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Database: UniProt
Entry: E3SAR6_PYRTT
LinkDB: E3SAR6_PYRTT
Original site: E3SAR6_PYRTT 
ID   E3SAR6_PYRTT            Unreviewed;      1173 AA.
AC   E3SAR6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=CAP-Gly domain-containing protein {ECO:0000259|PROSITE:PS50245};
GN   ORFNames=PTT_20289 {ECO:0000313|EMBL:EFQ84944.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ84944.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ84944.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00011010}.
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DR   EMBL; GL538167; EFQ84944.1; -; Genomic_DNA.
DR   RefSeq; XP_003306971.1; XM_003306923.1.
DR   AlphaFoldDB; E3SAR6; -.
DR   STRING; 861557.E3SAR6; -.
DR   EnsemblFungi; EFQ84944; EFQ84944; PTT_20289.
DR   KEGG; pte:PTT_20289; -.
DR   eggNOG; KOG0971; Eukaryota.
DR   HOGENOM; CLU_002523_1_1_1; -.
DR   OrthoDB; 9423at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR022157; Dynactin.
DR   PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR   PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12455; Dynactin; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Dynein {ECO:0000256|ARBA:ARBA00023017};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT   DOMAIN          24..66
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          74..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          983..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..105
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1009
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1173 AA;  131894 MW;  00486D3833615C16 CRC64;
     MTTIRVGQTV ETTSEQYGVV RYVGPIHVSE GTFVGIELPT PTGKNDGSVR GERYFNCPPG
     HGLFIRDSSI TRIISQPAPP STPQRAATPK AKPPATAPRP RPASVIAPKP RSATLTTKRQ
     SVVASPSQPP PRQPVRKASV ASISSNPATE FARPAPPPSR PSLASSQTSN AAKTSRDNNN
     IETLQTKIRH LEKQHSEDQD RLRELTQVRD ERDRFNGIIQ KLQAKCQNQY SEAQELREKV
     KILQQGHEAL EKTQQDQEVD LEDALVDKEM AEERADQAEA ELESLRKRVE EQSLELDILR
     DEAELFTTEM SEEQKQEAGY YRLQHENDRL RHALITLKEM TEEREQDQKA RILSLEADLQ
     QLEHYESENA TLHERLTESE SLVEHLKQQL DAANEYEDMV GELTHQNQNL QDRLAEQEMV
     VQDLENLREL NDELEVQHLE QEEDMLAELD AKNNELAEQA KLIADQTAII TDNESLISKF
     RDLVMDLQTR MADAESSKNM TEAQVKDTTG RFNEVMDLNR QLRAATVLST TREIEAALIS
     LKADQLAEKL EIWNETESKE FTRSESLQAY LTAERIAGKS DLLINVLRST NRQMSNGGRL
     DDAISRLICV KSISYLEVLK EGNNRLWSAI RGLSLTDFAN IGPTYQELLS VEQVLDQGLS
     ALKADTVNFE EFAGSLHRST KTHDAILSSH QDALAARPEG ELLSRMTSIH ARLDYIAYMY
     DLATFALQKV PTSILEECQY TLEHFKTPLE TTQSALAAST KLLRTIQALA EDNMYPRFPD
     GMDDAIQFDE GLSVAAEGIA NFTRALIEEV SKCSSLSDPE AVSASEIASI KANIDDLDTK
     QRTIFLTAGL NGLTFSLRHW TDHASVLSNN VEIEHGPTPW AQKAKEVESA RKKDDEAVRQ
     LQVLTAEHRA TVLKIHEREQ VIATKELEIE HLLAKIRDAA TKTEGVEALQ EELTKRHDKI
     MELQAANRAQ VLEMEALRER LANADEHGRN DSDLPADNTT ATAEQPQQAV DPRTVPGGLK
     TFIDALQNEN HWLRSRENKD SFDRNLRDMF NKMEYVRYEA AHHESMARLE LLELAWLSDD
     TDSLEGGVDT PPRLSSPIAQ DPSDLTYHIP PHMQASSGAG RLPKMSAVQL SGISLGWEER
     AMSRRVALEQ AEEEFLYLAT ITEEDDEALY GYL
//
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