ID   MDV1_ASPTN              Reviewed;         654 AA.
AC   Q0CJD8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Mitochondrial division protein 1;
GN   Name=mdv1; ORFNames=ATEG_06196;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU33957.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476601; EAU33957.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001215374.1; XM_001215374.1.
DR   AlphaFoldDB; Q0CJD8; -.
DR   SMR; Q0CJD8; -.
DR   STRING; 341663.Q0CJD8; -.
DR   PRIDE; Q0CJD8; -.
DR   EnsemblFungi; EAU33957; EAU33957; ATEG_06196.
DR   GeneID; 4321622; -.
DR   eggNOG; KOG4155; Eukaryota.
DR   OrthoDB; 927943at2759; -.
DR   Proteomes; UP000007963; 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; 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..654
FT                   /note="Mitochondrial division protein 1"
FT                   /id="PRO_0000330100"
FT   REPEAT          318..359
FT                   /note="WD 1"
FT   REPEAT          360..397
FT                   /note="WD 2"
FT   REPEAT          433..472
FT                   /note="WD 3"
FT   REPEAT          478..535
FT                   /note="WD 4"
FT   REPEAT          538..577
FT                   /note="WD 5"
FT   REPEAT          579..614
FT                   /note="WD 6"
FT   REPEAT          625..654
FT                   /note="WD 7"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          209..253
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        246..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  72248 MW;  DDD0D48B213CBDC9 CRC64;
     MDKHRRDESP SGLSDIVEPD GLLGTGLTSR HIEAFGRKVT TTAGHLMAPS STEATTGSHY
     HSAMVDIQRE LRRPNTQRRV FSLTQTTPTD LVRSKLSTTE IQSRAISSLP DDLLANIPED
     SSSYSLFEGF QASQDDHEYR KVHRRRISKG KKLLKDGDAR AALPSTPTDL KKDRDILSRR
     LDLMGVRKNM CSSEIHEIDN KIANLHNMRK IVLDRLAGLE MEEAELEHEL TELDNKLEDL
     QEEQPESQAA VATPKSSEAN EDSFVSEDPA MDASFMSESI YQKMSSPKSI KQRSIRKRSM
     PILHEHFAPG SQIKEMPAHN DMVTAIDFDF PFGTMVSAAL DDTVRVWDLN VGRCTGLLEG
     HNASVRCLQI EDNIVATGSM DASVKLWDLS RARSVTRDGR VNKDDEGEDT ADDAHELFQS
     TTLEDCYVYS LDAHVDEVTA LHFRGDTLIS GSADKTLRQW DLVKGRCVQT LDVLWAAAQA
     STLGGDTQWR PSGRLPDASA DFVGALQCFD AALACGTADG MVRLWDLRSG QVHRSLVGHT
     GPVTCLQFDD VHLVTGSLDR SIRIWDLRTG SIYDAYAYDK PVTSMMFDSK RIVAAAGENV
     VKVYDKADGH HWDCGAGVGA DAEGPSPATV ERVRLKDGFL VEGRKDGIVS AWTC