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Database: UniProt
Entry: K8Z9S8_9ENTE
LinkDB: K8Z9S8_9ENTE
Original site: K8Z9S8_9ENTE 
ID   K8Z9S8_9ENTE            Unreviewed;       872 AA.
AC   K8Z9S8;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=C683_0274 {ECO:0000313|EMBL:EKU27809.1};
OS   Catellicoccus marimammalium M35/04/3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Catellicoccus.
OX   NCBI_TaxID=1234409 {ECO:0000313|EMBL:EKU27809.1, ECO:0000313|Proteomes:UP000016057};
RN   [1] {ECO:0000313|EMBL:EKU27809.1, ECO:0000313|Proteomes:UP000016057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M35/04/3 {ECO:0000313|EMBL:EKU27809.1,
RC   ECO:0000313|Proteomes:UP000016057};
RX   PubMed=23405330;
RA   Weigand M.R., Ryu H., Bozcek L., Konstantinidis K.T., Santo Domingo J.W.;
RT   "Draft Genome Sequence of Catellicoccus marimammalium, a Novel Species
RT   Commonly Found in Gull Feces.";
RL   Genome Announc. 1:E00019-12(2013).
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, 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:EKU27809.1}.
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DR   EMBL; AMYT01000008; EKU27809.1; -; Genomic_DNA.
DR   RefSeq; WP_009488548.1; NZ_AMYT01000008.1.
DR   AlphaFoldDB; K8Z9S8; -.
DR   STRING; 1234409.C683_0274; -.
DR   PATRIC; fig|1234409.3.peg.245; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000016057; 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; 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; 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   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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016057};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          3..264
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          299..462
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          628..836
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   872 AA;  99833 MW;  FEC34BD90D034E1C CRC64;
     MSKKVVLIDG SSLSYRAFYA LGKQVDRFVN HEGLHTNAIY SFKLMLDALL EKEKPDYWLV
     AFDKSKKTFR HEQFSEYKAG RKKTPPEFLE QLPYIKELIA DQGGTVYELE GYEADDIIGT
     MAQKASQEEV VIYTGDRDLF QLVTDHVTVK WTKKGVKEVE VYTPEAIFEK YQLAPKQIID
     LKGLAGDTSD NIPGVTKVGE KTAIKLLTQY HSVENLYEHI DELKKSKMKE HLITDKEQAF
     LSKELATIET NAPIALSLED IKTKPVATEA LIELYEKLDF KQFLKAMDRP KVAVEKTQYQ
     WVDQVTAEMF HENQVVHLEL FEENYHTATP IGLAWGDQET IYVGKPDLIK EEVFQQFLAN
     DEKKWFFDVK KHWVLAQKEG ITLGEKVEDI YLGSYLLDTL NDSSDVESLT EYYDVSRVAN
     EEEIYGKGAK RAIPEEEILS SHLANKVKAF AEIVPKMRAQ LEEKNQMALY ETMEVPLAFV
     LAKMEYRGIK VDVEQLKAQE AELGAQIKEI EEKIYAEAGH SFNLNSPKQL GEVLFDELGL
     PVLKRTKTGY STSVDVLEKL EPDYPIVRDI LTYRQWSKLQ STYVTGLLKQ VHADGKVHTR
     YMQGLTQTGR LSSVDPNLQN IPVRMEEGKR IRKAFVPENP DWYILTSDYS QIELRVLASI
     CQDASLEQAF RDGEDIHDST ARRIFHLLPG EEVTPKMRRE AKAVNFGVVY GISDYGLSEN
     LGITRKEAKA FIDQYFHHYP GVKRYMDAIV EKAKEDGYVE TLFARRRYLP DIHSRNFNVR
     SFAERTAINS PIQGSAADIL KIAMNKMAKE LENSNYRAHL LLQVHDEVIL EVHPEDLEAV
     QALVEKTMDE AVKLSVPLVT DSSYGKTWYD AK
//
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