UniProt: M5DYC9

Database: UniProt
Entry: M5DYC9_9FIRM

LinkDB:  M5DYC9_9FIRM 
Original site:  M5DYC9_9FIRM

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (13)   
   Pfam (3)   
   PROSITE (1)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (29)   

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ID   M5DYC9_9FIRM            Unreviewed;       880 AA.
AC   M5DYC9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
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=HSACCH_00329 {ECO:0000313|EMBL:CCU78006.1};
OS   Halanaerobium saccharolyticum subsp. saccharolyticum DSM 6643.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=1293054 {ECO:0000313|EMBL:CCU78006.1, ECO:0000313|Proteomes:UP000012063};
RN   [1] {ECO:0000313|Proteomes:UP000012063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6643 {ECO:0000313|Proteomes:UP000012063};
RX   PubMed=23640197; DOI=10.1128/genomea.00187-13;
RA   Kivisto A., Larjo A., Ciranna A., Santala V., Roos C., Karp M.;
RT   "Genome Sequence of Halanaerobium saccharolyticum subsp. saccharolyticum
RT   Strain DSM 6643T, a Halophilic Hydrogen-Producing Bacterium.";
RL   Genome Announc. 1:217-225(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|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:CCU78006.1}.
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DR   EMBL; CAUI01000005; CCU78006.1; -; Genomic_DNA.
DR   RefSeq; WP_005487356.1; NZ_CAUI01000005.1.
DR   AlphaFoldDB; M5DYC9; -.
DR   STRING; 1293054.HSACCH_00329; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   InParanoid; M5DYC9; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000012063; Unassembled WGS sequence.
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:UP000012063};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          9..269
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          629..836
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   880 AA;  101338 MW;  391F707EFC70F3A4 CRC64;
     MSNKENKEKK TLFLLDGHSL THRAFYALPL LTNDDGEYTN AVFGFIRMLF SLNDEWNPDR
     MIITFDKKAP TFRHEEYEDY KGNRKKMPEE LVPQIPLLQQ TIEKLKIPMM AKEGYEADDL
     LGTLSKEAEE DGYKVYIVTG DRDALQLVSE NVNVLYTRKG ISDLVKFDLD KVMEKYELTP
     EKLIDRKGLM GDSSDNIPGV PGIGKKTALK LLKEFGTMEE ILANIDKVSG KKRKENLHKY
     ADQARMSYRL GKIKRDVPID INFDKCRLDL YDDQEAAEQF EKLGFTSLLD RFDFKEEANF
     EDLEIEELKE SDLKDFKEKI IKAGKIAVAL KLEKGNKAIS GKIEEFIFSI ENEDKIYLYY
     PEDKINLEIK EILESERIEK IMLNAKEVSL SLLNHQIEIL NISFEPLLAY YLLQPSSSLP
     EVEEVFSHKL TISFDQLETE KKEAVKISKL FELKEKLLPE LEKNNLLKLY QEIELPLIKV
     LARMEYNGVK VDKKWLNSLS ERLGKRLDII VDKAHELAGE EFNLNSPKQL GEILFEKLGL
     PVIKRTKTGY STNASVLEKL EGKHEIIPLI SEYRELAKLK STYIDSLPPL INEETGKIHT
     SFNQMVTATG RLSSTDPNLQ NIPIRTEEGR EIRKAFIPSR EEMILLAVDY SQIELRVFAH
     LSGDEKLKEA FNSGADIHTE TAAEVFEVAP EEVSPNLRRH AKVINFGIAY GMSAYGLSQD
     LDIPVEEAQE YIDKYFERFS GVKEYMDQTI TKVKECGYAE TMFGRRRYIP EINSSNYHRR
     SFAERTAVNT PIQGTAADIM KKSMLDVYDA LKEADFDLNI LLQVHDELVF EVNKNQLDQA
     AKLIKEKMEN TTKLDVPLLV DLQIGENWRD KEDYEVNYNA
//

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