MDV1_PHANO
ID MDV1_PHANO Reviewed; 681 AA.
AC Q0U2T3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Mitochondrial division protein 1;
GN Name=MDV1; ORFNames=SNOG_13958;
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: 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; CH445353; EAT78583.2; -; Genomic_DNA.
DR RefSeq; XP_001804158.1; XM_001804106.1.
DR AlphaFoldDB; Q0U2T3; -.
DR SMR; Q0U2T3; -.
DR STRING; 13684.SNOT_13958; -.
DR EnsemblFungi; SNOT_13958; SNOT_13958; SNOG_13958.
DR GeneID; 5981081; -.
DR KEGG; pno:SNOG_13958; -.
DR eggNOG; KOG4155; Eukaryota.
DR HOGENOM; CLU_012350_1_1_1; -.
DR InParanoid; Q0U2T3; -.
DR OrthoDB; 927943at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
DR GO; GO:0016559; P:peroxisome fission; IBA:GO_Central.
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..681
FT /note="Mitochondrial division protein 1"
FT /id="PRO_0000330110"
FT REPEAT 326..367
FT /note="WD 1"
FT REPEAT 369..405
FT /note="WD 2"
FT REPEAT 458..497
FT /note="WD 3"
FT REPEAT 505..561
FT /note="WD 4"
FT REPEAT 564..603
FT /note="WD 5"
FT REPEAT 605..640
FT /note="WD 6"
FT REPEAT 647..681
FT /note="WD 7"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 211..263
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 75048 MW; 580530869A6A30BA CRC64;
MASSFARDGS PSRGRSTSPR PRIPEESLEA SLMDGLPDTR QLQAFGRKVT ATAGSLIGTE
GVGQHYQNAL GELHRELRRP MLQRSVFSFA QTTPREIVRS RISVPEIQQR ALAYVPDDML
ANIPEDNNEF SLFQGFQATL PDEPETIKKK GKTHNARGQR LIGGELEDDE YSKLPPSMQR
LQKQKHSMSH QLEMMGVRKH MCVAEIHEID NKIANLNTMR KMVLDRLAGL EIQEEELAQD
LLGVDNEIED LQEELDDAAA LAPPKEDSRP TTSGSEAVSE TFMSESIYQK ISPKSKNRGK
KPIRRPSMRV LHEHLESGSK IKELPAHNDS ITAMDFDAPW GTLVTASLDD TVRVWDLNAG
RCIGMLEGHL SSVRCLQVEE SIVATGSMDA TIRLWDLSRA EYAPQDNRVN KRGGEGEGEG
DGDAQEDEDG LAFENSSDAP PAPPPTIMQD VPLFTLESHV DEITAIHFKG DTLVSGSADK
TLRQWDLVKG RCVQTLDVLW AAAQATATNN ASSEWRPTGR SMDASADFVG AIQVFDAALA
CGTADGMVRL WDLRSGQVHR SLVGHTGPVT ALQFDDVHLV TGSADRSIRI WDLRTGSIYD
AYAYDNPVTS MMFDSRRIVS AAGESVVKVY DKTDGRHWNC GPGVGADEDD NTSHAMIERV
RIKDGYLVEG RRDGTVGVWS C