GenomeNet

Database: UniProt
Entry: A0A2P5IC34_9PEZI
LinkDB: A0A2P5IC34_9PEZI
Original site: A0A2P5IC34_9PEZI 
ID   A0A2P5IC34_9PEZI        Unreviewed;       745 AA.
AC   A0A2P5IC34;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   28-JUN-2023, entry version 15.
DE   RecName: Full=ATP-dependent DNA helicase II subunit 2 {ECO:0000256|ARBA:ARBA00021792};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   AltName: Full=ATP-dependent DNA helicase II subunit Ku80 {ECO:0000256|ARBA:ARBA00031847};
GN   ORFNames=DHEL01_v201521 {ECO:0000313|EMBL:POS80077.1};
OS   Diaporthe helianthi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=158607 {ECO:0000313|EMBL:POS80077.1, ECO:0000313|Proteomes:UP000094444};
RN   [1] {ECO:0000313|EMBL:POS80077.1, ECO:0000313|Proteomes:UP000094444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7/96 {ECO:0000313|EMBL:POS80077.1,
RC   ECO:0000313|Proteomes:UP000094444};
RA   Baroncelli R.;
RT   "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL   Submitted (SEP-2017) 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   -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC       {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ku80 family.
CC       {ECO:0000256|ARBA:ARBA00007726}.
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:POS80077.1}.
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; MAVT02000071; POS80077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5IC34; -.
DR   STRING; 158607.A0A2P5IC34; -.
DR   InParanoid; A0A2P5IC34; -.
DR   OrthoDB; 5884at2759; -.
DR   Proteomes; UP000094444; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 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};
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:UP000094444};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT   DOMAIN          6..212
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
SQ   SEQUENCE   745 AA;  82397 MW;  36523B1148CDFF75 CRC64;
     MADKEAFVYI VDLGSTTSNC NNGRAESDLD FSMRYVWDKI ATTAQASRKT WNVGVIGLRT
     DETQNDYQDG DGYNNISVLK KLGPVSLANL KELSSLIKPS STEFGDAMSA IIVAAEMIGE
     LTKKLKYTRR IYLITDGQGP MDEDDVEEIS SRLNELQIEL VVLGVDFDDP EFGFKEEDKP
     QIKATNEAIL KSLVDNCNNG TFGTLAEAVE ELSIPRVKPV RLVKCYDGPL TIGNPAQFPS
     ATSINVERWP ATKVSRPAAA TTVTVKQDPY GTQSTHTLGE EMDGVEYGDP QFNSVKQHRT
     YRINDPGAPG GKRDVEFEEL NRGWAYGNTP VYIPDADKDL TTFGAAKSFS VVGFVSTNKV
     EPFLTLGETS VTVARSFDEE SKLALSALIH ALYESEMYAV SRLVSKDGRD PVIVLMRPSI
     DPDFECLYDV PLPFAEDVRS YRFPPLDKVV TIHGKVLTEH SRLLPDAELN QAMSDYVDAM
     DISEFDQDDE GNPAEYAALE DLYSPIIHRV NQAVRARAVA PDGNIAEVPD ILKKYSEPPE
     KLLKQAQPQI DALKEVAKLK NVPPKARGKW KRGSAKTESG RAVEPQFDID ELFRAGAEAA
     AKLKQGKLKI DKDNSIPMFK QLVQQLAETD NDKGIEAVTS SMGDVVKSLI QDSMGDTNYD
     RAIENIGELR DACIGLEVPE LFNDFLRDLK SKIFSDALGK GRRYMWTKLR ATSSGRLGLI
     AKSESEVSRI TDKEKQALRK GLPDQ
//
DBGET integrated database retrieval system