PRP5_PICGU
ID PRP5_PICGU Reviewed; 862 AA.
AC A5DDF4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; ORFNames=PGUG_01305;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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 (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; CH408156; EDK37207.2; -; Genomic_DNA.
DR RefSeq; XP_001485634.1; XM_001485584.1.
DR AlphaFoldDB; A5DDF4; -.
DR SMR; A5DDF4; -.
DR STRING; 4929.XP_001485634.1; -.
DR PRIDE; A5DDF4; -.
DR EnsemblFungi; EDK37207; EDK37207; PGUG_01305.
DR GeneID; 5127671; -.
DR KEGG; pgu:PGUG_01305; -.
DR VEuPathDB; FungiDB:PGUG_01305; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_2_1; -.
DR InParanoid; A5DDF4; -.
DR OMA; ANCLDVI; -.
DR OrthoDB; 245118at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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..862
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000294650"
FT DOMAIN 298..476
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 505..659
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 266..295
FT /note="Q motif"
FT MOTIF 424..427
FT /note="DEAD box"
FT COMPBIAS 40..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 311..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 862 AA; 95319 MW; A400BD67B4EFE6A7 CRC64;
MSQLHTNSKE VHASSSNSQD DKLQKRRARL AAWNQKKASS EKSENNEDKK PKIESSKLQE
WIKRRQQKSA TPEVPSTEAS QKPTSIKPIL RARLSTSSSK QTQLVPKKRS IFDDDDEQDD
AKTAKKDFRI PNEKKLPAST EEQESEDEEK VLERIRQAES GTSFLVESGF EQDLGADSGI
SGSEGDEEDD EEGQQRLLSE KLQKLTNKEK KLMALDYTQM EYTSVRKKFY TPPEELKDVP
PEKVTALRTA MDGIKVRGSD CPMPIQKWAQ LGLPSSIMTV LEEKLGYDTP SPIQSQALPA
IMSGRDIIGV ANTGSGKTLA FVIPLIRHIM DQPPLKSGDG PIGVILTPTR ELALQIQKEL
VNFTQAVELS VCCCYGGSPI ESQIADLKRG TEIIVGTPGR VIDLLAANGG RVTNLRRTTF
LVLDEADRMF DMGFEPQVNK VLSQIRPDKQ MVLFSATFPK KLESLARSFL VDPIEIVAGG
ISVVAPEITQ RVVLIDDSGD ISQKKLQALL KIVDEFSVED PEGKILIFVD KQEAADDLMV
RLLNNQISCI VIHGGKDQVD RKHAIKQFSD KNGLRVLIAT SIAARGLDVR GLNLVINYDA
PSHMEDYVHR VGRTGRAGAT GTAVTLVLSS QEREIRDLVR AMKMSGKVDD IPAELQSIAD
KFLKKVKSGE EKFNSGFGGK GLENLQERRD NVREIEMQMY GDKVKETNGV SNSSAGRKAL
GTPEAAEIAG IKLPDFDIVE GRAPETSGPD RCKFHSRIEI NDLPQKARWV VVNRDSLSKI
IDATSTSITS KGQYYPPNSK LPKPTIKYGR EIPPPPKLYL LVEGLTKSAV QEANKLLRQK
MIEGVDVATE EDAKAPIGRY NV
