DN7D_SACS2
ID DN7D_SACS2 Reviewed; 64 AA.
AC P39476; P81550;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=DNA-binding protein 7d {ECO:0000303|PubMed:3132977};
DE AltName: Full=7 kDa DNA-binding protein d;
DE AltName: Full=Sso7d {ECO:0000303|PubMed:3132977};
GN Name=sso7d; Synonyms=sso7d-1; OrderedLocusNames=SSO10610;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP PROTEIN SEQUENCE OF 2-64, DNA-BINDING, SUBUNIT, AND METHYLATION AT LYS-5;
RP LYS-7; LYS-61; LYS-63 AND LYS-64.
RC STRAIN=ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1;
RX PubMed=3132977; DOI=10.1016/0167-4781(88)90011-5;
RA Choli T., Henning P., Wittmann-Liebold B., Reinhardt R.;
RT "Isolation, characterization and microsequence analysis of a small basic
RT methylated DNA-binding protein from the Archaebacterium, Sulfolobus
RT solfataricus.";
RL Biochim. Biophys. Acta 950:193-203(1988).
RN [3]
RP PROTEIN SEQUENCE OF 2-64, METHYLATION AT LYS-5; LYS-7; LYS-61; LYS-63 AND
RP LYS-64, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=9720912; DOI=10.1016/s0014-5793(98)00848-5;
RA Oppermann U.C.T., Knapp S., Bonetto V., Ladenstein R., Joernvall H.;
RT "Isolation and structure of repressor-like proteins from the archaeon
RT Sulfolobus solfataricus.";
RL FEBS Lett. 432:141-144(1998).
RN [4]
RP PROTEIN SEQUENCE OF 2-64.
RX PubMed=7875327; DOI=10.1016/0014-5793(95)00098-t;
RA Fusi P., Grisa M., Tedeschi G., Negri A., Guerritore A., Tortora P.;
RT "An 8.5-kDa ribonuclease from the extreme thermophilic archaebacterium
RT Sulfolobus solfataricus.";
RL FEBS Lett. 360:187-190(1995).
RN [5]
RP PROTEIN SEQUENCE OF 2-58.
RX PubMed=8425540; DOI=10.1111/j.1432-1033.1993.tb19899.x;
RA Fusi P., Tedeschi G., Aliverti A., Ronchi S., Tortora P., Guerritore A.;
RT "Ribonucleases from the extreme thermophilic archaebacterium S.
RT solfataricus.";
RL Eur. J. Biochem. 211:305-310(1993).
RN [6]
RP PROTEIN SEQUENCE OF 2-13.
RX PubMed=1592111; DOI=10.1016/0014-5793(92)80470-2;
RA Guagliardi A., Cerchia L., De Rosa M., Rossi M., Bartolucci S.;
RT "Isolation of a thermostable enzyme catalyzing disulfide bond formation
RT from the archaebacterium Sulfolobus solfataricus.";
RL FEBS Lett. 303:27-30(1992).
RN [7]
RP FUNCTION.
RX PubMed=11709558; DOI=10.1074/jbc.m109496200;
RA Kvaratskhelia M., Wardleworth B.N., Bond C.S., Fogg J.M., Lilley D.M.,
RA White M.F.;
RT "Holliday junction resolution is modulated by archaeal chromatin components
RT in vitro.";
RL J. Biol. Chem. 277:2992-2996(2002).
RN [8]
RP DNA-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27853299; DOI=10.1038/srep37274;
RA Kalichuk V., Behar G., Renodon-Corniere A., Danovski G., Obal G.,
RA Barbet J., Mouratou B., Pecorari F.;
RT "The archaeal '7 kDa DNA-binding' proteins: extended characterization of an
RT old gifted family.";
RL Sci. Rep. 6:37274-37274(2016).
RN [9]
RP STRUCTURE BY NMR, DNA-BINDING, AND SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=7634092; DOI=10.1038/nsb1194-808;
RA Baumann H., Knapp S., Lundbaeck T., Ladenstein R., Haerd T.;
RT "Solution structure and DNA-binding properties of a thermostable protein
RT from the archaeon Sulfolobus solfataricus.";
RL Nat. Struct. Biol. 1:808-819(1994).
RN [10]
RP STRUCTURE BY NMR, AND DNA-BINDING.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=9665172; DOI=10.1038/836;
RA Agback P., Baumann H., Knapp S., Ladenstein R., Haerd T.;
RT "Architecture of nonspecific protein-DNA interactions in the Sso7d-DNA
RT complex.";
RL Nat. Struct. Biol. 5:579-584(1998).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9731772; DOI=10.1038/1822;
RA Gao Y.G., Su S.Y., Robinson H., Padmanabhan S., Lim L., McCrary B.S.,
RA Edmondson S.P., Shriver J.W., Wang A.H.;
RT "The crystal structure of the hyperthermophile chromosomal protein Sso7d
RT bound to DNA.";
RL Nat. Struct. Biol. 5:782-786(1998).
CC -!- FUNCTION: Can constrain negative DNA supercoils. May be involved in
CC maintaining the integrity of the genome at high temperature (By
CC similarity). Stimulates the Holliday junction cleavage activity of Hjc
CC (PubMed:11709558). {ECO:0000250|UniProtKB:P61990,
CC ECO:0000269|PubMed:11709558}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Highly stable from pH 0 to pH 12. {ECO:0000269|PubMed:27853299};
CC Temperature dependence:
CC Hyperthermostable. {ECO:0000269|PubMed:27853299};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:27853299,
CC ECO:0000269|PubMed:3132977, ECO:0000269|PubMed:7634092}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27853299}.
