ID A0A1V6YG12_PENNA Unreviewed; 712 AA.
AC A0A1V6YG12;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 22-FEB-2023, entry version 22.
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=PENNAL_c0021G08722 {ECO:0000313|EMBL:OQE86263.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE86263.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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}.
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:OQE86263.1}.
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DR EMBL; MOOB01000021; OQE86263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6YG12; -.
DR STRING; 60175.A0A1V6YG12; -.
DR OMA; WAMQYVW; -.
DR OrthoDB; 5884at2759; -.
DR Proteomes; UP000191691; 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:UP000191691};
KW Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 6..210
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 260..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 79538 MW; 8ED46DABE1BF2CA9 CRC64;
MAEKEATVYI VDMGRSMGER HHGRPITDLE WAMQYVWDRI TATVATGRKT ATVGIVGLRT
DGTINDLEEE NFSNISILFG LGQVLMPDIR KLRETIKPSN TNKGDAISSI VIAMQMIIEY
TKKNKYKRKI ILVTNGTGMM SDDNIEGIIE KMKEVNIELV VIGADFDDAE YGAKEEDKDS
RKAENEILLR SLTEDCEGVY GTLEQAVSEL DIPRIKVTKS MPSFKGNLTL GNPEEYDTAM
TIPVERYFRT YVAKPISASS FVPRSGTEPG SQAPVKGNAE GDALASVRTS RTYQITDESA
PGSKIDVERD DLAKGYEYGR TAVPIEQTDE NVANLQTFAG MGLVGFVQKD QYDRYMHMSN
TNIIIPQRAN DNASLALSSL IHALYELESY AVARLVTKES KPPMLVLLAP SVEADYECLI
EVQLPFAEDV RSYRFPPLDK IITVSGKVVT EHRNLPSAAL KDAMSNYVDS MDLVTTNDEG
QPTDDLPIDE SFSPLLHRIE SAVRYRAVHP NDPVLDPSER LTEFAHPSED MVKNAKSNLE
ELMSIADVKK VPPKTKGRKR QRETEKPLSG LDVDALLSLE PKRTKISTEN AIPEFKQTLS
RAENIDTIHD AVQQMAKIIE TQITHSLGHS NYDRVIEGLG TMREELVDYE EPAVYNDFVR
QLKGKMLREE LGGDRRELWW FVRKGKLGLI GKSEVDSSAV EEEEAQAFLA PN
//
