MS116_SCHPO
ID MS116_SCHPO Reviewed; 535 AA.
AC O13622;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ATP-dependent RNA helicase mss116, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=mss116; ORFNames=SPACTOKYO_453.03c, SPBC691.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; AB004535; BAA21410.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC37365.1; -; Genomic_DNA.
DR RefSeq; NP_595596.1; NM_001021492.2.
DR AlphaFoldDB; O13622; -.
DR SMR; O13622; -.
DR BioGRID; 277651; 7.
DR STRING; 4896.SPBC691.04.1; -.
DR iPTMnet; O13622; -.
DR MaxQB; O13622; -.
DR PaxDb; O13622; -.
DR PRIDE; O13622; -.
DR EnsemblFungi; SPBC691.04.1; SPBC691.04.1:pep; SPBC691.04.
DR GeneID; 2541136; -.
DR KEGG; spo:SPBC691.04; -.
DR PomBase; SPBC691.04; mss116.
DR VEuPathDB; FungiDB:SPBC691.04; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_1_3_1; -.
DR InParanoid; O13622; -.
DR OMA; CFVGGAN; -.
DR PhylomeDB; O13622; -.
DR PRO; PR:O13622; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
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; ISS:PomBase.
DR GO; GO:0090615; P:mitochondrial mRNA processing; ISS:PomBase.
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 InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
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; Mitochondrion; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Reference proteome; RNA-binding;
KW Transit peptide; Translation regulation.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..535
FT /note="ATP-dependent RNA helicase mss116, mitochondrial"
FT /id="PRO_0000256013"
FT DOMAIN 70..248
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 262..429
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 495..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 38..66
FT /note="Q motif"
FT MOTIF 195..198
FT /note="DEAD box"
FT COMPBIAS 505..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 535 AA; 59449 MW; 8FC4025C7EAAC0DA CRC64;
MNISLKGAIF STVGRFNLPK VQGFIRWNST MKSQQPTLFS EVASLSSTFK NSLSRAGFEK
MTPVQQRVLN EVFPNEENAV VQAKTGTGKT LAFLLVAFKD VLKGKPRLNS SKIHSVILSP
TRELALQIFE EARKLTYGTG IRVSYAIGGN SKMREENAIR RGNANLLIAT PGRLEDHLQN
PRILESLSTD SFILDEADRL MDMGFAESIL NIHEAVTTTK TRKLCFSATM PPKVSNVFRG
ILGTDFKLIN CLDPNEPPTH ERVPQFVIET KLDKVFSSSL SLLQQLTSSN PSSRIIVFLP
TISMVDFVGG VLENHLKIPC FILHSGLTTA QRRSITESFR KCQSGILFAT DVVARGMDFP
NITQVVQITG PSNTDDYIHR IGRTGRAGKT GEAYLILLEQ EKPFLNSIKH LPLKRATIEP
LSDQALSTLR SDIEKSSKFS RTNALKTLYG SKPHVFSGSS QRRATGKNIH ESAIALFSLH
DVPGLMEELI YKSRGRGSPK GFRGSQLKYP SSSSSSFQRR PRSLPSRGRY QQSRR
