ID E3Q366_COLGM Unreviewed; 636 AA.
AC E3Q366;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=PX domain-containing protein {ECO:0000313|EMBL:EFQ25045.1};
GN ORFNames=GLRG_00189 {ECO:0000313|EMBL:EFQ25045.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; GG697331; EFQ25045.1; -; Genomic_DNA.
DR RefSeq; XP_008089065.1; XM_008090874.1.
DR AlphaFoldDB; E3Q366; -.
DR STRING; 645133.E3Q366; -.
DR EnsemblFungi; EFQ25045; EFQ25045; GLRG_00189.
DR GeneID; 24405554; -.
DR VEuPathDB; FungiDB:GLRG_00189; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_014456_0_0_1; -.
DR OrthoDB; 5475877at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR044106; PX_Snx41/Atg20.
DR InterPro; IPR015404; Vps5_C.
DR PANTHER; PTHR46979; SORTING NEXIN-41; 1.
DR PANTHER; PTHR46979:SF2; SORTING NEXIN-41; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 114..230
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 70355 MW; 359DCB8FB713BEE5 CRC64;
MWNDEDNNPY AEGFDRRDSL TSSSANPASP TTHLDDSSDS TDADWETLDQ RFDIPQTPST
ASDEAPQNRS HAHEDSDVES SDNEPIARDR GDIVPRPKPG GYESRIEQIL WENPSLTILI
TDAGKSAESG GKYIVYTIRT GNLEVRRRYS EFASLREALT RLHPTLIIPP IPEKHTMADY
AANPTNAKQD QQIIDLRKRM LAVFLNRCRR MDEVRTDGVW WRFLDPNASW SEVLHSHPVS
SIPKSVLKAP PLDTANPTPA HSFLPVPATS AKLKTTGGPG VDPGAISGTG SHVFGRFPPD
SHALSEQELD PYFIAYEASI KELEQLLSGS MEKVNRRTLS HLSALAADLC ELGSKFNAFA
LSEQAPSLGP ALERVGQAAD SSYIATEELS GSLGASFAEP MRENAQFAGV VRSVLKYRVL
KRVQQEQTSD ELSKKIALLD QLERSEAEAK RIEQYLSSSQ QIAPAPKRST SLREANTSHH
QRDGSTEDTA SIDSDFPPTH GEPVPTATQG VPQRSNSTPG HKKAASSNSI TNKIFGPIRH
AIQGVADVDP ERTRRDMIGK TRESIEQLEQ AKVVSEHDVK EASSSILNDL KRFQGENEED
LRRYMLAYAK SQIEWAKKNK ETWEDAKAEV TKIDES
//