CC -!- SIMILARITY: Belongs to the 7 kDa DNA-binding/endoribonuclease P2
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK42679.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE006641; AAK42679.1; ALT_INIT; Genomic_DNA.
DR PIR; H90427; H90427.
DR PIR; S69085; S69085.
DR RefSeq; WP_009990119.1; NC_002754.1.
DR PDB; 1BBX; NMR; -; C/D=2-64.
DR PDB; 1BNZ; X-ray; 2.00 A; A=1-64.
DR PDB; 1C8C; X-ray; 1.45 A; A=1-64.
DR PDB; 1JIC; NMR; -; A=2-62.
DR PDB; 5B02; X-ray; 2.21 A; A/B/C/D=1-64.
DR PDB; 5B03; X-ray; 2.60 A; A/B/C/D=1-64.
DR PDB; 5B0I; X-ray; 2.26 A; A/B/C/D=1-64.
DR PDB; 5B0J; X-ray; 2.50 A; A/B/C/D=1-64.
DR PDB; 5B0K; X-ray; 2.75 A; A/B/C/D=1-64.
DR PDB; 5B0L; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-64.
DR PDB; 5B0M; X-ray; 3.05 A; A/B/C/D/E/F/G/H=1-64.
DR PDB; 5GWV; X-ray; 2.40 A; A/B/C/D=1-64.
DR PDB; 5GWW; X-ray; 2.30 A; A/B/C/D=1-64.
DR PDB; 5U1C; EM; 3.90 A; A/B/C/D=1-64.
DR PDB; 6J8V; X-ray; 2.23 A; A/B/C/D=1-64.
DR PDB; 6J8W; X-ray; 2.35 A; A/B/C/D=1-64.
DR PDB; 6PUT; EM; 2.90 A; A/B/C/D=1-64.
DR PDB; 6PUW; EM; 2.90 A; A/B/C/D=1-64.
DR PDB; 6PUY; EM; 2.80 A; A/B/C/D=1-64.
DR PDB; 6PUZ; EM; 2.80 A; A/B/C/D=1-64.
DR PDB; 6V3K; EM; 3.40 A; A/B/C/D=1-64.
DR PDB; 6VOY; EM; 3.70 A; A/B/C/D=1-64.
DR PDBsum; 1BBX; -.
DR PDBsum; 1BNZ; -.
DR PDBsum; 1C8C; -.
DR PDBsum; 1JIC; -.
DR PDBsum; 5B02; -.
DR PDBsum; 5B03; -.
DR PDBsum; 5B0I; -.
DR PDBsum; 5B0J; -.
DR PDBsum; 5B0K; -.
DR PDBsum; 5B0L; -.
DR PDBsum; 5B0M; -.
DR PDBsum; 5GWV; -.
DR PDBsum; 5GWW; -.
DR PDBsum; 5U1C; -.
DR PDBsum; 6J8V; -.
DR PDBsum; 6J8W; -.
DR PDBsum; 6PUT; -.
DR PDBsum; 6PUW; -.
DR PDBsum; 6PUY; -.
DR PDBsum; 6PUZ; -.
DR PDBsum; 6V3K; -.
DR PDBsum; 6VOY; -.
DR AlphaFoldDB; P39476; -.
DR BMRB; P39476; -.
DR SMR; P39476; -.
DR STRING; 273057.SSO10610; -.
DR iPTMnet; P39476; -.
DR EnsemblBacteria; AAK42679; AAK42679; SSO10610.
DR GeneID; 44128276; -.
DR KEGG; sso:SSO10610; -.
DR PATRIC; fig|273057.12.peg.2631; -.
DR eggNOG; arCOG05888; Archaea.
DR HOGENOM; CLU_2929990_0_0_2; -.
DR OMA; PKELMDM; -.
DR BRENDA; 1.8.99.B1; 6163.
DR EvolutionaryTrace; P39476; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR003212; DNA-bd_7kDa_arc.
DR Pfam; PF02294; 7kD_DNA_binding; 1.
DR PIRSF; PIRSF036912; Sac7; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Methylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1592111,
FT ECO:0000269|PubMed:3132977, ECO:0000269|PubMed:7875327,
FT ECO:0000269|PubMed:8425540, ECO:0000269|PubMed:9720912"
FT CHAIN 2..64
FT /note="DNA-binding protein 7d"
FT /id="PRO_0000213078"
FT MOD_RES 5
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:3132977,
FT ECO:0000269|PubMed:9720912"
FT MOD_RES 7
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:3132977,
FT ECO:0000269|PubMed:9720912"
FT MOD_RES 61
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:3132977,
FT ECO:0000269|PubMed:9720912"
FT MOD_RES 63
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:3132977,
FT ECO:0000269|PubMed:9720912"
FT MOD_RES 64
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:3132977,
FT ECO:0000269|PubMed:9720912"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1C8C"
FT STRAND 9..16
FT /evidence="ECO:0007829|PDB:1C8C"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1C8C"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:1C8C"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1C8C"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1C8C"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1C8C"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:1C8C"
SQ SEQUENCE 64 AA; 7280 MW; 0E4BBA5027B944DD CRC64;
MATVKFKYKG EEKEVDISKI KKVWRVGKMI SFTYDEGGGK TGRGAVSEKD APKELLQMLE
KQKK
