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A20_VACCC
ID   A20_VACCC               Reviewed;         426 AA.
AC   P20995;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=DNA polymerase processivity factor component A20;
GN   ORFNames=A20R;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
CC   -!- FUNCTION: Plays an essential role in viral DNA replication by acting as
CC       the polymerase processivity factor together with protein D4. May serve
CC       as a bridge which links the DNA polymerase E9 and the uracil DNA
CC       glycosylase (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the DNA polymerase catalytic subunit E9.
CC       Interacts with UDG. Component of the Uracil-DNA glycosylase(UDG)-A20-
CC       polymerase complex; A20 and UDG form a heterodimeric processivity
CC       factor that associates with E9 to form the processive polymerase
CC       holoenzyme. Interacts with D5 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P20995; P20536: UNG; NbExp=6; IntAct=EBI-984598, EBI-984584;
CC   -!- SIMILARITY: Belongs to the poxviruses A20 family. {ECO:0000305}.
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DR   EMBL; M35027; AAA48143.1; -; Genomic_DNA.
DR   PIR; D42519; D42519.
DR   PDB; 4OD8; X-ray; 1.85 A; C/D=1-50.
DR   PDB; 4ODA; X-ray; 2.20 A; C/D=1-50.
DR   PDB; 4YGM; X-ray; 1.85 A; C/D=1-50.
DR   PDB; 4YIG; X-ray; 2.70 A; B/F/J=3-50.
DR   PDB; 5JKR; X-ray; 2.60 A; C/D=1-50.
DR   PDB; 5JKS; X-ray; 2.79 A; C/D=1-50.
DR   PDB; 5JKT; X-ray; 2.49 A; C/D=1-50.
DR   PDB; 6ZXP; NMR; -; A=304-426.
DR   PDB; 6ZYC; NMR; -; A=304-426.
DR   PDBsum; 4OD8; -.
DR   PDBsum; 4ODA; -.
DR   PDBsum; 4YGM; -.
DR   PDBsum; 4YIG; -.
DR   PDBsum; 5JKR; -.
DR   PDBsum; 5JKS; -.
DR   PDBsum; 5JKT; -.
DR   PDBsum; 6ZXP; -.
DR   PDBsum; 6ZYC; -.
DR   SASBDB; P20995; -.
DR   SMR; P20995; -.
DR   DIP; DIP-2180N; -.
DR   IntAct; P20995; 4.
DR   MINT; P20995; -.
DR   Proteomes; UP000008269; Genome.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
DR   InterPro; IPR010267; Chordopox_A20R.
DR   Pfam; PF05941; Chordopox_A20R; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; Reference proteome.
FT   CHAIN           1..426
FT                   /note="DNA polymerase processivity factor component A20"
FT                   /id="PRO_0000099267"
FT   HELIX           4..19
FT                   /evidence="ECO:0007829|PDB:4OD8"
FT   HELIX           25..42
FT                   /evidence="ECO:0007829|PDB:4OD8"
FT   STRAND          306..308
FT                   /evidence="ECO:0007829|PDB:6ZYC"
FT   HELIX           313..323
FT                   /evidence="ECO:0007829|PDB:6ZXP"
FT   HELIX           331..340
FT                   /evidence="ECO:0007829|PDB:6ZXP"
FT   HELIX           342..350
FT                   /evidence="ECO:0007829|PDB:6ZXP"
FT   HELIX           353..361
FT                   /evidence="ECO:0007829|PDB:6ZXP"
FT   HELIX           365..373
FT                   /evidence="ECO:0007829|PDB:6ZXP"
FT   STRAND          375..380
FT                   /evidence="ECO:0007829|PDB:6ZXP"
FT   STRAND          383..390
FT                   /evidence="ECO:0007829|PDB:6ZXP"
FT   HELIX           394..396
FT                   /evidence="ECO:0007829|PDB:6ZXP"
FT   HELIX           398..405
FT                   /evidence="ECO:0007829|PDB:6ZXP"
FT   HELIX           407..424
FT                   /evidence="ECO:0007829|PDB:6ZXP"
SQ   SEQUENCE   426 AA;  49187 MW;  F316F8FDEC861DE3 CRC64;
     MTSSADLTNL KELLSLYKSL RFSDSAAIEK YNSLVEWGTS TYWKIGVQKV ANVETSISDY
     YDEVKNKPFN IDPGYYIFLP VYFGSVFIYS KGKNMVELGS GNSFQIPDDM RSACNKVLDS
     DNGIDFLRFV LLNNRWIMED AISKYQSPVN IFKLASEYGL NIPKYLEIEI EEDTLFDDEL
     YSIIERSFDD KFPKISISYI KLGELRRQVV DFFKFSFMYI ESIKVDRIGD NIFIPSVITK
     SGKKILVKDV DHLIRSKVRE HTFVKVKKKN TFSILYDYDG NGTETRGEVI KRIIDTIGRD
     YYVNGKYFSK VGSAGLKQLT NKLDINECAT VDELVDEINK SGTVKRKIKN QSAFDLSREC
     LGYPEADFIT LVNNMRFKIE NCKVVNFNIE NTNCLNNPSI ETIYRNFNQF VSIFNVVTDV
     KKRLFE
 
 
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