GYRA_ARATH
ID GYRA_ARATH Reviewed; 950 AA.
AC Q9CAF6; Q9SG75;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=DNA gyrase subunit A, chloroplastic/mitochondrial;
DE EC=5.6.2.2 {ECO:0000250|UniProtKB:P0AES4};
DE Flags: Precursor;
GN Name=GYRA; OrderedLocusNames=At3g10690; ORFNames=F13M14.2, T7M13.23;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15136745; DOI=10.1073/pnas.0400836101;
RA Wall M.K., Mitchenall L.A., Maxwell A.;
RT "Arabidopsis thaliana DNA gyrase is targeted to chloroplasts and
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7821-7826(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
RA Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
RT "Purification of a plant mediator from Arabidopsis thaliana identifies PFT1
RT as the Med25 subunit.";
RL Mol. Cell 26:717-729(2007).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded DNA in an ATP-dependent manner.
CC {ECO:0000269|PubMed:15136745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000250|UniProtKB:P0AES4};
CC -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA
CC breakage and rejoining; the B chain catalyzes ATP hydrolysis (By
CC similarity). Associated with the mediator complex.
CC {ECO:0000250|UniProtKB:P0AES4, ECO:0000269|PubMed:17560376}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15136745}. Mitochondrion
CC {ECO:0000269|PubMed:15136745}. Nucleus {ECO:0000305|PubMed:15136745}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000250|UniProtKB:P0AES4}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19580.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51377.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011560; AAG51377.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011708; AAF19580.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74943.1; -; Genomic_DNA.
DR RefSeq; NP_187680.2; NM_111905.3.
DR AlphaFoldDB; Q9CAF6; -.
DR SMR; Q9CAF6; -.
DR BioGRID; 5572; 21.
DR IntAct; Q9CAF6; 1.
DR STRING; 3702.AT3G10690.1; -.
DR iPTMnet; Q9CAF6; -.
DR PaxDb; Q9CAF6; -.
DR PRIDE; Q9CAF6; -.
DR ProteomicsDB; 247279; -.
DR EnsemblPlants; AT3G10690.1; AT3G10690.1; AT3G10690.
DR GeneID; 820238; -.
DR Gramene; AT3G10690.1; AT3G10690.1; AT3G10690.
DR KEGG; ath:AT3G10690; -.
DR Araport; AT3G10690; -.
DR TAIR; locus:2075765; AT3G10690.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_002977_6_1_1; -.
DR InParanoid; Q9CAF6; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 316973at2759; -.
DR PhylomeDB; Q9CAF6; -.
DR PRO; PR:Q9CAF6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9CAF6; baseline and differential.
DR Genevisible; Q9CAF6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR HAMAP; MF_01897; GyrA; 1.
DR InterPro; IPR005743; GyrA.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; DNA-binding; Isomerase; Mitochondrion;
KW Nucleotide-binding; Nucleus; Plastid; Reference proteome; Topoisomerase;
KW Transcription; Transcription regulation; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT CHAIN ?..950
FT /note="DNA gyrase subunit A, chloroplastic/mitochondrial"
FT /id="PRO_0000247945"
FT MOTIF 622..628
FT /note="GyrA-box"
FT /evidence="ECO:0000250|UniProtKB:P0AES4"
FT ACT_SITE 215
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AES4"
SQ SEQUENCE 950 AA; 104538 MW; 3998C233EA512797 CRC64;
MTPVLCHSTA SIPNPNSLMS LSSTLRLSSS LLRRSFFRFP LTDPLCRLRR TEPSATRFFS
SRTPRSGKFV VGAGKRGDEQ VKEESGANNG GLVVSGDESR IVPFELHKEA TESYMSYALS
VLLGRALPDV RDGLKPVHRR ILFAMHELGM SSKKPYKKCA RVVGEVLGKF HPHGDTAVYD
SLVRMAQSFS LRCPLIQGHG NFGSIDADPP AAMRYTECRL DPLAEAVLLS DLDQDTVDFV
ANFDNSQKEP AVLPARLPAL LLNGASGIAV GMATNIPPHN LGELVDVLCA LIHNPEATLQ
ELLEYMPAPD FPTGGIIMGN LGVLDAYRTG RGRVVVRGKA EVELLDPKTK RNAVIITEIP
YQTNKATLVQ KIAELVENKT LEGISDIRDE SDRNGMRVVI ELKRGGDPAL VLNNLYRHTA
LQSSFSCNMV GICDGEPKLM GLKELLQAFI DFRCSVVERR ARFKLSHAQQ RKHIIEGIVV
GLDNVDEVIE LITKASSHSS ATAALQSEYG LSEKQAEAIL EITLRRLTAL ERKKFTDESS
SLTEQITKLE QLLSTRTNIL KLIEQEAIEL KDRFSSPRRS MLEDSDSGDL EDIDVIPNEE
MLMAVSEKGY VKRMKADTFN LQHRGTIGKS VGKLRVDDAM SDFLVCHAHD HVLFFSDRGI
VYSTRAYKIP ECSRNAAGTP LVQILSMSEG ERVTSIVPVS EFAEDRYLLM LTVNGCIKKV
SLKLFSGIRS TGIIAIQLNS GDELKWVRCC SSDDLVAMAS QNGMVALSTC DGVRTLSRNT
KGVTAMRLKN EDKIASMDII PASLRKDMEE KSEDASLVKQ STGPWLLFVC ENGYGKRVPL
SSFRRSRLNR VGLSGYKFAE DDRLAAVFVV GYSLAEDGES DEQVVLVSQS GTVNRIKVRD
ISIQSRRARG VILMRLDHAG KIQSASLISA ADEEETEGTL SNEAVEAVSL
