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   27-MAR-2024, entry version 97.
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};
GN   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}.
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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   InParanoid; Q2FSF9; -.
DR   OrthoDB; 7529at2157; -.
DR   Proteomes; UP000001941; Chromosome.
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   NCBIfam; TIGR00354; polC; 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   PIRSF; PIRSF016275; PolC_DP2; 1.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 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
//