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Database: UniProt
Entry: A0A0C9MFI0_9FUNG
LinkDB: A0A0C9MFI0_9FUNG
Original site: A0A0C9MFI0_9FUNG 
ID   A0A0C9MFI0_9FUNG        Unreviewed;      1455 AA.
AC   A0A0C9MFI0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Intermediate filament protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MAM1_0109c05521 {ECO:0000313|EMBL:GAN06044.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN06044.1};
RN   [1] {ECO:0000313|EMBL:GAN06044.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN06044.1};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC       {ECO:0000256|ARBA:ARBA00010883}.
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DR   EMBL; DF836398; GAN06044.1; -; Genomic_DNA.
DR   STRING; 91626.A0A0C9MFI0; -.
DR   OrthoDB; 5392990at2759; -.
DR   Proteomes; UP000053815; Unassembled WGS sequence.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR013937; Sorting_nexin_C.
DR   PANTHER; PTHR22775; SORTING NEXIN; 1.
DR   PANTHER; PTHR22775:SF3; SORTING NEXIN-13; 1.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF02194; PXA; 1.
DR   Pfam; PF00615; RGS; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00313; PXA; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS51207; PXA; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT   DOMAIN          28..220
FT                   /note="PXA"
FT                   /evidence="ECO:0000259|PROSITE:PS51207"
FT   DOMAIN          480..618
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   DOMAIN          1033..1151
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          252..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          733..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          907..928
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1246..1281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..327
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..749
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..764
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..835
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1246..1279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1455 AA;  164840 MW;  558FF671E6F0CAB0 CRC64;
     MTHKSIWPQI TKIRQQQNEC REKPIAEDED INNAFNTLLQ NVIRDFIQSW YIKITNSASE
     QSFPSAVDGI IRSAAIKLTQ RLERTDLLSV ILNKIIPRMT SHISEFRAAE VSLLGKSLER
     SVTQSDELDL LLASRFRSGR LHRALTTVAM TTKPTEIAYL RQMIQRVLPY MIDHKELQSG
     PVRVVIREIV SNSVLQPVID MLADPDFWNQ NIDAYLGKAI IEQKMVRQLR EVIRQHSTHN
     DLDADEVMNV FHSADKQERK KKKKSDGKKR IGPQSQLSSA FLGTGISTND WNQQDNLNNH
     RKKGNADEDN EDEDEDEDED EDEQGGSIYD DYSSSRDSFG SSSNRLFKSA YDSNTPSKLI
     KKKQYGIGSI KMGRRTFQDF LKMIQEEKNL LDLKRVRNDI VTQIRKKKAH IVDRDPEEVV
     DGEKVQDIMV YVNRLGVAKK RVDKRIATLS GEQFDFRKST SQLFNYRKQS TSHVNGVGYS
     LSEILTNTSG LSYFMEFMDR RGDMLKLQFW LIVEGFNSTA ISNNDERKTF LQDVKMVYDT
     YFTDTAPHRL HIAEQFNEDL KNAIDLSFEK EQGDEESFAN QIRELNLRLY RIQQHVFWEI
     EKEHYPYFKR SDLYFKFLSS APPIQTNPIP EEVPARRSLD ESTLYTLNTP RSIKGNRPAS
     IHESSSSASI PVILTPTIST PLKESVSYFN TPKQALSDFS GRSRGHQRAL SDSTKSSRFL
     SFSNMFQSKS LWNYDEPRER APKSIKSTEE TEEEDEEDED EEFENGSERA RLVKSDTVDA
     VEAELRSILD GNNLDDLLMT DNKPAQPTAT KSTTTTTTTT TTTTTTTSTP QKSKKPASLP
     ADLPNKSISL VPPLVTKPSS SSSALLLCGS KGMKSTTADP VQNVSALPSW TSSGGTNAIS
     EIEHNSLESV ASTKSPSPSC KSEPLDHDGA IDDRALKAND EKEGSTPANV HFAPPGDLML
     ASKVEQLSAE VEKLTAQEAI VDALIIKAEA QNKLEELRIL KKSKTMFRQD LQQIQYQKSQ
     YELQESENVL MPDRSQANIT SATIGSDKNG EFALYVIEIQ QLGADGNYAS GWIVARRYSE
     FFALHQKLKE RYPAVRHIEF PAKWPLLKLQ KPFVEARRIS LERYLRKLMD DKDICNSQEF
     RSFLSQQNIF VPGPDAEWPF GSLFGSTTIL QTSSSSSSLQ SLMSPSVQNL QKSIAALDDT
     QQKKLSNKGF MQHIYKTVAA GLDDMLVGPS MLDLITQRLG EQVMEFDQNN TSPPASSSSS
     RSKMADSTDM NTAHVTEAST ELPDSLKAEG ITRFTEPLCD LFIEMFELKD KTNWLRRQAV
     VIILQQILEG TIERKLRELL KYLCSSSMIV FYFNKITNSL WPNGGSLTFK EARKPDEKIQ
     TREEANRKLS TWLPDLLGNM VGRQNARKGA RRLFTVLQNK RLNQDLIYTL LDEVIYALFP
     EITDINSSTT TTTIT
//
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