ID A0A444XNX0_ARAHY Unreviewed; 866 AA.
AC A0A444XNX0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=Ahy_B09g097161 {ECO:0000313|EMBL:RYQ91265.1};
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:RYQ91265.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ91265.1, 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:RYQ91265.1};
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 -!- 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}.
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:RYQ91265.1}.
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; SDMP01000019; RYQ91265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444XNX0; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000289738; Chromosome b09.
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; PTHR44366; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1.
DR PANTHER; PTHR44366:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1.
DR Pfam; PF13844; Glyco_transf_41; 2.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13414; TPR_11; 3.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00671; SEL1; 4.
DR SMART; SM00028; TPR; 13.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 5.
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:UP000289738};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT REPEAT 102..135
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 136..169
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 170..203
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 204..237
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 238..271
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 272..305
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 306..339
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 340..373
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 408..441
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 442..475
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 476..509
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 523..760
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
FT DOMAIN 773..866
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 97679 MW; BF8843B3647432D9 CRC64;
MISATGDNHR HHYHHHQPQH PGAVDASRPP IAGDRVEPFS VKQEPFSVKQ EAGSLPLLRG
HDSNEVDEDF HLSLAHQMYK AGNYKKALEH SNTVYERNPL RTDNLLLLGA VYYQLHDFDM
CVAKNEEALR IEPHFAECYG NMANAWKEKG NIDLAIRYYL IAIELRPNFA DAWSNLASAY
MRKGRLTEAA QCCRQALAIN PLMVDAHSNL GNLMKAQGLV QEAYSCYLEA LRIQPTFAIA
WSNLAGLFME SGDLNRALQY YKEAVKLKPS FPDAYLNLGN VYKALGMPQE AIACYQQALQ
ARPNYGMAYG NLASIFYEQG QLDMAILHYK QAVACDPRFL EAYNNLGNAL KDVGRVEEAI
QCYNQCLQLQ PNHPQALTNL GNIYMEWNMV SAAAQYYKAT LSVTTGLSAP YNNLAIIYKQ
QGSYADAISC YNEVLRIDPL AADGLVNRGN TYKEIGRVSE AIQDYIRAIA VRPTMAEAHA
NLASAYKDSG HVEAAIKSYR QALILRQDFP EATCNLLHTL QCVCSWEDRD QMFAEVEGII
RRQINMSVLP SVQPFHAIAY PLDPLLALEI SRKYAAHCSL VASRLALPPF NHPAPIPIKR
EGGYERLRIG YVSSDFGNHP LSHLMGSVFG MHNRKNVEVF CYALSPNDGT EWRQRIQSEA
EHFLDVSAMS SDMIAKMINE NKIQVLVNLN GYTKGARNEI FAMQPAPIQV SYMGFPGTTG
ATYIDYVVTD EFVSPLQYAH IYSEKIVHLP HCYFVNDYKQ KNLDVLDPNS PHKRSDYGLP
EDKFIFACFN QLYKMDPEIF TTWCNILKRV PNSALWLLRF PAAGEMRLRQ YAAAQGVQPD
QIIFTDVAMK NEHIRRSSLA DLFLDT
//