ID MAK5_YEAS7 Reviewed; 769 AA.
AC A6ZL85;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
DE AltName: Full=Maintenance of killer protein 5;
GN Name=MAK5; ORFNames=SCY_0355;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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; AAFW02000011; EDN64754.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZL85; -.
DR SMR; A6ZL85; -.
DR HOGENOM; CLU_003041_13_0_1; -.
DR Proteomes; UP000007060; 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 CDD; cd17946; DEADc_DDX24; 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; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF21; RNA HELICASE; 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; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..769
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000310212"
FT DOMAIN 198..395
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 448..611
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 73..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 167..195
FT /note="Q motif"
FT MOTIF 329..332
FT /note="DEAD box"
FT COMPBIAS 126..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 211..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38112"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38112"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38112"
SQ SEQUENCE 769 AA; 86607 MW; 57E6F1473A5A43AF CRC64;
MGKKRAPQKG KTVTKPQEII VDESKLNWKP VDIPDTLDDF GGFYGLEEID GVDVKVVDGK
VTFVTKKDSK VLKDSNKEKV GDDQESVENE SGSDSESELL EFKNLDDIKE GELSAASYSS
SDEDEQGNIE SSKLTDPSED VDEDVLKENV FNKDINIDDI SPVNLPEWTN LAPLSMTILQ
SLQNLNFLRP TEIQKKSIPV IMQGVDVMGK ASTGSGKTLA YGIPIVEKLI SNFSQKNKKP
ISLIFTPTRE LAHQVTDHLK KICEPVLAKS QYSILSLTGG LSIQKQQRLL KYDNSGQIVI
ATPGRFLELL EKDNTLIKRF SKVDTLILDE ADRLLQDGHF DEFEKIIKHL LVERRKNREN
SEGSSKIWQT LIFSATFSID LFDKLSSSRQ VKDRRFKNNE DELNAVIQHL MSKIHFNSKP
VIIDTNPESK VSSQIKESLI ECPPLERDLY CYYFLTMFPG TTLIFCNAID SVKKLTVYLN
NLGIPAFQIH SSMTQKNRLK SLERFKQQSA KQKTINHSNP DSVQLSTVLI ASDVAARGLD
IPGVQHVIHY HLPRSTDIYI HRSGRTARAG CEGVSAMICS PQESMGPLRK LRKTLATKNS
VSTDLNSRST NRKPIKWQNT VPLLPIETDI LSQLRERSRL AGELADHEIA SNSLRKDDNW
LKKAADELGI DVDSDEDDIS KSNSDTFLLK NKNKKMQKTI NKDKVKAMRA TLNELLSVPI
RKDRRQKYLT GGLVNLADNL VKKRGHNSII GHEKTNALET LKKKKKRNN
//
