ID A0A221R4Q2_9MICC Unreviewed; 923 AA.
AC A0A221R4Q2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=CGQ25_07180 {ECO:0000313|EMBL:ASN51879.1};
OS Sinomonas sp. R1AF57.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=2020377 {ECO:0000313|EMBL:ASN51879.1, ECO:0000313|Proteomes:UP000199767};
RN [1] {ECO:0000313|EMBL:ASN51879.1, ECO:0000313|Proteomes:UP000199767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1AF57 {ECO:0000313|EMBL:ASN51879.1,
RC ECO:0000313|Proteomes:UP000199767};
RA Sastre D.E., Santos L., Kagohara E., Andrade L.H.;
RT "Draft Genome Sequence of Sinomonas sp., Isolated from Brazilian Amazon
RT Soils with Potential for Applications in Biocatalysis.";
RL Submitted (JUL-2017) 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}.
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DR EMBL; CP022463; ASN51879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221R4Q2; -.
DR Proteomes; UP000199767; Chromosome.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
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; cd06140; DNA_polA_I_Bacillus_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; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
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 PRINTS; PR00868; DNAPOLI.
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.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000199767};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 30..293
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 679..886
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 98903 MW; A29A1EAB3DCB83C6 CRC64;
MATRLAPVTE TSKTLPARVP TSTAGGPGAG RPRLLVLDGH SMAFRAFFAL PAESFVNAEG
QHTNAIHGFT SMLINLVRDQ EPTHVAVAFD VSDETTHRRT EYSEYKAGRN ATPAEFSGQI
DYIKKVMAAL GIRTLELPGH EADDILATLA AQGAAAGFEV LLVSGDRDTF QLVNDHVSVL
YPRKGVSDIP RMDAAAIEEK YFVPPARYPD LAALVGESAD NLPGVPGVGP KTAAKWITQY
DGIEGVLEHA GEIKGKAGES LRANLESVER NRRLNRLLTD LELPLTLDDL ADPRPERAAV
EALFDELEFK ALRTRVYDVF GTEGPVAGED EFHVPPHTVP ADDDALAASL AALAEGAAAA
GGRPVAVAVR TDGGTPRPAA ESVALATKEA AVVVPLDGAL PCPLVAWLAD PAVPKAMAEY
KEGAKALRAL GAEVEGVVDD VSISGYLAEP DRRSYALADL AQHHLGIELA AGAPTAGQLA
LDLAGAEAAA AAMARQAAVV RALHDELAPQ LTELGAAALL QDMELPLSRV LLDMEWAGIT
VDVPQIDALM DELGATSEAA AEAAYAAIGH KVNLGSPKQL QAVLFEELEL PKTKKIKTGY
TTDAASLKEL LDKTGHPFLA SLMAHRESSK LRQMVETLKK AVTKDGRIHT TYAQTIAATG
RLSSNNPNLQ NIPIRSEEGR RVRDVFVAGE GYESLLSADY SQIEMRIMAH LSGDEGLIEA
YRSGEDLHRF VGSRIFHVAP ADVTSEMRSK VKAMSYGLAY GLSSFGLSKQ LEISVDEART
LMKDYFDRFG AVRDYLRGVV EQARQDGFTQ TIFGRRRYLP DLTSPNRVHR ELAERIALNS
PIQGSAADII KRAMIGVEGQ LKERGLGSRL LLQIHDELVV EVAPGEEAAV REVVEQEMGS
AADLSVPLDV QIGVGRTWNE AGH
//
