TOP1P_MIMIV
ID TOP1P_MIMIV Reviewed; 854 AA.
AC Q5UQB5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=DNA topoisomerase 1 type prokaryotic;
DE EC=5.6.2.1;
GN Name=TOP1P; OrderedLocusNames=MIMI_L221;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP LOCATION.
RX PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT "Mimivirus giant particles incorporate a large fraction of anonymous and
RT unique gene products.";
RL J. Virol. 80:11678-11685(2006).
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC is introduced during the DNA replication and transcription, by
CC transiently cleaving and rejoining one strand of the DNA duplex.
CC Introduces a single-strand break via transesterification at a target
CC site in duplex DNA. The scissile phosphodiester is attacked by the
CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC DNA strand. The free DNA strand then undergoes passage around the
CC unbroken strand, thus removing DNA supercoils. Finally, in the
CC religation step, the DNA 3'-OH attacks the covalent intermediate to
CC expel the active-site tyrosine and restore the DNA phosphodiester
CC backbone (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. {ECO:0000305}.
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DR EMBL; AY653733; AAV50494.1; -; Genomic_DNA.
DR RefSeq; YP_003986717.1; NC_014649.1.
DR SMR; Q5UQB5; -.
DR GeneID; 9924828; -.
DR KEGG; vg:9924828; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) 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 CDD; cd00186; TOP1Ac; 1.
DR Gene3D; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 1.
DR HAMAP; MF_00952; Topoisom_1_prok; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR42785; PTHR42785; 2.
DR Pfam; PF01131; Topoisom_bac; 2.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 3.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; SSF56712; 1.
DR TIGRFAMs; TIGR01051; topA_bact; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome;
KW Topoisomerase; Virion.
FT CHAIN 1..854
FT /note="DNA topoisomerase 1 type prokaryotic"
FT /id="PRO_0000145183"
FT DOMAIN 2..110
FT /note="Toprim"
FT REGION 158..163
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 802..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..854
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 302
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 32
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 134
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 135
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 138
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 143
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 304
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 505
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 854 AA; 96946 MW; 2D7361B66C8C0C0C CRC64;
MSILILLESP GKISKISSIL GKNYVVKASM GHFRDLDPKK MSIDFDNDFE PVYIVTKPDV
VKNLKSAMKN IDLVYLAADE DREGEAIAQS LYDVLKPSNY KRLRFNAITK DAIMSAIKNA
GDIDKNLVDA QKARRVLDRL FGYLISPILQ RQIGGKLSAG RVQSVTVRII IDKENEIKNF
INKNADSSYF KVSGTFNGAK ATLHESNDKK PFDLETAYKG KTAQIALINS ENPNSKVVNF
MKRCLKSQFF IHSVEDKMTT RSPAPPFTTS TLQQEANRKF GMSIDSTMKT AQKLYEGGYI
TYMRTDSVEI SAEGHRDIKK IITDQYGADY YQKNLYKNKA ANSQEAHEAI RPTHPELLTL
EGEIEDAYQI KLYKLIWQRT IASQMKPAKI KVTIIQISIS KYVEDKLNPF YYFQSQIETV
VFPGFMKVYV ESIDDPDTDN QITKNFTGKI PTVGSKVTME EIIARQEYMR PPPRYSEASL
VKKLEELGIG RPSTYVNTIK TIINREYVKI TDVPGIKKDI TIYSIKSENK KHIMEVYEDT
DTILLGKENK KIVPTNLGIT VNDFLMKYFP EFLDYKFTAN METDLDYVST GTKNWVDIVQ
DFYDKLKPIV DELSKQKGLS QSSERLLGED NDGNEITATK TKFGPVVRKK IGDKYVYAKI
KDPLTLDTIK LSDAIKLLEY PKNLGQYKGF DVLLQKGDYG FYLSYNKENF SLGEIDDPED
INLDTAIKAI EAKKANNIAE FNLTENGKKI KAIVLNGKYG YYVQVTRNRI KKNYPIPKDL
DPNNLTEQQI LSIISVKKTY KKSAPKGGSK TIRKPSQTKY SQTKSTKSTK STKSTNKKFV
GKSAKKTTKK TTKK
