ID N9UQ40_9SPHN Unreviewed; 937 AA.
AC N9UQ40;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=EBMC1_13928 {ECO:0000313|EMBL:ENY80469.1};
OS Sphingopyxis sp. MC1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY80469.1, ECO:0000313|Proteomes:UP000013072};
RN [1] {ECO:0000313|EMBL:ENY80469.1, ECO:0000313|Proteomes:UP000013072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|EMBL:ENY80469.1,
RC ECO:0000313|Proteomes:UP000013072};
RA Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L., Nielsen J.L.;
RT "Differential expression analysis of membrane associated proteins from
RT triclosan-degrading sphingopyxis.";
RL Submitted (FEB-2013) 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 -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541}.
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:ENY80469.1}.
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DR EMBL; AOUN01000014; ENY80469.1; -; Genomic_DNA.
DR RefSeq; WP_003048971.1; NZ_AOUN01000014.1.
DR AlphaFoldDB; N9UQ40; -.
DR PATRIC; fig|1174684.3.peg.2812; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR Proteomes; UP000013072; 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};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000013072};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 5..269
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 335..525
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 694..897
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 296..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 101916 MW; C5775D38009118BC CRC64;
MSQKNHLYLV DGSSYIFRAY HRLPPLTNPN GVPVGAVYGY TTMLWKLAKD LHDADGPTHL
AVILDHSSQS FRNEIYDQYK ANRPEPPEDL RPQFPLIRDA TRAFSLPCIE MEGYEADDLI
ASYAEAAVRE GWDVTIVSSD KDLMQLIREP ADGPHVDMLD TMKNVRLGID AVHEKFGVSP
DLVGDVLALM GDSVDNVPGV RGVGPKTATK LIQEYGNLTA ALDGAETMKA SKLRENLIEH
RAMAELSRVL VDLKRDCPLP DTLDSLKLDA IPPAPLKLFL DEHGFRSLSA KLDNGVAPGG
PPTLPRAGAA PAAAAPTGPT TPVLPAMPTI DRAAYECVTD LDALDRWIAA AKAAHVVAID
TETASLDSVT GELVGVSMAI APGQACYIPL GHGGTDMFAE KPHQIAMADA IARIGALFAD
DAVLKVGHNL KYDIGVLAQH GVRVAPYDDT LLMSFALDAG QHGHGLDELA KLHLDHVCLS
FKEVCGTGKS QISFAEVPLA RATEYAAEDA DVALRLWRLL KLRLPLEGGT RVYEMVDRPL
AGVVETMERA GIMVDRDYLA RLSGEFAQEM ARMETAIHAE AGQPFTIGSP KQLGEILFDK
LGLKGGRKGK SGDWSTDQNE LERLERDGVP IARMILEWRQ LAKLKSTYTD ALQQQINAKT
GRVHTSYSLV GAQTGRLSST DPNLQNIPIR SEIGRQIRDA FIAAPGHVLI AADYSQIELR
LAAHMADVPE LKEAFAQGQD IHAATAIELF GEVNRDTRAK AKTVNFSILY GISRWGLAGR
LEITPDEAQA LISRYFERFP GISDYIQGTL ERARERGYTE TLFGRKTWFP RIKAANQNER
QGSERAAINA PIQGTSADLI KRAMTRMPVA LAEAGLDEVK MLLQVHDELV FEAPEDKAEA
AGAVIRRVMA AAAEPVLTLS VPLEVEVGTG KSWGDAH
//
