ID A0A1L9UMU5_ASPBC Unreviewed; 558 AA.
AC A0A1L9UMU5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Mitochondrial division protein 1 {ECO:0000256|ARBA:ARBA00039789};
DE AltName: Full=Probable E3 ubiquitin ligase complex SCF subunit sconB {ECO:0000256|ARBA:ARBA00015819};
DE AltName: Full=Sulfur controller B {ECO:0000256|ARBA:ARBA00032113};
DE AltName: Full=Sulfur metabolite repression control protein B {ECO:0000256|ARBA:ARBA00030034};
GN ORFNames=ASPBRDRAFT_42823 {ECO:0000313|EMBL:OJJ73044.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ73044.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- FUNCTION: Component of the SCF(sconB) E3 ubiquitin ligase complex
CC involved in the regulation of sulfur metabolite repression, probably by
CC mediating the inactivation or degradation of the metR transcription
CC factor. {ECO:0000256|ARBA:ARBA00002730}.
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.
CC {ECO:0000256|ARBA:ARBA00043913}.
CC -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
CC -!- SUBUNIT: Component of the SCF(sconB) E3 ubiquitin ligase complex.
CC {ECO:0000256|ARBA:ARBA00011725}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004570}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004570}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004570}.
CC -!- SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family.
CC {ECO:0000256|ARBA:ARBA00038415}.
CC -!- SIMILARITY: Belongs to the WD repeat MET30/SCONB/SCON-2 family.
CC {ECO:0000256|ARBA:ARBA00007968}.
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DR EMBL; KV878683; OJJ73044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9UMU5; -.
DR STRING; 767769.A0A1L9UMU5; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_42823; -.
DR OMA; RHNWSRG; -.
DR OrthoDB; 1377096at2759; -.
DR Proteomes; UP000184499; Unassembled WGS sequence.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19855:SF12; WD REPEAT-CONTAINING PROTEIN 37; 1.
DR PANTHER; PTHR19855; WD40 REPEAT PROTEIN 12, 37; 1.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000184499};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT DOMAIN 24..70
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REPEAT 433..468
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 558 AA; 62360 MW; 3A10FA6845F42AB5 CRC64;
MPKRRNVEDL PPPKRLRTTP SRRLDHISTL SDELLLHILS FLPLPSLLVC QQLSRRFHAL
AGDSELWKRQ YYSRWVRPRA RRLPNAKRAL LSRSEIEYSP RVSTWLDHSH LAKEGVATNW
KRQYRLRYNW SKGVCRVTEV EFPQPLRRQM LVTFCAGIVF TADSDHGLRA WAAEKPEQCL
ARSPLTKSPS RSLPAPTAMA AATSGPQQSL VDVTVGFEDG SLGVYTLDTT TFWIETRFAY
VECTGEAITA MASCSPFLLL VSQHKVLSLY ETITDEDGWS LTPRLLTTLK ADSILEPISL
SVRAAGPKIV ASIVYSFYHI GCGWSLGIQE LQFALDGQQL SSRLATTVDC HYGMVSPTSR
SQSKRDYRTT YVIDSRNELN AWPPGPSISH CEPPTSVSYS HPYLLTSHAD NTLTVYLVVS
TSTSLSVTSC QRLWGHTSSV SAVQVSDRGK AVSVSSRGDD IRIWELESLV SSLGGHKALR
DGNSIRVSPE NKADQRHDSL DLVSESSHGQ LNATRSNSVD NTYGLTRMHN CIGFDDERVL
LLREKGVGTQ MLELYDFT
//
