ID I1MG10_SOYBN Unreviewed; 829 AA.
AC I1MG10;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Protein ROOT HAIR DEFECTIVE 3 homolog {ECO:0000256|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_03109};
DE AltName: Full=Protein SEY1 homolog {ECO:0000256|HAMAP-Rule:MF_03109};
GN Name=100800151 {ECO:0000313|EnsemblPlants:KRH11750};
GN ORFNames=GLYMA_15G127700 {ECO:0000313|EMBL:KRH11750.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH11750};
RN [1] {ECO:0000313|EMBL:KRH11750.1, ECO:0000313|EnsemblPlants:KRH11750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH11750};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH11750.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH11750}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH11750};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH11750.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH11750.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable GTP-binding protein that may be involved in cell
CC development. {ECO:0000256|HAMAP-Rule:MF_03109}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03109}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03109}.
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DR EMBL; CM000848; KRH11750.1; -; Genomic_DNA.
DR RefSeq; XP_003546242.1; XM_003546194.3.
DR AlphaFoldDB; I1MG10; -.
DR SMR; I1MG10; -.
DR STRING; 3847.I1MG10; -.
DR PaxDb; 3847-GLYMA15G13380-1; -.
DR EnsemblPlants; KRH11750; KRH11750; GLYMA_15G127700.
DR GeneID; 100800151; -.
DR Gramene; KRH11750; KRH11750; GLYMA_15G127700.
DR KEGG; gmx:100800151; -.
DR eggNOG; KOG2203; Eukaryota.
DR InParanoid; I1MG10; -.
DR OrthoDB; 1606at2759; -.
DR Proteomes; UP000008827; Chromosome 15.
DR ExpressionAtlas; I1MG10; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
DR CDD; cd01851; GBP; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.1180.10; Udp N-acetylglucosamine O-acyltransferase, C-terminal domain; 1.
DR HAMAP; MF_03109; Sey1; 1.
DR InterPro; IPR037157; Acetyltransf_C_sf.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008803; RHD3/Sey1.
DR InterPro; IPR046758; Sey1/RHD3-like_3HB.
DR PANTHER; PTHR45923:SF20; PROTEIN ROOT HAIR DEFECTIVE 3 HOMOLOG 2; 1.
DR PANTHER; PTHR45923; PROTEIN SEY1; 1.
DR Pfam; PF05879; RHD3_GTPase; 1.
DR Pfam; PF20428; Sey1_3HB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03109};
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03109};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03109};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03109};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_03109, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03109,
KW ECO:0000256|SAM:Phobius}.
FT TOPO_DOM 1..682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TOPO_DOM 704..706
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT TRANSMEM 707..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 728..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
FT DOMAIN 36..251
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000259|PROSITE:PS51715"
FT REGION 804..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03109"
SQ SEQUENCE 829 AA; 93007 MW; 646E1026089AC3AD CRC64;
MANDDCCATQ LIDGDGEFNV AGLDNFIRTV NLASCGLSYA VVAIMGPQSS GKSTLMNHLF
HTSFREMDAF RGRSQTTKGI WIAKCVGIEP STIAMDLEGT DGRERGEDDT AFEKQSALFA
LAISDIVLIN MWCHDIGREQ AANKPLLKTV FQVMMRLFSP RKTTLLFVIR DKTKTPLENL
EPILREDIQK IWDGVRKPQA HLHTPLSEFF NVEVTALSSY EDKEDKFKEE VAQLRQRFFH
SIAPGGLAGD RRGVVPASAF SISAQQIWKV IRENKDLDLP AHKVMVATVR CEEIANEKLN
RLRSDKGWLE LEEAIELGPV RGFGEKLSSI IDACLSQYDE EAIFFDEAVR NAKRKQLESK
ALDLVYPAYT TLLGHIRSKA LDDFKTKLEQ SLNNGEGFAS SVRTWTQSTM LQFDKASADA
AVRQANWGAS KVRDKLHRDI DSHTSSMRST KLSEITANFE KKLAKALTEP VESLFEAGGK
DTWLSIRELL KRETEIAVSE FSASVAGFEL DEETVERMQQ SLRDYARKVV ENKARDEAGK
ILIRMKDRFS TVFNHDNDSL PRVWTGKEDV RAITRDARSA SLKLLSDMAA IRLDEKPDRI
ESALHSSLID KTSAATSSQY LTREASVDPL ASSTWEEVSP EDVLITPVQC KALWRQFQGE
TEYTVTQAIS AQEAYKRSNN WLPPPWAIMA MVILGFNEFM LLLKNPLYLM FIFVAYLLGK
AIWVQMDIAG EFRHGTLPGL LSISSKFLPT FMNLIKRLAE EAQGNQTPQE SQGSASQTQI
FRNQVHKPDS VSTSISNVSS VGLSVDDNEY STTNLSQRRR TNAPEAEFS
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