DP2L_METMJ
ID DP2L_METMJ Reviewed; 1285 AA.
AC A3CXE7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Memar polC intein;
DE AltName: Full=Memar pol II intein;
GN Name=polC {ECO:0000255|HAMAP-Rule:MF_00324}; OrderedLocusNames=Memar_2124;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000562; ABN58047.1; -; Genomic_DNA.
DR RefSeq; WP_011844956.1; NC_009051.1.
DR AlphaFoldDB; A3CXE7; -.
DR SMR; A3CXE7; -.
DR STRING; 368407.Memar_2124; -.
DR MEROPS; N10.006; -.
DR EnsemblBacteria; ABN58047; ABN58047; Memar_2124.
DR GeneID; 4847324; -.
DR KEGG; mem:Memar_2124; -.
DR eggNOG; arCOG04447; Archaea.
DR HOGENOM; CLU_001154_0_0_2; -.
DR OMA; KRRNCDG; -.
DR OrthoDB; 559at2157; -.
DR Proteomes; UP000002146; 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: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; 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 PANTHER; PTHR42210; PTHR42210; 1.
DR Pfam; PF03833; PolC_DP2; 1.
DR PIRSF; PIRSF016275; PolC_DP2; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR TIGRFAMs; TIGR00354; polC; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 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 Transferase.
FT CHAIN 1..870
FT /note="DNA polymerase II large subunit, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000294688"
FT CHAIN 871..1035
FT /note="Memar polC intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000294689"
FT CHAIN 1036..1285
FT /note="DNA polymerase II large subunit, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000294690"
FT REGION 565..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1285 AA; 142303 MW; 7DF1F55811763A22 CRC64;
MEVSPAIARY FEELEGELDA AIRLAAAARA RGLDPRTEIE IPVASDLADR VEALLGYKGI
AARIRELEAE MSREEAALRI GDDFAARKFG ETTPEEILDH AIRAAMALLT EGVVAAPTEG
IGKVSLGKND DGTDYLKIYY AGPIRSAGGT AQALSVLVGD YVRQALGINR YIPRPEEVER
YIEEIRQYNN IMSLQYLPSE KELRMIIENC PVCIDGEPTE QQEVSGYRNL ERVETNTVRG
GMALVVAEGL ALKAPKVLKN VRKMKMEGWD WIEEMIGGGP KSDDDDASAA IKPKDKYIRD
LIGGRPVFSY PMRKGGFRLR LGRARNTGFA AAGFNPATLH ILGDFLAVGT QMKVERPGKA
AGVVPVDSIQ GPTVKLRSGE VRRVDDAAEA RRLAGQVDEI LDVGEMLVSF GEFMENNHPL
MPPAYCEEWW MLEGGPRHPE NELEAIEFAL DGVPLHPDYT YMWDDVAPAD IARLAEAVGT
GGTVEDGVLM IRNTPETKAI LEELLIPHHL SGDRLAIREH LAFLACLGLT LQLTKRPAWQ
DAPMENSLDL VMHLSGFTVR SRAGTRIGGR MGRPGKSKPR EMRPPPHSLF PIGDEGGARR
SFQAACSSKP RSNTDGGVIE AEVGERQCPA CGAFTYKNLC ECGAHTNPVF RCPRCGKDVG
QDVCPRCNAE TVCLQKVTIN VKAEYLAAME SLGVRESSVA LLKGVKGLIS RERPVEPIEK
GILRALQNLY VFKDGTVRYD MIDLPLTHFR PDEVGVPIER LRELGYTHDT YGRELVSDDQ
VLELRHQDIL VSEGCGEWLV RVAKFVDDLL VRLYGLEPFY KAEKPLDLVG HLLMGLAPHT
SAGVLVRLIG FSKAPVGYGH PFFHAAKRRN CFAGDTEITV SDGRRWMSLP IRQFVTENFD
ISKPGLDHVG TFYSDPRQPF YVRSIDSQGK TSLKRVTSVS VHRAPAHLVR FATRRGRVLT
VTPDHAMLVW DTDYLRKIKA LEVAVGDRVP VEEGGLVVAD EVVSRETVQA LDDRVYCLTV
AENHTLVANG IFCGQCDGDE DCVMLLLDGL INFSRAYLPE TRGGTMDAPL VLTTRIDPSE
VDKESHNVDV CDHYPIEVYN GCLAYAHPKD LDAFVDRVER RLGTPAQCEG FLFTHQTSNI
SAGPLESTYT RLGSMLDKLE AELDLAKRIR AVDEDDVAER VLNTHFIRDL QGNLNAFSKQ
KVRCMKCNAK YRRMPLAGKC TRCGGHVIPT VHEGSVKKYL EMSRNICATY AISDYTKQRV
EVLFMQIEST FGEPPEKQLG LADFM
