HAS1_SCHPO
ID HAS1_SCHPO Reviewed; 578 AA.
AC Q09916;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ATP-dependent RNA helicase has1;
DE EC=3.6.4.13;
GN Name=has1; ORFNames=SPAC1F7.02c;
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 [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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC sites A0, A1, and A2, leading to mature 18S rRNA.
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 -!- SUBUNIT: Associates in the nucleolus with the 60S and pre-60S ribosomal
CC subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {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. DDX18/HAS1
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA91949.1; -; Genomic_DNA.
DR PIR; S62574; S62574.
DR RefSeq; NP_594488.1; NM_001019917.2.
DR AlphaFoldDB; Q09916; -.
DR SMR; Q09916; -.
DR BioGRID; 278164; 12.
DR STRING; 4896.SPAC1F7.02c.1; -.
DR iPTMnet; Q09916; -.
DR MaxQB; Q09916; -.
DR PaxDb; Q09916; -.
DR PRIDE; Q09916; -.
DR EnsemblFungi; SPAC1F7.02c.1; SPAC1F7.02c.1:pep; SPAC1F7.02c.
DR GeneID; 2541668; -.
DR KEGG; spo:SPAC1F7.02c; -.
DR PomBase; SPAC1F7.02c; has1.
DR VEuPathDB; FungiDB:SPAC1F7.02c; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_26_5_1; -.
DR InParanoid; Q09916; -.
DR OMA; EYEFPAN; -.
DR PhylomeDB; Q09916; -.
DR PRO; PR:Q09916; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; ISO:PomBase.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR CDD; cd17942; DEADc_DDX18; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044773; DDX18/Has1_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
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; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 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 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..578
FT /note="ATP-dependent RNA helicase has1"
FT /id="PRO_0000055087"
FT DOMAIN 120..296
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 310..480
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 89..117
FT /note="Q motif"
FT MOTIF 243..246
FT /note="DEAD box"
FT MOTIF 322..338
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..68
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 578 AA; 65261 MW; 37E8FDB4081901E5 CRC64;
MAKSELKRKK HQSGNEEVKE KRQKPLKNDK KIAEELPQDE DDYEQEEENE DADQNTSVES
ESEELDNENE DERVQKSVNL NASSTSDIEK FSDLQLSENI QKAIKEMGFE TMTEIQKRSI
PPLLAGRDVL GAAKTGSGKT LAFLIPTIEM LYALKFKPRN GTGVIIISPT RELALQIFGV
AKELLKYHHQ TFGIVIGGAN RRAEADKLVK GVNLLVATPG RLLDHLQNTK GFVFRNLRSL
VIDEADRILE IGFEDEMRQI MKILPSENRQ TLLFSATQTT KVEDLARISL KPGPLYVNVD
SGKPTSTVEG LEQGYVVVDS DKRFLLLFSF LKRNLKKKVI VFMSSCASVK YMAELLNYID
LPVLDLHGKQ KQQRRTNTFF EFCNAEKGIL LCTNVAARGL DIPAVDWIVQ YDPPDDPRDY
IHRVGRTARG TKGTGKSLMF LAPSELGFLR YLKTAKVSLN EFEFPANKVA NVQSQLEKLV
SKNYYLQQSA KDGYRSYLQA YASYSLKSIF DINKLDLAKV AKSFGFAHPP NVNITIGASG
RTDKKERRAG YNKKNHVDVY SKQRSSAISQ DKERGWSR
