ID A0A0D2FTU1_9EURO Unreviewed; 448 AA.
AC A0A0D2FTU1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=Z518_06369 {ECO:0000313|EMBL:KIX05497.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX05497.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX05497.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX05497.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC the newly generated reducing end (the donor) to the non-reducing end of
CC another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC cell wall. {ECO:0000256|RuleBase:RU361209}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609,
CC ECO:0000256|RuleBase:RU361209}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU361209}.
CC Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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DR EMBL; KN847478; KIX05497.1; -; Genomic_DNA.
DR RefSeq; XP_013272633.1; XM_013417179.1.
DR AlphaFoldDB; A0A0D2FTU1; -.
DR STRING; 1442369.A0A0D2FTU1; -.
DR GeneID; 25294440; -.
DR VEuPathDB; FungiDB:Z518_06369; -.
DR HOGENOM; CLU_021855_1_0_1; -.
DR OrthoDB; 2783940at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31468; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR PANTHER; PTHR31468:SF5; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS5; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
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:UP000053617};
KW Signal {ECO:0000256|RuleBase:RU361209};
KW Transferase {ECO:0000256|RuleBase:RU361209, ECO:0000313|EMBL:KIX05497.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT CHAIN 19..448
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005112488"
FT REGION 363..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 47196 MW; 946EC1076FEF5216 CRC64;
MRTSTLATLA LGAGAASAAT LKRQSSLTPV TVKGNAFFAG NDRFYIRGVD YQPGGSSDVA
DPIADENGCQ RDISEFTKLG INTIRVYTVD NTADHDACMN ALADAGIYLV LDVNTPLYSL
NRGDPAPSYN DVYLQSVFAT IDAFQGYSNT LAFFSGNEVI NNPETSAAAP YVKAVTRDIR
QYIRNRGYRE IPVGYSAADV SENRLEMAEY MNCGTDDERS DFFAFNDYSW CDPSSFTQSG
WDQKVQNFTG YGLPLFLSEY GCNTNTRDFG EVEALYSTEM TGVYSGGLVY EYSQEPSNYG
LVEINGDSVT ELPDFDALMS QFANTPNPEG DGGYNSTGGA SGCPAYSEPN WLVKDDSLPA
IPDGAKKYMT DGAGEGPGLS GPGSQNAGGA STGTASAGSG APSQTGGSGS SSSSTSNAAV
STVPEWSLAP LVCGAVIVMS TFLGAALL
//
