DPO1_TREPA
ID DPO1_TREPA Reviewed; 997 AA.
AC P74933; O83143;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=TP_0105;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=10882092; DOI=10.1099/0022-1317-49-7-657;
RA Rodes B., Liu H., Johnson S., George R., Steiner B.M.;
RT "Molecular cloning of a gene (polA) coding for an unusual DNA polymerase I
RT from Treponema pallidum.";
RL J. Med. Microbiol. 49:657-667(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 3'-5' and 5'-3' exonuclease activity. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR EMBL; U57757; AAB17467.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC26553.1; -; Genomic_DNA.
DR PIR; F71365; F71365.
DR RefSeq; WP_010881554.1; NC_021490.2.
DR AlphaFoldDB; P74933; -.
DR SMR; P74933; -.
DR STRING; 243276.TPANIC_0105; -.
DR EnsemblBacteria; AAC26553; AAC26553; TP_0105.
DR KEGG; tpa:TP_0105; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR eggNOG; COG0847; Bacteria.
DR HOGENOM; CLU_004675_0_0_12; -.
DR OMA; NRPPMPD; -.
DR OrthoDB; 1220182at2; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR CDD; cd09898; H3TH_53EXO; 1.
DR Gene3D; 3.30.420.10; -; 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; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 2.
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; SM00479; EXOIII; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00593; pola; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..997
FT /note="DNA polymerase I"
FT /id="PRO_0000101261"
FT DOMAIN 174..261
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 428..589
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000255"
FT CONFLICT 782
FT /note="V -> A (in Ref. 1; AAB17467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 997 AA; 112217 MW; 764DE97E4CCD2054 CRC64;
MQEKKTLYLL DAYGLIYRSY HAFARAPLIN DSGANVSAVY GFFRSLHTLL CHYRPRYFVA
VFDSLTPTFR HVQYPAYKAK RDKTSAELYA QIPLIEEILC ALGITVLRHD GFEADDLIAT
LAKRVAAEHC HVVIISSDKD VLQLVCDTVQ VLRLDIDHKW TCCDAAYVQQ RWTVMPTQLL
DLFSLMGDSS DNVPGVRGIG PKTAAHLLHC FGTLDGIYRH TYSLKEALRT KIVCGKKDAF
FSRSLIELRD DVPCVFSLED SCCIPLDVTS AARIFVREGL HALAQQYRAC VQEIDTEATN
DTLQMTESSV LTSGRCANEC FLSQVEGRAS TPEVNSVLKS ELKTSAVSGA IPIENRDLRQ
DVMLARSAGH YRGVTDPVEL KRIIDCACAN GVVAFDCETD GLHPHDTRLV GFSICFQEAE
AFYVPLIVPD VSLHTESTQC TCARSTNVET EKECTEQHGV SASAVQDPAY VQAVMHQLRR
LWNDETLTLV MHNGKFDYHV MHRAGVFEHC ACNIFDTMVA AWLLDPDRGT YGMDVLAASF
FQIRTITFEE VVAKGQTFAH VPYECAVRYA AEDADITFRL YHYLKLRLET AGLLSVFETI
EMPLLPILAR MEEVGIFLRK DVVQQLTRSF SDLIQQYEHD IFSLAGHEFN IGSPKQLQTV
LFQELHLPPG KKNTQGYSTD HSVLKKLARK HPIAEKILLF RDLSKLRSTY TESLAKLADQ
TGRVHTSFVQ IGTATGRLSS RNPNLQNIPI KSTEGRKIRQ AFQATVGHEL ISADYTQIEL
VVLAHLSQDR NLLNAFRQHI DIHALTAAYI FNVSIDDVQP AMRRIAKTIN FGIVYGMSAF
RLSDELKISQ KEAQSFIYRY FETYPGVYAF STQVAEQTRK TGYVTSLAGR RRYIRTIDSR
NTLERARAER MALNTQIQSS AADIVKIAMI AIQRAFARRP LRAQLLLQVH DELIFEAPAA
ETAIVKEILF AEMEHAVELS IPLRIHVESG NSWGDFH
