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Database: UniProt
Entry: A8L1T2_FRASN
LinkDB: A8L1T2_FRASN
Original site: A8L1T2_FRASN 
ID   A8L1T2_FRASN            Unreviewed;       673 AA.
AC   A8L1T2;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=DNA-directed DNA polymerase {ECO:0000313|EMBL:ABW13154.1};
GN   ORFNames=Franean1_3759 {ECO:0000313|EMBL:ABW13154.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW13154.1};
RN   [1] {ECO:0000313|EMBL:ABW13154.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW13154.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA   Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT   "Complete sequence of Frankia sp. EAN1pec.";
RL   Submitted (AUG-2007) 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-A family.
CC       {ECO:0000256|ARBA:ARBA00007705}.
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DR   EMBL; CP000820; ABW13154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8L1T2; -.
DR   STRING; 298653.Franean1_3759; -.
DR   KEGG; fre:Franean1_3759; -.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_035229_0_0_11; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF00476; DNA_pol_A; 2.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE   3: Inferred from homology;
KW   DNA-directed DNA polymerase {ECO:0000313|EMBL:ABW13154.1};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ABW13154.1};
KW   Transferase {ECO:0000313|EMBL:ABW13154.1}.
FT   DOMAIN          431..631
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          113..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  68515 MW;  32A315120D6F4E90 CRC64;
     MVPTSRPVGT PAAAGAGSGA AAGSGAAAGA GAGAVAALRA AGVGRGGLVA VVPVSDVAVA
     LACAGAVWAQ PADPAAVLAE VECALAPRWV WWSAHSTGAL LTRSGASTIA GPRTGSGAYA
     GPGTHAGPGA GTGPGRSPIP AVCWDLAAAH RVLYGGHRDD PAAVWAGARG LPLPPPPPRP
     RADGQLDLLA LVDHPGGPGD GEADDPIGPD GQLRPGWAEE TLRGAGPGGT GAQLARATRL
     AQLALTVTAA QDEALRALPD PRARPAGLPL AVLTARAESG AELLARELRR DGLPVDRPTA
     EATIAAAVGP RPDGDAAGAA ARQARDAPVL RHLGTSVDLR NPVAVRSALA AVGIDVPDTR
     SGRLSALRGV HPVVEALLAW RKAERIATTY GYRWLDTHVG ADGRLRGEWR GSDGAAGRMT
     AAAGLHNLPA DLRVVVIAEP GYRFVRADLG QIEPRVLAVV SGDPELTRAT RQDDLYAPVA
     ASLGVDRPTA KVAVLAAMYG QTTGVAGQAL RQMRETYPVA LAYLDAADAT GRAAALGRPP
     PNPPVTDPQA RLRTFGGRRV PLRFAAVDDG ADENRVGMTW GRFARNAVVQ GAAAELFKAW
     AVTVRQAIAP LGGAIVLCLH DELLLHVPAP RAEAAAEATR RALDATVGYW AAGSGVRFVV
     DIAVVRRWSD AKA
//
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