DPOL_PYRAB
ID DPOL_PYRAB Reviewed; 771 AA.
AC P0CL77; G8ZK85; P77916; P77932;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=DNA polymerase 1;
DE EC=2.7.7.7;
DE AltName: Full=Pab polymerase;
GN Name=polI; Synonyms=pol; OrderedLocusNames=PYRAB17200; ORFNames=PAB1128;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50625.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71192.1; -; Genomic_DNA.
DR PIR; C75023; C75023.
DR RefSeq; WP_010868838.1; NC_000868.1.
DR PDB; 4FLT; X-ray; 2.90 A; A=1-771.
DR PDB; 4FLV; X-ray; 2.70 A; A=1-771.
DR PDB; 4FLW; X-ray; 2.15 A; A=1-771.
DR PDB; 4FLX; X-ray; 2.90 A; A=1-771.
DR PDB; 4FLY; X-ray; 2.30 A; A=1-771.
DR PDB; 4FLZ; X-ray; 3.20 A; A=1-771.
DR PDB; 4FM0; X-ray; 3.12 A; A=1-771.
DR PDB; 4FM1; X-ray; 3.00 A; A=1-771.
DR PDB; 4FM2; X-ray; 2.90 A; A=1-771.
DR PDBsum; 4FLT; -.
DR PDBsum; 4FLV; -.
DR PDBsum; 4FLW; -.
DR PDBsum; 4FLX; -.
DR PDBsum; 4FLY; -.
DR PDBsum; 4FLZ; -.
DR PDBsum; 4FM0; -.
DR PDBsum; 4FM1; -.
DR PDBsum; 4FM2; -.
DR AlphaFoldDB; P0CL77; -.
DR SMR; P0CL77; -.
DR STRING; 272844.PAB1128; -.
DR EnsemblBacteria; CAB50625; CAB50625; PAB1128.
DR GeneID; 1496021; -.
DR KEGG; pab:PAB1128; -.
DR PATRIC; fig|272844.11.peg.1837; -.
DR eggNOG; arCOG00328; Archaea.
DR HOGENOM; CLU_000203_6_0_2; -.
DR OMA; GNQKSPY; -.
DR OrthoDB; 35869at2157; -.
DR PhylomeDB; P0CL77; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; 2.
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 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..771
FT /note="DNA polymerase 1"
FT /id="PRO_0000407283"
FT STRAND 1..10
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:4FLW"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 305..337
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:4FLW"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:4FLW"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 449..469
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 494..498
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 508..531
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 553..570
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 578..590
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 593..597
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 617..631
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 636..651
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 657..660
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 662..665
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 678..688
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 698..705
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:4FLW"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:4FLW"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 729..734
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 737..746
FT /evidence="ECO:0007829|PDB:4FLW"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:4FLW"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:4FLW"
SQ SEQUENCE 771 AA; 89496 MW; 110A87045A8A5522 CRC64;
MIIDADYITE DGKPIIRIFK KEKGEFKVEY DRTFRPYIYA LLKDDSAIDE VKKITAERHG
KIVRITEVEK VQKKFLGRPI EVWKLYLEHP QDVPAIREKI REHPAVVDIF EYDIPFAKRY
LIDKGLTPME GNEELTFLAV DIETLYHEGE EFGKGPIIMI SYADEEGAKV ITWKSIDLPY
VEVVSSEREM IKRLVKVIRE KDPDVIITYN GDNFDFPYLL KRAEKLGIKL PLGRDNSEPK
MQRMGDSLAV EIKGRIHFDL FPVIRRTINL PTYTLEAVYE AIFGKSKEKV YAHEIAEAWE
TGKGLERVAK YSMEDAKVTF ELGKEFFPME AQLARLVGQP VWDVSRSSTG NLVEWFLLRK
AYERNELAPN KPDEREYERR LRESYEGGYV KEPEKGLWEG IVSLDFRSLY PSIIITHNVS
PDTLNRENCK EYDVAPQVGH RFCKDFPGFI PSLLGNLLEE RQKIKKRMKE SKDPVEKKLL
DYRQRAIKIL ANSYYGYYGY AKARWYCKEC AESVTAWGRQ YIDLVRRELE SRGFKVLYID
TDGLYATIPG AKHEEIKEKA LKFVEYINSK LPGLLELEYE GFYARGFFVT KKKYALIDEE
GKIVTRGLEI VRRDWSEIAK ETQAKVLEAI LKHGNVDEAV KIVKEVTEKL SKYEIPPEKL
VIYEQITRPL SEYKAIGPHV AVAKRLAAKG VKVKPGMVIG YIVLRGDGPI SKRAIAIEEF
DPKKHKYDAE YYIENQVLPA VERILRAFGY RKEDLKYQKT KQVGLGAWLK F