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Database: UniProt
Entry: A6ZL85
LinkDB: A6ZL85
Original site: A6ZL85 
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   31-JUL-2019, entry version 49.
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;
OC   Saccharomycetes; 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.,
RA   Wang X., Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S.,
RA   Li Y., Davis R.W., Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces
RT   cerevisiae 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
CC       60S ribosomal subunits and is required for the normal formation of
CC       25S and 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5
CC       subfamily. {ECO:0000305}.
DR   EMBL; AAFW02000011; EDN64754.1; -; Genomic_DNA.
DR   PRIDE; A6ZL85; -.
DR   EnsemblFungi; EDN64754; EDN64754; SCY_0355.
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: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   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   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    769       ATP-dependent RNA helicase MAK5.
FT                                /FTId=PRO_0000310212.
FT   DOMAIN      198    395       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      448    611       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     211    218       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       167    195       Q motif.
FT   MOTIF       329    332       DEAD box.
FT   MOD_RES     135    135       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P38112}.
FT   MOD_RES     138    138       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P38112}.
FT   MOD_RES     674    674       Phosphoserine.
FT                                {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
//
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