DP2L_METHJ
ID DP2L_METHJ Reviewed; 1286 AA.
AC Q2FSF9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Mhu polC intein;
DE AltName: Full=Mhu pol II intein;
GN Name=polC {ECO:0000255|HAMAP-Rule:MF_00324}; OrderedLocusNames=Mhun_2435;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD42136.1; -; Genomic_DNA.
DR RefSeq; WP_011449394.1; NC_007796.1.
DR AlphaFoldDB; Q2FSF9; -.
DR SMR; Q2FSF9; -.
DR STRING; 323259.Mhun_2435; -.
DR MEROPS; N10.006; -.
DR EnsemblBacteria; ABD42136; ABD42136; Mhun_2435.
DR GeneID; 3922423; -.
DR KEGG; mhu:Mhun_2435; -.
DR eggNOG; arCOG04447; Archaea.
DR HOGENOM; CLU_001154_0_0_2; -.
DR OMA; KRRNCDG; -.
DR OrthoDB; 559at2157; -.
DR Proteomes; UP000001941; 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 Reference proteome; Transferase.
FT CHAIN 1..872
FT /note="DNA polymerase II large subunit, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000294694"
FT CHAIN 873..1037
FT /note="Mhu polC intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000294695"
FT CHAIN 1038..1286
FT /note="DNA polymerase II large subunit, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000294696"
FT REGION 566..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1286 AA; 143304 MW; 7169201A09413EB2 CRC64;
MADISPRMQE YYDRLNAGLA QAMEVAKTAR KTGLDPETVV EIPIANDLAD RVEAQVGIPG
VAQMIRELEA VMSREEASLH IGDYFAEKKF GETTKEEILD HAIRTAMALL TEGVVSAPIE
GIAKVAVKKN DDGSEYLAIY YAGPIRSAGG TAQALSVLVG DYVRRILGMS RYMPREEEIE
RYIEEIRQYN SIMSLQYLPS EREIRLIISN CPVCIDGEPT EKEEVSGHRN LERVETNTVR
GGMALVIAEG LALKAPKVLK NVRKMKMDGW DWLEEMIQAT AGSSSSEEKE VGIHPKDKFL
RDLIGGRPVF SYPMREGGFR LVYGRSRNTG LAAAGLNPAT LHILGDFLAV GTQMKIERPG
KAAGISPVDS IQGPTVRLIN GDVVRIHDAK RARELSSQVS HIIDVGEILI SYGEFMENNH
VLVPSAYCES WWRLEGGTTR PADEDEAILQ CESGLYLHPD YLYLWDDLKP AEIRSLAEFI
HKHGTLADKT LILPLDPTIK EYLERVLCEH QVREGMIRIT PCRIVLKCLG LDSSLALSDS
WEKELPESAL DLVQFLSGMK MRSKAGTRIG GRMGRPGKSK PREMKPAPHV LFPVGEAGGS
RRSVQEASKF SYQANTEGGN LQLEMGVRRC PACGTESYKN RCSCGTHTEP VLSCSRCGIE
VQGPVCPQCG MEPTSVRQYT VNVRQMLQQA FADLGMRDRD VELVKGVKGL VSRNKPVELI
EKGVIRAANK LFVFKDGTVR FDIIDMPLTH FRPREIGVSV ERLRELGYLQ DIYGVPLQNP
DQVLELPPQD ILVPEGCGDY LFSCTRFIDT LLEKVYGLPP FYNLETRSDL VGHLVIGLAP
HTSAGVLARI IGFSKANVGY GHPFFHAAKR RNCFHGDTLI EIYADGILEE IPIRRFVLEH
LDLSQAGVDA LGTFYADPVR PAHVRSVDTG GIPHLRKITS VSVHKAPANL IQFSTSRGKN
LLVTPDHAML VWDVSYLRKI RALEVKIGDA VPVWESGVVI SDRIVSIDYV PCEDERVYCL
TVDRDHNVVG NGIFTGQCDG DEDCVMLLLD GLINFSRSFL PVTRGGSMDA PLVLTSRIDP
TEIDKESHNL DVCATYPIEV YETALRYGNA KDVESLVDRV ERRLNTPAQI EGFFFTHDTS
DISAGPLETM YTQLQSMLDK LDCELSLAKR IRAVDEHDVA ERVLKTHFIR DLQGNLSAFS
KQKFRCTKCN TSYRRMPLAG KCKCGGNIIP TVHEGSVKKY LQMSRQICEE YNITEYTRQR
IEVIDMNIES TFGEEKVEQM GLADFM
