ID M1Z0G9_NITG3 Unreviewed; 900 AA.
AC M1Z0G9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 ECO:0000313|EMBL:CCQ91195.1};
GN ORFNames=NITGR_590074 {ECO:0000313|EMBL:CCQ91195.1};
OS Nitrospina gracilis (strain 3/211).
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Nitrospina.
OX NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ91195.1, ECO:0000313|Proteomes:UP000011704};
RN [1] {ECO:0000313|EMBL:CCQ91195.1, ECO:0000313|Proteomes:UP000011704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3/211 {ECO:0000313|EMBL:CCQ91195.1,
RC ECO:0000313|Proteomes:UP000011704};
RX PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT of the major marine nitrite oxidizer.";
RL Front. Microbiol. 4:27-27(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 -!- 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:CCQ91195.1}.
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DR EMBL; CAQJ01000065; CCQ91195.1; -; Genomic_DNA.
DR RefSeq; WP_005009565.1; NZ_HG422173.1.
DR AlphaFoldDB; M1Z0G9; -.
DR STRING; 1266370.NITGR_590074; -.
DR HOGENOM; CLU_004675_0_0_0; -.
DR InParanoid; M1Z0G9; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000011704; 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; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000011704};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 5..261
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 305..492
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 658..864
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT COILED 522..549
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 900 AA; 101975 MW; 0BB3FEC18F265CC3 CRC64;
MASKKKLYLI DGSSYIFRAF FGIRHNLSNS KGQPTNALYG FTTMLMKVVR EEQPDYLAVV
FDSKEKTFRH DMYADYKANR DVPPEDLAVQ FPYFEPLVDA FNIKSLRKPG YEADDIIGTL
AREGEKAGMD VTIVSGDKDM MQLITDKIHM LDTMKEKRFG IDDVKEKFGV EPERVIEVMG
LMGDSSDHIP GVKGVGPKTA TDLIQKYGSI QGLYEHLDEI DKAKLKEKLE TDKDNALLSR
ELVTIKLDTP LDCKIEDLEA RDPDNNKLRE LFTDLEFKTL LAALPEGEGH DGAASASGSE
IKRDYDTILD DTALDDLIKK LKKAKAFALD LETTSKRPVK AKMVGISFSW AEGEACYIPV
AHRYLGVPEQ LDKQHVLDKL KPLLEDPKLE KYGHNIKYDL IVLHNEGVQL QGIVFDSMLA
SYVLDPSRRS HSLDDLALET FQHTTIKYSD VAGSASKQVG FDEVEIERAS EYAAEDSDVT
YRLTRHFEKQ LKGEDLELYE TIELPLLEVL AEMELTGVLL DTDHLKKLSK KLEKDLKKIE
DEIYALAGEP FNINSPKQLS TILFDKLNLR TVKKTKSGYS TDVSVLEELA AEHDLPDKIL
NYRQFAKMKS TYVDALQGEV FKETGRIHTS YNQTVAATGR LSSSDPNLQN IPIRSEVGRE
IRKAFLADKG CWLLSADYSQ IELRLLAHLS GDPALIRAFK NNEDIHSRTA AEIFGQPIDQ
VDPEGRRMAK AVNFGIVYGL SAYGLSRQLK ITPKEAKTFI DQYFDLYKNV KTFMDETIEM
ARHNGYTKTM MNRRRYMPDI NSKNRQVREA AERTAINSPV QGSAADYIKM AMLHIHDKML
KEKLESRMIL QVHDELIFEC PEGEKKTMEP LVKKAMEGVA KLKVPLTVNM DWGENWSDAH
//
