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Database: UniProt
Entry: V5ERU3_KALBG
LinkDB: V5ERU3_KALBG
Original site: V5ERU3_KALBG 
ID   V5ERU3_KALBG            Unreviewed;      1488 AA.
AC   V5ERU3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EST05648.1};
GN   ORFNames=PSEUBRA_SCAF5g02512 {ECO:0000313|EMBL:EST05648.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST05648.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
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DR   EMBL; KI545891; EST05648.1; -; Genomic_DNA.
DR   RefSeq; XP_016290637.1; XM_016438797.1.
DR   STRING; 1365824.V5ERU3; -.
DR   GeneID; 27421493; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_000537_6_0_1; -.
DR   OMA; MPWTKTS; -.
DR   OrthoDB; 76239at2759; -.
DR   Proteomes; UP000019377; Unassembled WGS sequence.
DR   GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR010610; EryCIII-like_C.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48050:SF26; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF06722; EryCIII-like_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          836..969
FT                   /note="Glycosyltransferase family 28 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03033"
FT   DOMAIN          1163..1270
FT                   /note="Erythromycin biosynthesis protein CIII-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06722"
FT   REGION          1..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1118..1169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1294..1360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1413..1458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..231
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1137..1155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1304..1345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1431..1458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1488 AA;  164877 MW;  67452CBCC6CF4F53 CRC64;
     MGLRPLFGTR ASVTNVRDSF GATAERAKTA EDEQANPLDN LDHDADDAPT SSEEPVSSQP
     QQSQSHQQQG GQGLAKFLNG AALMSNKDAQ SKAQDRHHQD KVVAPDSPDP SQQAHGPDAA
     DDTAAWKRTG NEAETSDQHE SNRARTKFGR TLKKVDAKIR STIGVNAPPT AEQMRSPYSI
     GNNDHLHSQD NLGAAELLND ARLETLQHLS DDEEEEDDNA EEGDIESTGH DSDDDDDART
     ISNDDKPDRA SMDKHLKKLE RADEDAERRR RSGSMDGARP GDSVRTHAPV EISSEDKMKA
     IIDEFGECAS LSNPNEPERL IVDHSGVLIK TVFIKGSLFL TNRRVCFLAY IPNAANSNGT
     EHHQAGLRSG KDSSEIRAPS DPNVENPILK SGPAIIHRPG KMRPKRRVWI ELRKDAFNAY
     SASNQLYKPL LSARLSNLYA ILPVDWAQPN VIRFVEGLKY SSVEFKTQEA ALDWRKELEA
     AAFHARNTAE KVRISIPLER VVGMDTANFL SVAKIVHFDV LVGAVNDAEA QKILKEQRER
     ADRQQLDHSW SSGHVFINCP KHPEIKCHVT QVALGFTHNR AAFVDLLQEA LKGPKAAQKQ
     TGFEEMLRAL PAPLLDLEGE KDVEDTSTDS NYSSDDQKQS LADRFCHAFG LPHQPEELRL
     VKAQLVRTLH THGTMAIGLD HLLFWRRAVG RDLKIRVPLN DVQGVDTYRS MLWHHYGLVV
     HIRAHADMHF DFMSQENRDM VLSTLKRIIQ AIDQRKQKAE RGSLDAASDD SSITKVEAAS
     HPADAKKSAN ESILLDTARD VPVFEPDVLA HLPKVVNMDR NVIRDVLRIP PMRIYCLTIG
     SRGDVQPYIA LCKALKEHGH TPVIVSHPEY RGWVEGHGIE YRGVGGDPAA LMKLSVEHRI
     FSPAFFKESI GKFRVWLDEL LRECWEECQG ADLLIESPST MAGIHVAEGL GIPYFRAFTM
     PWTKTSAYPQ AFSVPAMDMG SSYNSSSYTL FDQIMWVATS GQINRWRKHM VGIGATDMSK
     MDADSVPFIY NFSPAVVPMP NDWGDRVKIS GYWFLDNPDS NWSPPQEMSD FLERAKKDGK
     KIAYIGFGSI TIENAEEVSA NIMKAVREAD VRAIVAKGWS GRGGSKPKKK KQPKRSNSCR
     PAMQHKTSAV SSHTESEDTG TEEEHEPEIE IPDDVFVVDS VPHDWLFPQI DIAMHHGGAG
     TTGASLRAGL VTLIKPFFGD QFFWANRVQK LGAGAKVNGL SVHDLSDALK SAASDRVMVE
     KAQGVGEKIR SEDGVATAIE FLYKNIPLAN RRTQRKIERE ASQSHDAGTP SAGIGNALSF
     FSHSRTHSGS SSKDTPQRRS ATMPPTKPSS PSPLSPMGEK RSMTIFESPE TEEPKSPSLA
     SKLLPTLPSI NPLPSNMAAT LKEMVTFQNS TADTTADGED ASTPGRFKSF PPRVEGEEES
     DEQKMARLKG YKNAKAEDIR RRKLLEERLA REKIEREAKQ GEGEKAKQ
//
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