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MDV1_MALGO
ID   MDV1_MALGO              Reviewed;         674 AA.
AC   A8PTE4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Mitochondrial division protein 1;
GN   Name=MDV1; ORFNames=MGL_0411;
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966;
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(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}.
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DR   EMBL; AAYY01000001; EDP45422.1; -; Genomic_DNA.
DR   RefSeq; XP_001732636.1; XM_001732584.1.
DR   AlphaFoldDB; A8PTE4; -.
DR   SMR; A8PTE4; -.
DR   STRING; 425265.A8PTE4; -.
DR   EnsemblFungi; EDP45422; EDP45422; MGL_0411.
DR   GeneID; 5856942; -.
DR   KEGG; mgl:MGL_0411; -.
DR   VEuPathDB; FungiDB:MGL_0411; -.
DR   InParanoid; A8PTE4; -.
DR   OMA; IVGVWTC; -.
DR   OrthoDB; 927943at2759; -.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
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; 3.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
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..674
FT                   /note="Mitochondrial division protein 1"
FT                   /id="PRO_0000341597"
FT   REPEAT          329..368
FT                   /note="WD 1"
FT   REPEAT          371..408
FT                   /note="WD 2"
FT   REPEAT          434..471
FT                   /note="WD 3"
FT   REPEAT          519..562
FT                   /note="WD 4"
FT   REPEAT          565..604
FT                   /note="WD 5"
FT   REPEAT          606..641
FT                   /note="WD 6"
FT   REPEAT          645..674
FT                   /note="WD 7"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          202..260
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   674 AA;  74225 MW;  E2ED5676B8E20010 CRC64;
     MGSSSANKKH ASTSSAPSND VRAPHADTNR LLNDMAPQLM TPAMMNAMAR ISLQSTPIAT
     TRDPFPLQRA TLLLAPRFSM ENPARSLARI SSSLLQFSGL SKHSKSGREQ QRTPITSMDV
     GVLEESQRIL ATADADLDAS LDTSLLDDDN DTSDVAAAAD APVSLFRGYK ATVPQVSTSK
     TRRRQLQASE NIRRSKHEPH LLSLQELEVQ DRDMLAERRN LEIRRALYHA EIVHVDAKIA
     ALEATKASLQ QKLLHVREEE LELDDERQGV SELLELQRHR RAMPGGRGLD AGTVLPIGAG
     SSRWRKTPVF LPSEHDDLPH GIAFMSLNLE TGPITALDFS EPYGTLISAA LEDTVRVWDL
     STGEDVGRLR GHTDTVKCLQ VEDELCVSGS LDSTLRVWDL RRVDAFETAC RARMEGDGQD
     VPEADDPCIR TLAGHSRGIT ALAFDHETLV SGAADKTLRQ WDLETSQCVL TMDILWAMSN
     PSTSVDLRVP LESSAPLLDP LHGANQFAGP FSYPQPPYED GSWEMYTDFV GSVQFWGFAL
     ASGSGDGGVR LWDLRTGQAH RTLLGHTAPI TCLQFDDTHL ISGSLDKTIR VWDLRSGHVL
     ETLHYDYPVT ALQFDSRKII AAAGACAVDV YNRTSEKHSS LIKHGHTAPV ERLRYMDRYA
     VTGGRDSCIK VWSL
 
 
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