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Database: UniProt
Entry: A0A2E9CCN4_9ARCH
LinkDB: A0A2E9CCN4_9ARCH
Original site: A0A2E9CCN4_9ARCH 
ID   A0A2E9CCN4_9ARCH        Unreviewed;       911 AA.
AC   A0A2E9CCN4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=CME83_00040 {ECO:0000313|EMBL:MBS84941.1};
OS   Candidatus Heimdallarchaeota archaeon.
OC   Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX   NCBI_TaxID=2026747 {ECO:0000313|EMBL:MBS84941.1, ECO:0000313|Proteomes:UP000228988};
RN   [1] {ECO:0000313|Proteomes:UP000228988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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,
CC         ECO:0000256|RuleBase:RU000442};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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:MBS84941.1}.
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DR   EMBL; PBWW01000001; MBS84941.1; -; Genomic_DNA.
DR   Proteomes; UP000228988; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10322:SF20; DNA POLYMERASE 1; 1.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          103..356
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          471..840
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   911 AA;  103906 MW;  3F2FA33D7FD0C2EA CRC64;
     MINVSLEDFF ETTPPPKKPP KEKVVINEKK ELNTFNPPIT PQFPDYFTPK PIKNEKNIDN
     LFLLDVQYNG KLNLAQLIFY HEETQSLYYW NDNTNHKPYL ITMLSEESIN SIDQVVKSKD
     YLKIEKTSKY LPIEEQDMEV IKVYGDNPLA IGGSGTSFRN FLNPSFEADI RYHFNYVADK
     QLTPATYYKI ENGELKQIDQ NIGSIKNELE IEFKDENEEE KEMLNEYMPL LFQKMPDVTR
     CAYDIEIGSD KNRLPNITTT PDPIISIALV DNLGRKICWV LKRPEVDQPF NQIEDKSVNV
     LLYDSELDLL VDFFHIVDQX PIALSFNGDN FDNPYLINXA KKLGLDYNXX PIKQKGRSDT
     TFNNSIHVDL YLFXRQASIR LXAFGGKXER SSLQELSSSL XGEGKIDHPE VWINEMDLKT
     LVKYNVKDAE LTLQLTQFDN NVVLDLIFIL MRICKMPIFD FIRTAVSGWL KMWLIYEHRK
     RNFLIPRKED ILSAKGAAPT SDAIIEGKKF QGAIVLDPKP GVWWNVHVLD FASLYPSIIK
     TRNLSYETIL CNHEDCSDNV VPEVGHNICT KRVGLFAIVL GFVRDTRVKW FKPRSSDSNL
     PELERRNNDV IQSSLKVLIN AGYGVFGSDT FDFYCPPVAE STTAYARDAI KSTKNYVENT
     LGVDVLYGDT DSVFLYGPTE EQISKLLDWG LENIGVELGT DYVFRYVVFS DRKKNYFGIT
     TNGNIIVKGL MGKKSNTPQI IRKTFTNVLN ILKNVNNPDE FPIAREQIVN TLKQMVNKLE
     TGNFTPEDIS VRITLSKKLS DYSTWTQTVQ AAAQLLGDDN FNEEITVGST IEYIKLKTPK
     RIVVPNHKDL AFPSGESQKV SVKPVLLIKE GEKLDGKPVI EAAESTFSQI LSSIGSSWND
     VMGVMSLDDF F
//
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