ID A0A0D7B1W6_9AGAR Unreviewed; 155 AA.
AC A0A0D7B1W6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE RecName: Full=Mitochondrial fission 1 protein {ECO:0000256|ARBA:ARBA00014314, ECO:0000256|PIRNR:PIRNR008835};
GN ORFNames=CYLTODRAFT_359882 {ECO:0000313|EMBL:KIY63511.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY63511.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY63511.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY63511.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- FUNCTION: Has a role in mitochondrial fission.
CC {ECO:0000256|PIRNR:PIRNR008835}.
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; KN880691; KIY63511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7B1W6; -.
DR STRING; 1314674.A0A0D7B1W6; -.
DR OrthoDB; 1355881at2759; -.
DR Proteomes; UP000054007; 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:UP000054007};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 155 AA; 17366 MW; 4965832652699EED CRC64;
MTTDLPYAAD AEVSLSFDEL EVLRIQYAKE VESGHVTVQT KFNYSWGLVK SPVREHQVEG
VKLLQDLYRA EPSRRRECLY YLALGHYKMG NFDEARKFNG LLLEKEPANM QAQSLSTLID
RGVTREGYIG MALVGGVAAI STLLVAGLVR RAARK
//