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Database: UniProt
Entry: A0A1F8PZ26_9CHLR
LinkDB: A0A1F8PZ26_9CHLR
Original site: A0A1F8PZ26_9CHLR 
ID   A0A1F8PZ26_9CHLR        Unreviewed;       840 AA.
AC   A0A1F8PZ26;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-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=A2Z16_09210 {ECO:0000313|EMBL:OGO28420.1};
OS   Chloroflexi bacterium RBG_16_54_18.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797648 {ECO:0000313|EMBL:OGO28420.1, ECO:0000313|Proteomes:UP000177170};
RN   [1] {ECO:0000313|EMBL:OGO28420.1, ECO:0000313|Proteomes:UP000177170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGO28420.1}.
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DR   EMBL; MGNP01000131; OGO28420.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8PZ26; -.
DR   STRING; 1797648.A2Z16_09210; -.
DR   Proteomes; UP000177170; 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; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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; 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; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 2.
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          342..561
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          627..754
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   REGION          409..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   840 AA;  93055 MW;  4F88ECF76774B75A CRC64;
     MKQVCGWLLD VYPDLGGGKQ GRRGLLLWLL GEDGQRYCLR QTFPITFYAA GPPARLEALR
     LFIESQPGGA PVTLFQTERK ELFSQRPLQV LAVQVDTVAS QALLFNRISQ AFPDLTYFDT
     DIPLPLRHAA RFGTFPLARC AAAVDAQDTI QELQVLDSPW ELDPLEPPLR ILRMEPDPGP
     VPAMPGPHAG GRPPTHLLLH TGQQGTLRLA LQPERPLLVN LRALLTRLDP DLLLTAAGDT
     WMLPYLLERA RTARLPLPLN RDPVRQPAHR PERSYFSYGQ VIYRGRQVHL FGRWHIDRGN
     AMLWDDYDLQ GVLEVARVTG LPVQTAARVS PGTGISSMQI LTALRNEILV PWHKQQAETP
     KTALQMFAAD QGGLVYQPLV GLHHDVGEID FVSMYPGIMV HFNISPETVR SHGPSWQSQG
     SSTPDRSLTP FPQPDPAPGE TSTPAVALPA DELLKTPPPL PAAGDDPDDQ LGLIPKTLSP
     LLDKRLALKA HLAAMRTDPS QRWDPRCRAY EARASAHKWL LVTCFGYLGY KNARFGRIEA
     HEAVTAYGRE ALLRAKEAAE DLGFTVLHLY VDGLWVKKPG ASRVADFQPL LDAISERTGL
     PIALDGVYRW VAFVSSRIDA RWPVPNRYFG VFQDGSLKVR GIEARRDDTP PFITEVQMQL
     LELLAKQTAA GTSQTGEAPT YDLAPALDLL RRKLAALRQG RVPLHELVVN QRLSQEIEAY
     RQPSAAARAA MQLQSLGSSF RPGQRVRFLY TLGKPGVAAW DLPPYPAALD LKRYTRLLLR
     AAHAALGPFG VSEAQLGQLV TDLPARQLKF SQEVLATRLK NYIVNQKNQI PPSGAAESPR
//
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