ID A0A222X8M3_9CELL Unreviewed; 935 AA.
AC A0A222X8M3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=CBP52_05080 {ECO:0000313|EMBL:ASR54598.1};
OS Cellulomonas sp. PSBB021.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2003551 {ECO:0000313|EMBL:ASR54598.1, ECO:0000313|Proteomes:UP000214627};
RN [1] {ECO:0000313|EMBL:ASR54598.1, ECO:0000313|Proteomes:UP000214627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB021 {ECO:0000313|EMBL:ASR54598.1,
RC ECO:0000313|Proteomes:UP000214627};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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; CP021430; ASR54598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222X8M3; -.
DR KEGG; cez:CBP52_05080; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000214627; 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; 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.
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|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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 40..300
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 685..892
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 101361 MW; 72C068F153467C4E CRC64;
MADRLAPVSE GHRDVDREVG PGVGRDVDQD GRGGQRQEPA RLLLIDGHSM AYRAFFALPV
ENFATSSGQP TNAVFGFTSM LANLLRDEQP THVAVAFDLG RTTFRTEQYE AYKGTRDATP
EPFRGQVDVI RRVLEPLHIP VLTKERFEAD DVLATLATQA TAQGMHVLIC TGDRDAFQLV
RDDVTVLYPV RGVSELARMT PEAVAAKYGV PPERYSDLAA LVGETSDNLP GVPGVGPKTA
AKWLTQYDGL EGVVAAADRI TGKAGESLRA NLAQVQLNRQ LNQLVTDLEL PMGPEDLEAR
PWDRQALHSI LDELEFRTLR DRLFAMLPDE SSTSAVAVAA AALELAELAD GALEGWLAER
SDAVLGLDVR GSGAPAGGDA WGVAIADAEG RAAVVDLAEV SPADEHALAA WLADEARGKA
VHGAKVAAHA LRGRGLTLAG VRADTELAAY LCQPDRRAYD LPDLAIGYLH RELGEDDAAT
GGQGALDLEL DGTGEDRRAA VRAAAVRDLA DVLESEVEDR GAAHLLRDVE LPLQAVLVRM
EGTGIAVDAD WLHHLEREFD GQVTRAAQEA YAVIGREVNL GSPKQLQEVL FDQLQMPKTK
RIKTGYTTDA AALTDLFART QHPFLEHLLA HRDAIRLRQT VEGLQRSVAP DGRIHTTFQQ
TIAATGRLSS TDPNLQNIPI RTEAGRQIRR AFVVGDGFET LLTADYSQIE MRIMAHLSGD
EGLIEAFRSG EDLHSYVGSR VFGVPTDEVT AAQRSKIKAM SYGLAYGLSS YGLSQQLSIE
VSEAAELMKD YFARFGGVRE YLTGVVDTAR ATGYTATVLD RRRYLPDLTS DNRQRREAAE
RMALNAPIQG SAADLIKLAM LGVDAELRRR RLDSRMLLQV HDELVLEVAA GEQDEVEALV
REQMAAADSA LPDGRLDVPL DVSVGVGSSW HEAGH
//
