MS116_PICGU
ID MS116_PICGU Reviewed; 714 AA.
AC A5DEZ5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=ATP-dependent RNA helicase MSS116, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=MSS116; ORFNames=PGUG_01846;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: ATP-dependent RNA helicase required for mitochondrial
CC splicing of group I and II introns. Also required for efficient
CC mitochondrial translation (By 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 matrix {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. DDX18/HAS1
CC subfamily. {ECO:0000305}.
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DR EMBL; CH408156; EDK37748.2; -; Genomic_DNA.
DR RefSeq; XP_001486175.1; XM_001486125.1.
DR AlphaFoldDB; A5DEZ5; -.
DR SMR; A5DEZ5; -.
DR STRING; 4929.XP_001486175.1; -.
DR EnsemblFungi; EDK37748; EDK37748; PGUG_01846.
DR GeneID; 5127588; -.
DR KEGG; pgu:PGUG_01846; -.
DR VEuPathDB; FungiDB:PGUG_01846; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_21_0_1; -.
DR InParanoid; A5DEZ5; -.
DR OMA; IGFKEDL; -.
DR OrthoDB; 537587at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; 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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; 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 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; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Reference proteome; RNA-binding;
KW Transit peptide; Translation regulation.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..714
FT /note="ATP-dependent RNA helicase MSS116, mitochondrial"
FT /id="PRO_0000294630"
FT DOMAIN 106..296
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 335..498
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 581..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 74..102
FT /note="Q motif"
FT MOTIF 234..237
FT /note="DEAD box"
FT COMPBIAS 581..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 714 AA; 81388 MW; F45A637D356337AD CRC64;
MSWVRSVAIR TALCRQVRSR YQSYGSTRLF SSSLRSWEEP EVVTKTPKAD IDHEAVKAHQ
ESSPLKSIEV PFTSLEASRK FDKSIFRGLY NSKMKNMTVV QQRAIMPMMD TKTGVVVRAK
TGTGKTLAFA LPCIQAALEN PQQTQKGRIQ ALVVAPTRDL ALQIEAEFKK VLQHQTRNVH
RKTDTFVLIG GRKNDLHPKA KAAIVIATPG RLEAILRDPR MLPMFSDLKY RVYDEADRLL
DQGFAPTLEV IEERLRDAKA EALEPDNHFK TALFSATVDD AVTNFAHETI GKEYEYINCV
DKDAEESHEN IHQGIVRTQS IKDSFEASFS YILNHINDKY FKAIVFLPTI TGTEYYYRVL
QRAKREELYD SETATKKYGS RILRLHGKMS QSARDRTVKE FRRTSHGVLV CTDVAARGLD
FNDVSHVIQM CPSSSVADYI HKIGRTARAG ARGKARIFIS EPEMKFIETL QRERGIVFKE
DTEYVKDETS PDHFQRLGSY EQDALEEFLR TFLGFAASVS GVYRFNKQRI VEESFALYRH
ILNDPSAKLS VGRRFVSEVL RMPGRDAAEF FDVPGGFDMR SSNDRKSKRT FMGDGGSRSD
RGFSNDRYGN SGRSYNKSRS FDRNDRSYGN DRSYSNDRKS YGNKSYGDKS YGNKAYGDKS
YGDKSYGDKS YGKSYGNRSN DRSFSRGNDR GGYEKRNYGS QSRNTYGRRD DSDE
