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Database: UniProt
Entry: A0A219AKR3_9EURY
LinkDB: A0A219AKR3_9EURY
Original site: A0A219AKR3_9EURY 
ID   A0A219AKR3_9EURY        Unreviewed;       609 AA.
AC   A0A219AKR3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=BGI41_04235 {ECO:0000313|EMBL:OWT33090.1};
OS   Methanobrevibacter sp. 87.7.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=387957 {ECO:0000313|EMBL:OWT33090.1, ECO:0000313|Proteomes:UP000197485};
RN   [1] {ECO:0000313|EMBL:OWT33090.1, ECO:0000313|Proteomes:UP000197485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.7 {ECO:0000313|EMBL:OWT33090.1,
RC   ECO:0000313|Proteomes:UP000197485};
RA   Yeoman C., Mosoni P., White B.;
RT   "De novo assembly of methanobrevibacter sp 87.7.";
RL   Submitted (DEC-2016) 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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755}.
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:OWT33090.1}.
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DR   EMBL; MRCT01000061; OWT33090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A219AKR3; -.
DR   OrthoDB; 323192at2157; -.
DR   Proteomes; UP000197485; 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   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; 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; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA 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.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          65..319
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          395..596
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   REGION          414..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  71338 MW;  350ABAEF607C1A22 CRC64;
     MEREMIVLDI DYITEGEKPV IRLFGREPGE NPKRIIAFDN SFEPYFYIEA ENINQCLKDL
     EKYDTKNIEI VDKKDFQIPK KFIKITFTHP QEVPKYRDEI RELDSVIDIR EHDIPFYRRY
     LIDNNIVPMS LVSVKGDLIE SHESIDNNYD NLEILNLSEV PKSLNDTVSD FRIIAFDLEV
     YNPRGLPNSN VDEIIMIGLN SNFGIKKVLS TKTKVDADDS FIEKFDSEKQ MIEEFIRIIK
     DNQVDIIVGY NSDNFDFPYL NDRAKLYGID LDLSMDGSSI KFIKRGFTDA ASFKGLLHID
     LYFVMRRYMT LDRYTLERVY YELFGEEKKD VPGEIIWKYW DSNNEYLNEL FDYSLDDVVS
     TLMIAQQTLP LNLELTRIVG QPFFDITRMT TGQQAEWYLV KRAYDIDEII PNKPSAGDKS
     RTHDKNEGGF VKEPEPGLHE NLVQFDFRSL YPSIIISKNI CPDVLVTDKG NPLDTTDDAF
     PDEERYYVCP QHKHKFLKKP KGFIPSVIGD ILRERLRIKK QMKTSSNPTE KKVLNIQQLA
     IKRLINTMYG VYGYSRFRWY SFECAQAITA WGREYILYTI ESAKKYGFYA IYADTDGFYA
     EYRKDVNSN
//
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