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Database: UniProt
Entry: A0A2T3YZ65_TRIA4
LinkDB: A0A2T3YZ65_TRIA4
Original site: A0A2T3YZ65_TRIA4 
ID   A0A2T3YZ65_TRIA4        Unreviewed;      1046 AA.
AC   A0A2T3YZ65;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   RecName: Full=Rhoptry protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M441DRAFT_82921 {ECO:0000313|EMBL:PTB37843.1};
OS   Trichoderma asperellum (strain ATCC 204424 / CBS 433.97 / NBRC 101777).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB37843.1, ECO:0000313|Proteomes:UP000240493};
RN   [1] {ECO:0000313|EMBL:PTB37843.1, ECO:0000313|Proteomes:UP000240493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB37843.1,
RC   ECO:0000313|Proteomes:UP000240493};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center {ECO:0000256|ARBA:ARBA00004267}.
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DR   EMBL; KZ679267; PTB37843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3YZ65; -.
DR   STRING; 1042311.A0A2T3YZ65; -.
DR   OrthoDB; 76453at2759; -.
DR   Proteomes; UP000240493; Unassembled WGS sequence.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.58.90; -; 1.
DR   InterPro; IPR051756; Centrosomal_MT-associated.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240493}.
FT   DOMAIN          389..455
FT                   /note="PPC89 centrosome localisation"
FT                   /evidence="ECO:0000259|Pfam:PF14197"
FT   DOMAIN          574..637
FT                   /note="PPC89 centrosome localisation"
FT                   /evidence="ECO:0000259|Pfam:PF14197"
FT   DOMAIN          924..1000
FT                   /note="Cep57 centrosome microtubule-binding"
FT                   /evidence="ECO:0000259|Pfam:PF06657"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          109..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..719
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1046 AA;  117590 MW;  5E94112822ABCCDE CRC64;
     MESDAVTRYR SRILREMNAN RENPFNSPPS STGRASPTLS SVFSDPDGES TRLLNQDIAR
     VTAPKKLPIN WEAAHRKWPE FYAQPKKTFT VLDDQTDTKP LNEIPRSKNE RKTAQTIPKY
     IDDTTEDAWN GSKRTRSEMQ PRVDSESDLP QIISHPPVRK LSTYGLTKSA VHNPSPLSKV
     HIQSPPRERT SEQERQASIE KALEILRKAS STPGDLNRRV STHDQSSPIL SSAKSSMTAV
     PPSPPPLLSS PVRDTPNGRS FFMPDISHLD DFVTGTLKFN GTIKDGVPIL VKHGQVHDQK
     EKPFGVRHAE IDGVKIPEDE EKIFISMDMI REEIVSLQEH HDKIQDYAGS LQHEVERLEA
     QLRSSRKGLD GEPNIFGVNE QVLAQKKALE AEVASLQKRL DQATHRISTS DIENDTLAQE
     RDRVISRLQE ACEDINKLTR KLSVKEKELE TSHKQLNSTG QMRQDNDTLR RDVAALKQGR
     STLQRDNASL RAEIDELRRA QQNFLDEAQS LRSNGNDLRH DHQSLVNENR SLRANNKALM
     DENEDLRENL DGIQHELDVA REEIEALRQQ VQLMRQEKMT LREDNDSLVR HNDKYFNENK
     TLRRENSGFE RSIHDLHEKN IRLKEELEGV KKQFDRYRPS GKNDFPTRHD EETEENMTSA
     FFVPDITLKT NDTGPADATE SKDMPDLPEL TTHTDDLMTG SNEMQKRDAT SHSDKVDARH
     RSKSSVKSSP SKNAGTAQKV AFDLPDKATE KPLQGSKSTV ANQGSKRRSA SRLSLDPFGD
     DDTTGMLSVD NITQDLAVSL NLSTTDHKGK EIKQPRGLHT EKSAPKVVHI DSKSQSFKKS
     VMATEAGVRT VRIVDRDVCP ALSTNARRIL DDLCGHNCQN CTVCSRITSH SGVISSADLA
     AGKKRVSIPR PVPVSERGVS GGDHTVRPAH SPGYALALVI KGLEDESQHL QLELTRLQAR
     YNRSDKSMGR QERQDLAEAI RVLLKRVESK SDQIYSLYDV LEGQKAAGQE MTEEEVEMTV
     LNITGMTVRD ATNLSDQMTW EGIVEA
//
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