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YME2_PHANO
ID   YME2_PHANO              Reviewed;         823 AA.
AC   Q0V3D6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Mitochondrial escape protein 2;
DE   Flags: Precursor;
GN   Name=YME2; ORFNames=SNOG_01478;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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}.
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DR   EMBL; CH445326; EAT91127.2; -; Genomic_DNA.
DR   RefSeq; XP_001792116.1; XM_001792064.1.
DR   AlphaFoldDB; Q0V3D6; -.
DR   STRING; 13684.SNOT_01478; -.
DR   EnsemblFungi; SNOT_01478; SNOT_01478; SNOG_01478.
DR   GeneID; 5968961; -.
DR   KEGG; pno:SNOG_01478; -.
DR   eggNOG; ENOG502QS0P; Eukaryota.
DR   HOGENOM; CLU_007861_0_0_1; -.
DR   InParanoid; Q0V3D6; -.
DR   OrthoDB; 213553at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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           ?..823
FT                   /note="Mitochondrial escape protein 2"
FT                   /id="PRO_0000343128"
FT   TOPO_DOM        ?..281
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..823
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          174..266
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   823 AA;  92664 MW;  9105CF7B768986AF CRC64;
     MRVEDHCSVF AWSSLQASRP WPAAGRYASL QAGEDKTGHI SAGPNEGILF FNNVFPIQIR
     KIMGLPMPRI LDRLISPAMS GTDPNTVIQR AKAKRNLPIE STEILPRVRE GGAFVKFTHD
     GSTPTSEIEK TLQEYLRDEP VKPWWSPWKR MRAKVVKGRP WVEDMMRLPA PRLRVEFVPG
     EPGASVTEAV DLSQEQLFQF FRPYGKLSDI VMQESDSKVL PKFAYLDYSS IGKAIMAKNC
     MHGYLVSEAE GGGKKGTFLR LKYEQKIKPR YIRDWIINHP RIIIPIIAAL IAGTVAIVFD
     PIRTFFVKAH ITRTLHLEDN KWYKWIKGYA SDIIRGHKRD EDDSYDAIWD DRKGNIEQIQ
     TWLMETADTF IIVQGPRGSG KKELVVDQAL QDNKLKLVID CKPIQEARGD SPTISAAAAA
     VGYKPVFSWM NSISGMIDMA AQGATGMKTG FSETQETQLN KIWNTTTTAL KQIALERRHK
     DDRDANLADD DWLEAHPEHR PVVVIDNFLH KSHEGGIVYD KMAEWAARLT TTNIAHVIFL
     TNDVAFSKSL SKALPDRVFR QISLSDCSPD VAKKFVVTHL DADVEDDPAP KDGSEKKLPS
     QHRTDLAELD SCIDLLGGRL TDLEFLARRI KTGETPNKAV NEIIDQSASE ILKMYIFGAE
     DDGGRRKWSP EQAWMLIKEL AQKESLRYNE VLLDDILKTG GESALRDLEQ AELISIISGP
     NGRPSTIRPG KPVYHSAFKR LAQDKVLKSH LDYAILTNLT KIENATIDKC ENELLLLSKL
     RNQPAQTAGR VQYLLAKLSA SQVKVEKYET EIKGLKKVMA EED
 
 
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