MAK5_PICST
ID MAK5_PICST Reviewed; 836 AA.
AC A3GG51;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
GN Name=MAK5; ORFNames=PICST_28472;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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; AAVQ01000001; EAZ63874.2; -; Genomic_DNA.
DR RefSeq; XP_001387897.2; XM_001387860.1.
DR AlphaFoldDB; A3GG51; -.
DR SMR; A3GG51; -.
DR STRING; 4924.XP_001387897.2; -.
DR EnsemblFungi; EAZ63874; EAZ63874; PICST_28472.
DR GeneID; 4851250; -.
DR KEGG; pic:PICST_28472; -.
DR eggNOG; KOG0347; Eukaryota.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; A3GG51; -.
DR OMA; HYHVPRT; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
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 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..836
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000285145"
FT DOMAIN 253..451
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 508..665
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 222..250
FT /note="Q motif"
FT MOTIF 389..392
FT /note="DEAD box"
FT COMPBIAS 12..28
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 266..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 836 AA; 94475 MW; 54F866C945E5200B CRC64;
MAPNNKKIKG KSNVGKGSKS KKGQQTRKTP TLKQKLHRES KVVKAESLNW KTVEVPDNLD
DWEGFYGLEE IDGVDVKIVN GKAEFIVKDN KKVKKGKTEE QEELEDDEEQ DEDEESEADE
EQGEDEDEDE EHEEDKINEE NEDEFEEEEF TGFDDDSEIQ DGMEVEDILD EDINEIGEVD
ESVEPVQESK PEHDEELSEN VFQHSQFVLP DDEDINLPHW QNEDSNFSLS PYTLHGLSVL
GFDKPTPIQK KTIPLAAEGK DVVGKAITGS GKTLAYGIPI LEKYLSNLSI INQNRQKKII
NHPTGIIFAP TRELAHQVVS HLNSLAKYSP LSTNGIVSIT GGLSIQKQER LLSHGPGIIV
ATPGRILELL QKDEDLTKRL ASTDIIVLDE ADRLLQDGHF EEFETILDLF RKNRPKNKTF
PWKWQTLVFS ATFSRDLFGK LDKNQKSHKR NSEGSSLIGN DEILNLLNDK LKFKDTRPAL
VDANPKEIVS GNITEALVEC GPTERDLYLY YFLLMYKGST LVFANSIDSV KRLVPFLNNL
NIPAFAIHSS MIQKQRLRAL ERFQKASEKN DTAVLIASDV AARGLDIPNI DHVAHYHLPR
SADVYIHRSG RTARAGKEGV SVMFCSPQEA SGPLRKLRRL VANNSTKGGR LNMHNDVKLL
PIEMDLVSQL KPRVIIASKL ADADISNTST RKEDSWVKQA AEELGVDDLS DLDDFEDDII
KKQRKRKEGK MITKDEKKGL RYELKELLSK SIRKETRRSY LTSGLQNIAH QMVTGVGHED
VVGHSKVNAL DDLKGKKVAR SKAGKVTKPS QKKQEKKQKK QERKDTMRKQ KEGNRK
