ID E1F9F6_GIAIA Unreviewed; 973 AA.
AC E1F9F6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=GLP15_3837 {ECO:0000313|EMBL:EFO60919.1};
OS Giardia intestinalis (strain P15) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=658858 {ECO:0000313|EMBL:EFO60919.1, ECO:0000313|Proteomes:UP000008974};
RN [1] {ECO:0000313|EMBL:EFO60919.1, ECO:0000313|Proteomes:UP000008974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P15 {ECO:0000313|EMBL:EFO60919.1,
RC ECO:0000313|Proteomes:UP000008974};
RX PubMed=20929575; DOI=10.1186/1471-2164-11-543;
RA Jerlstrom-Hultqvist J., Franzen O., Ankarklev J., Xu F., Nohynkova E.,
RA Andersson J.O., Svard S.G., Andersson B.;
RT "Genome analysis and comparative genomics of a Giardia intestinalis
RT assemblage E isolate.";
RL BMC Genomics 11:543-543(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFO60919.1}.
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DR EMBL; ACVC01000535; EFO60919.1; -; Genomic_DNA.
DR AlphaFoldDB; E1F9F6; -.
DR STRING; 658858.E1F9F6; -.
DR EnsemblProtists; EFO60919; EFO60919; GLP15_3837.
DR VEuPathDB; GiardiaDB:GLP15_3837; -.
DR OMA; GKWSFAN; -.
DR OrthoDB; 166270at2759; -.
DR Proteomes; UP000008974; 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; 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; PS50880; TOPRIM; 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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 1..145
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 949..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..973
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 107587 MW; 5B8867158EC73F25 CRC64;
MILLIAEKPS IAEMISRNYG EGAKKLDSMS FPTYTFVQSF EGSKETFMCT SVAGHVFEID
FDAEFNGSSV PQERLFERGH VHYSFTDSGS TVAKHLKSIG GKATQLILCL DNDREGENIC
FEVLKVLKPT LRSNCRIRRA RFSAVTKAEI HNAFCNLDKP DQNLSDAVEA RQELDLKIGV
AFTRFQTAHL HAQFADLQSS VISYGPCQTP TLSFCVSRHD EIQRFRPKQI FSLDVCALIG
DQLCPLRWQG VPSESREVIE EKRARLLEKS ATKCLKVLSF KSSKSTLPRP LPMNTVALLK
AASTVLGLSP NSAMALAERL YIAGYISYPR TESTTYPSGY NLREIVLALK ESSSTRISQS
AQNLLPSSKK SVDENVRYTN PRKGTDQGDH PPIMPTGLIP HGVSGDELSL YNLITKHFLA
TVSPDAVYGH SSLTLQSVDV PSETFLFSVT EVIDQGWKAL YSTTEFTSMQ DNDLSDDLAD
ENLLLDKETL QAISATGATL TIASAAIKAG MTRPPAYLSE SDLLGLMEKH GIGTDASMAT
HIGNIVTRAY VELRVTGRRR CLVPTSMGIS LIHGYQLIDG DLSSPQLRAS IERDVTRIAE
GKIKKDVLVN QVLSKFLTKF LNFKQNISKL EALLNAKFTS IKKAGRPFIL CGECHRYTDL
IEQYPPRVYC VTCDKLYTIP MRGKLIEIPS RKCPYDGWPL ILHVAEATQR RTFFCLHCYT
FGLSKEEALM QLQTAAADGN IDIEQTKTIT CGMCLNSLCQ MSLPRTQVGA CWHCNADGRV
MLSVSRDGPD SNLKATNDTS VVACSPAVHE QTPEKAVESL SASAQSRKIS ITIKPQAKIS
LSIPQANKSS ENAPVVSVPK KVSNLAELVG GYLYLDAGTA RRFPGVYCNR CNFQITFQEC
KLSLSSDFCV CGRTKLRATD FSDKKSTNSE VYGCVHCDDE LFQTVAEYKD SSGHHPRRTA
QPKRHGPKGR RHR
//
