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MDV1_ASPNC
ID   MDV1_ASPNC              Reviewed;         657 AA.
AC   A2R3Z3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Mitochondrial division protein 1;
GN   Name=mdv1; ORFNames=An14g06000;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Involved in mitochondrial fission. Acts as an adapter protein
CC       required to form mitochondrial fission complexes. Formation of these
CC       complexes is required to promote constriction and fission of the
CC       mitochondrial compartment at a late step in mitochondrial division (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK42161.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM270325; CAK42161.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001401223.2; XM_001401186.2.
DR   AlphaFoldDB; A2R3Z3; -.
DR   SMR; A2R3Z3; -.
DR   PaxDb; A2R3Z3; -.
DR   EnsemblFungi; CAK42161; CAK42161; An14g06000.
DR   GeneID; 4987458; -.
DR   KEGG; ang:ANI_1_822124; -.
DR   VEuPathDB; FungiDB:An14g06000; -.
DR   Proteomes; UP000006706; Chromosome 1R.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..657
FT                   /note="Mitochondrial division protein 1"
FT                   /id="PRO_0000330098"
FT   REPEAT          319..360
FT                   /note="WD 1"
FT   REPEAT          361..398
FT                   /note="WD 2"
FT   REPEAT          436..475
FT                   /note="WD 3"
FT   REPEAT          481..538
FT                   /note="WD 4"
FT   REPEAT          541..580
FT                   /note="WD 5"
FT   REPEAT          582..617
FT                   /note="WD 6"
FT   REPEAT          628..657
FT                   /note="WD 7"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          210..250
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   657 AA;  72551 MW;  E3A2CB1AA90400AB CRC64;
     MDKHRRRDES PSGLSDIVEP DGLLGTGITS RHIEAFGRKV TSTAGHLMGP APDSSTGGHY
     HTAMADIQRE LRHPNTQRKV FSLTQTTPTD LVRSKLSTTE IQSRAISSLP DELLANIPDD
     SSSYSLFQGF QASQDDIEYR RAHRRRSSKS KKLLKDGETR GALPSAPSDL KKERDLLSRR
     MELMGVRKNM CSSEIHDIDN KIANLHNMRK IVLDRLAGLE MEEADLEHEL NEIENKLEDI
     QEEQQEAEVP PPATPKSSEA NDDSIVSEDP AMGASFMSES IYQKIPSPKS VKQRSIRKRS
     MPVLHEHFAP GSEIKEMPAH SDMVTAIDFD YPFGTMISAA LDDTVRVWDL NVGRCVGFLE
     GHNASVRCLQ IEDNIVATGS MDASVKLWDL SRARTTTRDN RVTRREDDEE SAQADDASMA
     SHSTTLEDCY VYSLDAHVDE VTALHFKGDT LISGSADKTL RQWDLVKGRC VQTLDVLWAA
     AQASTLGSET TWRPSGRLPD ASADFVGAVQ CFDAALACGT ADGMVRLWDL RSGQVHRSLV
     GHTGPITCLQ FDDVHLVTGS QDRSIRIWDL RTGSIFDAYA YDKPITSMMF DTKRIVAAAG
     ENVVKVYDKA DGHHWDCGAG VGVDDSGPQP ATVERVRLKD GFLVEGRKDG IVAAWTC
 
 
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