ID T0LUT3_COLGC Unreviewed; 1102 AA.
AC T0LUT3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Rhoptry protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CGLO_08338 {ECO:0000313|EMBL:EQB52060.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB52060.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB52060.1}.
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DR EMBL; AMYD01001677; EQB52060.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LUT3; -.
DR STRING; 1237896.T0LUT3; -.
DR eggNOG; ENOG502S7ZB; Eukaryota.
DR HOGENOM; CLU_005779_0_0_1; -.
DR OMA; MKSDQIY; -.
DR OrthoDB; 2729811at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR InterPro; IPR024957; Cep57_MT-bd_dom.
DR InterPro; IPR025925; PPC89_CLD.
DR PANTHER; PTHR19336:SF9; SPINDLE POLE BODY PROTEIN PPC89; 1.
DR PANTHER; PTHR19336; UNCHARACTERIZED DUF1167; 1.
DR Pfam; PF14197; Cep57_CLD_2; 2.
DR Pfam; PF06657; Cep57_MT_bd; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT DOMAIN 410..474
FT /note="PPC89 centrosome localisation"
FT /evidence="ECO:0000259|Pfam:PF14197"
FT DOMAIN 593..657
FT /note="PPC89 centrosome localisation"
FT /evidence="ECO:0000259|Pfam:PF14197"
FT DOMAIN 984..1060
FT /note="Cep57 centrosome microtubule-binding"
FT /evidence="ECO:0000259|Pfam:PF06657"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 499..603
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 124455 MW; 2853E5F236AD2A7D CRC64;
METDPVHNRY RSRILREMNA NRENPFNSPP SSTGSHGTVS PTMTSVFSDP DGESTRRLNE
EIARVTNRHN GKIQVDLEAA HRKWPEFYGK PKKADTKTDK ATTKANGSLR RKEDVSHRSI
VQKYLSNLDD DTQDDNTWQG SKRTRAEMQP RVDNESDLSS NISKPPFRFD INADNFRFNP
DQQRHQSPLA KHARTASGNY KAARRASMHA KNERRKSDFL APPTQATPKP APVESVPANN
ATPVTFDTIK NTFPSPATTD SPAQNNVTSR SFFMPDISHL NDFISGNLRF DGAVKNGVPV
FVKNGRVRDR VETLPPRDHA EVDGLAIPED EEKMFVSLDM IRDEICNLQE HDDLVQRHAL
DLEDQVGHLQ NELKRLKGRK ANDSALGSRT ESEPETAANE RYNTERTHIE SQLTALQSRL
DQATTRIGIS EVENNTLSLE RDRALKKLSE ACVNIGELMD KIEMQGKELH ETQEKLNATL
EINHNRETIQ KTSSFKHSND VLQVDNKSLQ ADNQTLRREQ YSLQQELEEV RKDNNILRRD
HESLIEENRS LRNNNRSLRS EIDELRQIAE NSKEDIQAAH EEVEALQVEL QTLDQEKGIL
KEDNDSLVRH NEKYFTENKL LRRENSGFEK SIHDLHDENM RLKEEIELLK QQLDHCRPLG
KTEEFSVRLD KNKEVEDDEE EEEEENMTSA FFMPDITIDS TQNSRVIDMT GEKETPRRAT
PSKRTLEITE TTEQTDRSIN DQDTFQSQQS SVAESRPKAR PSTSRARSSS SQGQKVAFSL
PDRSASTSKT KASNVANKGS KRSSNSRITS KSSLKNGSVP DLDPFQADDE DNMQSPEHTQ
TQSIVLDVKS RKEGSSKSRT VRQETTNTTR NLTSQSQKSV SVKSSAKPSQ NKSTTIDLIT
QGGLDNTTTE IKGNCPGLSS DARRVLDSLS GHSCTNCIVC TRIKAHRGTV TAADIAEGKK
RIKISRPVPP SEQYKQLGMS TEDNTVRPSQ APGHALAKVV KGLEDELEHM KMDRAKKQAR
YDGHNPALSE TKRKQLYADI QVMMTTEEVK KGQIYALYDV LEGQKQVGQD MSDEELDVTV
FSITGLSVRE ITEQITWEGI QG
//
