ID A0A182U9L4_9DIPT Unreviewed; 1007 AA.
AC A0A182U9L4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 28.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
OS Anopheles melas.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC016442-PA, ECO:0000313|Proteomes:UP000075902};
RN [1] {ECO:0000313|Proteomes:UP000075902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEC016442-PA}
RP IDENTIFICATION.
RC STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC016442-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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|ARBA:ARBA00000213,
CC ECO:0000256|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
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DR AlphaFoldDB; A0A182U9L4; -.
DR STRING; 34690.A0A182U9L4; -.
DR EnsemblMetazoa; AMEC016442-RA; AMEC016442-PA; AMEC016442.
DR VEuPathDB; VectorBase:AMEC016442; -.
DR Proteomes; UP000075902; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 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; IPR013498; Topo_IA_Znf.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF01396; zf-C4_Topoisom; 1.
DR Pfam; PF06839; zf-GRF; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 29..173
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 896..937
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 624..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 111559 MW; D712102A7673A552 CRC64;
MLRLAKASIS FIRRPQTRAL ASACSANMKY LNVAEKNDAA KTIAGLLSRG SSQRREGYSP
YNKIYEFSYN LHGQSIQMIM TSVSGHLLTH EFLPSFRGWH SCSPEDLFDA PVRKNCPEQY
EKIKKTLERE VRGCSALIIW TDCDREGENI GYEIIEVCRA VKPQLRVFRA KFSEITAPSI
KRAIENLVQP DARQNDAVNV RSELDLRIGA AFTRFQTLRL QKSFPQDISN NLVSYGSCQI
PTLGFVAQRY KEIENFIPQT FWKIKLTHTI DELTVEFHWS RNRLFDKQCC EAYLMLCQTN
PTAKVVNVTQ KPKNKWRPTP MDTVELEKLG SRKLKMNAKQ VMTIAEKLYT QGIISYPRTE
TNMFTGDMKL APLVQAQVAS DQWGSFAEKV LQWGVNPRNG KKSDQAHPPI HPTKLPTNLS
GDEWRVYELI ARHFLACVSR DATGSETIVN VVVAEEEEFT ASGLCIHERN YLEVYPYDRW
NAKEIHSYQV GHTFEPTELG LHEGSTTAPN MLTEADLIAL MEKHGIGTDA THAEHINTIK
ERGYIGERDR GFLVPGTLGM GLVEGYEMME LRLAHPELRA GLEADLKLVC EGRKNPNDVL
AEQIAKYKEV YRIMSQKARA LDRAMGQRLN QTPQEPPPDA GASAATATGT APMREVCKCP
KCGHKMCLRT KRDSSGYYLG CVAFPECRNN IWFDDSMREI NVLDDTCARC GSKKMTVKFR
SVRFYALLQS TDMDEYQFCI VCDDKFRNLF NINESSVRVA AGARSSSNTT TVPVAQPARS
STSTWGTGNQ SERRPANTAH NTTSSGIGWS NSSTGSSSSW GTGQSTSNNW GGSQSSNRGG
GSSTTTWGKP ANNRADGPAK KGGGFGDAGG AKQNSWHNPS NSSRVGIGEE DGEVMCRCGT
PASRFTVKKD GPNKGRPFFS CPNQASSCGF FKWGDENMPP ASSNNGGTGG GSVSWGSGGV
SNSGSSWGRS SNDTTNKTSR TTRKCGLCRQ EGHTKNKCPQ RALCEVL
//
