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DP2S_PYRHO
ID   DP2S_PYRHO              Reviewed;         622 AA.
AC   O57863;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=DNA polymerase II small subunit;
DE            Short=Pol II;
DE            EC=2.7.7.7;
DE   AltName: Full=Exodeoxyribonuclease small subunit;
DE            EC=3.1.11.1;
GN   Name=polB; OrderedLocusNames=PH0123;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- FUNCTION: Possesses two activities: a DNA synthesis (polymerase) and an
CC       exonucleolytic activity that degrades single-stranded DNA in the 3' to
CC       5' direction. Has a template-primer preference which is characteristic
CC       of a replicative DNA polymerase (By similarity). {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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.11.1;
CC   -!- SUBUNIT: Heterodimer of a large subunit and a small subunit.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit
CC       family. {ECO:0000305}.
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DR   EMBL; BA000001; BAA29192.1; -; Genomic_DNA.
DR   PIR; A71233; A71233.
DR   RefSeq; WP_010884237.1; NC_000961.1.
DR   PDB; 2KXE; NMR; -; A=1-72.
DR   PDBsum; 2KXE; -.
DR   AlphaFoldDB; O57863; -.
DR   BMRB; O57863; -.
DR   SMR; O57863; -.
DR   IntAct; O57863; 1.
DR   MINT; O57863; -.
DR   STRING; 70601.3256509; -.
DR   EnsemblBacteria; BAA29192; BAA29192; BAA29192.
DR   GeneID; 1444019; -.
DR   KEGG; pho:PH0123; -.
DR   eggNOG; arCOG04455; Archaea.
DR   OMA; FIGPGNH; -.
DR   OrthoDB; 11652at2157; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
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:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00325; DNApol_II_A_arch; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR024826; DNA_pol_delta/II_ssu.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR011149; Pol2_small_arc.
DR   PANTHER; PTHR10416; PTHR10416; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000803; Arc_Pol2_small; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW   Exonuclease; Hydrolase; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..622
FT                   /note="DNA polymerase II small subunit"
FT                   /id="PRO_0000096181"
FT   REGION          76..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           3..9
FT                   /evidence="ECO:0007829|PDB:2KXE"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:2KXE"
FT   HELIX           17..28
FT                   /evidence="ECO:0007829|PDB:2KXE"
FT   HELIX           34..44
FT                   /evidence="ECO:0007829|PDB:2KXE"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:2KXE"
FT   HELIX           51..61
FT                   /evidence="ECO:0007829|PDB:2KXE"
SQ   SEQUENCE   622 AA;  70283 MW;  28C4D84D9163274D CRC64;
     MDEFVKGLMK NGYLITPSAY YLLVGHFNEG KFSLIELIKF AKSRETFIID DEIANEFLKS
     IGAEVELPQE IKEGYISTGE GSQKVPDHEE LEKITNESSV ESSISTGETP KTEELQPTLD
     ILEEEIGDIE GGESSISTGD EVPEVENNNG GTVVVFDKYG YPFTYVPEEI EEELEEYPKY
     EDVTIEINPN LEVVPIEKDY EIKFDVRRVK LKPPKVKSGS GKEGEIIVEA YASLFRSRLR
     KLRRILRENP EVSNVIDIKK LKYVKGDEEV TIIGLVNSKK ETSKGLIFEV EDQTDRVKVF
     LPKDSEDYRE ALKVLPDAVV AFKGVYSKRG IFFANRFYLP DVPLYRKQKP PLEEKVYAVL
     TSDIHVGSKE FCEKAFIKFL EWLNGYVESK EEEEIVSRIR YLIIAGDVVD GIGIYPGQYS
     DLIIPDIFDQ YEALANLLSN VPKHITIFIG PGNHDAARPA IPQPEFYEEY AKPLYKLKNT
     VIISNPAVIR LHGRDFLIAH GRGIEDVVSF VPGLTHHKPG LPMVELLKMR HLAPTFGGKV
     PIAPDPEDLL VIEEVPDLVQ MGHVHVYDTA VYRGVQLVNS ATWQAQTEFQ KMVNIVPTPG
     LVPIVDVESA RVIKVLDFSR WC
 
 
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