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Database: UniProt
Entry: A0A2V0PFY7_9CHLO
LinkDB: A0A2V0PFY7_9CHLO
Original site: A0A2V0PFY7_9CHLO 
ID   A0A2V0PFY7_9CHLO        Unreviewed;      1007 AA.
AC   A0A2V0PFY7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase-like {ECO:0000313|EMBL:GBF98706.1};
GN   ORFNames=Rsub_11255 {ECO:0000313|EMBL:GBF98706.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF98706.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF98706.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF98706.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
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:GBF98706.1}.
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DR   EMBL; BDRX01000133; GBF98706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0PFY7; -.
DR   STRING; 307507.A0A2V0PFY7; -.
DR   InParanoid; A0A2V0PFY7; -.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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; 6.
DR   InterPro; IPR029489; OGT/SEC/SPY_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
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; PF13414; TPR_11; 1.
DR   Pfam; PF13432; TPR_16; 3.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 10.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:GBF98706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GBF98706.1}.
FT   REPEAT          224..257
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          265..298
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          336..369
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          370..403
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          404..437
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          498..650
FT                   /note="O-GlcNAc transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13844"
FT   DOMAIN          672..850
FT                   /note="O-GlcNAc transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13844"
FT   REGION          869..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..933
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1007 AA;  104693 MW;  DB3C8C3569F48BA2 CRC64;
     MTIVLEPSNN AGGVRDKVAQ AAPVEHNQPL LPRPGVAQAP SPSSTASAAA LARLLLAGGR
     AADALACVEA ALSAAPRSTE LLHLRGGCLL AAGNVPGAYA SLMAALAGEP SHVPALLDLA
     ALYSARGLLA EARDALEHAA AASPGDARVA EALATVLTDL GTATKCAGRL DQAVELYSAA
     AAAWPALAAA HYNLGVVASE AGRARWPEAL EHYARAVAAN PGYAQAHCNA GVIHREEGRL
     EEAVAAYEKA LAAAPSHEVV RTGLAAALTD LGTATKALGD TARGIALYER ALAVAPRHAD
     AAYNLAVALA EPGPAHAPDR ALFLYHTAAG LRPDCAEAWN NAGVLHRERG ELERAAECYL
     AALNIRPNFP QALNNLGVLY TSQGRAGEAI ALLQAAVTAA PLYAEAWNNL GVAQRDIGDV
     AGSIASYERA AALAPEQPNA AQNRLLALNY ARPGEDPWVC AEHAAWGRGF AARFQRLPPV
     SAGDRALQPR GAVGGAPRRL RVGYVSPDLF THSVSYFAEA PLSHHDAAAV EVYVYDCTPR
     RDAKSARLQQ QAEAAGATWR CVESLGDDAL AAVVRSDAID VLVELTGHTA HNRLGVMARR
     PAPVQVTWIG YPNSTGLAEV DYRLSDATCD ALDTAQTFVE ALVRLPGCFL CYTPPRDAPP
     VAPPPAAGRG FVTFGSFNAL AKVTDEVLAL WARVLAAVPG SRLVLKNQPF ACPQARALWM
     GRLAALGVAA WRVDLLPLAP SNAEHLAQYA LLDVALDPTP YAGTTTTAEA LFMGVPVITL
     HGRCHASNVG ASLLSAVGLA AEGWVAGDAD AYVARAVEAA ADIPRLAALR AGMRQRVLGS
     PLCAARPFVA RLEGVYTRLF QNWLDANGGS GGSGGSKPSA AAAAAGTSAS SSGGGENNAA
     ECDDGGSSGR SSRAHLSRLG SGGSDSPGDD SSDGGALSTP GEVHQESCVR AAQEQRHDQQ
     QQRNHQQQQQ QQEQRQEQER KGWCPEQQQQ EQQEAPHGVK RAAADDE
//
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