DPOL1_SACS2
ID DPOL1_SACS2 Reviewed; 882 AA.
AC P26811; O05707;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=DNA polymerase 1;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase I;
DE AltName: Full=Pol B1;
GN Name=dpo1; Synonyms=polS; OrderedLocusNames=SSO0552;
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 [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=1614858; DOI=10.1093/nar/20.11.2711;
RA Pisani F.M., Martino C., Rossi M.;
RT "A DNA polymerase from the archaeon Sulfolobus solfataricus shows sequence
RT similarity to family B DNA polymerases.";
RL Nucleic Acids Res. 20:2711-2716(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA Ragan M.A., Charlebois R.L.;
RT "Organizational characteristics and information content of an archaeal
RT genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL Mol. Microbiol. 22:175-191(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [4]
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 [5]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH PCNA3 AND PCNA2, SUBUNIT,
RP AND MUTAGENESIS OF 1-MET--ASP-9.
RX PubMed=12535540; DOI=10.1016/s1097-2765(02)00824-9;
RA Dionne I., Nookala R.K., Jackson S.P., Doherty A.J., Bell S.D.;
RT "A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus
RT solfataricus.";
RL Mol. Cell 11:275-282(2003).
CC -!- FUNCTION: This polymerase possesses two enzymatic activities: DNA
CC synthesis (polymerase) and an exonucleolytic activity that degrades
CC single-stranded DNA in the 3'- to 5'-direction. DNA polymerase I, DNA
CC ligase and the flap endonuclease may be constitutively associated with
CC the PCNA heterotrimer forming a scanning complex able to couple DNA
CC synthesis and Okazaki fragment maturation.
CC {ECO:0000269|PubMed:12535540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- ACTIVITY REGULATION: DNA synthesis is stimulated by PCNA heterotrimers.
CC {ECO:0000269|PubMed:12535540}.
CC -!- SUBUNIT: Interacts with PCNA subunit PCNA2 and weakly with PCNA3.
CC {ECO:0000269|PubMed:12535540}.
CC -!- INTERACTION:
CC P26811; Q980N4: cdc6-1; NbExp=4; IntAct=EBI-15778666, EBI-9026921;
CC P26811; Q9UXF8: cdc6-2; NbExp=5; IntAct=EBI-15778666, EBI-15778726;
CC P26811; Q97WM8: cdc6-3; NbExp=3; IntAct=EBI-15778666, EBI-9026919;
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; X64466; CAA45795.1; -; Genomic_DNA.
DR EMBL; U92875; AAB53090.1; -; Genomic_DNA.
DR EMBL; Y18930; CAB57747.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40869.1; -; Genomic_DNA.
DR PIR; F90201; F90201.
DR PIR; S23019; S23019.
DR RefSeq; WP_009991059.1; NC_002754.1.
DR PDB; 1S5J; X-ray; 2.40 A; A=36-882.
DR PDBsum; 1S5J; -.
DR AlphaFoldDB; P26811; -.
DR SMR; P26811; -.
DR DIP; DIP-48850N; -.
DR IntAct; P26811; 5.
DR STRING; 273057.SSO0552; -.
DR PRIDE; P26811; -.
DR EnsemblBacteria; AAK40869; AAK40869; SSO0552.
DR GeneID; 44129558; -.
DR KEGG; sso:SSO0552; -.
DR PATRIC; fig|273057.12.peg.562; -.
DR eggNOG; arCOG15272; Archaea.
DR HOGENOM; CLU_000203_6_0_2; -.
DR InParanoid; P26811; -.
DR OMA; WIRNMLY; -.
DR PhylomeDB; P26811; -.
DR BRENDA; 2.7.7.7; 6163.
DR BRENDA; 3.1.11.1; 6163.
DR EvolutionaryTrace; P26811; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Exonuclease; Hydrolase; Nuclease; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..882
FT /note="DNA polymerase 1"
FT /id="PRO_0000046483"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1..9
FT /note="Missing: No interaction with PCNA subunit PCNA2, DNA
FT polymerase no longer stimulated by PCNA heterotrimers."
FT /evidence="ECO:0000269|PubMed:12535540"
FT CONFLICT 139
FT /note="L -> H (in Ref. 1; CAA45795)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="A -> R (in Ref. 1; CAA45795)"
FT /evidence="ECO:0000305"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 356..360
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 379..387
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 403..419
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 423..439
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 451..466
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 473..478
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 504..515
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 562..576
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 578..582
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 589..614
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 623..645
FT /evidence="ECO:0007829|PDB:1S5J"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 658..663
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 666..679
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 684..695
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:1S5J"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 730..739
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 749..762
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 843..847
FT /evidence="ECO:0007829|PDB:1S5J"
FT HELIX 853..857
FT /evidence="ECO:0007829|PDB:1S5J"
SQ SEQUENCE 882 AA; 101224 MW; 77E3ED975AA1C81A CRC64;
MTKQLTLFDI PSSKPAKSEQ NTQQSQQSAP VEEKKVVRRE WLEEAQENKI YFLLQVDYDG
KKGKAVCKLF DKETQKIYAL YDNTGHKPYF LVDLEPDKVG KIPKIVRDPS FDHIETVSKI
DPYTWNKFKL TKIVVRDPLA VRRLRNDVPK AYEAHIKYFN NYMYDIGLIP GMPYVVKNGK
LESVYLSLDE KDVEEIKKAF ADSDEMTRQM AVDWLPIFET EIPKIKRVAI DIEVYTPVKG
RIPDSQKAEF PIISIALAGS DGLKKVLVLN RNDVNEGSVK LDGISVERFN TEYELLGRFF
DILLEYPIVL TFNGDDFDLP YIYFRALKLG YFPEEIPIDV AGKDEAKYLA GLHIDLYKFF
FNKAVRNYAF EGKYNEYNLD AVAKALLGTS KVKVDTLISF LDVEKLIEYN FRDAEITLQL
TTFNNDLTMK LIVLFSRISR LGIEELTRTE ISTWVKNLYY WEHRKRNWLI PLKEEILAKS
SNIRTSALIK GKGYKGAVVI DPPAGIFFNI TVLDFASLYP SIIRTWNLSY ETVDIQQCKK
PYEVKDETGE VLHIVCMDRP GITAVITGLL RDFRVKIYKK KAKNPNNSEE QKLLYDVVQR
AMKVFINATY GVFGAETFPL YAPAVAESVT ALGRYVITST VKKAREEGLT VLYGDTDSLF
LLNPPKNSLE NIIKWVKTTF NLDLEVDKTY KFVAFSGLKK NYFGVYQDGK VDIKGMLVKK
RNTPEFVKKV FNEVKELMIS INSPNDVKEI KRKIVDVVKG SYEKLKNKGY NLDELAFKVM
LSKPLDAYKK NTPQHVKAAL QLRPFGVNVL PRDIIYYVKV RSKDGVKPVQ LAKVTEIDAE
KYLEALRSTF EQILRAFGVS WDEIAATMSI DSFFSYPSKG NS
