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   16-JUN-2009, entry version 27.
DE   RecName: Full=DNA polymerase II large subunit;
DE            Short=Pol II;
DE            EC=2.7.7.7;
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; Synonyms=polA2; OrderedLocusNames=HQ3461A;
OS   Haloquadratum walsbyi (strain DSM 16790).
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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)
CC       and an exonucleolytic activity that degrades single stranded DNA
CC       in the 3'- to 5'-direction. Has a template-primer preference which
CC       is characteristic of a replicative DNA polymerase (By similarity).
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
CC   -!- CATALYTIC ACTIVITY: Degradation of single-stranded DNA. It acts
CC       progressively in a 3'- to 5'-direction, releasing nucleoside 5'-
CC       phosphates.
CC   -!- SUBUNIT: Heterodimer of a large subunit and a small subunit (By
CC       similarity).
CC   -!- PTM: This protein undergoes a protein self splicing that involves
CC       a post-translational excision of the intervening region (intein)
CC       followed by peptide ligation (Potential).
CC   -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC   -!- SIMILARITY: Contains 2 DOD-type homing endonuclease domains.
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DR   EMBL; AM180088; CAJ53557.1; -; Genomic_DNA.
DR   RefSeq; YP_659142.1; -.
DR   GeneID; 4194482; -.
DR   GenomeReviews; AM180088_GR; HQ3461A.
DR   KEGG; hwa:HQ3461A; -.
DR   NMPDR; fig|362976.6.peg.2460; -.
DR   HOGENOM; Q18ER3; -.
DR   OMA; Q18ER3; FRANIAP.
DR   BioCyc; HWAL362976:HQ3461A-MON; -.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:HAMAP.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IEA:HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR   HAMAP; MF_00324; atypical; 1.
DR   InterPro; IPR003586; Hedgehog_hint_C.
DR   InterPro; IPR003587; Hedgehog_hint_N.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_splicing_site.
DR   InterPro; IPR004475; PolC_DP2.
DR   InterPro; IPR016033; PolC_DP2_N.
DR   Pfam; PF03833; PolC_DP2; 1.
DR   SMART; SM00305; HintC; 2.
DR   SMART; SM00306; HintN; 2.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 2.
DR   TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR   TIGRFAMs; TIGR00354; polC; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; FALSE_NEG.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Complete proteome; DNA replication;
KW   DNA-binding; DNA-directed DNA polymerase; Endonuclease; Exonuclease;
KW   Hydrolase; Intron homing; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Protein splicing; Repeat; Transferase.
FT   CHAIN         1    966       DNA polymerase II large subunit, 1st part
FT                                (Potential).
FT                                /FTId=PRO_0000294680.
FT   CHAIN       967   1495       Hwa polC 1 intein (Potential).
FT                                /FTId=PRO_0000294681.
FT   CHAIN      1496   1524       DNA polymerase II large subunit, 2nd part
FT                                (Potential).
FT                                /FTId=PRO_0000294682.
FT   CHAIN      1525   2068       Hwa polC 2 intein (Potential).
FT                                /FTId=PRO_0000294683.
FT   CHAIN      2069   2289       DNA polymerase II large subunit, 3rd part
FT                                (Potential).
FT                                /FTId=PRO_0000294684.
FT   DOMAIN     1222   1367       DOD-type homing endonuclease 1.
FT   DOMAIN     1755   1911       DOD-type homing endonuclease 2.
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
//