PRP5_DEBHA
ID PRP5_DEBHA Reviewed; 913 AA.
AC Q6BML1; B5RU90;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; OrderedLocusNames=DEHA2F04466g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382138; CAR66268.1; -; Genomic_DNA.
DR RefSeq; XP_002770738.1; XM_002770692.1.
DR AlphaFoldDB; Q6BML1; -.
DR SMR; Q6BML1; -.
DR STRING; 4959.XP_002770738.1; -.
DR EnsemblFungi; CAR66268; CAR66268; DEHA2F04466g.
DR GeneID; 8998872; -.
DR KEGG; dha:DEHA2F04466g; -.
DR VEuPathDB; FungiDB:DEHA2F04466g; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_2_1; -.
DR InParanoid; Q6BML1; -.
DR OMA; ANCLDVI; -.
DR OrthoDB; 245118at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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; Coiled coil; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..913
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000232362"
FT DOMAIN 348..526
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 564..713
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..265
FT /evidence="ECO:0000255"
FT MOTIF 316..345
FT /note="Q motif"
FT MOTIF 474..477
FT /note="DEAD box"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 913 AA; 102477 MW; 85BD0853C21DBBA2 CRC64;
MNSTGSNYSL KHNNTQDNNH NSEESVTNKT GELDKPGVKD GQALSKEEKL KRRQEQLAAW
MQKRQQENQE PSGKVTISAT DETNIDKEKL IRQQRIEEWK RKRLQKSEGL ETDRSKIKTF
EVKSSNEPTI KINASMKKTI TPANGRSKKR PIFGDEDEDD EKESKPKFKK PTLDLAEIEE
KKPEKSIDTE IDELDKYLSL LEEKEQGVEN KKIENHDDDG IANGPGVGNV NESDDEEIDE
DQKQQDILSS KLNRLQNKQK QLDDVDHNQI QYHPFRKDFY TEPTEISKLP EEEVANLRLK
LDGIKVRGVN CTRPIIRWSQ LGLPSTIMSI IEGRLNYSSP SSIQAQAIPA IMSGRDIIGV
AKTGSGKTLS FVLPLLRHIQ DQPPLKKGDG PIGLIMTPTR ELALQIHKEL NHFTKKLNIS
SCCCFGGSSI ESQIAELKKG AQIIVGTPGR IIDLLAANSG RVTNLQRVTY LVLDEADRMF
DMGFEPQVTK VFTRVRPDRQ TVLFSATFPR KMELLAKKIL DNPMEIVVGG ISVVASEITQ
KVELFENEDD KSLEEAKFSK LLSTLNDYGD KDAECKILIF VEKQIAADEL LVKLLTEKYP
CLAIHGGKDQ IDRKHAIREF SSSNSGVNIL IATSIAARGL DVKGLNLVIN YEAASHMEDY
VHRVGRTGRA GRKGTAITFV SSKQGRAITD LVKAMRLSKV SEDEINPRLI EISTKFLEGV
KSGKEKYNFG FSGKGLDNLQ EIRESNRDLE RKVYGEENDS STFKANEKKQ NKTDIHQSDL
DVKLPDFHII EGRAPETAGP DKCKFHSRIT INDLPQKARW ITVNRDSLSK VIESTGTSIT
NKGNYYPPNS KIPKTIKQNG KEVTPPPKLY LLVEGLTEKA VHDAIILLRE KMIEGLEVAA
KEESMGPTGK YTV
