(data stored in ACNUC16935 zone)

SWISSPROT: C8VLB2_EMENI

ID   C8VLB2_EMENI            Unreviewed;       524 AA.
AC   C8VLB2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   10-MAY-2017, entry version 42.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   ORFNames=ANIA_11152 {ECO:0000313|EMBL:CBF84598.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF84598.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(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; BN001307; CBF84598.1; -; Genomic_DNA.
DR   ProteinModelPortal; C8VLB2; -.
DR   EnsemblFungi; CADANIAT00007915; CADANIAP00007915; CADANIAG00007915.
DR   InParanoid; C8VLB2; -.
DR   OMA; RVNMADY; -.
DR   OrthoDB; EOG092C1TYR; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0031362; C:anchored component of external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
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; C8VLB2.
DR   SWISS-2DPAGE; C8VLB2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
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:UP000000560};
KW   Signal {ECO:0000256|RuleBase:RU361209};
KW   Transferase {ECO:0000256|RuleBase:RU361209,
KW   ECO:0000313|EMBL:CBF84598.1}.
FT   SIGNAL        1     19       {ECO:0000256|RuleBase:RU361209}.
FT   CHAIN        20    524       1,3-beta-glucanosyltransferase.
FT                                {ECO:0000256|RuleBase:RU361209}.
FT                                /FTId=PRO_5005125835.
FT   DOMAIN      381    469       X8. {ECO:0000259|SMART:SM00768}.
SQ   SEQUENCE   524 AA;  55885 MW;  2CB403B233A24919 CRC64;
     MKFALAAAAA SALFGQVMAD VDPIIIKGSK FFYSSNNTQF YIRGVAYQQD YTTNSTSSSD
     SSYKDPLADE TACKRDIPIL QDLNTNTIRV YAIDPTKNHT TCMNMLADAG IYVIADLSDP
     SESIDRNDPR WETALYTRYT NVIDAMAGFS NTLGFFAGNE VSNTVQTTDA SAFVKAAVRD
     MKAYIKAQNY RSGLGVGYAT NDDKSIRVQL ADYFNCESEE DSIDFWGYNI YSWCGDSTYT
     ESGYKDRTEE FANYSVPVFF AEYGCNEVTP RKFTEIEALF GDKMNGVWSG GIVYMYFQEA
     NDYGLVSVVD STSVSTMADY KYYSSQINAV SPSGTNKASY TPTNTALQSC PAVTSGSWLA
     KATPLPPTPN TDLCSCMDKT NACVVDSSVD SDDYADLFSI VCGLTECAGV SANGTTGSYG
     AYGMCQSKQQ LNWALNKYYS EQGSVASACD FDGSATTTAT TAATGSCSSM MSQAGTDGTG
     TVTATATGSG SSATETESSG ANALNVGVSA GAGGFVVAVL GYLL
//

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