ID Q2HGF5_CHAGB Unreviewed; 428 AA.
AC Q2HGF5;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=CHGG_00699 {ECO:0000313|EMBL:EAQ92464.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ92464.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408029; EAQ92464.1; -; Genomic_DNA.
DR RefSeq; XP_001219920.1; XM_001219919.1.
DR AlphaFoldDB; Q2HGF5; -.
DR GeneID; 4386725; -.
DR VEuPathDB; FungiDB:CHGG_00699; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_1_0_1; -.
DR InParanoid; Q2HGF5; -.
DR OMA; CADFFAC; -.
DR OrthoDB; 2783940at2759; -.
DR Proteomes; UP000001056; 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:UP000001056};
KW Transferase {ECO:0000256|RuleBase:RU361209}.
FT REGION 351..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 46335 MW; 3274AAB8372FBCC7 CRC64;
MENDRCRGPL LTRRAPAFWQ GDTRFYVRGV DYQPGGSSAM QDPLADTDIC LRDIAQFKEL
GINTIRVYTT DNSANHDECM KALADAGIYV VIDANNPLYS INRLDPAPSY NTKYLQSIFA
SVDEFIKYDN TLAFFSGNEV INENVKSTKA ARYVKAVTRD MRAYIKSRGY RAVPVGYSAA
DVSQNRMQLA HYMNCGTEDE RSDFFAFNDY SWCNTNFEQS GWDQKVKNFT DYGIAIFLSE
YGCTTNGRDF GEIAALMSDK MTHVYSGGLM YEYALEANGF GIAKIPSPKA KQIEKKEGFD
KFAKALKQNP APKGDGGFTS TTRAVACPTK DANWLVDSTL LPAIPEGAKK LMSDGAGTGP
GLKGDGSQNA GEGTSTGDAT PGSGTVTATG RPNNSDNAAG MNAPPVEKTP LVIAGLVMAL
SLGGTLLL
//
