ID F7VXD4_SORMK Unreviewed; 1088 AA.
AC F7VXD4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=WGS project CABT00000000 data, contig 2.11 {ECO:0000313|EMBL:CCC10176.1};
GN ORFNames=SMAC_02753 {ECO:0000313|EMBL:CCC10176.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC10176.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC10176.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC10176.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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:CCC10176.1}.
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DR EMBL; CABT02000011; CCC10176.1; -; Genomic_DNA.
DR RefSeq; XP_003352320.1; XM_003352272.1.
DR AlphaFoldDB; F7VXD4; -.
DR STRING; 771870.F7VXD4; -.
DR GeneID; 10809943; -.
DR KEGG; smp:SMAC_02753; -.
DR VEuPathDB; FungiDB:SMAC_02753; -.
DR eggNOG; ENOG502RM76; Eukaryota.
DR HOGENOM; CLU_007315_0_0_1; -.
DR InParanoid; F7VXD4; -.
DR OMA; INGWIIH; -.
DR OrthoDB; 2727031at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR003114; Phox_assoc.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR013937; Sorting_nexin_C.
DR PANTHER; PTHR22775:SF47; MEIOTICALLY UP-REGULATED GENE 122 PROTEIN; 1.
DR PANTHER; PTHR22775; SORTING NEXIN; 1.
DR Pfam; PF08628; Nexin_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02194; PXA; 1.
DR SMART; SM00313; PXA; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS51207; PXA; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000001881}.
FT DOMAIN 174..356
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 409..449
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 118411 MW; 9F77ADFBFD5ADAC4 CRC64;
MTDKDAPTPG AIPDDVMSSP TTKDPVAADP VPQAKEDHDY FNDEAKGGGG FSSAASDITS
TTTNKEEDLA TQAFRFLATA TPGTLGGVAV GLGAVTYFVL GPLGLVLIGA FGGVVGYIQW
EQRNAEVARA LKGEKGVDLI ARLLETKTKA EVTQSEQDVD KQEAALALRL EDFQPETREA
INELIDAVIS GYVKWWYSPL VPSDKFFPLA CKRTLTSFIL AISNHLKRKR PADAFLDFLT
NSSSIVIVFL SELTNAFAEF PADVKVSAAD ALYTYLAANP DSNLAQLLNK RQQAGKFRMV
AEDLLAFLDK PTYECDPARV FLREILAGVV LEMTLQNCCK PEWINSWIVY LLEAGEPDFS
QAIDEGMQTG PAAADATFAD FDGNVGNIGL TRGNRNSFET EKVRRKESIA SHKKKLSKAD
EEVELMEDMK KLNEMIAEQE SKRDKEAKDI MAKSGSVPLQ QTVVAEEPDQ FADAFKRSSE
EHPHAVQPIA ARTEPESKGS TSSNGSSGTS NTIKTPPTPL SGKSSPTPEQ APSRPDGPSR
FTSFDQIVPP ARAETPVDEQ RPKPPPLTLH NANITILDEP GDRNLGSKPG WDYLVQIEPA
TSIYPGWMIV RKYPDFERLH EVLRRIAAIS GATEFNTKHK ALPQWKGATR TSLREELERY
VKDACSYKPL AESEGMKKFL ERDTANMPVR PKSGFEAFEK IGKGVFDVMT SAPLEGSKAL
VDGFTGVLGT IGLGHKKNAA SSASGNSTSG APQSALTDVT AASRLSMSTI PRPDSSASLN
RIRESIDSQR SSIISTQPSK VDPMDRRTST DYRTEVESAR YGRTSARDSR DQSRASSRAP
PSLRSPSSLS LTLESLRLPP PPDMMPDNYQ NSPVSPAPSS RIHDYPPHHA RSLTMPTLSA
SHSRSQSRSP GPGAAPLQGF KSYPKLSEEE TRVAVELLFA VINELYTLSS AWNFRRTLLA
AAKSFLLRPG NPSLSSIQSL IQSSVLDANT SDDGLAAHLR KLRENALPTE EERANWPGEM
SDEEKEKLRV KARKLLIESG VPAALSGVMG QSATGEALGR LFDCLQIEEV ARGLMFGVLL
QAVRTVTH
//