Y1548_ARCFU
ID Y1548_ARCFU Reviewed; 174 AA.
AC O28724;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Uncharacterized protein AF_1548;
GN OrderedLocusNames=AF_1548;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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DR EMBL; AE000782; AAB89701.1; -; Genomic_DNA.
DR PIR; C69443; C69443.
DR RefSeq; WP_010879045.1; NC_000917.1.
DR PDB; 1Y88; X-ray; 1.85 A; A=2-174.
DR PDBsum; 1Y88; -.
DR AlphaFoldDB; O28724; -.
DR SMR; O28724; -.
DR STRING; 224325.AF_1548; -.
DR DNASU; 1484776; -.
DR EnsemblBacteria; AAB89701; AAB89701; AF_1548.
DR GeneID; 1484776; -.
DR GeneID; 24795296; -.
DR KEGG; afu:AF_1548; -.
DR eggNOG; arCOG07526; Archaea.
DR HOGENOM; CLU_086368_0_0_2; -.
DR EvolutionaryTrace; O28724; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR007560; Restrct_endonuc_IV_Mrr.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR Pfam; PF04471; Mrr_cat; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..174
FT /note="Uncharacterized protein AF_1548"
FT /id="PRO_0000128019"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:1Y88"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1Y88"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:1Y88"
FT STRAND 21..33
FT /evidence="ECO:0007829|PDB:1Y88"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1Y88"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1Y88"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:1Y88"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1Y88"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1Y88"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1Y88"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1Y88"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1Y88"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1Y88"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:1Y88"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1Y88"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1Y88"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:1Y88"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:1Y88"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:1Y88"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:1Y88"
SQ SEQUENCE 174 AA; 19765 MW; D72F0F2BC3296C33 CRC64;
MARLLEEHGF ETKTNVIVQG NCVEQEIDVV AERDGERYMI ECKFHNIPVY TGLKEAMYTY
ARFLDVEKHG FTQPWIFTNT KFSEEAKKYA GCVGIKLTGW SYPEKEGIEV LLESKGLYPI
TILRIDKEVL DELVRAGLVF CRDVVSAGEE KLREIGLSAK KAREVIAEAK KVIG