ID A0A178AM17_9PLEO Unreviewed; 1222 AA.
AC A0A178AM17;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Intermediate filament protein-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ06DRAFT_225669 {ECO:0000313|EMBL:OAK98686.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK98686.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK98686.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK98686.1,
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 -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; KV441715; OAK98686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AM17; -.
DR STRING; 765868.A0A178AM17; -.
DR InParanoid; A0A178AM17; -.
DR OrthoDB; 5392990at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd06876; PX_MDM1p; 1.
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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 103..292
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 414..553
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 874..992
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 585..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 838..865
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 651..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1222 AA; 136482 MW; 38ED2D99FBA03752 CRC64;
MALKRRDVIL AAVAVFIAWG YLTHWQPKLH YLPYAFVTGF FAALGLVAWL VVTTSWKKDA
RSGGEVNYGP RHVAFVASDK WKAEREALTK RNMYMMEPLY PASYVVSDSI DVLVGLILRD
FVKSWYGNIS KSPTFVNEVD KAVRAAMGEL RDRILAVDMV ETVVSRIIPI ITEHLRASYE
AERIVRGRKL SRNVTDSEEL DVAIAAKYKD GRLHPAASLA YSNTKPIQQQ HLRSIVARLL
PRIMPPSMAT SRAVNILIKE IVACAVLSPV MQMLADPDTW NQLMEGYERK TVRKLRAALD
EHAPASPKTP KNVQFPKLAP GDNERRFERF IRAIRQTNTL ADARRFRSEV SSQLRKDSMV
EGQDPVYLRR LETARQILDT KVTNLSTGGT VRAKVEAQEK PKHKRTASKF ANASLREVLY
DASGLSCFME FMDQAELMRL VQFWIVVDGF RNPLEVDTDE PPDDAGSFPA WTDSDRTDLA
QIHEAYLSKP ELKILPEARK AVSDFLRAGK KATPLQYHNA RRSLLDAQTA AYDQLQEPYF
RRFKKSTLYY KWLAMDEAAN GGNSGVRTTA VARTLDDPAS IAPAMSRTQS GQRLTVQPPH
GDLRRAVASS SDLKSQGIIR TIDPPPRRSL DLGTPTTPRA ALFDDDYDTD PLAQSTASLD
SDHGQDRNNG NNSQVVDAMQ AALTDIMGDE PEGSIFYEGH NSGLHGTDSH RGSVDLPRAL
SPMPTTQQRA LSPNPFTQQS KDKPSIASLG LVGAPNTRGV FNDDLFGDEE KFLEDEIEDP
LPKTKAEDEE IHEAAPGDLG LAEAIDALTA DIERLVTQES IVDSLTTKAE LTNNAAELRI
LRKSKASLQR EIQRKELQRQ QYIVQESDNS LYGRATVFIQ SIMVGTEEDG KEYAMYVIEV
RRRAGDQMPA ATWVISRRYS EFHDLNKKLR GKFAQVRNLE FPRRQMMLKL QKDFLHKRRI
GLEKYLRELL LIPAVCRSRE LRAFLSQAAI NPADALKNQD LNSNDFVSRI YNSVADGMEE
FLGNIPVLDQ LSVAGQNLIS AATTQLASTN GAVSATGTQP GSLASSGMLG SEPNNDAEAE
AELLAFEKQE LPPFVKPISD LFLETFELNR ENNWLRGRAV IVVLHQLLGG TIERKVRESF
DSLLSENSIA NYIDTLKDSM WPNGRLKQGV ERTPQERGKS RKEAATVLNT LVPELTSSVV
GRQNAQIAAR KLEGTLNNAR LK
//
