ID B2WJ66_PYRTR Unreviewed; 742 AA.
AC B2WJ66;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDU43076.1};
GN ORFNames=PTRG_10025 {ECO:0000313|EMBL:EDU43076.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU43076.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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DR EMBL; DS231626; EDU43076.1; -; Genomic_DNA.
DR RefSeq; XP_001940357.1; XM_001940322.1.
DR AlphaFoldDB; B2WJ66; -.
DR STRING; 426418.B2WJ66; -.
DR EnsemblFungi; EDU43076; EDU43076; PTRG_10025.
DR GeneID; 6348324; -.
DR eggNOG; KOG3565; Eukaryota.
DR HOGENOM; CLU_015390_1_0_1; -.
DR InParanoid; B2WJ66; -.
DR OMA; TPMMEEP; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:EnsemblFungi.
DR CDD; cd20824; C1_SpBZZ1-like; 1.
DR CDD; cd11912; SH3_Bzz1_1; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035459; Bzz1_SH3_1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF12; CDC42-INTERACTING PROTEIN 4, ISOFORM B; 1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..276
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 406..456
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 576..636
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 684..742
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 469..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 322..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 478..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 81761 MW; 6B434518B15E1ED5 CRC64;
MEVDIAPQFG AELKDGFKSV NAWVSGGISW LDDIQQFYRE RSAIEKEYAA KLSALAKKYY
EKKAKKQTSL SVGDTPTVTP GSLECASLTT WGVQLNTLES RATEHDQFAG ALITQLADPL
KVLGTRTEEL RKLHGDYAAK LEKERDHQYS ELRKQKGKYD SVCQEVESRR KKVDGAFDHG
KGKARNAFEQ QQVEMRNVKN TYLISINVTN KQKQMYYHEY VPELLDSLQD LSETRVNKLN
SIWSLAAQIE TQTLMRSTDY LKHLSGEIPR NNPLLDSMMF VRHNAGAWQE PGDFQFEPSP
VWLDDNAIAV DDSATVFLRN VLTKSKAALA EHRRELEKKR KEVETAKTIR QNIREGKDKR
DEVDIVRSTF AIQEAMHEVE RQKVSAEVEV STITAVVGDL SIGARNHNFK SQTFKIPTNC
DLCGDRIWGL SAKGFDCQDC GYTCHSKCEM KVPADCPGEQ SKVEKKKLKE ERQKAAHTVT
AAATTNGTST ASTADLPRLG RSDTVNSMNT LSSGYSATAQ RSVAGGMSPT AEETPPPVEK
KAPAPAPGPR KNRIVAPPPA QYIKPDNDLP PPAPKSNEVK GRMLYAYQEN GEGEITVTDG
MDVTIVEPDD GSGWTKVRAG HKEGLVPAAY VEVVVATPPT TASTFSSNRP DSTYSASSAS
TTNIAAAAPG KKKGPAVAPK RGAKKLKYVE ALYDYTAQSD VEHSMSEGDR FVLINMEAGD
GWADVEKDGV VRSVPANYVQ QV
//
