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Database: UniProt
Entry: K0BZB8_CYCSP
LinkDB: K0BZB8_CYCSP
Original site: K0BZB8_CYCSP 
ID   K0BZB8_CYCSP            Unreviewed;       905 AA.
AC   K0BZB8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
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=polI {ECO:0000313|EMBL:AFT66239.1};
GN   Synonyms=polA {ECO:0000256|RuleBase:RU004460};
GN   OrderedLocusNames=Q91_0199 {ECO:0000313|EMBL:AFT66239.1};
OS   Cycloclasticus sp. (strain P1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT66239.1, ECO:0000313|Proteomes:UP000006282};
RN   [1] {ECO:0000313|EMBL:AFT66239.1, ECO:0000313|Proteomes:UP000006282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1 {ECO:0000313|EMBL:AFT66239.1,
RC   ECO:0000313|Proteomes:UP000006282};
RX   PubMed=23144416; DOI=10.1128/JB.01837-12;
RA   Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT   "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus
RT   sp. strain P1.";
RL   J. Bacteriol. 194:6677-6677(2012).
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}.
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DR   EMBL; CP003230; AFT66239.1; -; Genomic_DNA.
DR   RefSeq; WP_015005011.1; NC_018697.1.
DR   AlphaFoldDB; K0BZB8; -.
DR   STRING; 385025.Q91_0199; -.
DR   KEGG; cyq:Q91_0199; -.
DR   PATRIC; fig|385025.3.peg.205; -.
DR   HOGENOM; CLU_004675_0_1_6; -.
DR   Proteomes; UP000006282; Chromosome.
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; 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   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.
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   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:UP000006282};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          3..258
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          307..494
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          663..869
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   905 AA;  100176 MW;  A9E3F768206EA059 CRC64;
     MAEKTLVLVD GSSYLFRAYH ALPLLTNSKG EYTNAILGVT NMLKKLVETY PEAYFGVIFD
     APGKTFRNDM YPEYKANRAS MPDELREQIK PLHQLIKAMG LPLVMEPGVE ADDVIGTLAK
     QAEEEDLNVV ISTGDKDIAQ LVTNKTSLIN TMNNQWLDEE GVKEKFGVSP DMIIDYLALM
     GDTSDNIPGV PKVGPKTAAK WLNAYGSLDE IIARADEVKG KVGESLRDHL DAIPLSKELV
     TIKCDVPLDK APADLIRTQP DTETLKEMVS HYEFNSWLKQ LGGTKASTVA SEQVDEKPLP
     AKTELTVETI LDEATFNQWL AKLTEAELFA FDTETTHLDY TKALVVGVSF AIEAGHAAYV
     PLAHSYPGAP QQLSRQWVLD QLKPLLESES ARKVGQNLKY DANVLANHGI SLAGICHDTM
     LQSYVLNSTA SRHNMDALAE KYLGQETIHY EDVAGKGAKQ ICFDQVSIEL AAPYAAEDAD
     ITLRLHQHIF PQLKQIDSLA TVYETIEMPL VPVLARMEQT GVLVDEQMLS QQSGELTASI
     KALETQAHEA AGQPFNLGSP KQIQEILYDK LGLPVLKKTP KGQPSTAESV LQDLAVDFPL
     PRLILEHRSL SKLRSTYTDK LPKQINPVTG RVHTSYHQAV AATGRLSSSD PNLQNIPVRS
     EEGRRIRQAF IAEEGFTVMA ADYSQIELRI MAHLSQDTGL LQAFKEGLDV HKATAAEVFG
     VPVDQVETHQ RRSAKAINFG LIYGMSAFGL AKQLDIDRGA AQGYINLYFE RYPGVKQYMD
     ETRELAREQG YIETLFGRRL YLPDILAKNG QRRQYAERTA INAPMQGTAA DIIKLAMLSV
     DNWLQVDKPA VRMVMQVHDE LVFEVENSYL DQAASIIQQK MSGAASLDVP LVVDVGMGKN
     WDEAH
//
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