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YME2_ASPFU
ID   YME2_ASPFU              Reviewed;         871 AA.
AC   Q4WJ38;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Mitochondrial escape protein 2;
DE   Flags: Precursor;
GN   Name=yme2; ORFNames=AFUA_1G07350;
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: Plays a role in maintaining the mitochondrial genome and in
CC       controlling the mtDNA escape. Involved in the regulation of mtDNA
CC       nucleotide structure and number. May have a dispensable role in early
CC       maturation of pre-rRNA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the YME2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL88444.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000007; EAL88444.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_750482.1; XM_745389.1.
DR   AlphaFoldDB; Q4WJ38; -.
DR   STRING; 746128.CADAFUBP00000758; -.
DR   PRIDE; Q4WJ38; -.
DR   GeneID; 3507741; -.
DR   KEGG; afm:AFUA_1G07350; -.
DR   VEuPathDB; FungiDB:Afu1g07350; -.
DR   eggNOG; ENOG502QS0P; Eukaryota.
DR   HOGENOM; CLU_007861_0_0_1; -.
DR   InParanoid; Q4WJ38; -.
DR   OrthoDB; 103839at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd12433; RRM_Yme2p_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR018850; Mt_escape_2_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR039627; Yme2_C.
DR   InterPro; IPR034260; Yme2_RRM.
DR   PANTHER; PTHR32198; PTHR32198; 1.
DR   Pfam; PF10443; RNA12; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; mRNA processing;
KW   Reference proteome; RNA-binding; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..871
FT                   /note="Mitochondrial escape protein 2"
FT                   /id="PRO_0000343113"
FT   TOPO_DOM        ?..336
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..871
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          229..321
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   871 AA;  99161 MW;  F3694E2085B8631B CRC64;
     MIDVIIRHQA SPLIESALVY QSITIIFGNA HLQSSFRKRN VILAAMMRTR IPGLVPRICQ
     TPLPWKRPTQ MTRVRYARWS TSHAVTWLET GHIDLKENEG LLFINNIFPS RLQWLLRGPL
     GGMRSYEAAV KRIDRPHLAA SDTFQIIQRV VPKNLNVQVK EVVPRFREGG AFVKYTRPGD
     VNDADIEASI KENLKEHPIR PWFNPFQEVQ VCRVIGRPWI EDLYRLPSPR LKVSFHPVSP
     EASAADLNTE TLYTLFRPYG KIRDIETQPS DGKVTPRYAY VEFSRPKYAG MAKNCMHGFT
     IPEQEGGGKS GTRLKIKYER KIKLSMIKDW LLNHPRIVIP VLAALLAAIT VTIFDPMRTF
     FIELKIKSTL QTEENGVMQW IRKQVNKANI IYFGRKGADP RGLTAIWEDR QEDITRLQSW
     LMENVETFII IHGPRGSGKR ELVLDRALVD YKYKIVIDCK QIQDARGDSA KIARAASQVG
     YRPVFSWMNS ISSFIDLAAQ GMIGTKAGFS ETLDAQLSNI WQNTATALKK VTLEHRKKND
     NDSHLTDEEY LEAHPELRPV VVIDNYLHNA SESSVVYDKI TEWAAGLTAG NIAHVIFLTT
     DVSYAKPLSK ALPNSVFRTI TLGDCSLEVG RKFVMSHLAY ESKDGKTQPR RAEELEDLDA
     CIEALGGRVT DLEFMAHRIE AGETPRGAVN RIIEQSASEI LKMFLLTPET IEQSWTHEQA
     WYLIKRLAES KDGSLSYNEI VLSELFKENG EITLRALEHA ELISIAAVNG CPQRIRPGKP
     VLRAVFKKVT ENKALSSRMD LAIIAKKINK ENKSIEKYEE ELSLLGSLPR QPRELTDRIQ
     WLLNKVYSSQ NKIAKYEKES AYLQKILRSE H
 
 
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