ID   DP2L_HALWD              Reviewed;        2289 AA.
AC   Q18ER3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 112.
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=Hwa polC 1 intein;
DE     AltName: Full=Hwa pol II 1 intein;
DE   Contains:
DE     RecName: Full=Hwa polC 2 intein;
DE     AltName: Full=Hwa pol II 2 intein;
GN   Name=polC {ECO:0000255|HAMAP-Rule:MF_00324}; Synonyms=polA2;
GN   OrderedLocusNames=HQ_3461A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ53557.1; -; Genomic_DNA.
DR   RefSeq; WP_011572651.1; NC_008212.1.
DR   AlphaFoldDB; Q18ER3; -.
DR   SMR; Q18ER3; -.
DR   STRING; 362976.HQ_3461A; -.
DR   GeneID; 4194482; -.
DR   KEGG; hwa:HQ_3461A; -.
DR   eggNOG; arCOG03145; Archaea.
DR   eggNOG; arCOG03147; Archaea.
DR   eggNOG; arCOG04447; Archaea.
DR   HOGENOM; CLU_001154_0_0_2; -.
DR   Proteomes; UP000001975; Chromosome.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006308; P:DNA catabolic process; 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   GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR   CDD; cd00081; Hint; 2.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 2.
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; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004475; PolC_DP2.
DR   InterPro; IPR016033; PolC_DP2_N.
DR   NCBIfam; TIGR01445; intein_Nterm; 1.
DR   NCBIfam; TIGR00354; polC; 1.
DR   PANTHER; PTHR42210; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR   PANTHER; PTHR42210:SF1; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR   Pfam; PF14890; Intein_splicing; 2.
DR   Pfam; PF03833; PolC_DP2; 1.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 2.
DR   SMART; SM00306; HintN; 2.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 2.
DR   SUPFAM; SSF55608; Homing endonucleases; 2.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Endonuclease; Exonuclease; Hydrolase;
KW   Intron homing; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Protein splicing; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..966
FT                   /note="DNA polymerase II large subunit, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000294680"
FT   CHAIN           967..1495
FT                   /note="Hwa polC 1 intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000294681"
FT   CHAIN           1496..1524
FT                   /note="DNA polymerase II large subunit, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000294682"
FT   CHAIN           1525..2068
FT                   /note="Hwa polC 2 intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000294683"
FT   CHAIN           2069..2289
FT                   /note="DNA polymerase II large subunit, 3rd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000294684"
FT   DOMAIN          1222..1367
FT                   /note="DOD-type homing endonuclease 1"
FT   DOMAIN          1755..1911
