ID   DP2L_HALSA              Reviewed;        1370 AA.
AC   Q9HMX8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=DNA polymerase II large subunit;
DE            Short=Pol II;
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};
DE   Contains:
DE     RecName: Full=Hsp-NRC1 polC intein;
DE     AltName: Full=Hsp-NRC1 pol2 intein;
GN   Name=polC; Synonyms=polA2; OrderedLocusNames=VNG_2338G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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;
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:0000250}.
CC   -!- PTM: This protein undergoes a protein self splicing that involves a
CC       post-translational excision of the intervening region (intein) followed
CC       by peptide ligation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC       {ECO:0000305}.
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DR   EMBL; AE004437; AAG20443.1; -; Genomic_DNA.
DR   PIR; G84384; G84384.
DR   RefSeq; WP_010903745.1; NC_002607.1.
DR   AlphaFoldDB; Q9HMX8; -.
DR   SMR; Q9HMX8; -.
DR   STRING; 64091.VNG_2338G; -.
DR   MEROPS; N10.006; -.
DR   PaxDb; Q9HMX8; -.
DR   EnsemblBacteria; AAG20443; AAG20443; VNG_2338G.
DR   GeneID; 5953348; -.
DR   KEGG; hal:VNG_2338G; -.
DR   PATRIC; fig|64091.14.peg.1810; -.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   InParanoid; Q9HMX8; -.
DR   OMA; KRRNCDG; -.
DR   OrthoDB; 559at2157; -.
DR   PhylomeDB; Q9HMX8; -.
DR   Proteomes; UP000000554; 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   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   HAMAP; MF_00324; DNApol_II_L_arch; 1.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004475; PolC_DP2.
DR   InterPro; IPR016033; PolC_DP2_N.
DR   PANTHER; PTHR42210; PTHR42210; 1.
DR   Pfam; PF03833; PolC_DP2; 1.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; SSF51294; 1.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR   TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR   TIGRFAMs; TIGR00354; polC; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Exonuclease; Hydrolase;
KW   Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Protein splicing;
KW   Reference proteome; Transferase.
FT   CHAIN           1..925
FT                   /note="DNA polymerase II large subunit, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007301"
FT   CHAIN           926..1120
FT                   /note="Hsp-NRC1 polC intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007302"
FT   CHAIN           1121..1370
FT                   /note="DNA polymerase II large subunit, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007303"
FT   REGION          279..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1081
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..297
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1370 AA;  150296 MW;  07878AA9976790C9 CRC64;
     MRPTDETYFE TLETGLDDAF EVAEAARERG EDPTPNVEIP VAKDMADRVE NILGIDGVAE
     RVRDLDGEMS REEAALELVA DFVDGRVGDY DTDAGKIEGA VRTAVALLTE GVVAAPIEGI
     DRVEVNDNDD GTQYVAVYYA GPIRSAGGTA QALSVLVADY ARAMLGIDAF KPRDDEIERY
     AEEVDLYDSE TGLQYSPKDA ETTFITEHCP VMLDGEATGN EEVDGFRDLE RIDTNSPRGG
     MCLVLAEGIA LKAPKIQRYT RNLDEVAWPW LQDLIDGTIG ADDADEDTPD AGSDSDATDE
     GDAPSASTDA EEPPRAAPSD KFLRDLIAGR PVFGHPSKNG GFRLRYGRAR NHGNATAGVH
     PATMHLLDDF LATGTQIKTE RPGKAAGIVP VDSIEGPTVK LANGDVRHIN DPADALDVRN
     GVAEILDVGE YLVNYGEFVE NNHELAPASY APEWWIQDLD AAGADVQALR DSPYVDLTAP
     TADQAMAWAT DYDAPLHPAY TYLWHDIDVE QFRALADAVA DAHTDASDDD DRGVLVLDHT
     TTVRETLEAL LVTHHQGDDT IRVDDWLPLA RSLGVTESLD REWETLSEAA AEWPNAVRAV
     NEVAPFSVQE RAPTRIGNRM GRPEKSESRD LSPAVHTLFP IGDAGGSQRD VADAARYAPD
     MSDTPGEIPV RVGDRVCPSC DEHTYESRCP DCGDWTDPHY ECRDCGAVAT PDESGRVECP
     NCGRDLDNVT TQVIDINDEY HGALRAVGER ENAFDQLKGV KGLLSAEKTP EPMAKGVLRA
     KHDVTAFKDG TVRYDMTDLP VTAVTPAELD VTAGQFRELG YNQDIHGDPL EHDDQLVELR
     VQDVVLSDGA ADHMLKTADF VDDLLTQYYG LDAFYDLDDR DDLVGELVFG MAPHTSAAVV
     GRVAGFTSAS VGYAHPYFHA AKRRNCFHPE TNVWFRDESG EWHHDPIETL VEARLDPDTA
     DEDDFGALVQ ALDGDVFVPS VTEDGEETLQ RVEAVSKHPA PDHLLAVETK RGRELTVTPD
     HSMRRWTGDG IERVDARELT AGDALPAPTQ VPGDGETATS ELRSESLDGT HPQRRFGDGG
     SVRTDEVVSV EPVRSSVDHT YSLTVAETNT LVANGLFTGQ CDGDEDCVML LMDGLINFSK
     SYLPDKRGGR MDAPLVMSSR IDPAEIDDEA HNIDIDREYP REFYEATREL ADPEDVADLI
     TLAESTVGTD EEYTGFGHTH ATSNIHLGPS LSAYKTLGSM MDKMDAQLEL ARKLRSVAET
     DVAERVIEYH FLPDLIGNLR AFSRQETRCL DCGEKYRRMP LSGDCRECGG RVNLTVHEGS
     VNKYMDTAMR VATEYDCREY TKQRLEIMDR RLESVFEDDT NKQSGISDFM