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Database: UniProt
Entry: M9MBY8_PSEA3
LinkDB: M9MBY8_PSEA3
Original site: M9MBY8_PSEA3 
ID   M9MBY8_PSEA3            Unreviewed;       809 AA.
AC   M9MBY8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=PANT_2c00032 {ECO:0000313|EMBL:GAC71272.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC71272.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
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; DF196768; GAC71272.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9MBY8; -.
DR   STRING; 1151754.M9MBY8; -.
DR   OrthoDB; 21093at2759; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00788; KU70; 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; IPR018247; EF_Hand_1_Ca_BS.
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   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   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; PS00018; EF_HAND_1; 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, ECO:0000313|EMBL:GAC71272.1};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Kinase {ECO:0000313|EMBL:GAC71272.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895};
KW   Transferase {ECO:0000313|EMBL:GAC71272.1}.
FT   DOMAIN          769..803
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
SQ   SEQUENCE   809 AA;  90474 MW;  F87C44A2C6D44C49 CRC64;
     MHQRGTKDGG RSIRTGIAAA PHIHSWARSN RFTPTKSRPT LPKRARAKIP TDANLRKRLE
     SGSVASTRTK GCLNPERLLP VSPLACSRPP SRTLPTMPKA YFVNKREAAR AFNSDDDDDD
     DELEQLDLDA TYQKDMVLFC IDAGESMHRI DPATNTSPLY SALKAAASLM QKKLISSPHD
     HVGVLIFNCA DTLFRSAKPG EYYKGSYELQ SVRQVNVPDT YNLKALLSRA ATDPKHLRTV
     LPPANKQMRI DWALANAGVA MVAAANAGSK RVFWITDNDD PHPMSSDPKA TKARRACLDK
     MNEFRKIGVR IEPFFINPTD GAASDEASTS DLSRGFEVNR FYADVFAQYD DDLEEAEARS
     QPRLPAGFGK TAAEQLKGQE PRRSLWDSAV RFQELEDDIA TRETPKRVVF NIRFELAALD
     APTADTQTQK QGSAAEEQLP QARMRGRKWQ IGIKGYSLVS RTTKGNPVKV IVDDDCGELK
     EVVTHQHYID ANSGKPLSKE QVIPAFQFGN SSSLRGQVTF TPQELKSIKS FGMLPCLKLI
     GFRDRDDLLR FEWNVKHAYF IYPSDVEWKG SKKTFTALLN SMVSKGKVGL GLFMPRQNVV
     PVFVAIVPQQ EELTEEGQQL APPGMHLITL PYADDVRDIP TNLLHTEDAK DAQVDRAVAF
     IERYQKKQPF NPDHYPNPAL NHHYAVLMAT AFQEEQPAGP TDLTVPQYAT IRKRTAHLIQ
     EWHASIDEDP RLAMVAEGSS KQAKTSTGVR KTSFEDDSEI LDLWQKGKLS AYTVAELKSA
     CEFYRLDAKG RKADLLVRLD AHIRKQRKG
//
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