MAK5_VANPO
ID MAK5_VANPO Reviewed; 763 AA.
AC A7TEG8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
GN Name=MAK5; ORFNames=Kpol_1036p17;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480380; EDO19275.1; -; Genomic_DNA.
DR RefSeq; XP_001647133.1; XM_001647083.1.
DR AlphaFoldDB; A7TEG8; -.
DR SMR; A7TEG8; -.
DR STRING; 436907.A7TEG8; -.
DR EnsemblFungi; EDO19275; EDO19275; Kpol_1036p17.
DR GeneID; 5547611; -.
DR KEGG; vpo:Kpol_1036p17; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; A7TEG8; -.
DR OMA; HYHVPRT; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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 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 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..763
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000310211"
FT DOMAIN 223..411
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 450..619
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 192..220
FT /note="Q motif"
FT MOTIF 352..355
FT /note="DEAD box"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 763 AA; 85615 MW; B82B1DAF881C7A81 CRC64;
MVNKFLAGRL KKSKGKSFKG SSSKGNSKTV KSNNNDNVVV NAADLKWKPV EIPDTLDDFE
GFYGLEEIDG VGVKIVGGQV QFVAHDDTKI NGNEDNLDSK DKIEIDEDAP ENDLVEFKNM
DDMKDGELTD NSQSESEAEA ESEAESEEEE EKTGDDEGED GAEKVDNEVL KTNVFNTDID
LEDITPSDLP EWTEKVGELS FTTLHGLTKL GFNKPTLIQE EAIPMALKGE DIMGKASTGS
GKTLAYGIPI IEKLMKSKSN TAPIGLIFTP TRELAKQVTD HLRKIASLIV DKSPHAILSL
TGGLSIQKQE RLLKYEGSGR IVVATPGRFL ELIEKDKTLV ERFSQISTLV LDEADRLLQD
GHFDEFENIL KYLGRESKNR KHNWQTMIFS ATFATDLFDK LSHASWKNMK TPSKNENEME
IVLKHLMTKI HFKSKPILID ANPEDKVSSQ IKESLIECAA TERDLFCYYF VSMYPGKTLI
FCNAIDSVKK LTAYLNNLNI SCFQIHSSMT QKNRLRNLER YQQQSEKNKI LGKPTVLVGS
DVAARGLDIP GIQHVIHYHL PRTADVYIHR SGRTARANNE GVSVMICSPE EAMGPLRKLR
KTLANKSGKD IIMGKKKWQK TVTMLPIDDT ILSQLKERSR LASELADHDL ASSSLQKDDT
WMKKAAEDLG VDIDSDDEIK DTFLAKNINK KRNKTLGKDQ KKVLVAQLND LLKRPLRKDM
RQRYLTGGLV NLADSLVKKR GHDHIIGHEK TDALETLKNK KRK
