(data stored in SCRATCH zone)

SWISSPROT: C5DDB4_LACTC

ID   C5DDB4_LACTC            Unreviewed;       543 AA.
AC   C5DDB4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 47.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   OrderedLocusNames=KLTH0B09812g {ECO:0000313|EMBL:CAR21775.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21775.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21775.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and
CC       transfers the newly generated reducing end (the donor) to the non-
CC       reducing end of another 1,3-beta-glucan molecule (the acceptor)
CC       forming a 1,3-beta linkage, resulting in the elongation of 1,3-
CC       beta-glucan chains in the cell wall.
CC       {ECO:0000256|RuleBase:RU361209}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU361209}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|RuleBase:RU361209}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC       {ECO:0000256|RuleBase:RU361209}.
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DR   EMBL; CU928166; CAR21775.1; -; Genomic_DNA.
DR   RefSeq; XP_002552213.1; XM_002552167.1.
DR   STRING; 381046.XP_002552213.1; -.
DR   EnsemblFungi; CAR21775; CAR21775; KLTH0B09812g.
DR   GeneID; 8291057; -.
DR   KEGG; lth:KLTH0B09812g; -.
DR   HOGENOM; HOG000164982; -.
DR   InParanoid; C5DDB4; -.
DR   KO; K22832; -.
DR   OMA; NRYVTVV; -.
DR   OrthoDB; 728071at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004886; Glucanosyltransferase.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR012946; X8.
DR   PANTHER; PTHR31468; PTHR31468; 1.
DR   Pfam; PF03198; Glyco_hydro_72; 1.
DR   Pfam; PF07983; X8; 1.
DR   SMART; SM00768; X8; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DDB4.
DR   SWISS-2DPAGE; C5DDB4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Glycoprotein {ECO:0000256|RuleBase:RU361209};
KW   GPI-anchor {ECO:0000256|RuleBase:RU361209};
KW   Lipoprotein {ECO:0000256|RuleBase:RU361209};
KW   Membrane {ECO:0000256|RuleBase:RU361209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Signal {ECO:0000256|RuleBase:RU361209};
KW   Transferase {ECO:0000256|RuleBase:RU361209}.
FT   SIGNAL        1     21       {ECO:0000256|RuleBase:RU361209}.
FT   CHAIN        22    543       1,3-beta-glucanosyltransferase.
FT                                {ECO:0000256|RuleBase:RU361209}.
FT                                /FTId=PRO_5005125147.
FT   DOMAIN      381    469       X8. {ECO:0000259|SMART:SM00768}.
SQ   SEQUENCE   543 AA;  58222 MW;  062D2B1A77862382 CRC64;
     MRFATSSLLL SLLSVLQLAL ADGNDTTPAI EVKGNKFFFS NNGSQFYMKG VAYQADTANS
     TAGDEDTIVD PLADYETCSR DLPYLLGVHT NVVRVYALNT SLDHSKCMNA FADAGIYVIA
     DLSEPSESIN RDSPAWTLDL YERYTSVVDA VANYSNVLGF FAGNEVTNNK SNTNASPFVK
     AAIRDTKKYM KDKGYRNIPV GYSSNDDEET RVSMADYFAC GDDDVKADFY GINMYEWCGS
     STFQSSGYED RTKEFSNLSI PAFFSEYGCN ESPPRKFQEV EALYGDDMTD VWSGGIVYMY
     FEEANKYGLV STSGNTVKTL DDYNNLKKEI ASVSPSSVNK NSYTPSTTSL KCPATGTNWN
     ASTELPPTPD KDVCDCLKSS LSCVLADDVE SKDYGDLFSY LCDKIGCDEI TADGSAGNYG
     EYSFCDADIK LSFLLDKYYQ KNGKNKSDCS FSGSASLASS TSQASSCQAK LSSATASAKS
     TGSSNSNSSG SSASSSNSSS SASSSSNSKK SGGIQVKPAS PAGLWLVAIM VASASVGLGS
     IVF
//

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