ID V9KNJ4_CALMI Unreviewed; 384 AA.
AC V9KNJ4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO99851.1};
RN [1] {ECO:0000313|EMBL:AFO99851.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:AFO99851.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TOP6A family.
CC {ECO:0000256|ARBA:ARBA00006559}.
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DR EMBL; JW867334; AFO99851.1; -; mRNA.
DR AlphaFoldDB; V9KNJ4; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IEA:InterPro.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR013048; Meiotic_Spo11.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10848; MEIOTIC RECOMBINATION PROTEIN SPO11; 1.
DR PANTHER; PTHR10848:SF0; MEIOTIC RECOMBINATION PROTEIN SPO11; 1.
DR Pfam; PF21180; TOP6A-Spo11_Toprim; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01551; SPO11HOMOLOG.
DR PRINTS; PR01550; TOP6AFAMILY.
DR SUPFAM; SSF56726; DNA topoisomerase IV, alpha subunit; 1.
PE 2: Evidence at transcript level;
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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 97..158
FT /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04406"
FT DOMAIN 207..378
FT /note="Topoisomerase 6 subunit A/Spo11 TOPRIM"
FT /evidence="ECO:0000259|Pfam:PF21180"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFO99851.1"
SQ SEQUENCE 384 AA; 43449 MW; 62FBE9A3DF4CAAB2 CRC64;
RALEQHRAAL LRAAPQRPAA APTPARAEAF ASSNVLVAIE SVIKEVLTYF AKGEAAVITL
DKRSSWENIW FDDTVGLQMV FDCTVTKVKC ENLKSMQRFA LILKILSMIY KLVQSNTYAT
KRDLFYSDTQ VFGSQSVLDA IINDISCLLK VPRRYLHILS TARGYIAGDL YYTEEDGTRV
NCSCNSTAIL VPSNVDGVKY LNSTAKFVLI VEKDATFQRL LDDAFCTKLS PCIIITGKGV
PDLNTRLMVR KLWDTLHIPV FALVDADPYG IEIMCIYKYG SMSMSFEAHN LTVPIIRWLG
LLPSDIQRLN VPKEVLIPLN KRDISKLTIL QKRPFIDWQP QWKNEMEIME KCKMKAEIQA
LASISSDYLT RVYLPNKIKF GGWI
//
