ID Q31JN2_HYDCU Unreviewed; 939 AA.
AC Q31JN2;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 126.
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 OrderedLocusNames=Tcr_0044 {ECO:0000313|EMBL:ABB40641.1};
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025 {ECO:0000313|EMBL:ABB40641.1};
RN [1] {ECO:0000313|EMBL:ABB40641.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XCL-2 {ECO:0000313|EMBL:ABB40641.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Scott K.M., Sievert S., Kerfeld C.,
RA Freyermuth S., Dobrinski K., Boller A., Fitzpatrick K., Thoma P., Moore J.,
RA Richardson P.;
RT "Complete sequence of Thiomicrospira crunogena XCL-2.";
RL Submitted (JUL-2006) 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 -!- 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; CP000109; ABB40641.1; -; Genomic_DNA.
DR AlphaFoldDB; Q31JN2; -.
DR STRING; 317025.Tcr_0044; -.
DR KEGG; tcx:Tcr_0044; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_6; -.
DR OrthoDB; 9806424at2; -.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 12..266
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 333..527
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 697..903
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 297..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..283
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 301..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 105413 MW; C732A7684BEA8435 CRC64;
MTQILPEFNP DSPFILVDGS SYLFRAFHAM PPLTNTKGHA TGAIFGVINM IGKLLEQYQP
ERIAVVFDAK GKNFRHELYE DYKAHRPPMP DELRIQIEPI HEIIKALGIP LLVIDGVEAD
DVMGTLAHQA TQAKMDALLS TGDKDMAQLV NEHITLVNTM NDTLMTPDSV FEKFHVKPEQ
IIDYLALMGD SSDNIPGIPK CGPKTAAKWI SEYGSIDNLI EHAEEIKGKI GENLRANLEQ
LKLSQQLTTI RLDCDLPIAL NDIKRHEADM EALEALFSEY DLRNWLTRVL KGELPFSKSS
GRKAHSETVT NGQSKKANTS PSTETPKADS QPYETIVDWH TFDQWLKKLE ASDVFAIDTE
TTSLNAMEAK IVGVSFAYAE KKDQAWQNFA AYVPLTHDYD GAPEQLPIQE VLAKLKPLLE
NPAIKKVGQN FKYDWHIFKN AGIEVQGMAY DTMLESYCFN SVATRHNMDD LALTYLNHST
IHFKDIAGTG KKQKTFNQIE LETASPYAAE DADITLQLHQ TLLPKLQAEP TLYKVFEEIE
MPLMPVLAKM ERNGVLIDRQ MLADQSYELG QKLTELEQKA HLIAGTPFNL NSSKQLQEVL
FERLELPIVK KTPKGQPSTA EPVLVQLAED GHEMPNLILE YRSLAKLKST YTDSLPKQIN
QQTGRVHTSY QQAVASTGRL SSTEPNLQNI PIRSAEGRRI RQAFIAQPGY RLMASDYSQI
ELRIMAHLSG DASLLKAFAE GKDIHQATAA EIFNMPLEEV TSEQRRSAKA VNFGLIYGMS
AFGLAKQLNI SRGLAQEYIN LYFARYPGVA NYMESTKENA KQTGYVETLM GRRLYLPDIN
AKNGQLRQYA ERTAINAPMQ GTAADIIKTA MVKMQQWLDQ TPCDIKMLMQ VHDELVFEVA
EADMDQARKE IKTIMEAALK LDVPLIVEIG DGLNWDEAH
//
