ID   F1SVL0_METKA            Unreviewed;       984 AA.
AC   F1SVL0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Topoisomerase V {ECO:0000313|EMBL:AAM02649.1};
GN   OrderedLocusNames=MK1436 {ECO:0000313|EMBL:AAM02649.1};
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC   Methanopyraceae; Methanopyrus.
OX   NCBI_TaxID=190192 {ECO:0000313|EMBL:AAM02649.1, ECO:0000313|Proteomes:UP000001826};
RN   [1] {ECO:0000313|EMBL:AAM02649.1, ECO:0000313|Proteomes:UP000001826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938
RC   {ECO:0000313|Proteomes:UP000001826};
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
RN   [2] {ECO:0007829|PDB:4GFJ}
RP   X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 1-685 IN COMPLEX WITH ZINC, AND
RP   DISULFIDE BONDS.
RX   PubMed=23125368; DOI=10.1093/nar/gks1017;
RA   Rajan R., Prasad R., Taneja B., Wilson S.H., Mondragon A.;
RT   "Identification of one of the apurinic/apyrimidinic lyase active sites of
RT   topoisomerase V by structural and functional studies.";
RL   Nucleic Acids Res. 41:657-666(2013).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009439; AAM02649.1; -; Genomic_DNA.
DR   PDB; 4GFJ; X-ray; 2.91 A; A=1-685.
DR   PDBsum; 4GFJ; -.
DR   AlphaFoldDB; F1SVL0; -.
DR   SMR; F1SVL0; -.
DR   STRING; 190192.MK1436; -.
DR   PaxDb; 190192-MK1436; -.
DR   EnsemblBacteria; AAM02649; AAM02649; MK1436.
DR   KEGG; mka:MK1436; -.
DR   HOGENOM; CLU_302809_0_0_2; -.
DR   InParanoid; F1SVL0; -.
DR   OrthoDB; 374074at2157; -.
DR   EvolutionaryTrace; F1SVL0; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   Gene3D; 1.10.150.740; -; 1.
DR   Gene3D; 1.10.8.1010; -; 2.
DR   Gene3D; 6.10.250.950; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 6.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR049334; Topo-V_HhH2_2nd.
DR   InterPro; IPR024065; TopoV_catalytic_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF14520; HHH_5; 4.
DR   Pfam; PF13412; HTH_24; 1.
DR   Pfam; PF21616; Topo-V_HhH_2_2nd; 1.
DR   SMART; SM00278; HhH1; 11.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 6.
DR   SUPFAM; SSF140979; Topoisomerase V catalytic domain-like; 2.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4GFJ}; Metal-binding {ECO:0007829|PDB:4GFJ};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001826};
KW   Zinc {ECO:0007829|PDB:4GFJ}.
FT   DOMAIN          411..430
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          447..466
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          468..487
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          560..579
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          622..641
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          656..675
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          732..751
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          855..874
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          887..906
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          912..931
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   DOMAIN          944..963
FT                   /note="Helix-hairpin-helix DNA-binding motif class 1"
FT                   /evidence="ECO:0000259|SMART:SM00278"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:4GFJ"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:4GFJ"
FT   DISULFID        314..338
FT                   /evidence="ECO:0007829|PDB:4GFJ"
SQ   SEQUENCE   984 AA;  112207 MW;  63ABCC55177571D6 CRC64;
     MALVYDAEFV GSEREFEEER ETFLKGVKAY DGVLATRYLM ERSSSAKNDE ELLELHQNFI
     LLTGSYACSI DPTEDRYQNV IVRGVNFDER VQRLSTGGSP ARYAIVYRRG WRAIAKALDI
     DEEDVPAIEV RAVKRNPLQP ALYRILVRYG RVDLMPVTVD EVPPEMAGEF ERLIERYDVP
     IDEKEERILE ILRENPWTPH DEIARRLGLS VSEVEGEKDP ESSGIYSLWS RVVVNIEYDE
     RTAKRHVKRR DRLLEELYEH LEELSERYLR HPLTRRWIVE HKRDIMRRYL EQRIVECALK
     LQDRYGIRED VALCLARAFD GSISMIATTP YRTLKDVCPD LTLEEAKSVN RTLATLIDEH
     GLSPDAADEL IEHFESIAGI LATDLEEIER MYEEGRLSEE AYRAAVEIQL AELTKKEGVG
     RKTAERLLRA FGNPERVKQL AREFEIEKLA SVEGVGERVL RSLVPGYASL ISIRGIDRER
     AERLLKKYGG YSKVREAGVE ELREDGLTDA QIRELKGLKT LESIVGDLEK ADELKRKYGS
     ASAVRRLPVE ELRELGFSDD EIAEIKGIPK KLREAFDLET AAELYERYGS LKEIGRRLSY
     DDLLELGATP KAAAEIKGPE FKFLLNIEGV GPKLAERILE AVDYDLERLA SLNPEELAEK
     VEGLGEELAE RVVYAARERV ESRRKSGRQE RSEEEWKEWL ERKVGEGRAR RLIEYFGSAG
     EVGKLVENAE VSKLLEVPGI GDEAVARLVP GYKTLRDAGL TPAEAERVLK RYGSVSKVQE
     GATPDELREL GLGDAKIARI LGLRSLVNKR LDVDTAYELK RRYGSVSAVR KAPVKELREL
     GLSDRKIARI KGIPETMLQV RGMSVEKAER LLERFDTWTK VKEAPVSELV RVPGVGLSLV
     KEIKAQVDPA WKALLDVKGV SPELADRLVE ELGSPYRVLT AKKSDLMRVE RVGPKLAERI
     RAAGKRYVEE RRSRRERIRR KLRG
//