ID B9WEQ2_CANDC Unreviewed; 873 AA.
AC B9WEQ2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5 {ECO:0000256|ARBA:ARBA00041162};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5 {ECO:0000256|ARBA:ARBA00040918};
GN OrderedLocusNames=Cd36_86690 {ECO:0000313|CGD:CAL0000167860};
GN ORFNames=CD36_86690 {ECO:0000313|EMBL:CAX43164.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX43164.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX43164.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
CC -!- FUNCTION: ATP-dependent RNA helicase involved spliceosome assembly and
CC in nuclear splicing. Catalyzes an ATP-dependent conformational change
CC of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP
CC association with intron RNA. {ECO:0000256|ARBA:ARBA00037330}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC subfamily. {ECO:0000256|ARBA:ARBA00038511}.
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DR EMBL; FM992690; CAX43164.1; -; Genomic_DNA.
DR RefSeq; XP_002419569.1; XM_002419524.1.
DR AlphaFoldDB; B9WEQ2; -.
DR GeneID; 8046957; -.
DR KEGG; cdu:CD36_86690; -.
DR CGD; CAL0000167860; Cd36_86690.
DR VEuPathDB; FungiDB:CD36_86690; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_2_1; -.
DR OrthoDB; 5477821at2759; -.
DR Proteomes; UP000002605; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17953; DEADc_DDX46; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47958:SF35; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CAX43164.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAX43164.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 281..310
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 313..492
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 528..678
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 281..310
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 99324 MW; 2EBEC3332B1467AE CRC64;
MSIDNETSTA LRNSGQEVKN DTNQTSELSK EEKLRKRREQ LELWRQKKQQ QQAQNKVTKI
EDNTNNGSTD EVKKTRQQRI EEWKRARLQK QQATKEKTTT ITIKKKVHQP TTRSTLKRNL
DFGDDEDEMK NSHRPVFKKP SLEYDEISEH QEDKESEDEL DAFLASIRES ELKSDDTKAE
KSIKSVREDD NHSLADDEEE EEVDEESRLQ ELISTKLTKL QNKGKELQSI DHSHENYQEF
RKVFYNETYE LSSLSNEQVE LIRQDLDNIK VKGTDVPRPI LKWSHLALPT NLSSVIHDKL
KFEKPSAIQS QALPTILSGR DVIGIAKTGS GKTLSYVLPM LRHIHDQQFL KDNQGPIGLI
LSPTRELALQ IEKEILNFTK KNNYLRVCCC YGGSSIENQI NELKKGVEII VGTPGRVIDL
LAANSGRVTN LKRCTFVVLD EADRMFDLGF EPQVNKIFTQ IRPDRQTVLF SATFPRKMET
LAKQILADPV VIIVGGISVV APEIKQDVIL FETSLEEQDK YKQQRIEKLH DILSNYQIER
PDSKILVFTE KQNDADELVA NLLSNKYPAI AIHGGKDQMD RKYAIKEFAS MDSGINILIA
TSIAARGLDV RNLGLVINFD PPNHMEDYVH RVGRTGRAGA KGNAVTFVSS SQPKEVFNLV
KALKLSHSDI DPKLEEIANK FINKVKAGKE KIGSGFGGKG LDNLQEVRDN KLKLEKQRFG
DQQPPQNQQE ETETKKPNNE PATDIALPEF NIIEGNTPET SGPDKCKFYC RIVINDLPQK
VRWNIVQREN LSKIIDESRT SITTRGQYYP PGSKPLSNDQ ERSGSLAKLY LLVEGLTLQS
VTEAITLIKK KMLESLDIMN QRENLQPTGR YVV
//
