MAK5_SCHPO
ID MAK5_SCHPO Reviewed; 648 AA.
AC O74393;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ATP-dependent RNA helicase mak5;
DE EC=3.6.4.13;
GN Name=mak5; ORFNames=SPBC4F6.07c;
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-85; SER-566 AND SER-567, 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-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {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, 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. DDX24/MAK5
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA20727.1; -; Genomic_DNA.
DR PIR; T40504; T40504.
DR RefSeq; NP_596107.1; NM_001022024.2.
DR AlphaFoldDB; O74393; -.
DR SMR; O74393; -.
DR BioGRID; 277391; 4.
DR STRING; 4896.SPBC4F6.07c.1; -.
DR iPTMnet; O74393; -.
DR MaxQB; O74393; -.
DR PaxDb; O74393; -.
DR PRIDE; O74393; -.
DR EnsemblFungi; SPBC4F6.07c.1; SPBC4F6.07c.1:pep; SPBC4F6.07c.
DR GeneID; 2540874; -.
DR KEGG; spo:SPBC4F6.07c; -.
DR PomBase; SPBC4F6.07c; mak5.
DR VEuPathDB; FungiDB:SPBC4F6.07c; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; O74393; -.
DR OMA; HYHVPRT; -.
DR PhylomeDB; O74393; -.
DR PRO; PR:O74393; -.
DR Proteomes; UP000002485; Chromosome II.
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; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; ISS:PomBase.
DR GO; GO:0042254; P:ribosome biogenesis; ISS:PomBase.
DR GO; GO:0006364; P:rRNA processing; 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; 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 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..648
FT /note="ATP-dependent RNA helicase mak5"
FT /id="PRO_0000232239"
FT DOMAIN 153..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 378..523
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 52..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 122..150
FT /note="Q motif"
FT MOTIF 275..278
FT /note="DEAD box"
FT COMPBIAS 52..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 648 AA; 73250 MW; 07CA3668698B426A CRC64;
MPKKAALDEL KWKEVKLPDH LDDFDGFMGL EEIEGVDIKY QPKGAMKEVI YELPEVHEKK
DKKPEKRKKD QKEASEKKKK GKRTSPTIEM TSLGSKVTSK NYNEFSTLEE EDEHNSHGVD
VSAWAHFSLS PEMLGSLSKA GFSKPMPIQS LVIPEASIGF DIIGKADTGS GKTLAFGIPI
LEHCLRNVDA KYVQALVVAP TRELAHQICQ HFELIKPSPN IRVMSITGGL AVQKQQRLLN
KHPHVVVATP GRLWSVINEN NLTGNFKKIK CLVLDEADRL LQKSHFEELS KLLEILGNPM
HTQRQTFIFS ATFDEGLQQR LKKNMKGNIT EKYNSPMENM LKEVRFFGKP KFLDANPQSA
VASRVLEGLI ECAPAEKDLY LYYLIMRYPG KTMVFANGIE DIKRITPFLN ELKVPSYPLH
AQLDQKKRLQ SLEKFKNNPK GVLVCTDVAA RGIDIPSVTH VIHYHVPHTA DMYVHRSGRT
ARANEDGVSI LMCGPKELSQ LKRLCYRLKK KIETFINFPV DMSILDILKT RVVLAHKIVN
LTRKDGRVGR EEAWLKSMAQ ELGVESSDDE DPDLPKKSES SKNKKQIAHL RSELAPLLHE
KIRTGFSGRY LTSGLVNMAE KLANEEVHDN IIGMDSISAL EVLQKRKK
