ID A0A0C1RD27_9CYAN Unreviewed; 419 AA.
AC A0A0C1RD27;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Glycosyltransferase {ECO:0000313|EMBL:KAF3886073.1, ECO:0000313|EMBL:KIE10150.1};
GN ORFNames=DA73_0216080 {ECO:0000313|EMBL:KIE10150.1}, DA73_0400011775
GN {ECO:0000313|EMBL:KAF3886073.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE10150.1};
RN [1] {ECO:0000313|EMBL:KIE10150.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE10150.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3886073.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3886073.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00004760}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KIE10150.1}.
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DR EMBL; JHEG04000001; KAF3886073.1; -; Genomic_DNA.
DR EMBL; JHEG02000048; KIE10150.1; -; Genomic_DNA.
DR RefSeq; WP_038078399.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1RD27; -.
DR STRING; 1479485.DA73_0216080; -.
DR OrthoDB; 549798at2; -.
DR Proteomes; UP000029738; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008120; F:ceramide glucosyltransferase activity; IEA:UniProt.
DR InterPro; IPR025993; Ceramide_glucosylTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12726; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR12726:SF0; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF13641; Glyco_tranf_2_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KIE10150.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 419 AA; 47513 MW; FCD59FED1C4A2674 CRC64;
MKELAILLSR NLLGWAAVQT FFTLLFISYL RSSRKNLLAD EQLPKVAVVL CLRGADPFLP
NCLQALLNQN YPQYDIKIVV DSQDDPAWNI VTDSIYKQAV GRVQISSLRV PKNNCSLKCS
SLIQAVSDLD DSYKVVAFVD ADAVVHPNWL RELVGPLSHP KIGATTGNRW YLPTGRYWGS
LVRYIWNISA VLQMSLYRIA WGGSLAIKTE LIHQTGLLEK WGQAYGEDTM IRNVLAKHGK
QVKFVPSVLI LNREECDLPR LIGWLKRQLL ASRLYHPWWW AVVADSISTI LVPNLLLIIF
LAAFWTKQWS TAAFCLASFS IYTVTLLLLA IALEKEAQQI LRQYNPVTTE LSPATILKML
IAIPLTQWVS ALAMVVSFGM RRVNWRGVTY RIKGPWDISL VEYRPYKLCD KFGDSKVSI
//
