ID A0A0P7HT08_9EURY Unreviewed; 1422 AA.
AC A0A0P7HT08;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA polymerase II large subunit {ECO:0000256|HAMAP-Rule:MF_00324};
DE Short=Pol II {ECO:0000256|HAMAP-Rule:MF_00324};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00324};
DE AltName: Full=Exodeoxyribonuclease large subunit {ECO:0000256|HAMAP-Rule:MF_00324};
DE EC=3.1.11.1 {ECO:0000256|HAMAP-Rule:MF_00324};
GN Name=polC {ECO:0000256|HAMAP-Rule:MF_00324,
GN ECO:0000313|EMBL:KPN29818.1};
GN ORFNames=SY89_00536 {ECO:0000313|EMBL:KPN29818.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN29818.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|Proteomes:UP000050535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA Schwartz K.J., Yoon K.;
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025068,
CC ECO:0000256|HAMAP-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:0000256|HAMAP-
CC Rule:MF_00324};
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 Evidence={ECO:0000256|ARBA:ARBA00024632, ECO:0000256|HAMAP-
CC Rule:MF_00324};
CC -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC {ECO:0000256|ARBA:ARBA00011315, ECO:0000256|HAMAP-Rule:MF_00324}.
CC -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family.
CC {ECO:0000256|ARBA:ARBA00011053, ECO:0000256|HAMAP-Rule:MF_00324}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPN29818.1}.
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DR EMBL; LGUC01000001; KPN29818.1; -; Genomic_DNA.
DR RefSeq; WP_054583003.1; NZ_LGUC01000001.1.
DR STRING; 699431.SY89_00536; -.
DR PATRIC; fig|699431.3.peg.557; -.
DR OrthoDB; 7529at2157; -.
DR Proteomes; UP000050535; Unassembled WGS sequence.
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: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 CDD; cd00081; Hint; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
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 NCBIfam; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
DR PANTHER; PTHR42210; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR PANTHER; PTHR42210:SF1; DNA POLYMERASE II LARGE SUBUNIT; 1.
DR Pfam; PF03833; PolC_DP2; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_00324};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00324};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_00324};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00324};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00324}; Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00324}.
FT DOMAIN 985..1109
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00306"
FT DOMAIN 1131..1178
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00305"
FT REGION 13..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..309
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1422 AA; 157297 MW; E99BE17AA822A0D3 CRC64;
MREDDERYFE RIEDQLDDAF DRAEAAREQG RDPQPEIEIP VAKDMADRVE NILGIPGVAE
RVRELEGQMS REEAALELVE DFVDGNVGDY DSREGKIEGA VRTAVALLTE GVVAAPIEGI
DRAELLQNDD GTEFVNVYYA GPIRSAGGTA QALSVLVADY ARSLLGIEEF HARDDEIERY
AEEIALYEKE TGLQYTPKDK ETKFIAEHMP IMLDGEATGD EEVSGFRDLE RVDTNSARGG
MCLVMAEGIA LKAPKIQRYT RQLDEVDWPW LQDLIDGTYY DGAADDGSDE GDEAAAADDG
DAEADADEPA EPEGPVRAES ATKYLRDLIA GRPVFGHPSE SGGFRLRYGR SRNHGFATAG
VHPATMHLVD DFLATGTQIK TERPGKAAGV VPVDSIEGPT VKLANGDVRR IDDPQEALDV
RNGVDEILDL GEYLVNYGEF VENNHPLVPA SYSVEWWEQE FDDAGADVQA LRDDPHVDLD
EPDPRTALDW AERYDCPIHP EYTYLWHDVT VAEYDALAAA AADGEIDDDG LLIERRDDAQ
RALERLLVEH TATEDTLRVP EYRPLLRSLG VTAELEREWQ PADLSERART WGAADDGPDE
AVADGGQQAP PSTGSDDSRQ APPTAEADTG VAVRDESDTA AEAEHTEGAD SVPLPGTNAI
EAVNEVASFA VRERAPTRIG NRMGRPEKSE SRDLSPAVHT MFPIGEAGGS QRDVAKAAKD
RTDAGRGVIE VSLGERECPE CGEHTYENRC PECESHTEPY YECDDCGIEV EPDESGRVVC
PRCEWEVESP EERVIDLNAI YHDALDSVGE REGSFSILKG VQGLMSANET PEPMEKGVLR
AKHDVSSFKD GTVRYDMTDL PVTSVRPEEL DTTAAEFRRL GYETDVDGEP LRHDDQLVEL
KVQDIVLPDG AAEHMMRTAD FVDDLLEEFY GLEPFYGVEE RDDLVGELVF GMAPHTSAAV
VGRVVGFTSA AVGYAHPYFH AAKRRNCFHP ETKVWFRDES ESWHHDEIRT LVEDRLNPET
ADEDDFGTLV QELDGDVFVP SIDADGDEVV KPVEAVSKHP APEHMVRVET RSGREITVTP
DHELCRWTSG VESIVATEIE VGDEIPVPST GTGEQPASIR GDAETAVIAD GGAPVTDEVA
TVEYVEAESD HTYCLTVEET HTLVANDMYS AQCDGDEDCV MLLLDGLLNF SKEFLPDQRG
GRMDAPLVMS SRIDPSEIDD EAHNMDIVRQ YPQEFYEATL EMADPGEVEE LIQLGEDTLG
TDDEYRGFDH THDTSDIALG PDLSAYKTLG DMETKMDAQL ELSRKLRAVD QTDVAERVIE
NHFLPDLIGN LRAFSRQETR CLDCGEKYRR MPLTGDCREC GGRMTLTVHR GSVNKYMDVA
IEVAEEYGCR DYTKQRLEVL ERSLESIFEN DKNKQSGIAD FM
//
