ID A0A164B3A6_9SYNE Unreviewed; 1004 AA.
AC A0A164B3A6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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_2 {ECO:0000313|EMBL:KZR88165.1};
GN Synonyms=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=MITS9508_02308 {ECO:0000313|EMBL:KZR88165.1};
OS Synechococcus sp. MIT S9508.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR88165.1, ECO:0000313|Proteomes:UP000076799};
RN [1] {ECO:0000313|EMBL:KZR88165.1, ECO:0000313|Proteomes:UP000076799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR88165.1,
RC ECO:0000313|Proteomes:UP000076799};
RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KZR88165.1}.
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DR EMBL; LVHU01000012; KZR88165.1; -; Genomic_DNA.
DR RefSeq; WP_067097664.1; NZ_LVHU01000012.1.
DR AlphaFoldDB; A0A164B3A6; -.
DR STRING; 1801629.MITS9508_02308; -.
DR PATRIC; fig|1801629.3.peg.2471; -.
DR Proteomes; UP000076799; 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 6..289
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 373..575
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 746..968
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 337..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1004 AA; 109632 MW; 9EDE7E59C8FB06A2 CRC64;
MPQTKEKPLL LLVDGHSLAF RSFYAFSKGG EGGLATKDGR PTSVTYGFLK ALLDNCKGLK
PQGVAIAFDT AEPTFRHKAD PNYKAHRDVA PDVFFQDLDQ LQLILRNQLQ LPLCLAPGFE
ADDVLGTLAN RAASSGWRVR ILSGDRDLFQ LVDDQRDIAV MYMGGGPYAK SSGPTLIDEA
GVQFKLGVMP DKVVDLKALT GDSSDNIPGV KGVGPKTAIN LLKENVDLDG VYKVLAEVEA
EGPKARRGAV KGALKGKLSA DRDNAYLSRQ LAEILVDIPL PEEPILELGP VDGDGLEVQL
KDLELNSLVR QVPGFIATFS TGGLAANAHL LETKVSKDSA QADRSKDAAT QQQDAPDAFS
QDSTASSQPN LKPQLICSDA ALHDLMQRLQ SCTDATAPVA LDTETTDLNP FKAQLVGIGV
CWGPGDADLA YIPVGHRAAT EATLEPDRPL VQLPLETVFE QMAPWLASPE HPKALQNAKY
DRLILLRHGL PLAGVAMDTL LADYLRDAAA KHGLDAMATR MYGITPTLFS DLVGKPKDGK
ASCFAEVDLD QAALYCGMDV HLTRRLAIDL RQQLQATGES LPSLLDNVEL PLEPVLALME
ATGIRIDMPY LSALSTEMGD ILQRLEKEAK EAAGTDFNLA SPKQLGELLF NTLGLDRKKS
RRTKTGYSTD ATVLEKLEAD HPVVPLVLEH RVLSKLKSTY VDALPQLVEA ETGRVHTDFN
QAVTATGRLS SSNPNLQNIP VRTDYSRRIR KAFLPQENWT LLSADYSQIE LRILTHLSGE
EVLQQAYREG DDVHALTARL LLDKAEVNSD ERRLGKTINF GVIYGMGAQR FARETGVNQA
EAKDFLLRYR ERYPKVFSFL ELQERLALSR GYVETIMGRR RPFHFDRNGL GRLLGKEPME
IDLDVARRGG MEAQQLRAAA NAPIQGSSAD IIKLAMIQLQ AAIEQQGLPA RLLLQVHDEL
VLEVDPDALE SIQKLVVNTM ENAVTLSVPL VAETGLGANW MDAK
//
