJF60666.1};
KW Hydrolase {ECO:0000313|EMBL:AJF60666.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nuclease {ECO:0000313|EMBL:AJF60666.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 304..401
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 165..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 365..516
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 687 AA; 79387 MW; 836024A412FA1B1E CRC64;
MIKRVYLENW RSHAKSEFEF GKGTNVLIGK MGSGKSSVMN AISFALYGTF PELNARALKL
EEIIMAKPTI QSESIIKVGF DYNGKNYSVE RIVKRHGSNQ AKLFEEDRLI AGPQPTDVTR
KIEELTEIPY ELFSRGVYSE QNQIDFFLKL NASQRKEKFD DLLQLNRYER VRSNAISVLN
RLKRDVLERK KWVEEQRKSF DSKQLEETEK KRKEKEEKIG ELKKSLEQKK SKLLEVSKAV
EEMEKKEKEF KFFKELIVKT ETKIEETQKS LEEIRAKTMG KSLEEIEANS KELKIKVAEK
EKQAKELKEN EKLLQKELNH LLQSKGLLEQ KAFELKESSV GLAEAKAECP VCRRKLEEHT
KKELIDENNA ERQKIIQEMK TVERKEKQAV EKISENEENI RLKEEAIEKL KEHGLELREL
LEKAKNAGKK QQEAIALKEE KEKLEKQLSG LEFDEEKLQK KRNLATELKE SASSVRKEIS
LDEEFIAELS QHIKAVKQQL EKIRELEETT KEIEGTNEKF SLFINALRAA QTELRTTLID
AVNDAMEDIW PRIYPYNDYV SARVHINEAG NYEIEVKEMD GKWVNTEGIL SGGERSAAAI
TVRIAVSLVL TQNLGWLILD EPTHNLDSST VSGLSKMMKE HLPELVEQIF IITHDREMTN
AASSTLYILE REKDENGVTV PVSQGIE
//
