ID A0A1S4E5M8_CUCME Unreviewed; 1215 AA.
AC A0A1S4E5M8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
DE AltName: Full=Omega-protein {ECO:0000256|ARBA:ARBA00032877};
DE AltName: Full=Relaxing enzyme {ECO:0000256|ARBA:ARBA00032235};
DE AltName: Full=Swivelase {ECO:0000256|ARBA:ARBA00030003};
DE AltName: Full=Untwisting enzyme {ECO:0000256|ARBA:ARBA00031985};
GN Name=LOC103503742 {ECO:0000313|RefSeq:XP_016903546.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_016903546.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_016903546.1}
RP IDENTIFICATION.
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_016903546.1; XM_017048057.1.
DR AlphaFoldDB; A0A1S4E5M8; -.
DR OrthoDB; 167550at2759; -.
DR Proteomes; UP000089565; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 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 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; IPR013498; Topo_IA_Znf.
DR InterPro; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
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 Pfam; PF13368; Toprim_C_rpt; 2.
DR Pfam; PF01396; zf-C4_Topoisom; 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:UP000089565};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 416..531
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 172..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 134767 MW; 07121E967A2242A5 CRC64;
MSQLQRSLSL ASSSSNAISS SVFSTALSAF SSSRLRHFST KLQGSTLQNY TSKCIPVLPF
PTACSSARCS QLIFRKGGVT FAVKTERAKA GQYRACDGPS VFTLYSRLPL RFPHSAASPN
ASNQQLLNCT FTHKLPNYRA FGRKFFSNTT EASSGTKNKN VKYLRNGTST IEGLNKKSKG
AKPVATSRKK TRISASAPSG STHVDGTNSS DQLVGATKEA NLVSSNSSSS IRRASKGLNE
KKSWSKKKKK AISSTNDADV EAVCKDSQSK SFGSSNTDQD VVQDPKKEAI SSTIRKASKG
LNEKKSWSKN KKEAISSTND ADVEAVCKDG QSKSFGSSNT DQDVVQDPKK NVTKGTSKDS
GSTKQQSNKK KCNSSRNKEA TKGANKLQQK PNVIVDTRGT SQGKTTFKQL YPPMGKSVLV
VESVTKAKVI QDYLGDMFVV LPSHGHVRDL AARSGSVRPE DDFIMVWEVP SAAWTHLKSI
ELSLNGAENL ILASDPDQEG EAIAWHIIEM LQHQHALHEG ISIARVVFHE ITEASIKSAL
QSPRVIDENL VQAYLARRAL DYLIGFNISP LLWKKLPGCR SPGRVQSAAL ALICDRETEI
DKFQAQEYWT IDVKLNQKDP CSSVEDFAVP AHLTHFDSKK LNQFPISSNM EAKNIETALK
SVNFQVLSSR KNIVQTNPPM PYITSTLQQD AAKKFNFPAT YTMKLAQKLY EGIQLADGKA
AGLITYPRTD GLHISDEAVK DIHSLIMQRF GQDFVSKSGH KYFKKVKNAQ EADEAIRPTD
VQRLPSMLVG TLDEDSHKLY SLIWLRTMAC QMEPSITEEI KIDCGLADES IIARSTCSRV
QFRGFRVVFE DPEVHAVKHK DHEESGRDEL FRILNPLKPG DQLSLGAVEL KQHFTQPPPR
YSEGTLVKKM EELGIGRPST YATTLKVLKD RKYVSVKSRV LHPEFRGRMV SAFLSHHFSE
VTDYSFTADM ENELDNVSAG LTEWKGLLRD YWTRFSSYFE RVNSVHIHQV EKMLEKKYGD
FLFSFLPDNS RACPSCQEGT LIFKLSRFGP GYFIGCDQHP RCKHIAKTLH GEDEDNDNSF
KEPKLLGLHP DLNEKILLKK GPFGFYVQLG EDRKGFLPKR ASLSQIKDVS SITLEDAVER
LCYPVTLGKH PKDGEPVIIK MARVGFAVGH RRTTASIPEN LKPNDIDLAK ALELLSSSSI
RRSGRSKSNP KVASC
//
