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
//