ID A0A0A1NJ96_RHIZD Unreviewed; 152 AA.
AC A0A0A1NJ96;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Mitochondrial fission 1 protein {ECO:0000256|ARBA:ARBA00014314, ECO:0000256|PIRNR:PIRNR008835};
GN ORFNames=BCV71DRAFT_193929 {ECO:0000313|EMBL:ORE21982.1};
OS Rhizopus microsporus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=58291 {ECO:0000313|EMBL:ORE21982.1, ECO:0000313|Proteomes:UP000242381};
RN [1] {ECO:0000313|EMBL:ORE21982.1, ECO:0000313|Proteomes:UP000242381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11559 {ECO:0000313|EMBL:ORE21982.1,
RC ECO:0000313|Proteomes:UP000242381};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
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; KV921272; ORE21982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1NJ96; -.
DR VEuPathDB; FungiDB:BCV72DRAFT_109243; -.
DR OMA; QFNYAWG; -.
DR OrthoDB; 1355881at2759; -.
DR Proteomes; UP000242381; 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:UP000242381};
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..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 152 AA; 17028 MW; 2ADD25274646B799 CRC64;
MKFNPTPSVQ DADIALSPAE LEVLRRQYIK EGEYATIQTK FNYAWGLIRS TKPDHIELGI
KLLTEIYTDA PERRRECLYF LAIGNYKISN YSEARRFNDQ LLKLEPRNEQ AASLKKLIDD
KVSTEGVIGL AIVSGVVAVG AALIAAVVKR SK
//
