ID PRP5_CHAGB Reviewed; 1064 AA.
AC Q2HAD8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; ORFNames=CHGG_02816;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408030; EAQ90881.1; -; Genomic_DNA.
DR RefSeq; XP_001229332.1; XM_001229331.1.
DR AlphaFoldDB; Q2HAD8; -.
DR SMR; Q2HAD8; -.
DR STRING; 306901.Q2HAD8; -.
DR GeneID; 4388898; -.
DR VEuPathDB; FungiDB:CHGG_02816; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_3_1; -.
DR InParanoid; Q2HAD8; -.
DR OMA; HSIRKRF; -.
DR OrthoDB; 5477821at2759; -.
DR Proteomes; UP000001056; 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 CDD; cd17953; DEADc_DDX46; 1.
DR CDD; cd22474; KH-I_PRP5_like; 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; 1.
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..1064
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000256033"
FT DOMAIN 460..638
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 665..813
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 22..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 429..457
FT /note="Q motif"
FT MOTIF 586..589
FT /note="DEAD box"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1064 AA; 114993 MW; B805B9BF997B6314 CRC64;
MTITEAVAVM EEAIETVVGH ATEAQTERDR QIAEDNGAEM VTGTTAPAKS TPTQAQTEAE
KKAERLRKLQ AMKEKHAQKE AKEAAVTAGS TRMLLAEMDQ KASGTPGPNS PVAGAMSPAP
TSPAPPMPYA GKFDPKAIAK SSKAARPQSP TRLGDVKLAA PAPKPLGLKK EANLKGAGLL
PANRAKSSTK RKIDMDDEEV IKRKLVKLPD FVPENADSTP DAEGEGEEEA DDLDLLMAQN
EEEMAEAHRV LQERRDERIQ KEGMAMDVDT ETPNGETKDE AENEANVESK DEAVLPAPSM
DVDEDVDPLD AFMADLEQTG SAGGIGSVPA RQKQKAGKGF EPEAYFSDDD YGYEEDKADP
SSILAMASKK KKKDIPTIDY SKIELNQIRK NFWVEPQELS QMTEDDIADL RLELDGIKVS
GKNVPKPVQK WSQCGLTRPI LDVVEGLGYE KPTSIQMQAL PVIMSGRDVI GVAKTGSGKT
MAFVLPMLRH IKDQDPVTGD DGAIALIMTP TRELCTQIYS DLLPFAKALK LRAIAAYGGN
AIKDQIAELK RGAEIIVATP GRMIDLLAAN SGRVTNLKRA TYLVLDEADR MFDMGFEPQV
MKIFNNVRPD RQTILFSATM PRIIDALTKK VLREPVEIQV GGRSVVAPEI TQIVEILDEG
KKFVRLLELL GELYADDDDV RALIFVERQE KADDLLREVL RRGYGCMSIH GGKDQEDRNS
TISDFKKGVC PIMIATSVAA RGLDVKQLKL VVNYDAPNHL EDYVHRAGRT GRAGNTGTAV
TFITEEQENC APGIAKALEQ SGQPVPEQLN EMRKAWKEKV KTGKAKDASG FGGKGLERLD
KEREAARVRE RKTHKAEGEE DDFKEEETAE DAAKKDKAKS AILAAASAIV SRESAKADAS
EAKPLPAAAE GAVKGGVTVN AGKGGALDKA ASAISEINAR LARAGQLRPG QPIDNKGPDA
GAFHATLEIN DFPQKARWAV TNRTNVAKIL EATSTSITTK GNYYPPGKEP PSGSDPKLYI
LIEGDTELAV GKALSELTRL LREGTIAAAD AESRAPASGR YTIA
//
