PRH1_SCHPO
ID PRH1_SCHPO Reviewed; 719 AA.
AC Q03319;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable ATP-dependent RNA helicase prh1;
DE EC=3.6.4.13;
GN Name=prh1; ORFNames=SPAC2G11.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1454545; DOI=10.1093/nar/20.21.5841;
RA Inoue S.B., Sakamoto H., Sawa H., Shimura Y.;
RT "Nucleotide sequence of a fission yeast gene encoding the DEAH-box RNA
RT helicase.";
RL Nucleic Acids Res. 20:5841-5841(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: May be involved in pre-mRNA splicing.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; D13249; BAA02516.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91176.1; -; Genomic_DNA.
DR PIR; S35546; S35546.
DR PIR; S62466; S62466.
DR RefSeq; NP_593091.1; NM_001018489.2.
DR AlphaFoldDB; Q03319; -.
DR SMR; Q03319; -.
DR BioGRID; 278244; 4.
DR STRING; 4896.SPAC2G11.11c.1; -.
DR iPTMnet; Q03319; -.
DR MaxQB; Q03319; -.
DR PaxDb; Q03319; -.
DR PRIDE; Q03319; -.
DR EnsemblFungi; SPAC2G11.11c.1; SPAC2G11.11c.1:pep; SPAC2G11.11c.
DR GeneID; 2541750; -.
DR KEGG; spo:SPAC2G11.11c; -.
DR PomBase; SPAC2G11.11c; prh1.
DR VEuPathDB; FungiDB:SPAC2G11.11c; -.
DR eggNOG; KOG0922; Eukaryota.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; Q03319; -.
DR OMA; HIHRTTP; -.
DR PhylomeDB; Q03319; -.
DR PRO; PR:Q03319; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:PomBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; mRNA processing; Nucleotide-binding;
KW Reference proteome; RNA-binding.
FT CHAIN 1..719
FT /note="Probable ATP-dependent RNA helicase prh1"
FT /id="PRO_0000055155"
FT DOMAIN 106..269
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 294..466
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 216..219
FT /note="DEAH box"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 719
FT /note="T -> HLTFQLLKKIKKAHILSHYILVNLETTIF (in Ref. 1;
FT BAA02516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 719 AA; 80605 MW; E6EB16EEED852115 CRC64;
MVKVSGKLRN GGSITKQNLT DGLVGGQRIK APNKKKNRKA SKNTTKKSTV SVVNFLEQDT
DFGANEVVGS DNSSPEKRSE NSPSKRKDIL EQRKNLPIWE AHDTLCQQIQ DNRVIVVVGE
TGSGKSTQIP QFLNECPYAQ EGCVAITQPR RVAAVNLAKR VAAEQGCRLG EQVGYSIRFD
DTTSKKTRIK YLTDGMLLRE LINDPILSQY HTLILDEAHE RTLMTDMLLG FVKKIIKKRP
ALRVIIMSAT LNAERFSEFF DGAEICYISG RQYPVQIHYT YTPEPDYLDA CLRTIFQLHT
KLPPGDILVF LTGQDEIEAL EALIKSYSKQ LPSNLPQIQA CPLFASLPQE QQLQVFLPAL
ANHRKVVLST NIAETSVTIS GIRYVIDTGL AKIKQFNSKL GLESLTVQPI SQSAAMQRSG
RAGREAAGQC YRIYTEADFD KLPKETIPEI KRIDLSQAVL TLKARGQNDV INFHYMDPPS
KEGLLRALEH LYSIGALDDN GHINDLGYQM SLIPLLPSLA RAVLAAREHN CLSEVIDVVS
CLSTDSMFLF PQEKRDEAIE ARLKFLHSEG DLLTCLNALR QYLESSHDSR KQWCSQNFIN
RRALKTILDI RKQLREHCLK DGWELNSSPE VNSENLLLSF LSGYITNTAL LHPDGSYRTI
IGNQTISIHP SSSLFGKKVE AIMYHELVFT TKSYVRGVSS IRSNWLNAVA PHYLARRST