ID A0A2K5M9E7_CERAT Unreviewed; 682 AA.
AC A0A2K5M9E7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA topoisomerase I {ECO:0000256|RuleBase:RU365101};
DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU365101};
DE AltName: Full=DNA topoisomerase 1 {ECO:0000256|RuleBase:RU365101};
GN Name=TOP1MT {ECO:0000313|Ensembl:ENSCATP00000021825.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000021825.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000021825.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC introduced during the DNA replication and transcription by transiently
CC cleaving and rejoining one strand of the DNA duplex. Introduces a
CC single-strand break via transesterification at the specific target site
CC 5'-[CT]CCTTp 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-(3'-phosphotyrosyl)-enzyme intermediate and the
CC expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes
CC passage around the unbroken strand thus removing DNA supercoils.
CC Finally, in the religation step, the DNA 5'-OH attacks the covalent
CC intermediate to expel the active-site tyrosine and restore the DNA
CC phosphodiester backbone. {ECO:0000256|RuleBase:RU365101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213,
CC ECO:0000256|RuleBase:RU365101};
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00006645, ECO:0000256|RuleBase:RU365101}.
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DR AlphaFoldDB; A0A2K5M9E7; -.
DR STRING; 9531.ENSCATP00000021825; -.
DR Ensembl; ENSCATT00000046028.1; ENSCATP00000021825.1; ENSCATG00000034601.1.
DR GeneTree; ENSGT00940000162943; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000034601; Expressed in colon and 12 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00659; Topo_IB_C; 1.
DR CDD; cd03488; Topoisomer_IB_N_htopoI_like; 1.
DR Gene3D; 1.10.132.10; -; 1.
DR Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 1.
DR Gene3D; 1.10.10.41; Yeast DNA topoisomerase - domain 1; 1.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
DR InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR InterPro; IPR001631; TopoI.
DR InterPro; IPR018521; TopoI_AS.
DR InterPro; IPR025834; TopoI_C_dom.
DR InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR InterPro; IPR013500; TopoI_cat_euk.
DR InterPro; IPR008336; TopoI_DNA-bd_euk.
DR InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
DR InterPro; IPR013499; TopoI_euk.
DR InterPro; IPR048045; Topoisomer_I_DNA-bd.
DR PANTHER; PTHR10290; DNA TOPOISOMERASE I; 1.
DR PANTHER; PTHR10290:SF1; DNA TOPOISOMERASE I, MITOCHONDRIAL; 1.
DR Pfam; PF14370; Topo_C_assoc; 1.
DR Pfam; PF01028; Topoisom_I; 1.
DR Pfam; PF02919; Topoisom_I_N; 1.
DR PRINTS; PR00416; EUTPISMRASEI.
DR SMART; SM00435; TOPEUc; 1.
DR SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR SUPFAM; SSF46596; Eukaryotic DNA topoisomerase I, dispensable insert domain; 1.
DR SUPFAM; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1.
DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365101};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365101};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 196..573
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 146..173
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 480..547
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 682 AA; 77434 MW; FC9802822ECC0A91 CRC64;
MRVVRLLRLR AALTLLGEVP RRPASRGVPG SRRTQKGSGT RWEEEKREDR VKWRQLEHKG
PYFAPPYEPL PNGVCFFYDG KPMRLSVKAE EVATFYGRML DHEYTTKEVF RKNFFNDWRK
EMTAEEREVI KSLDKCDFTE IHRYFVDKAA ARRVLTREEK QKLKEEAEKL QQEFGYCILD
GHREKIGNFK TEPPGLFRGR GDHPKMGMLK RRVMPEDVVI NCSRDSKIPK PPAGHQWKEV
RSDNTVMWLA AWTESIQNSI KYVMLNPCSK LKGEKAWQKF ETARRLRGFV DEIRSQYRAD
WKSQEMKTRQ RAVALYFIDK LALRAGNEKE DGEAADTVGC CSLRVEHVQL HPEADGCQHV
VEFDFPGKDS IRYYNRVPVE KPVYKNLQLF MKNKDPQDDL FDRLTTTSLN KHLHELMDGL
TAKVFRTYNA SVTLQEQLRA LTRAEDSIAA KILSYNRANR AVAILCNHQR ATSSTFEKSM
QNLQTKIQVK KEQVAEARAE LRKARAEHKA QGDGKSGSVL EKKRRLLEKL QEQLAWLSVQ
ATDKEENKQV ALSTSKLNYL DPRISIAWYV CLGSQFPPVA SGGPGFSRGL CSVPALLLSP
VSSGVSAGPP CDRDPDAASC VISSPCPERW DGQGEVGVLT VAWDSASSAG PVELSLPTGS
GRWLGALLSG HLGHSRLSLT PR
//
