ID A0A2K5MN70_CERAT Unreviewed; 407 AA.
AC A0A2K5MN70;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA topoisomerase {ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU362092};
GN Name=TOP3B {ECO:0000313|Ensembl:ENSCATP00000026683.1};
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:ENSCATP00000026683.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000026683.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC target site in duplex DNA. Releases the supercoiling and torsional
CC tension of DNA introduced during the DNA replication and transcription
CC by transiently cleaving and rejoining one strand of the DNA duplex. The
CC scissile phosphodiester is attacked by the catalytic tyrosine of the
CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC intermediate and the expulsion of a 3'-OH DNA strand.
CC {ECO:0000256|RuleBase:RU362092}.
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|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|RuleBase:RU362092}.
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DR AlphaFoldDB; A0A2K5MN70; -.
DR Ensembl; ENSCATT00000050923.1; ENSCATP00000026683.1; ENSCATG00000036736.1.
DR GeneTree; ENSGT00940000156516; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000036736; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
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:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Topoisomerase {ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 10..127
FT /note="DNA topoisomerase type IA central"
FT /evidence="ECO:0000259|Pfam:PF01131"
FT REGION 366..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..389
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 45418 MW; 3D7002D923AD2C80 CRC64;
MPWQSVPLEE SLPTCQRGDT FPVGEVKMLE KQTSPPDYLT EAELITLMEK HGIGTDASIP
VHINNICQRN YVTVESGRRL KPTNLGIVLV HGYYKIDAEL VLPTIRSAVE KQLNLIAQGK
ADYRQVLGHT LDVFKRKFHY FVDSIAGMDE LMEVSFSPLA ATGKPLSRCG KCHRFMKYIQ
AKPSRLHCSH CDETYTLPQN GTIKLYKELR CPLDDFELVL WSSGSRGKSY PLCPYCYNHP
PFRDMKKGMG CNECTHPSCQ HSLSMLGIGQ CVECESGVLV LDPTSGPKWK VACNKCSVVA
HCFENAHRVR VSADTCSVCE AALLDVDFNK AKSPLPGDET QHMGCVFCDP VFQELVELKH
AASCHPMHRG GPGRRQGRGR GRARRPPGKP NPRRPKDKMS ALAAYFV
//
