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Database: UniProt
Entry: M9LR00_PSEA3
LinkDB: M9LR00_PSEA3
Original site: M9LR00_PSEA3 
ID   M9LR00_PSEA3            Unreviewed;      1454 AA.
AC   M9LR00;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=ATP-dependent DNA helicase CHL1 {ECO:0000256|ARBA:ARBA00017386};
DE   AltName: Full=ATP-dependent DNA helicase chl1 {ECO:0000256|ARBA:ARBA00016387};
DE   AltName: Full=Chromosome loss protein 1 {ECO:0000256|ARBA:ARBA00029709};
GN   ORFNames=PANT_14c00100 {ECO:0000313|EMBL:GAC75216.1};
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:GAC75216.1, 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   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
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DR   EMBL; DF196780; GAC75216.1; -; Genomic_DNA.
DR   STRING; 1151754.M9LR00; -.
DR   OrthoDB; 124793at2759; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR00604; rad3; 1.
DR   PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:GAC75216.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          23..438
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
FT   DOMAIN          1003..1082
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1138..1175
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          86..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1177..1201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..865
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1177..1199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1454 AA;  158264 MW;  646792F9D5C30FDF CRC64;
     MVDLNSGLKL PVPGATSDPT LASRDFSFPY PQAYSIQLDL MRQVFSTIED GKVGLFESPT
     GTGKSLSLIC AAFTWLRQNA KRGTHGLGAR GSDDEPDWVV QHAQDRKRKA HESHELELKE
     RIAAARARQS SLKRRRLDES IPETRSHADR EQDSDDDLLI DQDEGEKGAR ALRMATYTRT
     ALADSSVQQD NLSPAVRALM QQYEQTHHRA QDDDEEPETL PRVVYASRTH SQLSQFVAEL
     KKTSFGEVDV LNPTDLPVRT IALGSRKQMC INESVQHIAR RKGTEAMNER CLELMKAKKG
     KCAALPSFDL AGRAQILEFR DAAMAQVGDI EDLVQLGRDT KTCPYFAART SAKQAELVTL
     PYNLLLQKDA RQALGISLEG CVVLIDEAHN LIDTILGTHS VAIDSRQIAQ ATRQIDAYLD
     RFALRLKGSN EANLRKVRKL LAGMSTFFSQ HAAKKGEAEV VMSAAELVRG LAGSLDQINL
     VTLETWLKET QIARKISGYA DKHAQRAATG SAVNAAGSAR RPAQRTPKSS QVEKDTPGPS
     AISSMHAIEA FILSLAHRSE DGRVVLSRAD DAGEPYVRAK YQLLNPSHAF KSLVDEARSV
     ILAGGTMEPL SDFRQQLLPF LPRDKLVEFS CGHVIPPSNL MVSVLGSSPK GLPFEFKFDS
     RANAELIDEL GRTLINLCNV APAGLVVFVP SYAFLDRIMA RWKDAASGEL HKRLGAKKKI
     FSEPKTTMEV DGVLQDYTAA IRDAGSAGGA IMFAVVGAKL SEGINFSDDL ARAVVMVGMP
     FANMHSPELA ERMKYVRELA KQHPPGTKSV DPVSAPPRLP DTETDNATNR SLPVAGRAGP
     RAVHEPVHES GQPVDRPRRA PPERLCGAHP ARSALRPARD QAAPSRVDSQ RGQRRRPVWR
     THQTDRCVLQ GSKDGSILGS TQWTFNHTRS DAVAMSFDEE SGIAIMLTRT ALRRTLRLAA
     AARGRSAPLL ARTYVQSSTL STPIVVGSTS TTLRSFATTP RRLATEVKPY LLADVGEGIT
     ECEIIKWFVQ PGAVVQEFDP ICEVQSDKAS VEITSRYAGT IKRLMHKEGD VAKVGHALCE
     IEMQSDGEAA EKEVDQEQVE VTGVSKESEF GGVEMEGFVS AEHKHSGASP AGGAREVLAT
     PAVRRVSREH KVDLSQVQGT GRDGRITKED VLNFVQRGSQ SAQPSASSPS PTPSAPVSAG
     GTTEVIDLTP VQRAMFKAMT ATLSTPHFAY SDEIDVTELD SVRKMLSASI PERYTQAGEA
     SYTKLTLLPL LVKAMSLALN DHPMFRSILN ADQKLVRRSS HDVSIALTSK VGLLTPCITD
     VQTKSIYDLS GFITRLQNLA ASPKGLAPAD LKPTGTITLS NVGAVGGGTY THPLLPPTGQ
     LAIGALGRSR ILPRFASEIP SLNCNDPDKI VRRLIMSVSF TGDHRVVEGA DLARLVNRWK
     QLVENPSLWL GLLA
//
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