ID A0A1C0VXS0_9CYAN Unreviewed; 1130 AA.
AC A0A1C0VXS0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=BCD67_01125 {ECO:0000313|EMBL:OCR02518.1};
OS Oscillatoriales cyanobacterium USR001.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales.
OX NCBI_TaxID=1880991 {ECO:0000313|EMBL:OCR02518.1, ECO:0000313|Proteomes:UP000093314};
RN [1] {ECO:0000313|EMBL:OCR02518.1, ECO:0000313|Proteomes:UP000093314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USR001 {ECO:0000313|EMBL:OCR02518.1};
RA Te S.H., Tan B., Thompson J., Gin K.;
RT "Draft genomes of Oscillatoriales USR001.";
RL Submitted (JUL-2016) 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:OCR02518.1}.
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DR EMBL; MBRE01000017; OCR02518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C0VXS0; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000093314; Unassembled WGS sequence.
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; 7.
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; IPR013105; TPR_2.
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; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13414; TPR_11; 3.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00671; SEL1; 6.
DR SMART; SM00028; TPR; 15.
DR SUPFAM; SSF48452; TPR-like; 3.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50005; TPR; 13.
DR PROSITE; PS50293; TPR_REGION; 8.
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:UP000093314};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 12..45
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 80..113
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 114..147
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 148..181
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 182..215
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 317..350
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 351..384
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 385..418
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 419..452
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 455..488
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 489..522
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 523..556
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 557..590
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 945..1114
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
FT REGION 228..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 128176 MW; 7DF4E8197DE20CBA CRC64;
MITESLVNLE AAQTYFNKAN WLKSVGQLDP AIDNYKKALE FNSEDAESHQ KMAEVYILKG
QLDAAIASCE LSLKIKPDFA PAYLTMGNAL QSQDRLEMAI QAYSQALAID QYFAEAHANL
GSMYYKLGRL EEAVSSYKKA IVNNPNLASV CLMLGNVLQH QGNLNDAIFY YSRLLELQPK
LLKNYYKLGE AFTKNNDFNA AIDCYQKALK LQPNDAEAAA KLSSLQQLKS PENQQASVTE
KPTQSQFLEI EKEGEGQPPE GVKKDEEYGL QPSSLNLPQF AQDSNLNLPF ESVEETTKEV
SNFNLNPPEQ VANFPEVEEY KKRAEAYLIE GNFKEAIASC HLALKIKPDF TNAYVTLGNT
LQAQGKTDAA IRAYEKALEL QPKYGEVYAN IGSMYFKMGN LEESVIYYQK ALAFRPDLAG
IHWNLGKAFQ KQGKSQEAIA CFQKTAELNP HLVGADFHFN LASTLLNEGK RDEAIVSYER
AIAVKPDWAE AYANIGSVLM QQSKLQEAAE YYQKAIAIKP ELKVLHFNIA NTLLSQGKYE
EAVNNYQEAI KHNPEWPDAI ANLGNAFSMQ GKLEEAIATY QKALVYKPDW AEIYCRMGHI
QKQDRPLEAI AYFEKAIELN PYFSEAHQQL CDLLSHSSNL AGARKVADKY CEYCGESVPV
MSATAYVFSY LQSGVSELAL QKLIEIEKLS YQKCETFSVI DIKLLYEIFI FAVSHLRDDR
EKNANFYKLI AQEYYKKAIP QRHSDRQLKP SNYPVKQRHL RIGFLSKHFR RHSVGWCSEA
LIRELTYITP HVHLYVTGKL QKDEVTTRFE QMAGKFYWPK KYPNGFADGG EILEEVLQDN
LDILVDLDSM TVPTNVEVLY HYPASVCVTW LGFDAPYLSD KHYFLCDQYT HPAGVEKHYI
EQLVRLPGCS VAISGLQSIS ADRNGLRKSL GIGLDQMTYL CVAPGRKTNP EMLRAQVKIL
QEVPDSLLIR KGQGDPDVIH TSYRQECEDQ GVDFNRIKFL GQTKTEEEHR AIYYVADVML
DSYPYNGGTH NLEALWANLP VVTRAGNQYL SRMGYAFLKS VNLDIGVAWN WEEYTQWGIK
FGRDAALRNA VREHLIRSKE PEHLAPLWNP KKLANEMYEV FQNLVAKQIQ
//