ID   DP2L_HALMA              Reviewed;        1395 AA.
AC   Q5UZ40;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
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};
DE   Contains:
DE     RecName: Full=Hma polC intein;
DE     AltName: Full=Hma pol II intein;
GN   Name=polC {ECO:0000255|HAMAP-Rule:MF_00324}; Synonyms=polA2;
GN   OrderedLocusNames=rrnAC2691;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(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   -!- 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:0000255|HAMAP-Rule:MF_00324}.
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DR   EMBL; AY596297; AAV47463.1; -; Genomic_DNA.
DR   RefSeq; WP_011224375.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UZ40; -.
DR   SMR; Q5UZ40; -.
DR   STRING; 272569.rrnAC2691; -.
DR   MEROPS; N10.006; -.
DR   PRIDE; Q5UZ40; -.
DR   EnsemblBacteria; AAV47463; AAV47463; rrnAC2691.
DR   GeneID; 40153559; -.
DR   KEGG; hma:rrnAC2691; -.
DR   PATRIC; fig|272569.17.peg.3278; -.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   OMA; KRRNCDG; -.
DR   Proteomes; UP000001169; Chromosome I.
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; IPR036844; Hint_dom_sf.
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   SUPFAM; SSF51294; SSF51294; 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..965
FT                   /note="DNA polymerase II large subunit, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000294677"
FT   CHAIN           966..1145
FT                   /note="Hma polC intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000294678"
FT   CHAIN           1146..1395
FT                   /note="DNA polymerase II large subunit, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000294679"
FT   REGION          279..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..310
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..672
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..704
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1395 AA;  153633 MW;  99996EC3A54B3F07 CRC64;
     MREADEQYFE TLETQLEAAF DVAERAKERG GDPKPEVEIP TARDMADRVE NILGIDGVAE
     RVRELEGQMS REEAALELVE DFVEGTVGDY DSREGKVEGA VRTAVALLTE GVVAAPIEGI
     DRVELLENDD GTEFINVYYA GPIRSAGGTA QALSVLVADY ARALLGIDQY KAREEEIGRY
     AEEIDLYDKD TGLQYSPKEK ETKFIAEHMP IMLDGEATGD EEVSGYRDLE RVDSNSPRGG
     MCLVLAEGIA LKAPKIQRYT RNLDEVDWPW LQDLIDGTIG KDEADEGDSA EDANGDDAGE
     GADDDGGDEA DEQAGPPRVE PADKYLRDLI AGRPVFSHPS KSGGFRLRYG RSRNHGFATA
     GVHPATMHLV DDFLATGTQI KTERPGKAAG VVPVDTIEGP TVRLANGDVR RIDDAEEALA
     VRNGVEKILD LGEYLVNYGE FVENNHPLAP ASYTVEWWEQ DLAAAGADVQ AMQDSPHIDL
     ADPSAEEAIE WATEYDAPLH PKYTYLWHDV SIEQVCALAD AVEDAQVAQA DGAYADPEMD
     GTAGDAHSDD GALVLPRSDA VQQTLEHLLI GHTQDEETIT VTDWVPLVRT LGFSRSLERD
     WTREDLSEHA RTYGESESLD AIGVAEDAER EDGQNAIKAI NEVAPFQVRE RAPTRIGNRM
     GRPEKSERRD LSPAVHTLSP IGEAGGAQRD VAKATKHADD MSDTPGQVEV EVARRRCPDC
     GTETHQANCA ECSGTTEPVY VCPDCEAEVE RDESGRAECG RCETLASPTQ YKVLDLQEAY
     RDALQNVGER ETAFEQLKAV KGLTSEEKVP EPMEKGILRA KHDVSAFKDG TVRYDMTDLP
     VTAVRASELD VSAERLRGLG YTEDIHGDPL THEDQLVELK VQDIVLSDGA AEHMLQTARF
     VDDLLEQYYG LERFYEFDDR EDLVGELVFG MAPHTSAATV GRVVGFTSAA VGYAHPYFHA
     AKRRNCFHPD TRLWYEDEND DWEYGTIEEL VESRLDDPQE DDFGTLVQEL DGDLTVSSLG
     ENGPCRQPVD AVSKHPAPDH LVEVAVGDRT LRVTPDHTML RAGPDGIEEV PASDLAAGDD
     LPAYDGGETT TMTARGEAST AATDGAAPTD TVEAVEYVES DVDHVYCLTV ADTHRVAVEG
     TYVGQCDGDE DCVMLLMDGL LNFSKSYLPN QRGGQMDAPL VMSSRIDPSE IDDEAHNMDI
     MDAYPREFYE ATREMKDPTE VEDVMKIAEE TLGTDREYTE FRHTHDTANI AAGPDLSAYK
     TLGSMEDKMD AQLEISRKLR AVVESDVAER IIEYHFLPDL IGNLRAFSRQ EVRCLDCGES
     FRRAPLTGDC RECGGRVNLT VHEGSVNKYI DTAIRVADEF GARDYTKQRL KILERKIESV
     FENDHNKQSG IADFM