ID A0A0D2I1V0_9EURO Unreviewed; 705 AA.
AC A0A0D2I1V0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE RecName: Full=ATP-dependent DNA helicase II subunit 2 {ECO:0000256|ARBA:ARBA00021792, ECO:0000256|PIRNR:PIRNR016570};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|PIRNR:PIRNR016570};
GN ORFNames=Z518_11131 {ECO:0000313|EMBL:KIW99718.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIW99718.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIW99718.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIW99718.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|PIRNR:PIRNR016570};
CC -!- SUBUNIT: Heterodimer of Ku70 and Ku80. {ECO:0000256|ARBA:ARBA00011584}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR016570}.
CC -!- SIMILARITY: Belongs to the ku80 family. {ECO:0000256|ARBA:ARBA00007726,
CC ECO:0000256|PIRNR:PIRNR016570}.
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DR EMBL; KN847485; KIW99718.1; -; Genomic_DNA.
DR RefSeq; XP_013266855.1; XM_013411401.1.
DR AlphaFoldDB; A0A0D2I1V0; -.
DR STRING; 1442369.A0A0D2I1V0; -.
DR GeneID; 25299202; -.
DR VEuPathDB; FungiDB:Z518_11131; -.
DR HOGENOM; CLU_010975_1_1_1; -.
DR OrthoDB; 5884at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0043564; C:Ku70:Ku80 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042162; F:telomeric DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd00873; KU80; 1.
DR Gene3D; 1.10.1600.10; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 1.25.40.240; Ku, C-terminal domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR024193; Ku80.
DR InterPro; IPR036494; Ku_C_sf.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR014893; Ku_PK_bind.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12604; KU AUTOANTIGEN DNA HELICASE; 1.
DR PANTHER; PTHR12604:SF4; X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 5; 1.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF08785; Ku_PK_bind; 1.
DR PIRSF; PIRSF016570; Ku80; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF101420; C-terminal domain of Ku80; 1.
DR SUPFAM; SSF100939; SPOC domain-like; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR016570};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR016570};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|PIRNR:PIRNR016570};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR016570};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR016570};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PIRNR:PIRNR016570};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR016570};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR016570};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR016570};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 5..210
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
SQ SEQUENCE 705 AA; 79425 MW; 3055502B3E7ED87C CRC64;
MEKEATIYVI DLARSMGQTR SGRDLSDLDW ALQYVWDKIT NIVFTGRKTL QIGIVGLGTD
ETSNDMQGDE SYKNISILQP IAQILMPELQ ALPSMLKPSK TDDRDVLSGI IIAVDMMMKH
CKKLKYKKKI VVITSATGHI DDDDIESTAY QFKNNDIELV VLGIDFDDPD YGFKEKDKPV
QKTKNEQILK HLVELGGGIL GTMQEAIDEL SRPQIIPVRP TPTFKGQLRL GDPQNYDTAL
CIDVERYFKV SVKRAPTASS YVVRDTASSA TDENLATIYN MQKYKVKDES YEGGIRLLER
DELAKGYEYG RTAVAISETE QNITKLETEM AYDIIGFIPV EKVERYMLLD NTNMIVSQKG
NDKAAFALSS VIHALFELGS AAVGRLVKKD MSEPILTLLS PLAESDFECL VENILPFAED
VRTYRFPPLD KVITVSGKEL TEHRNLPNEK LLQSMSDFVD SASLVHDDEE EMAMEDTFSP
VLHTIEGAIK YRAVHPNDDI PEKSEVFLAC SKQPGEVQER SKAALSRLMA AADVKKVPPK
AKGRKRPREV EKPLSGLNVE DLFRREKRTR ISPDNAIPEY KRMLGTSDDI DTLKEANSQM
TKIVEDLIQN SFGEANDDRV LEMLNVIRQE MLAYEEPRAY NDILRQIKEK LMAGELGGNR
GELWWKIRVS KLGLISNEAS HVSDVSRTDA DAFMTMRMDV SVNHD
//
