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Database: UniProt
Entry: F4XJS3_9CYAN
LinkDB: F4XJS3_9CYAN
Original site: F4XJS3_9CYAN 
ID   F4XJS3_9CYAN            Unreviewed;       996 AA.
AC   F4XJS3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=LYNGBM3L_08270 {ECO:0000313|EMBL:EGJ35353.1};
OS   Moorena producens 3L.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Moorena.
OX   NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ35353.1, ECO:0000313|Proteomes:UP000003959};
RN   [1] {ECO:0000313|Proteomes:UP000003959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX   PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA   Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA   Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA   Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA   Gerwick W.H., Gerwick L.;
RT   "Genomic insights into the physiology and ecology of the marine filamentous
RT   cyanobacterium Lyngbya majuscula.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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:RU004460};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR   EMBL; GL890823; EGJ35353.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4XJS3; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_3; -.
DR   Proteomes; UP000003959; Unassembled WGS sequence.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
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:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR   CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 1.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   CDD; cd09859; PIN_53EXO; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR00593; pola; 1.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU004460};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU004460}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          22..294
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          383..569
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          739..960
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          335..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   996 AA;  111163 MW;  02E5F95FFF497F0E CRC64;
     MPRSTSSENS PPVPDDSPMV ASPLLILIDG HSLAFRSYFA FAKSRQGGLR TKTGIPTSVC
     FGFIKSLLEV MESENPNAIA IAFDTKEATF RQQADATYKA NRTETPEDFL PDVKNLQQLL
     QGLRIPVITS PGYEADDVLA TLAHQAIDQG YRVKVVSGDR DLFQLVAPDK GITVLYLSGP
     FSRGSATVGP TEYGLEEVEA KLGVLPSQVV DYKALCGDPS DNIPGVKGIG AKTAVKLLKE
     YQNLDNIYAS LDTIKGAVKK KLEVGKSDAE HARYLAQLRF DTPIDIDLDQ CQLQGFDPQV
     LKPLLERLEL KSFISQIDKL QQRFGGVVLE DIETSAPNDT VSDTVSNTDS DTDTQEDDDI
     SFFSVAETEE FQEQGSNTGS IQPQIIDTVD KLNQLVEQLK YYTDAGNPVA WDTETSDLEP
     RDAQLVGIGC CWGKEFTDVA YIPIGHKDGT NLDKDIVLES LRPILESSDY PKVLQNSKFD
     RLVLRCNGIQ LAGVVFDTML ASYVLNPETS HKLSDLGLHY LGIEAQSYND LVPKGKTIRD
     LDIPTVADYC GMDAYTTFGI VFKLREELEQ IPALQQLLLE VEQPLEPVLA EMEYQGIRID
     KDYLQQFSQE LEKDLVAIKQ QAYQDAGEEF NLGSPKQLSQ LLFEKLGLDR RKSRKTKTGY
     STDATILAKL QGDHPVVDAI VEYRSLSKLK STYVDALPAL MRSDTKRVHT DFNQTVTTTG
     RLSSSSPNLQ NIPIRTDFSR QIRKGFIPES GWLLVSADYS QIELRILAHL SQEPVLVEAY
     QTQADVHTLT AQMLFDKEDI TAEERRLGKI INFGVIYGMG AQRFAREAKV STAEGKEFID
     RLNQRYPLVF AYLEETKKKA IAQGYVETIL GRRRYFSFGG NSLRRLQGKP LDQIDLDKLK
     SINPYDAGSL RAAANSPIQG SSADIIKIAM IKLYQELQKY KARLLLQVHD ELIFEIPPDE
     WEELQLKIRE TMESAVELTV PLVVEIHAGD NWMEAK
//
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