ID   DP2L_PICTO              Reviewed;        1080 AA.
AC   Q6L1K9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=DNA polymerase II large subunit {ECO:0000255|HAMAP-Rule:MF_00324};
DE            Short=Pol II {ECO:0000255|HAMAP-Rule:MF_00324};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00324};
DE   AltName: Full=Exodeoxyribonuclease large subunit {ECO:0000255|HAMAP-Rule:MF_00324};
DE            EC=3.1.11.1 {ECO:0000255|HAMAP-Rule:MF_00324};
GN   Name=polC {ECO:0000255|HAMAP-Rule:MF_00324}; OrderedLocusNames=PTO0558;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- FUNCTION: Possesses two activities: a DNA synthesis (polymerase) and an
CC       exonucleolytic activity that degrades single-stranded DNA in the 3'- to
CC       5'-direction. Has a template-primer preference which is characteristic
CC       of a replicative DNA polymerase (By similarity). {ECO:0000250}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00324};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.11.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00324};
CC   -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00324}.
CC   -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC       {ECO:0000255|HAMAP-Rule:MF_00324}.
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DR   EMBL; AE017261; AAT43143.1; -; Genomic_DNA.
DR   RefSeq; WP_011177359.1; NC_005877.1.
DR   AlphaFoldDB; Q6L1K9; -.
DR   SMR; Q6L1K9; -.
DR   STRING; 263820.PTO0558; -.
DR   PRIDE; Q6L1K9; -.
DR   EnsemblBacteria; AAT43143; AAT43143; PTO0558.
DR   GeneID; 2844296; -.
DR   KEGG; pto:PTO0558; -.
DR   PATRIC; fig|263820.9.peg.587; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   OrthoDB; 559at2157; -.
DR   Proteomes; UP000000438; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00324; DNApol_II_L_arch; 1.
DR   InterPro; IPR004475; PolC_DP2.
DR   InterPro; IPR016033; PolC_DP2_N.
DR   PANTHER; PTHR42210; PTHR42210; 1.
DR   Pfam; PF03833; PolC_DP2; 1.
DR   PIRSF; PIRSF016275; PolC_DP2; 1.
DR   TIGRFAMs; TIGR00354; polC; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1080
FT                   /note="DNA polymerase II large subunit"
FT                   /id="PRO_0000294699"
SQ   SEQUENCE   1080 AA;  121576 MW;  02273EA4918062BC CRC64;
     MIDHSLFDYN ERLRKETYEC YEIAKKARAM GLDVSDEVEI PIANDMAERV EELIHISGIA
     GEIRELSKSM SREELSLHIS KKVASLLKDN RVEALDKAVR VGLAILTEGI LVAPLEGIKD
     VKINKNDDGT EYVSIVYSGP IRSAGGTAQA LSVLIADIVR RELNIGSFSP TDDEIERYIE
     EVEAYNRLKH LQYMPTPDEI RLVLKNSPVM IDGEGSEEEE VSGHRDMKRI TTNRIRGGMC
     LVLCEGLIQK AKKVLKYTNV MHLNEWNILE NIGKNKSDEK TENKSEKYLK DIIAGRPVFG
     YPNRPGGFRL RYGRSRVSGL AAASINPVTM KILNDFIAIG SQIKVELPGK AAAITPCDSI
     DGPMVLTRSG DHIKVKSIEQ AEKIKNDIER ITDLGEILIA YGDFLENNRN LDLSPFTREW
     WEYYLNDELS IYKSRDPDQF DAVNISRKYK MPMFPGYDYF WHDITMEELN LLINAIANGI
     INDDSMMLDA SVSEILIKLG IEFKKHNNKL ILHEYYPLIV SCGFDLINEK IVKVSDERKN
     DVLGTVNALS GIEIKPRAPV RVGARLGRPE KAGDRKMKPK VHGLFPLMNY GGSTRSIINA
     ARSGSIMDIE LGARICRACG TETPFVRCPK CGMPTEDSDS EKKFKIDISK ALDDAALRVS
     TDIGTIKELK GVKKLMSRRS VIEPLEKAIL RAKHGISINK DGTCRYDMSD IPITHFKYNE
     ISLTRQRLME LGYSDSDINE IYPQDIIIPR DAASYLLNVS KFIDDLLVNY YGLGPYYMCN
     SEDDLIGHLV IGLAPHTSGG IVGRIIGFSD VNGCYAHPFF HAAKRRNCDG DEDSIMLLLD
     GLLNFSKKYL PSTTGGLMDA PLVLTLILDP EEIDKEALNV DTLQRYPLDF YIATEKNAPP
     ASIENMMKTM KVLIKDGRYT GISYSFDTGD ISYGTRLSAY KTIGSMEEKI EKQLGLARIL
     RSVDENDVAA RVLSSHFLPD IYGNFRSFFT QEFRCTKCNA KYRRVPLSGR CLRCGSSNII
     LTIHHGSIVK YLNETKKVMN EYKLPDYLVF RINRLLEQIE STFDIENGND TTLDALIENE