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TOP2_ASFP4
ID   TOP2_ASFP4              Reviewed;        1192 AA.
AC   P0C9C0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=DNA topoisomerase 2 {ECO:0000250|UniProtKB:Q00942};
DE            EC=5.6.2.2 {ECO:0000250|UniProtKB:Q00942};
DE   AltName: Full=DNA topoisomerase II;
GN   OrderedLocusNames=Pret-124;
OS   African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=561443;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kutish G.F., Rock D.L.;
RT   "African swine fever virus genomes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Type II topoisomerase. Processively relaxes supercoiled DNA.
CC       Displays DNA-supercoiling activity only when associated with the viral
CC       histone-like protein. {ECO:0000250|UniProtKB:Q00942}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000250|UniProtKB:Q00942};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P11388};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P11388};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P11388};
CC       Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC       with both the protein and the DNA. Can also accept other divalent metal
CC       cations, such as Mn(2+) or Ca(2+). {ECO:0000250|UniProtKB:P11388};
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:Q00942}.
CC       Note=Localizes to the cytoplasmic viral factories.
CC       {ECO:0000250|UniProtKB:Q00942}.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR   EMBL; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C9C0; -.
DR   Proteomes; UP000000859; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 1.10.268.10; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR031660; TOPRIM_C.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF16898; TOPRIM_C; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Early protein; Host cytoplasm; Isomerase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Topoisomerase.
FT   CHAIN           1..1192
FT                   /note="DNA topoisomerase 2"
FT                   /id="PRO_0000373130"
FT   ACT_SITE        800
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q00942"
FT   BINDING         64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q00942"
FT   BINDING         438
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P11388"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P11388"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11388"
FT   BINDING         541
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11388"
FT   SITE            799
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1192 AA;  135435 MW;  91725AFB830FFC53 CRC64;
     MEAFEISDFK EHAKKKSMWA GALNKVTISG LMGVFTEDED LMALPIHRDH CPALLKIFDE
     IIVNATDHER ACHSKTKKVT YIKISFDKGV FSCENDGPGI PIAKHEQASL IAKRDVYVPE
     VASCHFLAGT NINKAKDCIK GGTNGVGLKL AMVHSQWAIL TTADGAQKYV QHINQRLDII
     EPPTITPSRE MFTRIELMPV YQELGYAEPL SETEQADLSA WIYLRACQCA AYVGKGTTIY
     YNDKPCRTGS VMALAKMYTL LSAPNSTIHT ATIKADAKPY SLHPLQVAAV VSPKFKKFEH
     VSVINGVNCV KGEHVTFLKK TINEMVVKKF QQTIKDKNRK TTLRDSCSNI FIVIVGSIPG
     IEWTGQRKDE LSIAENVFKT HYSIPSSFLT SMTKSIVDIL LQSISKKDNH KQVDVDKYTR
     ARNAGGKRAQ DCMLLAAEGD SALSLLRTGL TLGKSNPSGP SFDFCGMISL GGVIMNACKK
     VTNITTDSGE TIMVRNEQLT NNKVLQGIVQ VLGLDFNCHY KTQEERAKLR YGCIVACVDQ
     DLDGCGKILG LLLAYFHLFW PQLIIHGFVK RLLTPLIRVY EKGKTVPVEF YYEQEFDAWA
     KKQTSLANHT VKYYKGLAAH DTHEVKSMFK HFDNMVYTFT LDDSAKELFH IYFGGESELR
     KRELCTGVVP LTETQTQSIH SVRRIPCSLH LQVDTKAYKL DAIERQIPNF LDGMTRARRK
     ILAGGVKCFA SNNRERKVFQ FGGYVADHMF YHHGDMSLNT SIIKAAQYYP GSSHLYPVFI
     GIGSFGSRHL GGKDAGSPRY ISVQLASEFI KTMFPAEDSW LLPYVFEDGQ RAEPEYYVPV
     LPLAIMEYGA NPSEGWKYTT WARQLEDILA LVRAYVDKNN PKHELLHYAI KHKITILPLR
     PSNYNFKGHL KRFGQYYYSY GTYVISEQRN IITITELPLR VPTVAYIESI KKSSNRMTFI
     EEIIDYSSSE TIEILVKLKP NSLNRIMEEF KCTEEQDSIE NFLRLRNCLH SHLNFVKPKG
     GIIEFNTYYE ILYAWLPYRR ELYQKRLMRE HAVLKLRIIM ETAIVRYINE SAELNLSHYE
     DEKEASRILS EHGFPPLNQT LIISPEFASI EELNQKALQG CYTYILSLQA RELLIAAKTR
     RVEKIKKMQA RLDKVEQLLQ ESPFPGASVW LEEIDAVEKA IIKGRNTQWK FH
 
 
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