ID M7WMM9_RHOT1 Unreviewed; 2018 AA.
AC M7WMM9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Polypeptide N-acetylglucosaminyltransferase, glycosyltransferase family 41 protein {ECO:0000313|EMBL:EMS19301.1};
GN ORFNames=RHTO_04493 {ECO:0000313|EMBL:EMS19301.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS19301.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS19301.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS19301.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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DR EMBL; KB722670; EMS19301.1; -; Genomic_DNA.
DR RefSeq; XP_016270420.1; XM_016418159.1.
DR GeneID; 27368506; -.
DR eggNOG; KOG4626; Eukaryota.
DR HOGENOM; CLU_001721_0_1_1; -.
DR OrthoDB; 34780at2759; -.
DR Proteomes; UP000016926; 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; 3.
DR InterPro; IPR029489; OGT/SEC/SPY_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44998; -; 1.
DR PANTHER; PTHR44998:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1.
DR Pfam; PF13844; Glyco_transf_41; 2.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:EMS19301.1};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:EMS19301.1}.
FT REPEAT 799..832
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 1211..1244
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 1245..1278
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1468..1654
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
FT DOMAIN 1750..1909
FT /note="O-GlcNAc transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13844"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2018 AA; 217371 MW; FEC8F5387785ABAB CRC64;
MTGPPPPRPS GTPTGSTSLP SGTNAPPPSA VPSAQLPLPT SSDLGTVGSP AKKRKSSVSG
AMPILAPSEP VARDAGDRTD EGESEELSRR APRTQANGTT SSSSSTIPPA QLPTAEPKNA
ALSTRLSPPP LAPLSLPTFP VLPPSIPSPS QTFQTPSQVS SILSLPPNLL LQLARTDSPL
EQQAIAEKKG VKGYLSSMAI PPPSPTTLVT TLVKEGGGGG LIGLPVVNEA SEKEELAAVP
TGSAGGLPAR TSTPSPLPAY SLPPDLSLTS SSATTSSALV TTSTSPSPSS PTGAGHPAIP
VLLGQIFAPP PLTPGVLAPI PGTSGIGEIL RGHGPASVRE FASVEDWSYR TAKDQVFSSL
STSASTAAAA RPALATSPSF TEREISSLAS QIKDWALSEQ EKLISHQVVE SKSAAVVLAA
AHATSSVAEK EQGGEDLSAY AEVYKKQLDA LASGYFAQLH RDALKRLTEE KVGSQGVGSR
RGSETDQAVE APLPSTSGGG PDSSLSSVPV LSSSQAPTLT SLTSLTSSRS QAEAMHVRAS
AAAAVAAQVM AATSLARQAG EKLADLGVDP RKVVEEVEEL VGSREGRRGS AGMEELGKIL
ERAGSRRGSR QEERDEKGKG KEEVVVVPAR RASEAGRSDA MSIEEVGQQP AAAATSGDAV
ASTSSSAQVA DARPASAADL ASLPTAQRPS RTSPSSSRSA SVAQAAPPAP VFVAPQQPAD
LAALASPAKR DYLLAYAHQL YSTNPASEEL LPLLHTLENV HPDHLPTLLL ISCVYYTRGE
LESSLYYNKR LLEHDPSYVE AMSNIGTTLR AMGKWNEAEA WWWKAIKLRP TYWDATENLL
GVLCNPATAA SPEALAAAGV APPPIEPRYQ EALALCDYVE SQIFAHAASL AHPAVPPTAA
YFDPVPYLPR PRTLPSVIPQ NHVHRLQNLL YAKGNLRLTT QDPALAQDEY EKAIELALSL
PEWARRLPSL LWPVEGCTTR DLVVAATVVG KILAAFAEAG SNPASAQKVS QMAQQLGVAD
ERGSVPFERL LRTIKDGGDA YVQRLLAMGG GVVPTVLLEP QMLVQLPTML FSEMRGTLPS
MLDPAIVSGE AHEARDPTRQ QTVQSTNQTT STMLLTLAKG LQDSLGPTSA SRSTIGGIPA
SQSLLLPLYY VALALYPSPS TCNNLGILLS TLNATTIVAG ADPSKPPVVV TGQMLALRYY
EAGLKLDPKH PHLYTNYGSL LKDLGKLPEA VAMYKRAVEF NPNFDVALAN LANAVKDTGQ
IQESIPYYRR AVELNPSFPE AICGLVNALG GVCDWQNRGG VDEEWIVDDK LQLHHVKKPT
NGRRIQEGYH GAIADLVRKQ LHDGYSYGVG SLAACGTIQQ WLSVISQALY GVEPAQVGDL
MKPWAARLTS LSGKHDRAAS LVNEGGYLIR LVERLMRRIQ RRWYLATFGP QVYANPAAPA
PQPIFPKTSD IAHYRRPMLP PSLPAIPVPT VLPFHCFTLP VTARETRLIS HRTGLRISHA
TLNQPWMPPI VYPPPRPPVD GKINVGYVSS DLGNHPLSHL MQSVFGLHDL SRFNVFVYAT
SPSDKSPYRQ KIEAESQHFL DVSHLGTQQI VERIVHDQIH ILINLSGYTK GARNEVFAAR
PSPVQMSYMG FASTLSAGWC DYFIVDPIVC PPHLISGNQW RYNNGYTLGR LPNAQPSPRS
TDFEGDIDPE SDSNRFVYTE KLIYLPHSYF VTDHKQAWRE EETAAPVTTS LARSEETTWA
LEEAKRLQMR RQMFPNLRDD TVIFANWNQL YKIDPFIFRI WLEILKKHPN SVLWLLRFPA
PGEAHLKETA LRWAGKEVAD RVIFTDVANK NDHIHRGRIA DLFLDTTECN AHTTAADILW
SGTPILTFPR HAHKMCSRVA ASIAMATGFG PQMIVNNEHE YERRALELAA GLVYDTIPAD
PSKPPTTLEG REQRRSKGEL AELRKKLFLT REQSPLFDTK RWVRNLEKGL VEAWTRWVQG
TEFEDAPEWT AGPGRASAAI FIPDDVDGAN LESRKPYF
//
