ID I7M423_TETTS Unreviewed; 1369 AA.
AC I7M423;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN ORFNames=TTHERM_00465030 {ECO:0000313|EMBL:EAS04755.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS04755.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
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 EMBL; GG662441; EAS04755.2; -; Genomic_DNA.
DR RefSeq; XP_001025000.2; XM_001025000.2.
DR STRING; 312017.I7M423; -.
DR GeneID; 7839907; -.
DR KEGG; tet:TTHERM_00465030; -.
DR eggNOG; KOG1957; Eukaryota.
DR InParanoid; I7M423; -.
DR OrthoDB; 166270at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
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: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 PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 243..392
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 21..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1369 AA; 157618 MW; 5EB0540815DC6E79 CRC64;
MEQDFQGKFN RSFNMQQDQF KAQHSFIQDK QNQGQKSTFQ YTQNAQQKFQ HNPRFNKFDH
EADQSSYSLK QFDRAQSYGK NYGKDRNMHI EKDGSDLQEQ STGAAPLRKG SLNQYQKDQS
SFQGKFNQRK DSNNEQFQSL RGLSQDDSKV PAKTGYLGKN FDPNYKNRLA KQREGSLENQ
EDGEIKANSN PLRQPRNNSS SFQGSSGSVH QPPRQQNQPY FSNVHAKGLL PYSVDEGFDS
FVTVLMVAEK PSIARSIAEA LGGAGFTTRK GICKFSNVFT FYGHIFGKKA LIKVTSVIGH
IYTSDFTQEY QDWRRVDPYK LFNATTLKKE TNPNSQIIQH LQKEAMGASY LILWLDNDRE
GENICFEVLT ICKPELIKED FQQIFRAKFS SITPIDIRKA FDELSIGPNF NESQAVDARQ
IIDLKVGVAF SRFQTRYLVR KYEDLNNKKI TFGPCQTPTL SFCVQRDDEI KDFISKPFYR
IIPKISLVPN ELINLEWTKE RTYDQQEALD VKQELESIGQ TSVVKVDNKE TQKIKPVALN
TVNFLKMASK QYGLGPQNAM QVAEKLYLGG FITYPRTEST KYPDKFDFNS VLHAVCQYHQ
NQNISIYAQK LQQNGIHKSR LGKDVGDHPP ITPTNKIMRQ QLSRDEQNIY ELVCRHFLAT
VSSDCRLYKK KVLFQTGNQT FSLIGTAVID KGYLEALPWQ KIYENEIPNF SEGDQIYLHS
VDIHSGKTQP PDHLTESDLI SLMEQNGIGT DASMAQHIQN ICDREYVQVV GQARRLVPTE
LGSSLIHAYA EIDPELVAPN LRSSIERSVD LISQGELDKD QVLQSVIELF KNKYLYFVSK
VGVLDKYFDP IYQSIETTIS QAQYFTKCGR CKCNMKILDK IGKIFCERCK FMYGLPRDSK
YSIAGECFCP IDGFQLVLIE STVKGNTKRF TICPLCFQKT PELENYSSEE KYQRTSCNLC
SNRSCQFSMV NNEIGPCPHC KYEKGGRLVL DWPDNNNYTM TCNACMYQYL IVKNGKLIRS
QMKCANCNCF QVKIETSDGF SALGCLFCDI QTKNRMEERP PTEPQGESSL RNQRYFNEDL
DKSIEDQPLK LKQPQALQIN NNQKVIGLKN NIMEIENQIT EADQPIKKRR GRPPKAATEF
NFQEKENIQD EANTKPQTRK PRATKAIKKL SQEEGEADED EEQFSKPTHP TVDFVKKGIQ
KAPKSYGNTF NQFKAQQQQK IDNQFQNSNF EDILEDSHKQ DLEFFSKFPR NNIIKENQET
YEILKESTML LSEIDGHSTF KNYSSLENSF QQNNRKPRQM NNFKQNQFNN QQFQGNSFKQ
NISTNSSIQQ NNFQQQRKPN YEKEMNNSFQ NKNNSALDSS SILLKQLDF
//
