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Database: UniProt
Entry: A0A445EFI2_ARAHY
LinkDB: A0A445EFI2_ARAHY
Original site: A0A445EFI2_ARAHY 
ID   A0A445EFI2_ARAHY        Unreviewed;       799 AA.
AC   A0A445EFI2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   08-OCT-2025, entry version 17.
DE   RecName: Full=GTD-binding domain-containing protein {ECO:0000259|PROSITE:PS51775};
GN   ORFNames=Ahy_A02g008931 {ECO:0000313|EMBL:RYR74276.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR74276.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR74276.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR74276.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:RYR74276.1}.
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DR   EMBL; SDMP01000002; RYR74276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445EFI2; -.
DR   SMR; A0A445EFI2; -.
DR   STRING; 3818.A0A445EFI2; -.
DR   Gramene; arahy.Tifrunner.gnm2.ann2.Ah02g095500.1; arahy.Tifrunner.gnm2.ann2.Ah02g095500.1-CDS; arahy.Tifrunner.gnm2.ann2.Ah02g095500.
DR   OrthoDB; 1047602at2759; -.
DR   Proteomes; UP000289738; Chromosome A02.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0080115; F:myosin XI tail binding; IEA:UniProtKB-ARBA.
DR   InterPro; IPR007656; GTD-bd.
DR   InterPro; IPR039306; MYOB.
DR   PANTHER; PTHR31448; MYOSIN-BINDING PROTEIN 2; 1.
DR   PANTHER; PTHR31448:SF39; MYOSIN-BINDING PROTEIN 4-RELATED; 1.
DR   Pfam; PF04576; Zein-binding; 1.
DR   PROSITE; PS51775; GTD_BINDING; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          489..587
FT                   /note="GTD-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51775"
FT   REGION          172..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          491..589
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        285..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..404
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..473
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   799 AA;  89072 MW;  DF90EA426D72C8DA CRC64;
     MGVHGATLLT SAVCEWFLIF LLFFESALSY FLARFARYCH LQFPCLLCTR LDRFFGKDKQ
     EFYQNLFCTD HRSELASLAS YHAHGKIADG KRMCDDCLLS CTTSTKPNMK SHKLLVGKLG
     MVNGGSSSQS PSLSKDSLNG AKGPSTCTGC DKLCKSEQNA LRSIQLKSPK RTFIKPPYIP
     LPQVPRQSRS NHRDNLKKTK GQSSGSEDKR SHRQPSRVVY NEPKIYSDSE SDFPFSDDDV
     ASVLPGHTSR FKPVVPPRHV LRGLNLPNPN ISSPKAMPSC PDSSEEPKIS KHHDVPEEIN
     LKPENQSSSE LPELISLDDV PSSPNAEKIP RRESDGVKTT SPSQNSLPTS ISELMTLDGI
     AASLNKSEDV TKSSGVELAT EEDRKDTKKI DTRQKASGET DKVVSDSSPL SHTQENSNNM
     SQSPVSTKEN VTASGSDNSE VLANHVQSTE RHVEASDSNE VKPPSSSSSV GSDFEYLDGS
     KVNEIEGESI IDQLKRQIEY DKKCLEALQK ELEEERNASA IATNQTMNMI TRLQEEKAAL
     QMEALQYLRM MEEQAEYDRD ELDKVNDLLT EKEKELQDLE AELEFYRENW PEEPMVQISN
     LKVENVAEQK TATDITNAVT ISGSKLTKVS KIRDEDPVGA TSSPLDFEEE KQCILNRLKS
     LQNRLKELYG NEVSSEKIEG KKLDQQGSSN GEEEIDSSMQ KNVNNMSNGN HTDKDGSASL
     DSDDCSHSNG NNHSRKEVEL DALENEISDL SERLEAIEFN HNLLEHIFNS LRSGDDGKQF
     IQDLAIQLRD IRKIGIRSR
//
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