ID A0A1U8PRY9_GOSHI Unreviewed; 940 AA.
AC A0A1U8PRY9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN Name=LOC107962151 {ECO:0000313|RefSeq:XP_016753891.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016753891.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016753891.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016753891.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446}.
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DR RefSeq; XP_016753891.1; XM_016898402.1.
DR AlphaFoldDB; A0A1U8PRY9; -.
DR OrthoDB; 167550at2759; -.
DR Proteomes; UP000189702; Chromosome 11.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 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 HAMAP; MF_00952; Topoisom_1_prok; 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; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034149; TOPRIM_TopoI.
DR NCBIfam; TIGR01051; topA_bact; 1.
DR PANTHER; PTHR42785:SF1; DNA TOPOISOMERASE; 1.
DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 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.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 326..441
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 161..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 104981 MW; 290A6D11EB1A8058 CRC64;
MQRCLLSSPP TSNCAALRLH PSLMPKFQLK VVKLISSIPS HPRFKKLRPP SSLMPSYPNF
ATLHSAFTFA LPPNHITYTL PRNRNVISTC VTPQAMRSTS AFVPLFKMFF SHSPPVATKN
DGMSVRDGKS SGFSFRRFHR HWKKLKGVAA LKGDKAAPFE SPASTSLLNS AKPDSTSNSL
VNTANPDSTS TSLVINAKPE SKASLKKKKQ SRSKNKKEQV SSTVVSEETP VAKSSKTSSL
VGTSNISKKN GQRLKQTSEK ISTGNLLTEA PDGSASTKKQ SKKNSTGSGR KRQPVADVHE
PVQKQVQKNI SQREKPLKQL YPPTAKSVMV VESVTKAKVI QGYLGDMFEV LPSYGHVRDL
AARSGSVRPD DDFSMVWEVP SAAWTHLKSI KVALSGAENL VLASDPDREG EAIAWHIIEM
LQQQDALGEN VTVARVVFHE ITEASIKSAL QMPREIDVNL VHAYLARRAL DYLIGFNISP
LLWRKLPGCQ SAGRVQSAAL SLICDRETEI DEFKPLEYWS IEVRFEEPNS FPAHLTHFNS
KKLGQFSISS DTEAKDVQQK INIENFKVIN SKRNTMRRNP PAPYITSTLQ QDAANKLNFP
ATYTMKLAQK LYEGIQLSDG KATGLITYSR TDGLHISDEA VKDIRSLVME RYGSRFTPEN
ACKYYKKVKN AQEAHEAIRP TNIRRLPSML VGALDEDSLK LYTLIWSRTM ACQMEPSILE
QIQLETGNCD ESIIFRSSCS RVEFLGYQSA YQDVESGTIR FKDNEASHNA EAFGILSSLK
KGDQLCIGEV EIKQHHTQAP PRYSEGSLVK KLEELGIGRP STYASTLKVL QDRNYVTVKS
RVLYPEFRGR MVSAFLSHHF SEVTDYSFTA DMETELDNVS VGLTEWKGLL RDYWTRFSSY
CSRAESVHIH QVEKMLEKTF GDFLFASLPN KSRTCPSLLL
//
