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Database: UniProt
Entry: W9WG24_9EURO
LinkDB: W9WG24_9EURO
Original site: W9WG24_9EURO 
ID   W9WG24_9EURO            Unreviewed;       553 AA.
AC   W9WG24;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   ORFNames=A1O5_09718 {ECO:0000313|EMBL:EXJ67072.1};
OS   Cladophialophora psammophila CBS 110553.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ67072.1, ECO:0000313|Proteomes:UP000019471};
RN   [1] {ECO:0000313|EMBL:EXJ67072.1, ECO:0000313|Proteomes:UP000019471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ67072.1,
RC   ECO:0000313|Proteomes:UP000019471};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL   Submitted (MAR-2013) 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   -!- 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:EXJ67072.1}.
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DR   EMBL; AMGX01000017; EXJ67072.1; -; Genomic_DNA.
DR   RefSeq; XP_007748487.1; XM_007750297.1.
DR   AlphaFoldDB; W9WG24; -.
DR   STRING; 1182543.W9WG24; -.
DR   GeneID; 19194414; -.
DR   eggNOG; ENOG502QPST; Eukaryota.
DR   HOGENOM; CLU_021855_2_1_1; -.
DR   OrthoDB; 2783940at2759; -.
DR   Proteomes; UP000019471; 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: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   Lipoprotein {ECO:0000256|RuleBase:RU361209};
KW   Membrane {ECO:0000256|RuleBase:RU361209, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019471};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361209};
KW   Transferase {ECO:0000256|RuleBase:RU361209};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT   CHAIN           24..553
FT                   /note="1,3-beta-glucanosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT                   /id="PRO_5005151973"
FT   TRANSMEM        532..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          382..474
FT                   /note="X8"
FT                   /evidence="ECO:0000259|SMART:SM00768"
FT   REGION          483..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  57899 MW;  3EFB5B2E1DFB8B62 CRC64;
     MKGFSAVATA VAGATLFLKA AYANVDPIVI KGSKFFYQTN GTQFYIKGVA YQQDYLGNGT
     TSSGNNNYVD PLADASTCQR DIPYLIQLGT NTIRVYAVDP TQNHDECMSM LANAGIYVIS
     DLSSPSTSIN RDSPTWNDDL YARYTAVIDN MAKYTNTLGF FAGNEVSNNN TNTDASAFVK
     AAVRDMKAYI KQQNYRSIGV GYATNDDADI RVNLANYFDC GNPTDAIDFW GYNIYSWCGD
     SSYTLSGYDQ RTKEFSTYNV PVFFAEYGCN VVQPRTFTEV QALYGPQMSP VWSGGIVYMY
     FQEANDYGLV TVSGGSVSTL ADFNALSTQI AKIDPTGVNA KDYTPTNTAP AACPTVGADW
     QASSSLPPTP NQQLCQCMFD ALTCRPNNVA EAEIGNLFGI VCGLAQGVCN GIAANATTGD
     YGAYGMCNPE QQLGWALNTY YEQQAAQGNG ASACDFSGSA STASPTSPTG SCATLINQAG
     SGGTGTVTSA PSGTGGSGSS SGSSSGSSSG SGGSGSTSNA GMPGVSTPGH MGVLQLVVYL
     TIAFVSGAGM ILL
//
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