ID DPOL1_AERPE Reviewed; 959 AA.
AC O93745;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=DNA polymerase 1;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase I;
GN Name=polA; OrderedLocusNames=APE_0099;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-959.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RA Ishino Y., Cann I.K.;
RT "Isolation of the genes encoding two alpha-like DNA polymerases from
RT Aeropyrum pernix.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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-B family. {ECO:0000305}.
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DR EMBL; AB017500; BAA75662.1; -; Genomic_DNA.
DR EMBL; BA000002; BAA79008.1; -; Genomic_DNA.
DR PIR; F72763; F72763.
DR AlphaFoldDB; O93745; -.
DR SMR; O93745; -.
DR STRING; 272557.APE_0099; -.
DR EnsemblBacteria; BAA79008; BAA79008; APE_0099.
DR KEGG; ape:APE_0099; -.
DR PATRIC; fig|272557.25.peg.63; -.
DR eggNOG; arCOG15272; Archaea.
DR BRENDA; 2.7.7.7; 171.
DR Proteomes; UP000002518; Chromosome.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05783; DNA_polB_B1_exo; 1.
DR CDD; cd05530; POLBc_B1; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10322:SF20; DNA POLYMERASE 1; 1.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..959
FT /note="DNA polymerase 1"
FT /id="PRO_0000046474"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 193
FT /note="L -> H (in Ref. 1; BAA75662)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..362
FT /note="RDGVEFT -> PGGSRFY (in Ref. 1; BAA75662)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="R -> G (in Ref. 1; BAA75662)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="I -> V (in Ref. 1; BAA75662)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="K -> R (in Ref. 1; BAA75662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 959 AA; 109749 MW; 05F6A6B9C8DBFF85 CRC64;
MRVRGGQEAA QDKETSLDSD EERGRRGLRQ TTLLDYMAGP AKPKKPEPPP TLHREREPES
KYQNTLPETT GKEPASMSLR RNQPSSKHEE YNSESGDVRG LTLEPSPQSE LSDDDVILEL
VREPWVESVR GYLLDVRYDG SLGKAVLMLY DPSSGSLVKW ADRTGHKPYF LTDARPEDLR
AAGVDVSHDE SFLQYDLVEK FHPIDRKLVK LTKIVVSDPL AVRRLREKVS SAGFSVWEAD
IKYHHNYIFD RQLIPGILYE VGGVRIVHTL PLEMDDATRI VDEIFREEPR EVRERAREWL
RIFEAPPPKL PLIAFDIEVY SPIATRLPDP STAPYPVISA ATADSSGRSR VVLLYRDGVE
FTEGALPEGT EVEIYDSERA MLLDLVRILQ RYPLVVSFNG DNFDLPYIAR RLEVLGVPRE
FAPIELKQDY ATFRRSLHID LHKLFGIRAL QVYAFGNKYR ELSLESISRA LLGKGKVELK
APVSELNLNK LIEYNLQDAR LTLELLTFSN NLVFNLIIMV MRTSKLGIED ITRSQISNWI
RGLMYWEHRR RRWLIPSRGE IEKLSSAGAR VGAIIKDKKY RGAIVLDPPV GIFFRVLVLD
FASLYPSLIK QWNLSYETVN NPNCRDTIEV PEVGHRVCRE FKGISNEIVG MLRDFRVRLY
KKKSKDKSLR EEERLWYDVV QSAMKVYINA SYGVFGSEKF SLYSLPVAES VTALGRAVLR
GTLEKSRELN LHIVYGDTDS LFIWDPPKDV LNDLVDYVER TYGLELELDK VFRAILFSGL
KKNYLGITEE GDIVIKGMVA KKSNTPEFIK DEFSKAVKIL SKLEKPEDVE AILAELRDHI
NTVYNNVKKK VYTLDQFAIK VMLSKNPREY DKNTPQHVKA AMLLQRLGLT LSRGDIVYYV
KTRDKLGVKP VQLARLSDVD PGKYVEHVKT AFEQMLMAFG ISWDDISGVR KLDRLLFDS
//
