DP2L_HALWD
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 03-AUG-2022, entry version 103.
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 PRIDE; Q18ER3; -.
DR EnsemblBacteria; CAJ53557; CAJ53557; 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 OMA; KRRNCDG; -.
DR Proteomes; UP000001975; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.28.10; -; 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 PANTHER; PTHR42210; PTHR42210; 2.
DR Pfam; PF03833; PolC_DP2; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 2.
DR SMART; SM00306; HintN; 2.
DR SUPFAM; SSF51294; SSF51294; 2.
DR SUPFAM; SSF55608; SSF55608; 2.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR TIGRFAMs; TIGR00354; polC; 1.
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
