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Database: UniProt
Entry: S0DUM3_GIBF5
LinkDB: S0DUM3_GIBF5
Original site: S0DUM3_GIBF5 
ID   S0DUM3_GIBF5            Unreviewed;       644 AA.
AC   S0DUM3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   13-SEP-2023, entry version 50.
DE   RecName: Full=ATP-dependent DNA helicase II subunit 1 {ECO:0000256|ARBA:ARBA00021796};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   AltName: Full=ATP-dependent DNA helicase II subunit Ku70 {ECO:0000256|ARBA:ARBA00031811};
GN   ORFNames=FFUJ_04557 {ECO:0000313|EMBL:CCT64243.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT64243.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|EMBL:CCT64243.1, ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
CC   -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase.
CC       Involved in non-homologous end joining (NHEJ) DNA double strand break
CC       repair. DNA-binding is sequence-independent but has a high affinity to
CC       nicks in double-stranded DNA and to the ends of duplex DNA. Binds to
CC       naturally occurring chromosomal ends, and therefore provides
CC       chromosomal end protection. Required also for telomere recombination to
CC       repair telomeric ends in the absence of telomerase. KU70, of the
CC       KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA
CC       component of telomerase. Involved in telomere maintenance. Interacts
CC       with telomeric repeats and subtelomeric sequences thereby controlling
CC       telomere length and protecting against subtelomeric rearrangement.
CC       Maintains telomeric chromatin, which is involved in silencing the
CC       expression of genes located at the telomere. Required for mating-type
CC       switching. {ECO:0000256|ARBA:ARBA00024890}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC       {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ku70 family.
CC       {ECO:0000256|ARBA:ARBA00005240}.
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DR   EMBL; HF679024; CCT64243.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0DUM3; -.
DR   STRING; 1279085.S0DUM3; -.
DR   EnsemblFungi; CCT64243; CCT64243; FFUJ_04557.
DR   VEuPathDB; FungiDB:FFUJ_04557; -.
DR   HOGENOM; CLU_014815_3_0_1; -.
DR   OrthoDB; 21093at2759; -.
DR   Proteomes; UP000016800; Chromosome 2.
DR   GO; GO:0099115; C:chromosome, subtelomeric region; IEA:EnsemblFungi.
DR   GO; GO:0140445; C:chromosome, telomeric repeat region; IEA:EnsemblFungi.
DR   GO; GO:0043564; C:Ku70:Ku80 complex; IEA:InterPro.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042162; F:telomeric DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR   GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0000723; P:telomere maintenance; IEA:EnsemblFungi.
DR   CDD; cd00788; KU70; 1.
DR   CDD; cd01458; vWA_ku; 1.
DR   Gene3D; 1.10.1600.10; -; 1.
DR   Gene3D; 2.40.290.10; -; 1.
DR   Gene3D; 4.10.970.10; Ku70, bridge and pillars; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR006165; Ku70.
DR   InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR   InterPro; IPR027388; Ku70_bridge/pillars_dom_sf.
DR   InterPro; IPR047087; KU70_core_dom.
DR   InterPro; IPR005160; Ku_C.
DR   InterPro; IPR005161; Ku_N.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR016194; SPOC-like_C_dom_sf.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   NCBIfam; TIGR00578; ku70; 1.
DR   PANTHER; PTHR12604; KU AUTOANTIGEN DNA HELICASE; 1.
DR   PANTHER; PTHR12604:SF2; X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 6; 1.
DR   Pfam; PF02735; Ku; 1.
DR   Pfam; PF03730; Ku_C; 1.
DR   Pfam; PF03731; Ku_N; 1.
DR   Pfam; PF02037; SAP; 1.
DR   PIRSF; PIRSF003033; Ku70; 1.
DR   SMART; SM00559; Ku78; 1.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   SUPFAM; SSF100939; SPOC domain-like; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CCT64243.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT   DOMAIN          606..640
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..582
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        25
FT                   /note="Schiff-base intermediate with DNA; for 5'-
FT                   deoxyribose-5-phosphate lyase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003033-1"
SQ   SEQUENCE   644 AA;  72107 MW;  E8EF8AC30A3AEF8A CRC64;
     MADKQPWRKE DEDEEEQELD ENNYKAQKDA ILLAIDVSKS MLEPPPPSDS KKADRDSPVQ
     AALKCAYHLM EQRIISNPKD MMGILLFGTK KSKFQDSVEG PSGLGYPHCY LFTDLDVPAA
     EDIQALKTLV EDGEDEDEVL TPSDEPVSMS NVLFCANQIF TTKAANFGSR RLFIVTDNDN
     PHASDKQAKS AAAVRAKDLY DLGILIDLFP ITRGDGKFDL HKFYDDIIYR DPVGEANMTE
     VRTSKSGNGL TLLNSLISNV NSKQTAKRAL FSNLPFEIAP GLRISVKGYN IVHRQTPART
     CYVWLDGEKP QIATSETTRI AEDSARTVEK AEIKKAYKFG GEYVYFSPDE QKSLKDFGSP
     IIRIIGFKPR SLLPIWASTK KSTFIFPSEE DYVGSTRVFT ALWQKLLKDD KMGVAWCITR
     ANAQPMLAAI IPSRERSDHG SGTPYLPAGL WIYPLPFQDD LRNINPPSEV LRSSGELTTQ
     MRTIIQQLQL PKAMYDPLKY PNPALQWHYR ILQALALEEE VPEKADDATE PKYKAISKRA
     GGYLEEWSES LEEESGKVAN KKSTKRETDD EDMERPVKKS RGSSEKATGS SFSMAQLKAA
     IEGGTIQKMT VAQLKDILAT KGMSTAGRKV ELIERIEEWI EESS
//
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