ID A0AAD8Q7B8_LOLMU Unreviewed; 1164 AA.
AC A0AAD8Q7B8;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=GTD-binding domain-containing protein {ECO:0000259|PROSITE:PS51775};
GN ORFNames=QYE76_016821 {ECO:0000313|EMBL:KAK1597009.1};
OS Lolium multiflorum (Italian ryegrass) (Lolium perenne subsp. multiflorum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type);
OC Loliodinae; Loliinae; Lolium.
OX NCBI_TaxID=4521 {ECO:0000313|EMBL:KAK1597009.1, ECO:0000313|Proteomes:UP001231189};
RN [1] {ECO:0000313|EMBL:KAK1597009.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=02402/16 {ECO:0000313|EMBL:KAK1597009.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAK1597009.1};
RA Chen Y., Copetti D., Kolliker R., Studer B.;
RT "A chromosome-level genome assembly of Lolium multiflorum.";
RL Submitted (JUL-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the TPX2 family.
CC {ECO:0000256|ARBA:ARBA00005885}.
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:KAK1597009.1}.
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; JAUUTY010000639; KAK1597009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD8Q7B8; -.
DR Proteomes; UP001231189; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0080115; F:myosin XI tail binding; IEA:UniProtKB-ARBA.
DR InterPro; IPR007656; GTD-bd.
DR InterPro; IPR039306; MYOB.
DR InterPro; IPR027329; TPX2_C.
DR PANTHER; PTHR31448:SF33; EXPRESSED PROTEIN; 1.
DR PANTHER; PTHR31448; MYOSIN-BINDING PROTEIN 2; 1.
DR Pfam; PF06886; TPX2; 1.
DR Pfam; PF04576; Zein-binding; 1.
DR PROSITE; PS51775; GTD_BINDING; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP001231189};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 872..963
FT /note="GTD-binding"
FT /evidence="ECO:0000259|PROSITE:PS51775"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 913..972
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1102..1129
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..10
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..213
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..326
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1001
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1056
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 126568 MW; 53CDDBFDB83D13F8 CRC64;
MAASGEGGGD ASAAARRRWD LTSKAPENIP MVKEAVEIST DEESDGIVIC PPDGNARDCE
EVVSGSEHDS SPEGQATSVE PAIDGETEED KLVNQDSLKL IDQENLALPK SPAKPSMSGS
ERSKRTVPQP FTLSTQRRAS GGGNGGVAHP SSDGEKSGKG SSASPASMIK KTPLMAPKKT
SQPSHTFHPQ EDDSCSVTSS TTTSTRAGKT KTTVAFAPSF VCDDRADKRK EFYTKLEEKQ
KALEEEKNQA ETRKKDEQEA ALKQLRKSLV IKAKPMPNFY QEGPPPKAEL KKVAPTRAKS
PKFTRRKSYS DTPPTPESAT ASAASQRSHR HSIGTSKDAN KAQCSPKSGV GAKARAVKPL
ASSAPGPGNG GDLSFVSSPS PDSLLLVKHK EDRSTTAWTN GMKERSNPVN PLTAYSSTHS
SIPKSRSMAP RTRTASSTAC RYQQFSALLS SAVFEWVLML LMLLEGLLSY LATSFARLCK
LPPPCPMCAR LDHVFGDARY RDLMCGSHKA EASSWAFCHV HQNLADVHGM CEGCLLSFAA
DGRSNLETYR SLTGKLGGAG IGDAGCGHGL SWGSGSGGKG MEDGALCSCC SVTVKSRSFP
FAVLQRDDGD VGVGGVLRGV SRDRCVDEVD HAGYSVLKTS DSESELLQRV GESRRSPKDA
AAINNLKEEF TFGHTEIKIA DGNAEEEVPN YSELTQVQDH VTDKIHTEIP KECPNIKANI
QSNNLPRTDG EQITRNSDTR DKPDDDVWHN ALDSTEESPG TTTNSDKSSE TKAATDEPKP
EFSDRTTTRQ DSFIVHHDLK LLLSQVSTSY RTPDPSDVFA ADTPNSQEQQ HEQAVLRNIT
RVLSLQRNYS GVSDGSMLNT EGEAEGGGEC SSTVDALRRQ VELDRRSMAL LWKELEEERS
ASAVATSQAM AMITRLQEEK AAMRTEAAQY RRVMEEQSAY DREDAERLAG EVRDLEAEVK
RCRAELSDQA IACDIRDQMR LFPRPRGGRS VSGLSAGEES SGGFGDEENA YISKQLRNLT
AKLHRFSNDS SRIMTPDLAG DEQEDVNDGG EEEEDRAETS EVGRRVRNAD NFTKWQQLQY
MEVTKVRVGD NGAVVGGESE NMAVLEDEIS ELSGRLQALE ADRSFLEHSV NSLRNGREGE
AVIHDIAHSL RELRRTLGND VFDR
//
