ID   MDV1_VANPO              Reviewed;         706 AA.
AC   A7THX0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Mitochondrial division protein 1;
GN   Name=MDV1; ORFNames=Kpol_1031p36;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: Involved in mitochondrial fission. Has a partially redundant
CC       function to CAF4 in acting as an adapter protein required to form
CC       mitochondrial fission complexes. Formation of these complexes is
CC       required to promote constriction and fission of the mitochondrial
CC       compartment at a late step in mitochondrial division (By similarity).
CC       {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; DS480393; EDO18132.1; -; Genomic_DNA.
DR   RefSeq; XP_001645990.1; XM_001645940.1.
DR   AlphaFoldDB; A7THX0; -.
DR   SMR; A7THX0; -.
DR   STRING; 436907.A7THX0; -.
DR   EnsemblFungi; EDO18132; EDO18132; Kpol_1031p36.
DR   GeneID; 5546402; -.
DR   KEGG; vpo:Kpol_1031p36; -.
DR   eggNOG; KOG4155; Eukaryota.
DR   HOGENOM; CLU_012350_1_0_1; -.
DR   InParanoid; A7THX0; -.
DR   OMA; HASINCM; -.
DR   OrthoDB; 927943at2759; -.
DR   Proteomes; UP000000267; 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; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 4.
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..706
FT                   /note="Mitochondrial division protein 1"
FT                   /id="PRO_0000330113"
FT   REPEAT          394..434
FT                   /note="WD 1"
FT   REPEAT          437..476
FT                   /note="WD 2"
FT   REPEAT          495..534
FT                   /note="WD 3"
FT   REPEAT          554..593
FT                   /note="WD 4"
FT   REPEAT          596..635
FT                   /note="WD 5"
FT   REPEAT          637..672
FT                   /note="WD 6"
FT   REPEAT          677..706
FT                   /note="WD 7"
FT   REGION          160..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          227..264
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        310..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   706 AA;  80436 MW;  720CFE313A53AC60 CRC64;
     MDDNEQFSQL RNVISTTASA LLGIENLDKS ILSSNSRYKK ILSETIKNLG GDDSLVKLRK
     NFSNLKRQEE SHDAYERYSG DDYFRNQLTD SRTTFRVLTY LSDEILKASL DDEKSNHDQG
     LLEFTNEEES GTKNTSSLFQ GFEASLPILN ERLENNDKNK YIKNSEGNDH NNNNDNNDDK
     NDKLFEFTNN YISSVSIDTE KISRSYSMKY LKTLSEDVLR KLNFTLIQED VTKEEVEDLS
     IKLERLKERH QSACKRLETV EQDELFLENA LSLIKDRMKF IQEYDLELES NDPEIEDINQ
     NEKSYNEAKE SNDLNTSQQN VEDLKPNTFV NNDKDVTVAK SEAIVSKVKT KNQKTINRLQ
     RFYNEENRKS RKLPTTLLQS HYEPGTNIAT IEKAHENGVY CMDFDMPFGT LCTAGYLDHT
     VNVWDLTRKV KVAEMSGHLA TIQCMQLGSH YNMLITGGKD AMLKIWDINL ATQLYQEDQS
     SIESDYNSCI HTFDSHSGGI TALSFDSVHL VSASQDKTIR QWDLVNGKCI QTIDLSSVVK
     QNQTDIVNIP DFYSSSEPFV TGSLQCFDAA LATGTRDGLV RLWDMRSGKV VRTFMGHTNA
     VTSLKFDSYN LISGSLDKSI RTWDLRTGSL SDLFAYDSPV YSIDFDSSNL VSAIGETSFK
     VYNRKDDKQW ECVNSAEDTS SIYHVKYKNN YAVTGSNDGT IKAWVV