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DPOL1_AERPE
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   25-MAY-2022, entry version 114.
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; Crenarchaeota; 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   OMA; WIRNMLY; -.
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   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 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   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; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 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
 
 
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