ID A0A398ANL2_BRACM Unreviewed; 921 AA.
AC A0A398ANL2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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};
GN ORFNames=BRAPAZ1V2_A02P51170.2 {ECO:0000313|EMBL:CAG7896165.1},
GN BRARA_B03872 {ECO:0000313|EMBL:RID76923.1};
OS Brassica campestris (Field mustard).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3711 {ECO:0000313|EMBL:RID76923.1, ECO:0000313|Proteomes:UP000264353};
RN [1] {ECO:0000313|EMBL:RID76923.1, ECO:0000313|Proteomes:UP000264353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA Yotsui I., Zachgo S., Schmutz J.;
RT "WGS assembly of Brassica rapa FPsc.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAG7896165.1, ECO:0000313|Proteomes:UP000694005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Genoscope - CEA;
RA William W.;
RL Submitted (JUL-2021) to the EMBL/GenBank/DDBJ databases.
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 EMBL; LS974618; CAG7896165.1; -; Genomic_DNA.
DR EMBL; CM010629; RID76923.1; -; Genomic_DNA.
DR Proteomes; UP000264353; Chromosome a2.
DR Proteomes; UP000694005; Chromosome A02.
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; 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; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR InterPro; IPR001878; Znf_CCHC.
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; PF06839; zf-GRF; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS50158; ZF_CCHC; 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:PRU00047}.
FT DOMAIN 10..154
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 807..846
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 901..918
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 386..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 102640 MW; 7BF391439AE2EF6F CRC64;
MSRRGGGPVT VLNVAEKPSV AKSVAGILSR GSFRTREGRS RYNKIFEFDY AINGQPCRMM
MTSVIGHLME LEFADRFRKW HSCDPADLYQ APVMKHVPED KKDIKKTLEE EARRSDWLVL
WLDCDREGEN IAFEVVDVCR AVKQNLYIRR AHFSALIDRE IHEAVQNLRE PNQLFAQAVD
ARQEIDLRIG ASFTRFQTML LKDRFVIDST GDEERSRVIS YGPCQFPTLG FIVERYWEIQ
AHEPEEFWTI NCSHESEEGL ATFNWMRGHL FDYASAAILY EMCVLEPTAT VMNVPHPREK
FKYPPYPLNT IELEKRASRY FRLSSEHTMK VAEELYQAGF ISYPRTETDS FSSRTDLRAM
VEEQTRHPAW GPYAQRLLEP EGGLWRNPGN GGHDDKAHPP IHPTKFSSGE SNWSRDHLNV
YELVVRHYLA CVSQPAVAAE TTVEIDIAGE RFSASGRAIL AKNYLEVYRF ESWGGSVIPV
YDKGQQFIPT RLTLDSAVTR PPPLLCEADL LSCMDKAGIG TDATMHDHIK KLLDRGYATK
DANTRFSPTN LGEALVMGYD DMGYELWKPN LRAIMEHDMN EVSVGNKTKA EVLETCLQQM
KACFLDARVK KTKLLEAMTI FFERTNNTDE GENQTAGEVV RRCNLCHESD MALRKNQDGN
FMVGCMSYPQ CRNAVWLPGP TLEASVTTDI CQSCGPGPVY KIRFKFRQIR IPPGFDVIHL
GCVGGCDDVL KQLIDICGTG SRSQARAAPG ATPNYVRGSN IRQNNVCIHC QQGGHTSANC
PTRASGYRNP RATGTANPRN NETTVSCATC GTPCAIRTAN TEANRGRKFY SCPSQGCNFF
TWEDSISNGT GNATTGSNSG GSGRRGRGGG RGNRGGGQRG GGRGGGGTSF VSATGEPVSG
RRCFSCGDPS HFANACPNRN S
//
