(data stored in SCRATCH zone)

SWISSPROT: C6WFC8_ACTMD

ID   C6WFC8_ACTMD            Unreviewed;       923 AA.
AC   C6WFC8;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 67.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00744975};
DE            EC=5.99.1.2 {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00721057};
DE   AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
GN   Name=topA {ECO:0000256|HAMAP-Rule:MF_00952};
GN   OrderedLocusNames=Amir_0291 {ECO:0000313|EMBL:ACU34260.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34260.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34260.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA,
CC       which is introduced during the DNA replication and transcription,
CC       by transiently cleaving and rejoining one strand of the DNA
CC       duplex. Introduces a single-strand break via transesterification
CC       at a target site in duplex DNA. The scissile phosphodiester is
CC       attacked by the catalytic tyrosine of the enzyme, resulting in the
CC       formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the
CC       expulsion of a 3'-OH DNA strand. The free DNA strand then
CC       undergoes passage around the unbroken strand, thus removing DNA
CC       supercoils. Finally, in the religation step, the DNA 3'-OH attacks
CC       the covalent intermediate to expel the active-site tyrosine and
CC       restore the DNA phosphodiester backbone. {ECO:0000256|HAMAP-
CC       Rule:MF_00952}.
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining. {ECO:0000256|HAMAP-
CC       Rule:MF_00952, ECO:0000256|SAAS:SAAS00721095}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00721088};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952,
CC       ECO:0000256|SAAS:SAAS00709415}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00721110}.
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DR   EMBL; CP001630; ACU34260.1; -; Genomic_DNA.
DR   STRING; 446462.Amir_0291; -.
DR   EnsemblBacteria; ACU34260; ACU34260; Amir_0291.
DR   KEGG; ami:Amir_0291; -.
DR   eggNOG; ENOG4105C73; Bacteria.
DR   eggNOG; COG0550; LUCA.
DR   eggNOG; COG1754; LUCA.
DR   HOGENOM; HOG000004020; -.
DR   KO; K03168; -.
DR   OMA; IDFPGFF; -.
DR   OrthoDB; POG091H02BN; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03363; TOPRIM_TopoIA_TopoI; 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; IPR013825; Topo_IA_cen_sub2.
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   InterPro; IPR034149; TOPRIM_TopoI.
DR   PANTHER; PTHR42785; PTHR42785; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF13368; Toprim_C_rpt; 4.
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   3: Inferred from homology;
DR   PRODOM; C6WFC8.
DR   SWISS-2DPAGE; C6WFC8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721076};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721131, ECO:0000313|EMBL:ACU34260.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00721141};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00721137};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721067}.
FT   DOMAIN       19    143       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   REGION      192    197       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   ACT_SITE    340    340       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00952}.
FT   SITE         49     49       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        168    168       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        169    169       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        172    172       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        177    177       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        184    184       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        342    342       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        543    543       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
SQ   SEQUENCE   923 AA;  100078 MW;  CCDFF6AE5C389E1D CRC64;
     MAGSTRTRKS TGGSAGGNRR LVIVESPTKA RKIASYLGNG FVVESSKGHI RDLPRGAADV
     PAKYKGQPWA RLGVDVDHDF EPLYIVTPDK KSTVAELKEL LKGVDELYLA TDGDREGEAI
     AWHLLETLKP SVPVRRMVFH EITEPAILAA AASPRDLDLS LVDAQETRRI LDRLYGYEVS
     PVLWKKVMPK LSAGRVQSVA TRIVVERERE RMKFVTASFW DVSATIDAGA EATPRQFAGR
     LVSVDGTRLA TGRDFGSDGR LKDGVEVKVL DEAHARAIAE GLTGAAMRVA SVEEKPYTRK
     PYPPFMTSTI QQEAGRKLRF SADRTMRAAQ KLYENGYITY MRTDSTALSE TAITAARAQA
     TDLYGAQYVA KEPRQYTRKV KNAQEAHEAI RPAGEVFRTP GQVARELDSD EYKLYELIWQ
     RTIASQMADA RGNTTSVRVA GRTGGGEDVL FASSGRTITF AGFLKAYVET VDSEAGGNAD
     DAESRLPQLV AEQPVSAAEL SADGHSTSPP PRFTEPSLIK TMEDLGIGRP STYASIISTI
     QDRGYVWKKG SALVPSWVAF AVVGLLEQHF GRLVDYDFTA ALEDELDGIA EGRQERTTWL
     SGFYFGGDVG PESSIGRSGG LKKLVGSSVE EIDAREINSI PLFSDEGGHT VVVRVGRYGP
     YLEREVDGAS QRANLPDDLP PDELSLEIAE KLFATPQEGR SLGNDPATGH EIVAKEGRFG
     PYVTEVLPEP AEGKKAGKPR TSSLFKSMSL DTVTLEDALR LLSLPRVVGA DPESGAEITA
     QNGRYGPYLK RGTDSRSLTS EDQLFTVTLD EALKIYAEPK KRGRAAAAPP LKELGNDPVS
     GKPMVVKEGR FGPYVTDGET NASLRKSDNV ETLSDERGSE LLAEKRAKGP STKKKPAART
     TKAAAKPAAK KPAAKKTPAK SKG
//

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