ID A0A178AYT0_9PLEO Unreviewed; 152 AA.
AC A0A178AYT0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 18.
DE RecName: Full=Mitochondrial fission 1 protein {ECO:0000256|ARBA:ARBA00014314, ECO:0000256|PIRNR:PIRNR008835};
GN ORFNames=IQ06DRAFT_292334 {ECO:0000313|EMBL:OAL03106.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL03106.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL03106.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL03106.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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 -!- DOMAIN: The C-terminus is required for mitochondrial localization,
CC while the N-terminus is necessary for mitochondrial fission.
CC {ECO:0000256|PIRNR:PIRNR008835}.
CC -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000256|ARBA:ARBA00008937,
CC ECO:0000256|PIRNR:PIRNR008835}.
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DR EMBL; KV441709; OAL03106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AYT0; -.
DR STRING; 765868.A0A178AYT0; -.
DR InParanoid; A0A178AYT0; -.
DR OrthoDB; 1355881at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000266; P:mitochondrial fission; IEA:UniProtKB-UniRule.
DR CDD; cd12212; Fis1; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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 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 PIRSF; PIRSF008835; TPR_repeat_11_Fis1; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR008835};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|PIRNR:PIRNR008835};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|PIRNR:PIRNR008835};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 152 AA; 17000 MW; 0C1F52CF6CC495B9 CRC64;
MSPSLPYAAD VESPLKPEEL QVLRAQYEKE GEYVGLQTKF NYAWGLIKSN SRPDQQEGVR
LLSEIFRNSR ERRRECLYYL ALGNYKLGNY AEARRYNELL LELEPANLQA GSLKGLIDDK
VAKEGMVGAA IVGGLVVAAG VVGSMMMRGR KR
//
