PRP5_CANAL
ID PRP5_CANAL Reviewed; 884 AA.
AC Q5ADL0; A0A1D8PKR2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; OrderedLocusNames=CAALFM_C306720WA;
GN ORFNames=CaO19.14123, CaO19.6831;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017625; AOW28678.1; -; Genomic_DNA.
DR RefSeq; XP_719923.1; XM_714830.1.
DR AlphaFoldDB; Q5ADL0; -.
DR SMR; Q5ADL0; -.
DR STRING; 237561.Q5ADL0; -.
DR PRIDE; Q5ADL0; -.
DR GeneID; 3638447; -.
DR KEGG; cal:CAALFM_C306720WA; -.
DR CGD; CAL0000188191; PRP5.
DR VEuPathDB; FungiDB:C3_06720W_A; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_2_1; -.
DR InParanoid; Q5ADL0; -.
DR OMA; ANCLDVI; -.
DR OrthoDB; 245118at2759; -.
DR PRO; PR:Q5ADL0; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..884
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000232359"
FT DOMAIN 325..504
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 540..690
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 293..322
FT /note="Q motif"
FT MOTIF 452..455
FT /note="DEAD box"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 338..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 884 AA; 100398 MW; A6E78EA6701DB3A0 CRC64;
MSIDNQASTA LKNSGQEVKN NTNQTSELSK EEKLRKRREQ LELWRQKKQQ QQQEQEEVQN
KAKKTEDSTN NTSTEEVKKS RQQRIEEWKR ARLQKQQATK EKTTTITIKK KVHSQTTRPT
LKRNLDFGDD EDDRKNSHRP VFKKPSLEYD EISEHQNDKE SEDELDVFLA SIRESELKSD
NTKAEKAIES IPEGDVENEK ENDDYGGDGD EEDESDEESR LQDLISTKLT KLQNKGKELQ
SIDHSQENYQ EFRKVFYREA YELSALSDEQ VELIRQDLDN IKVKGTDVPR PILKWSHLAL
PTNLSSVIHD KLKFEKPSAI QSQALPTILS GRDVIGIAKT GSGKTLSYVL PMLRHIQDQQ
FSKDNQGPIG LILSPTRELA LQIEKEILNF TKRNNNLRVC CCYGGSSIEN QINELKKGVE
IIVGTPGRVI DLLAANSGRV LNLKRCTFVV LDEADRMFDL GFEPQVNKIL TQIRPDRQTV
LFSATFPRKM ETLAKQILTD PVVIIVGGIS VVAPEIKQEV VLFETSAEEQ DKYKQQRVEK
LHDILTNYQI EHPDSKILVF TEKQNDADEL VANLLSNKYP AIAIHGGKDQ MDRKYAIKEF
ASMDSGINIL IATSIAARGL DVRNLGLVIN FDPPNHMEDY VHRVGRTGRA GAKGNAITFV
SSSQPKEVFN LVKALKLSHS DIDPKLEEIA NKFVTKVKAG KEKISSGFGG KGLDNLQEVR
DNKLKLEKQR FGDQQPQRQQ EETETKKSND EPVPDIALPE FNIIEGNTPE TSGPDKCKFY
CRIVINDLPQ KVRWNIVQRE SLSKIIDESR TSITTRGQYY PPGSKPLSND QERNGSLAKL
YLLVEGLTLQ SVTEAITLIK KKMLESLDIL NQRENLQPTG RYVV
