ID A0A066X5I1_COLSU Unreviewed; 1314 AA.
AC A0A066X5I1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative CAP-Gly domain-containing protein {ECO:0000313|EMBL:KDN62949.1};
GN ORFNames=CSUB01_06998 {ECO:0000313|EMBL:KDN62949.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN62949.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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}.
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:KDN62949.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JMSE01001282; KDN62949.1; -; Genomic_DNA.
DR STRING; 1173701.A0A066X5I1; -.
DR eggNOG; KOG0971; Eukaryota.
DR eggNOG; KOG4568; Eukaryota.
DR HOGENOM; CLU_002523_1_1_1; -.
DR OMA; LFEMEPV; -.
DR OrthoDB; 9423at2759; -.
DR Proteomes; UP000027238; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; 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, ECO:0000256|SAM:Coils};
KW Dynein {ECO:0000256|ARBA:ARBA00023017};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238}.
FT DOMAIN 24..66
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 76..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1013..1153
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 90..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1314 AA; 146147 MW; 33E5F1AA5BB2D833 CRC64;
MSDLAPGQTV RLSDGRTGIV RFVGGTHFAS GDWVGVELED DSGKNDGSVQ GERYFDCAMG
HGMFVRPTTL VITAQAPAPA AKPARRPSRP SSFNPGSGRT ASDAGLTKRM SLNAPSPSPG
PKASRPPSIL RSPTKSPTKQ LGSTISSTAP SRTTTPSSTR TPVAGAKARP GAAPSRTSMG
PPAIPPSRTT RQPSASSAPT RPTPGRPTSG RLSMAGRTTS ARRPSADLGA GKNTADSGDD
GTMSPNRDGE NSPVRARTKA LEKLTSGSAA TTPANSTKPA TTARSTTTAA AANREIEDLK
AKLKVLERKR LEDREKLKQL DQVQGERDRF QSIIEKLQAK YQPQQSENNE LRKQLKEAEE
RFESIEAMQM EHETALELAT LDREMAEETA EVLKVELEAL KQKSEELELE VEILREENAE
FGQGMSSEER ASTGWLQMER TNERLREALL RLRDLTQQQE EELKDQIKTL EDDLKEFGTV
KEQFDAAKDK LAQSEAAVED LRQQLDNALG AEDMIEELTE RNMSMSEQIE ELKAVIEDLE
NLKEINDELE INHVQNEKEM QEELDFKDSV ITEQARRAGE QEEALEDMEY TLSRFRGLVT
SLQSDLEDMR ASHAVTETES EQLNSKSRAM MDLNMKLQIS ASKAQVKTID LELRRLEAQE
AEQHLEIVKM FLPDTYKEDQ DSVLALLRFR RLAFKAQLLQ SFIKERVNGQ PHSGHEDDIF
AGCDAIDKLT WVASMCERFT NSISHCSIEQ FQRFQNALFE LEPVERALNG WIDGLRRDEL
KEQKCADELQ RTIALMSHLA EVHLTNELPD FAEDTYMQTV IMQSHLESAG STFATLRAMV
QRVIPAESEE DEMALHFSKK SEFVVNQTRS AKVIAGKAVR ALQDLKSRSL ALPQETKESF
EQCQDATRQL AALAREIGFD LHTLLHEEGR TEPYTYREVQ DTISKATTKV TMSSESDLFS
TYLSKLRTLT SQISDLAALS ADLSQTQEFD VSPAPWKLRA QELKATKTIP VDAEEELRRL
KEEHNDARRA IAQRDENLST ANLKIETLES RMKDANAKAS RIEDLEAQIE AAKQKAASLQ
EDIDKQDREL KALETDRDKW KKIAGDSKVF ADGAGAAGAK AGQERAVATA REMDALKSEI
ASLQAAVRYL REDNRRARTT EQHNYDWLAE PLTKPPSVVE QRRALVLAEG KDALSELVKF
TTSARVYDLA ALPEDKLAWK PARSTPQYHA AKQREDLAAW TSWRDAVLKK SEVVLGRKDA
AAAEKRQTMK SVAARLQIRL PDADGKTVPG SGRDVQIVGS REWEGMQGRL AAAI
//
