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MS116_ASPFU
ID   MS116_ASPFU             Reviewed;         655 AA.
AC   Q4WRP2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=ATP-dependent RNA helicase mss116, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=mss116; ORFNames=AFUA_1G15620;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000004; EAL90890.1; -; Genomic_DNA.
DR   RefSeq; XP_752928.1; XM_747835.1.
DR   AlphaFoldDB; Q4WRP2; -.
DR   SMR; Q4WRP2; -.
DR   STRING; 746128.CADAFUBP00001485; -.
DR   EnsemblFungi; EAL90890; EAL90890; AFUA_1G15620.
DR   GeneID; 3509952; -.
DR   KEGG; afm:AFUA_1G15620; -.
DR   VEuPathDB; FungiDB:Afu1g15620; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_6_1; -.
DR   InParanoid; Q4WRP2; -.
DR   OMA; KTQREGC; -.
DR   OrthoDB; 537587at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
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   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; 2.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 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..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..655
FT                   /note="ATP-dependent RNA helicase mss116, mitochondrial"
FT                   /id="PRO_0000256008"
FT   DOMAIN          116..307
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          341..503
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          594..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           84..113
FT                   /note="Q motif"
FT   MOTIF           251..254
FT                   /note="DEAD box"
FT   COMPBIAS        605..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         129..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   655 AA;  73931 MW;  38D02DB831783CB5 CRC64;
     MMLGAVRRYG VVHALRASVP RTICRPSNSQ LLRCQTSPVT ACPQSVRLLH KSSPFFSSAS
     AQAQAQPDDL QSAAPQEPLR EFTDLAERGL VDPKIIRAIV KDMNIKTMTD VQSQTLREIL
     QGDDVLAQAK TGTGKTLAFL TPVFQNIMKD PSLKGLNWRR SQASSSDIRA IIISPTRELA
     EQIAVEARRL AAHSGVIVQT AVGGTQKREG LRRIQREGCH VLIGTPGRLK DVLSDSYNGV
     TAPNLSTLVL DEADRLLDDG FSDAIIDIQR LLPDPMKVDR QTLMFSATVP REVMQMVRKT
     MKPNFKFVKT VRDDEVPTHL TVPQKYVILR GYENAMPALL EFVTKYVEGE KENPNQRPFK
     AIVYFNSTVQ TNLVYETFRN IVEQRHHPLR RVRVYEIHSQ LTQARRTRSS DFFRAAKSAI
     LFSSDVTARG MDFPDVTHVI QVSIPRDRAT YIHRLGRTAR ANKTGEGWVL THRGELPEFL
     KQLEGIPLNL DKETFATATV DMTKPELDPK SPATRFIQEI KDAVREVPES LKRRAYTSLL
     GPLRGYFARK QDLIQAINNC VVHGYGLPVP PQLSPTLARN LGLDRVPGVR IANYRGSSDN
     MSTRPDYRGG DRDMWASNSR RGREFNSDRR ESRFGNHRNA DDFFGGRRRA YRDDY
 
 
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