FT                   /note="DOD-type homing endonuclease 2"
FT   REGION          279..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2289 AA;  255812 MW;  A5E70294203AFF05 CRC64;
     MRDADKQYFE TLESHLEQAF ARARQAKGQG YDPKPEVEIP VARDMADRVE NILAIPDVAE
     RIRELDDERS REEVALELVT DFVEGTVGDY DTREGKIEGA VRTAVALLTE GVVAAPIEGI
     DRVEILSDDD GSEFVNVYYA GPIRSAGGTA QALSVLVADY ARSLLDIDEY SARTDETERY
     AEEVSLYDRE TGLQYSPKDK ETKFITKHMP IMLDGEATGN EEVSGYRDLE RVDTNAARGG
     MCLVLAEGIA LKAPKIQRYT RQLAEVEWPW LQDLIDDTIG SDEHSNNSVK NGEADIVKTD
     KDTNESETED GIDNDDYNDS GLEPANSPRA DATNKYLRDL IAGRPVFGHP SAAGAFRLRY
     GRARNHGFAT AGVHPATMHI VDDFIATGTQ LKTERPGKAG GVVPVDSIKG PTVRLANGDV
     RCINDPEEAE KLQNGVEKIL DLGEYLVNFG EFIENNHPLA PAAYVFEWWI QEFEASNADV
     QALRDDPTVD LESPTFENAM RWAKKHDIPL HPAYTYLWHD ISVTEFDHLA DAVAAGEITM
     NEVSDTNSAS GNTSLRANTN TDDTLTIDTT PAIRETMERL LIEHHQDSDS IHIPAWRALA
     LSLGIKIESD NDTGIGDRMW SLTDLSKHAR KQDDGKSAIA AVNEVAPFQV RERAPTRIGS
     RMGRPEKSED RDLSPAVHTL FPIGEAGGNQ RNLSDAAQSF GDNTERGQIS VQLGKRRCPY
     CETVGFELQC AECGRHTEPQ FVCRECESVL SPDESGRVHC DRCERDVTSA EWQDIDLHQR
     YRDALDRVDE RESSFEILKG VKGLTSSNKT PEPLEKGILR AKHGVSSFKD GTVRYDMTDL
     PVTAVRPKEL DVTAAHFREL GYQTDINGNP LQFDDQLVEL KVQDIVLPDG AAEHMMKTAD
     FVDDLLEQFY ELNQFYQIDE RDDLIGELVF GMAPHTSAAV VGRIVGFTSA AVGYAHPYFH
     AAKRRNCFHP ETKIWFRDTD NEWHHETIQT FVEDRLDDPE IDAVGTLVQE VDDNTDREIS
     VPSIDDNGNE RLQSVTAVSK HRAPNHLVQI ETISGREITI TPDHEMHIFE QGNLVSKQAS
     KITSGEYAVI PKRLQTISPS SHTPQHDLLR EFLTRDELTA DRLIIHTSDP VRLCNRVFPE
     EVTSCKDAVE IMQNTACHLD KNKETLIGWL GEGRIPVALL RGFVETDEAL LMSIPDDVQI
     GLRGEKVRID RHIGFTEELT SLLGYYAAAG IVHTQTNPIS YESAQQEQSR ITFYNIDTQT
     QTDLLNALNS VFEIEPIQYN LDGEILGVPG ELIRRVFDTV FDVGTQPSHK RIPQALFDAS
     ESHITSYLRC FFSTHDSLTT DTRDISATTV SREFKEDIIA ALRRLGITAE VTTQQSRSVP
     EVLPDWYAID DITHHDADNS LNLTRSYVIS IASSDAVTLQ RDRQAQEQIK YDAQGLIANN
     NAIHQSRQVT DGGRKDYITE PITDIEYVDA DIDYTYCLTV SETHSLIVND LSQKQCDGDE
     DCVMLLMDGL LNFSREYLPD KRGGSVAADS RLVAVSPDDK IVFTTIEDFW KKLNTPIERN
     GKFRKRTCVS EGWQTYAFDE NHEASLRPIE KAIRYTADES EQLRRITTQL GRSLDITDEH
     SLFRYDDGIE EVAGDDLTAG DIIVAPRTLD VEVTQTTLDL SEYIHDNERC PSEQTGSGEL
     NLASKSAISD SRNKETPGVT HNILPQRSKF TDEMTTLSPT AVGGLESEQN ETLRVGESTG
     AIERYINVDD SFGWLLGQFI AQRSISTDAL TMTVHTAAEK HAERIVATSD SVFGIKPTVN
     SIERGYEIVF PSVFDTIVSG LTAKEQSEPE QDVDHTHTDE IGIPECILHA PDDIVLSFLQ
     GFILAENAQR KGNAASEASE MVSESETTVT LETPSVGVKD GLVFLCHRLG VITDISEKSG
     EEYSVHFEES RYTVSIATEG KTNPLDQILN GERPTMPEGV SVPVPDALLT IHESIANSPH
     IDQVIPDTVV QQETVSLETL QSLLTGLSTV DLPAQLEAKR DELTLLTEGD LSYLRVESVE
     CVDYDGYLYD LQVGGEPVFT ANWLYAHNSM DAPLVMSSRI DPSEIDDEAH NMDIVRQYPR
     EFYEATRRME DPDEWEEEVT IAEEYLDTDN EYTGFNHTHD TTDIAAGPDL SAYKTLDSMM
     DKMDAQLELA RKLRAVDETD VAERVIEYHF LPDLIGNLRA FSRQQTRCLD CGESYRRMPL
     TGECRECGGR VNLTVHEGSV NKYMDTAIHI AEEFDCREYT KQRLEVLERS LESIFEDDTN
     KQSGIADFM
//