ID M3K7G5_CANMX Unreviewed; 2513 AA.
AC M3K7G5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=G210_5910 {ECO:0000313|EMBL:EMG51130.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG51130.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG51130.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EMG51130.1}.
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DR EMBL; AOGT01000005; EMG51130.1; -; Genomic_DNA.
DR STRING; 1245528.M3K7G5; -.
DR eggNOG; KOG0926; Eukaryota.
DR HOGENOM; CLU_228445_0_0_1; -.
DR OrthoDB; 1330687at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR GO; GO:0006396; P:RNA processing; IEA:UniProt.
DR CDD; cd17982; DEXHc_DHX37; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR037701; Pom152.
DR PANTHER; PTHR28206; NUCLEOPORIN POM152; 1.
DR PANTHER; PTHR28206:SF1; NUCLEOPORIN POM152; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EMG51130.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1325..1349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1355..1382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 427..611
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 695..875
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 25..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..736
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2513 AA; 286316 MW; 95F435B31B7B4B36 CRC64;
MGKYRKRFNE KARAGMLAKQ AALKKARNKQ FYRQDDGEDE EVQDEVPDTT QIFNNQDSNS
EILKPVTEEE RLARKRVLEE SLFSQNAKQE KMSRSKKKRL EKYIDHQLKR EEKKILLEKL
SETKMDTSNL SALKELGKGK QTRKEEMVEA LSLERQGRGD DRTKEILYEE REIKDGNESF
DEFDEDIEEE QQPTSSFVDN RPSKFGGQGF GFGFANIPVI KKDISSEPKK KYSWRKRVEE
EERKKLKLEE EDDFNSSSDE EVEDEEEDDD DEEEDVEEES EDDNELDEEE IDEEGDSEEE
SDDESDDESE EGESESEPEE QSKLMQSKPR HSSIAKSFKE WAEQQVRKME GRENIALNPE
VSEEIKKKYA TQTVRDEDVD HSSDEEGYIP INKNLQREAF VVEVERDETI QQQRVLLPVF
AEEHKIMEAI YHHDCVILCG ETGSGKTTQV PQFLYEAGFG NLENNLYPGM IGITQPRRVA
AVSMAERVGN ELGNHRHRVG YQIRFDTTIK NEGQKDGTAM KFMTDGVLLR EMMSDFLLTK
YSSIIIDEAH ERNINTDILI GMLTRIMKLR RKYHSENPDK FKPLKLIIMS ATLRVSDFSE
NPVLFKNPPP IINVQARQFP VSIHFNKKTN YDYVDEAFNK ACKIHRKLPE GGMLIFLTGQ
NEITTLVKKL RQEFPLKKKS TIKYDEDIEV KLSENVQQEV EDVDFSVDTK PEESYDDYDD
VTGSDAEEEE GFEEAVDTKE SELGPLYVLP LYSLLPTKQQ MKVFDEPPAG SRICIVATNV
AETSLTIPGI RYVIDCGRSK ERKFNRENGV QSFEVDWVSK ASADQRAGRA GRTGPGHCYR
LYSSAVYEEF FPQFSVPEIL RMPFESIVLN MKSMGIDQIA NFPFPTPPDR RALQKAEELL
IILGALDKEN KEVTDLGKKM SLFPLSPRFA KILIIGNQQE CLSYIIAIVS ALSVGDPFIS
ENELVGGKTD EARKEFRTKY YQSQALFSRL DAASDCMMLL SAVCAYDHVP KDNQHEFLQA
HYLRHKMMEE IQKLRKQVTF IVENSIMASS GIQLKSDVKL PIPNKKQVSA MKQMIASGFI
DQVAIRGDLI SSDVKVVNKT KTTDVPYCPV MPIDEGPFVY IHPNSLVAKS GGIPSSYLVY
QSLNARGSAT GGDNENPKVR MRPLVDISGK QLANVSKNSI LLTYSKPLGH PYAPKNLSPT
KRECYVVPRF GAAIGSGGVG WDLPAIKVIQ EKRKGVWKSN KLLTLNYIIM DSTERDRGRK
RNRERSYVSR PLIPTNVLDQ ASQRMFIISL FIIIQSWKIY DLVLLKTEIP FSDTPLTSLN
NFTFVLKYSF LDGLFIFFLP ILNIQYLTFS PFHTIIIFVT LFGSSIFLVS SMALPLLSNV
FLPVWKFLLQ KKELNIVGES IDRNKVIDMD SHFKGQLTIQ YLPDSSARMN PFHYDQTCLG
LENNHLLNMP IEFNTTSGIG YLQIQRTTPD NQIEYLNYTG HSLRSLFKKD YSHLAKEREY
KKSDPRVFYL EYPIQNPGMY RIKNVLDNKG NSIKTYKSEF AISDCPSAKF FYPPNFETSN
GFKCMSSLED DTFPLPWIEL FSTTPASIKL NLKVDGNEFK MMNLSIGQES SGHGSRTNFN
WLKASKLVRN ILYENILNSK YSFLKNADSV LEFQLLQVQD SLGNIHRYQP LSKDKDVWYK
LKLKKSSTIG LYDTQKDREL LIGGTKTLSV SHLDSFGEDD FPVAISVEHV TKEGAQNITA
TFKNKGEMKN GITIDKPGTY RLITAKDKYC PCEISGEPID IQYASLPDLD IIAEPVSDRC
LGTVGYNFGF NFTGKTPFKV QYKIYSNSSG VLEPVPSETG RFNRELTSYE KSHSFKFKPP
SEGSYAIVFS NLRDANYNKD PIKLDETKHI YSTYFRQASQ IGFQVSQRTL RTCYGQAAHI
PVSFKGSGPF TFEYEFLDIN SKKKLLDTVH VDKVDSYTID PPNQLLGKAY EVRIVSAKDK
FGCDAIITDK SRPLNIISRS EIPEVEFDQS EKNVSIVEGS SVNIPLKFKS SVAVSGNDKI
EMKYLSPQSN NDPVVIQAQL SGSSVKLSKE GTYWLSSYTS NGCQGHVVNE QKSVIVNYFP
KPSMRIVAAE KMLQHSDDST IHLKPVCYGC DNEVKLQMTG KAPFVVDYEI KLPNGKLETH
SMNIAGNEIS IKLPTKASGR FEHQFKRVYD SLYTKNKGKI INANVPKLIY DVNPLPTAQF
LPDNHFAQIC DNKLSESSIV ANIPIQLSGS YPFDIYAVLT NEKTGKTHEL TFRNVMSDSI
VLENLSFLKL GDYSLSFTKI IDNNGCVGNK FQANDKFIVS ITEPPNIFKT DPNKKHYCVG
DHVSYNLTGV YPVTIYYEYN NKLRNAESYN YFERLASRPG VLNIHGLQDS GINSCTVNYT
FDAVKQEELR LQVHEIPTVE VNKGDYIIED LHEGDQTELI FTFLGEPPFK LTYIRTVDIK
KNKKTVRKLV EKETISDIWE HQLVVMASLE GTYEAIEIED KYCRAIKKVD YIE
//
