ID A0A1W6LQ42_9BACT Unreviewed; 917 AA.
AC A0A1W6LQ42;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:ARN57887.1};
GN ORFNames=STSP1_02313 {ECO:0000313|EMBL:ARN57887.1};
OS Sedimentisphaera salicampi.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Sedimentisphaeraceae; Sedimentisphaera.
OX NCBI_TaxID=1941349 {ECO:0000313|EMBL:ARN57887.1, ECO:0000313|Proteomes:UP000193334};
RN [1] {ECO:0000313|Proteomes:UP000193334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-PulAB-D4 {ECO:0000313|Proteomes:UP000193334};
RA Spring S., Bunk B., Sproer C.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (APR-2017) 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 -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; CP021023; ARN57887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6LQ42; -.
DR STRING; 1941349.STSP1_02313; -.
DR KEGG; pbp:STSP1_02313; -.
DR Proteomes; UP000193334; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000193334};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 3..259
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 325..510
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 674..881
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 917 AA; 103206 MW; CE18B63BD9112D8F CRC64;
MPDKFYLIDG HALIYSSYFA PMRTNLSSPK GEPTKASYIF TTTLLGLINR KNPDMLAVAM
DSKEKSFRSD IFPEYKAQRP PMPEDMPQQI DRIEQILEAM KIPILRVEKY EADDIIGTLA
EKAAKEGIET YICSGDKDML QLIEENVFVH DIKKDSVKDL NWLETEKQMS PAQFLDALAL
MGDTADNIPG VPDVGPKTAE QWIRKYGSLE KLYENAGEIK GKRGNSLRES KEQAMLSREL
VEIKRDCPVE LRPKAFRLSE FDYDRLAEIF YELGFQRLYK SVGLEGKLDE LSTETKNQGT
SNKKQTALFD TDTEYDSMKD GKQNYKLAGS EEELEKLCRE LEKQEIFAID TETSSIEPMR
AELVGISISW KENEAYYIPV KAAGNDKTIG IEKVKEILGG ILSNPKIKKA GQNVKYDIEV
LWNAGLSLEG VSFDTMIASY LLNAERSSNS MDAMAKDYLN YECQPISDLI GKGKSQITFD
KVPAADAADY ACEDADITFR LYEYLNKRLN EQPKLKKLFE ELEMPLMKVL CKMEIEGVSI
DCSVLDKMSK EIASQIETLR DSIFAQSGSV FNIESPKQLS EVLFDKLKLP QIKKRSTDAS
VLEKLADFHP VIEDIQQFRQ LVKLKGTYID KLGTMVNPKT NRLHCSFNQT ITATGRLSSS
NPNLQNIPIR TDIGRKIRAA FVPAEKDGVI LSADYSQVEL RLLAHFSQDS QLLEAFNNDM
DIHSFVASEL LGADPENPEP ELRAKAKAVN FGIIYGQGPY ALSQSLGITQ GEAKEFIDSY
FQRYSSIKEF MQSVIDGAKS NGYVSTILGR RRAVPGINSA AKREKSSAER MAFNTTIQGS
AADLIKAAMI EVQNEIDAGK LKAKMIIQIH DELVFECSRD NAEQNAKRIS EIMENAIELR
VRLKVDTGWG ENWMTGH
//
