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Database: UniProt
Entry: B2WCR7_PYRTR
LinkDB: B2WCR7_PYRTR
Original site: B2WCR7_PYRTR 
ID   B2WCR7_PYRTR            Unreviewed;       432 AA.
AC   B2WCR7;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Dynamitin domain containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PTRG_07776 {ECO:0000313|EMBL:EDU50695.1};
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:EDU50695.1, 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; DS231622; EDU50695.1; -; Genomic_DNA.
DR   RefSeq; XP_001938108.1; XM_001938073.1.
DR   AlphaFoldDB; B2WCR7; -.
DR   STRING; 426418.B2WCR7; -.
DR   EnsemblFungi; EDU50695; EDU50695; PTRG_07776.
DR   GeneID; 6346050; -.
DR   eggNOG; KOG3958; Eukaryota.
DR   HOGENOM; CLU_038287_0_0_1; -.
DR   InParanoid; B2WCR7; -.
DR   OMA; TTPHIEA; -.
DR   OrthoDB; 2734083at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005869; C:dynactin complex; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   InterPro; IPR028133; Dynamitin.
DR   InterPro; IPR036543; Guanylate-bd_C_sf.
DR   PANTHER; PTHR15346; DYNACTIN SUBUNIT; 1.
DR   PANTHER; PTHR15346:SF0; DYNACTIN SUBUNIT 2; 1.
DR   Pfam; PF04912; Dynamitin; 1.
DR   SUPFAM; SSF48340; Interferon-induced guanylate-binding protein 1 (GBP1), C-terminal domain; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          282..309
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          369..403
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        30..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  48466 MW;  59DADA85A9BADC6B CRC64;
     MSEATRPKYD NLPGIDTAPD IYETPELAED VSTIQASTAV SESEGESDDS AEDSAVRHQR
     LQPDQARNRF QPARIDARGV DFSDNITAQR QSYRTSTRRQ RRRGDIIGDD SDEEEESFAK
     KLLRIKRELA GLEDEYERRV ESGDKSKIEE QDPKEMMEII ASKVDTMYAT HKGGARGAQA
     ILDRTVQKFD SYKPFEPSPK ISKAIANQPP LPGTQIQKSQ LEFVLNQAAD FDKRITQMEN
     SLGLNGNTMP ELSDHTPFPV SNTLTRLEQT LGLIGDASTN NLDAVTQNVK KLTAEAEHLK
     EVRQEAAQTG SVSGDNKVPT YPDQEAKINA LYGTLPSIDK LSPILPLVLE RLRTLRLVHT
     SAWQADEVLS ELERRQTAQE NEIKNWERQL EIVEKDMKKA ETTMVNNIKT VGDDVKMLEE
     KMAKLLAVSP DE
//
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