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Database: UniProt
Entry: A0A1C0VXS0_9CYAN
LinkDB: A0A1C0VXS0_9CYAN
Original site: A0A1C0VXS0_9CYAN 
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
//
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