ID A0A094FCT1_9PEZI Unreviewed; 764 AA.
AC A0A094FCT1;
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=V498_07488 {ECO:0000313|EMBL:KFY86518.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY86518.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY86518.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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:KFY86518.1}.
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DR EMBL; JPKA01002080; KFY86518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094FCT1; -.
DR HOGENOM; CLU_021597_2_0_1; -.
DR Proteomes; UP000029270; 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 CDD; cd16667; RING-H2_RNF126-like; 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 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 527..568
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 240..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 83317 MW; 7798F40D92305199 CRC64;
MTTLPYAADA ESPLKPSELQ VLRAQYEKEG EYVGVQTKFN YAWGLIKSNQ RSEQQTGVRL
LSDIFRDSAE RRRECLYYIA LGNYKLGNYA EARRHNDLLL DREPTNMQAG SLRALIDDKV
AKEGLMGVAI LSGVAVAAAL RRTGLALSLG LTALAAYQGV RDAMADQPQE QRRRLDATGS
REVVYCHQCE NDWYRDESGL LCPRCGGDIT EIISGENDPR PPELPTPLSA DELRGLREHD
PWEHHHDDSD PEEGDIREFV RDNPQGRTTF ISRTFRSPPR EVFSSGSSRQ PPNPDDPAAQ
HIQDFQGIIS GLLGPNVRVT GQPGEHQASP FGPPGPRPGE PSGPPPGAPP GWGNFRPLDD
QHQPRIYGGR VTFQFGGPPR ASNAGEDQGP QGPQEPDLNT YAPPSQRPPA VLIVVMQGRP
NEPPRILRDL LLVLQPPAAN ANAEGGTNGR IPITGLQGLF AGLLNPANAV AGDAVYSQEA
LDRIISTLME QHPTSNAPGP APAEAIAALP KKKIDKEMLG AEGKAECSVC MDDVVLGEEV
VALPCSHWFH ETCVKAWLSE HNTCPICRTG VARDGTAVPA GTTPPTSPPT STPANAGGQN
SPDPFEGVEG LPPYTRRSTF LRRRPSNNET RLESIRQTAG IQSEYDDPGP LHHTVRLNPS
SRRERSASPP SHVPGAFSSG NNRNTIFRRQ ESDTDAGSTG RRDQEREREL ERERSRNHER
GPERRGERAR PGSDHSNNSS NNTIGGAFGS WFRRFSGGGN GRHD
//
