ID V2XG85_MONRO Unreviewed; 551 AA.
AC V2XG85;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=Moror_300 {ECO:0000313|EMBL:ESK98183.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK98183.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK98183.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK98183.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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|RuleBase:RU361209};
CC Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU361209}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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:ESK98183.1}.
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DR EMBL; AWSO01000004; ESK98183.1; -; Genomic_DNA.
DR RefSeq; XP_007842485.1; XM_007844294.1.
DR AlphaFoldDB; V2XG85; -.
DR STRING; 1381753.V2XG85; -.
DR KEGG; mrr:Moror_300; -.
DR HOGENOM; CLU_021855_2_2_1; -.
DR OrthoDB; 2783940at2759; -.
DR Proteomes; UP000017559; 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:0042123; F:glucanosyltransferase activity; IEA:UniProt.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0071840; P:cellular component organization or biogenesis; IEA:UniProt.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IEA:UniProt.
DR Gene3D; 1.20.58.1040; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR31468; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR PANTHER; PTHR31468:SF2; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 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 Hydrolase {ECO:0000313|EMBL:ESK98183.1};
KW Lipoprotein {ECO:0000256|RuleBase:RU361209};
KW Membrane {ECO:0000256|RuleBase:RU361209, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|RuleBase:RU361209};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 531..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 390..493
FT /note="X8"
FT /evidence="ECO:0000259|SMART:SM00768"
SQ SEQUENCE 551 AA; 57441 MW; 153FD72A1A33DA8D CRC64;
MIPRFNVATV LVAAASYVFS VNAISKVTRT GRYLYTDDGN RFYIKGIAYQ EQGVVVQDPN
NPFGEPSSFF DPLADANACA RDVPHLSDLG VNTIRVYSVD STKNHDSCMQ ALSDAGIYTI
IDLSLPLNGS IDRVNPSWST NILNQYINTI DAFSKYDNVL GYNVANEAVL SDGTGISPYV
KAAARDIRAY LNSKSSSALV GYAAIDGDPS WRNALANYLA CDPSGSNSDA TAIDIYGLNN
YEWCGDSTFQ NSYAGTTSDY ENYNVVAYFS EFGCVSQPPR LWTEVEALFS SQMSNVWSGG
IAFSYFPASS AAGQFGMVTV SSDGRSVSTS EDFTRLKDMY ANASGPNSPS RGSVTASYPA
CSPPTSAFVA STTLPPTPDE NACNCLQNTL SCKFTPATAN YSGVLGELVG TACGLLSQRS
ISCEDIGGNG TTGTYGRIAG CDPSIKLSYV MSEFYEASNR DGQACSFSGN GTVNPLAPSS
AAAANAAASS CISNPSSTFI PSGPSGSAGG GSSSSGSGNN GAVALVGNKN AIFGMVGVIV
VGALSAVWTL A
//
