ID A0A094DIX6_9PEZI Unreviewed; 742 AA.
AC A0A094DIX6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 03-MAY-2023, entry version 28.
DE RecName: Full=Mitochondrial fission 1 protein {ECO:0000256|ARBA:ARBA00014314};
GN ORFNames=V497_04317 {ECO:0000313|EMBL:KFY59405.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY59405.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY59405.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has a role in mitochondrial fission. Has a role in outer
CC membrane fission but not matrix separation.
CC {ECO:0000256|ARBA:ARBA00025016}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004572}.
CC -!- SIMILARITY: Belongs to the FIS1 family.
CC {ECO:0000256|ARBA:ARBA00008937}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY59405.1}.
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DR EMBL; JPJZ01000893; KFY59405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DIX6; -.
DR STRING; 1420910.A0A094DIX6; -.
DR HOGENOM; CLU_021597_2_0_1; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000029268; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000266; P:mitochondrial fission; IEA:InterPro.
DR CDD; cd12212; Fis1; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016543; Fis1.
DR InterPro; IPR033745; Fis1_cytosol.
DR InterPro; IPR028061; Fis1_TPR_C.
DR InterPro; IPR028058; Fis1_TPR_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13247:SF0; MITOCHONDRIAL FISSION 1 PROTEIN; 1.
DR PANTHER; PTHR13247; TETRATRICOPEPTIDE REPEAT PROTEIN 11 TPR REPEAT PROTEIN 11; 1.
DR Pfam; PF14853; Fis1_TPR_C; 1.
DR Pfam; PF14852; Fis1_TPR_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 523..564
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 304..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..376
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 80572 MW; 7BA02AC5255A1953 CRC64;
MTTLPYAADA ESPLKPSELQ VLRAQYEKEG EYVGVQTKFN YAWGLIKSNQ RSEQQTGVRL
LSDIFRDSAE RRRECLYYIA LGNYKLGNYA EARRHNDLLL DKEPTNMQAG SLRALIDDKV
AKEGLMGVAI LSGVAVAAGV YPEYLDYATS TDDGFLSLNS SALRRTGLAL SLGLTALAAY
QGVRDAMADQ PQEQRRRLDV TGSREVVYCH QCENEWYRDE NGLVCPRCDG DMTEIISAEN
DPRPPELPAP LSSDELRGLR EHDPWEHHHD DDSDPEVGDI REFIRENPQG GRTTFVQRTF
RSAPREVFSS GSSRQPPNSN DPASQTLRDF EGIISGILGP NTRVSGQPGE RHESPFGPPG
PRPGEPAGPP PGMPPGWGNF RTAEAPGDHQ PRIFGGRVTF QFGGPPPRAF NAGEDQGPQE
QDLNTILRDL MLVLQPPGAN GGAGAQGPLG GLHGLFAGLL NPANAVSGDA VYSQEALDRI
ISTLMEQHPT SNAPGPAPAE AIAALPKKKV DKEMLGSEGK AECSVCMDDV VLDEEVVSLP
CSHWFHEACV KAWLSEHNTC PICRTGVARD GTAVPAGTNP PTSPVNSGGP NSPEPVEGAE
GPFSRRSTFL RRRPSINENR LASIRQAAGL DPEHSDLGAQ SSGVTMNPSS RRERSASPPS
HMPGAFSSGN NRNTIFRRQE SDTDAGSTGR RDRERELETE RSRNHERADR SSDAARPDSD
HSNNSSNSIG GSFGSWLRRL GR
//
