ID   MRH4_PICST              Reviewed;         593 AA.
AC   A3LT90;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MRH4; ORFNames=PICST_31323;
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 mitochondrial RNA
CC       metabolism. Required for maintenance of mitochondrial DNA (By
CC       similarity). {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: Mitochondrion {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. MRH4 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000498; ABN66365.2; -; Genomic_DNA.
DR   RefSeq; XP_001384394.2; XM_001384357.1.
DR   AlphaFoldDB; A3LT90; -.
DR   SMR; A3LT90; -.
DR   STRING; 4924.XP_001384394.2; -.
DR   EnsemblFungi; ABN66365; ABN66365; PICST_31323.
DR   GeneID; 4838839; -.
DR   KEGG; pic:PICST_31323; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_18_0_1; -.
DR   InParanoid; A3LT90; -.
DR   OMA; FHALKMQ; -.
DR   OrthoDB; 1223767at2759; -.
DR   Proteomes; UP000002258; Chromosome 4.
DR   GO; GO:0005739; C:mitochondrion; 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   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   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; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT         1..106
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           107..593
FT                   /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT                   /id="PRO_0000285157"
FT   DOMAIN          181..399
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          433..593
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          42..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           130..137
FT                   /note="Q motif"
FT   MOTIF           347..350
FT                   /note="DEAD box"
FT   COMPBIAS        46..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         194..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   593 AA;  66206 MW;  93CCFD0F5E2BF953 CRC64;
     MFPLRAQSAS LGANSTLFFR AYAVSHRKSG SKIQAWKGLK RGANGANRAN GTNSSQPESQ
     SSKAVFQSGK FSQLHQPSKK VYEKSSSGLD SISTFEQLRI FPTVRAAMVA EIKSTYNMKG
     PRYQSKDELV LKPTPIQVAA IRKINQPRLK NNKNVKEEEV SAGRKSAPST ADLVNEEFKK
     INSLQKLKVF TLAAETGSGK TWAYLSSLLS KLKEDEFGLY ESSEEKYRAS RNAQMVKSVV
     LVPTHDLVEQ VYSTLERANS IKFDVEKIGA NSRLKEFLQL PEQNGSLNLS ILKWGSGEAH
     KKLFDRCLKG RVDVLVTTPG KLASLSKLQN VNRPYRFLNH VEYCVLDEAD TLMDESWIET
     TMPVIEKFKK LRDLIICSAT IPKRFQTTLN RIFPTDDSII NIVTPSLHKL PKQIKVSVID
     SELSPYHGSK TRALAQALYA ITRDGTEPGL VKRVIVFVNK KESVNSLVDT LVNKFSHRPE
     DVIGITGEDK PEERSEKLEP FIKPAESIEE DPLNSKIKVL VTSDLMARGV NFVGIKNVII
     MDIPHNSVDL VHRIGRTGRM NQSGRVILIV DKKKNKAWLS GLPNAVKRGI QMG