ID F7VNH3_SORMK Unreviewed; 646 AA.
AC F7VNH3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 13-SEP-2023, entry version 67.
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=SMAC_00927 {ECO:0000313|EMBL:CCC06902.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC06902.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC06902.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC06902.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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}.
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:CCC06902.1}.
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; CABT02000002; CCC06902.1; -; Genomic_DNA.
DR RefSeq; XP_003350038.1; XM_003349990.1.
DR AlphaFoldDB; F7VNH3; -.
DR STRING; 771870.F7VNH3; -.
DR GeneID; 10807547; -.
DR KEGG; smp:SMAC_00927; -.
DR VEuPathDB; FungiDB:SMAC_00927; -.
DR eggNOG; KOG2327; Eukaryota.
DR HOGENOM; CLU_014815_3_0_1; -.
DR InParanoid; F7VNH3; -.
DR OMA; FWANVKH; -.
DR OrthoDB; 21093at2759; -.
DR Proteomes; UP000001881; 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-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: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; 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};
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:UP000001881};
KW Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 608..642
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 26
FT /note="Schiff-base intermediate with DNA; for 5'-
FT deoxyribose-5-phosphate lyase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003033-1"
SQ SEQUENCE 646 AA; 72435 MW; 780251BAFA50A02F CRC64;
MSWRKDDEER PDSDEGDEEL DENDYKTQKD AVLFAIEVSK SMLKPPAATG DKKADKDSAL
TAALKCAYQI MQQRIIAQPR DMMGVLLFGT EKSKFRDDSG NGTGYPHCYL LSDLDVPGAE
DVKKLRALVE DDEDEDEIMV PSKEPVIMSN MLFCANQVFT TNAANFGSRR LFIVTDNDDP
HAGDKQAKSS AAVRAKDLYD LGIVIELFPI SREGKKFDLS KFYDDIIYRD PAAEVGELGG
PKTSKAGDGL TLLNSLISNI NSKQTPKRSY FSNLPFELAP GLTISVKGYI PLNRQTPSRS
CYVYEGEEQA QVVQSETAQV DFAARTVEKT ELRKGYKFGG EHICFKPEEL AELKQMGKKT
LRIIGFKKRS KIPSWASVKK SLFIFPSEEQ YVGSTRVFSA LWQKLLKDDK VGIAWFVARE
NAHPVMVAIF PSGNPDDEES NTPYLPAGLW LYPLPFADDV RSVDHVTAPA RPADELTDQM
RQVIQNLQLP KAMYDPRKYP NPSLQWHYRI VQAIALDEEM PESMEDLTLP KYRQIDKRVG
GYLAEWKEML AKKASDLQNN RAFKREFEDD DDERPAKRAK PTKKATSGGG GPANSNADLK
KAFEQGMLGK MTVAELKDIM ASKGISTAGR KAELVERLEQ WIEGNL
//
