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Database: UniProt
Entry: V7BEW6_PHAVU
LinkDB: V7BEW6_PHAVU
Original site: V7BEW6_PHAVU 
ID   V7BEW6_PHAVU            Unreviewed;       929 AA.
AC   V7BEW6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY {ECO:0000256|ARBA:ARBA00019143};
DE            EC=2.4.1.255 {ECO:0000256|ARBA:ARBA00011970};
GN   ORFNames=PHAVU_007G153100g {ECO:0000313|EMBL:ESW16394.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW16394.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|EMBL:ESW16394.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC       transferase subfamily. {ECO:0000256|ARBA:ARBA00005386}.
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DR   EMBL; CM002294; ESW16394.1; -; Genomic_DNA.
DR   EMBL; CM002294; ESW16395.1; -; Genomic_DNA.
DR   RefSeq; XP_007144400.1; XM_007144338.1.
DR   RefSeq; XP_007144401.1; XM_007144339.1.
DR   AlphaFoldDB; V7BEW6; -.
DR   STRING; 3885.V7BEW6; -.
DR   EnsemblPlants; ESW16394; ESW16394; PHAVU_007G153100g.
DR   EnsemblPlants; ESW16395; ESW16395; PHAVU_007G153100g.
DR   GeneID; 18625980; -.
DR   Gramene; ESW16394; ESW16394; PHAVU_007G153100g.
DR   Gramene; ESW16395; ESW16395; PHAVU_007G153100g.
DR   KEGG; pvu:PHAVU_007G153100g; -.
DR   eggNOG; KOG4626; Eukaryota.
DR   OMA; MMQFDLA; -.
DR   OrthoDB; 6694at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000226; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0097363; F:protein O-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.11380; -; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR   InterPro; IPR029489; OGT/SEC/SPY_C.
DR   InterPro; IPR006597; Sel1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44835:SF1; PROTEIN O-GLCNAC TRANSFERASE; 1.
DR   PANTHER; PTHR44835; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE SPINDLY-RELATED; 1.
DR   Pfam; PF13844; Glyco_transf_41; 2.
DR   Pfam; PF00515; TPR_1; 4.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   SMART; SM00671; SEL1; 5.
DR   SMART; SM00028; TPR; 10.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50005; TPR; 9.
DR   PROSITE; PS50293; TPR_REGION; 3.
PE   3: Inferred from homology;
KW   Gibberellin signaling pathway {ECO:0000256|ARBA:ARBA00022941};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REPEAT          81..114
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          115..148
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          156..189
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          190..223
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          224..257
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          299..332
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          333..366
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          367..400
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          401..434
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          480..637
FT                   /note="O-GlcNAc transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13844"
FT   DOMAIN          654..834
FT                   /note="O-GlcNAc transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13844"
FT   REGION          866..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   929 AA;  103466 MW;  28AA1F14802DB447 CRC64;
     MAWVEDKDGD NGRENKLVGE NGFLKVTERS SDGSVGDVGS VSKRCEGKGD VSYANILRSR
     NKFEDALALY ERVLVDDGGN VEALIGKGIC LQMQNVGRLA FESFNEAIRL DPQNACALTH
     CGILYKDEGR LMEAAESYQK ALQVDPSYKA AAECLAIVLT DIGTNIKLAG NTQEGIQKYF
     EALKIDPHYA PAYYNLGVVY SEMMQYDMAL NFYEKAALER PMYAEAYCNM GVIYKNRGDL
     EAAITCYERC LAVSPNFEIA KNNMAIALTD LGTKVKLEGD INRGVAFYKK ALYYNWHYAD
     AMYNLGVAYG EMLKFDMAIV FYELAFHFNP HCAEACNNLG VIYKDRDNLD KAVECYQLAL
     GIKPNFSQSL NNLGVVYTVQ GKMDAAASMI EKAIIANPTY AEAYNNLGVL YRDAGDISLA
     INAYEQCLKI DPDSRNAGQN RLLAMNYIDE GNDDKLFEAH RDWGRRFMRL YSQFTSWDNS
     KDPERPLVIG YVSPDYFTHS VSYFIEAPLV YHDYTNYKVI VYSAVVKADA KTSRFREKVV
     KKGGLWRDIY GTEEKKVADM VREDQVDILV ELTGHTANNK LGMMACRPAP VQVTWIGYPN
     TTGLPTIDYR ITDSQADPPE TKQKHVEELV RLPDCFLCYT PSPEAGPICP TPALSNGFVT
     FGSFNNLAKI TPKVLRVWAR ILCAIPNSRL VVKCKPFCCD SVRQRFLSRL ENLGLEALRV
     DLLPLILLNH DHMQAYSLMD ISLDTFPYAG TTTTCESLYM GVPCVTMAGS VHAHNVGVSL
     LSKVGLGHLI AKNEDEYEKL ALKLASDVSA LQKLRMSLRE LMSKSPLCDG AKFIRGLEST
     YRQMWRRYCK GDVPALKCME LLQQHVSTSD PTNNNGESTR NVNLSEGSPG SVMANGFSLT
     QPLKPNVHSC EENGGSLNHN SKQGMVGSS
//
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