ID A0A0A8L622_9SACH Unreviewed; 470 AA.
AC A0A0A8L622;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=KLDO_g2783 {ECO:0000313|EMBL:CDO94520.1};
OS Kluyveromyces dobzhanskii CBS 2104.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO94520.1, ECO:0000313|Proteomes:UP000031516};
RN [1] {ECO:0000313|EMBL:CDO94520.1, ECO:0000313|Proteomes:UP000031516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA Nystedt B., Astrom S.;
RT "The genome of Kluyveromyces dobzhanskii.";
RL Submitted (MAR-2014) 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|RuleBase:RU361209};
CC Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU361209}. Membrane
CC {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}.
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:CDO94520.1}.
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DR EMBL; CCBQ010000038; CDO94520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8L622; -.
DR OrthoDB; 2783940at2759; -.
DR Proteomes; UP000031516; 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:SF14; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS4; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622,
KW ECO:0000256|RuleBase:RU361209};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622, ECO:0000256|RuleBase:RU361209};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU361209};
KW Membrane {ECO:0000256|RuleBase:RU361209};
KW Signal {ECO:0000256|RuleBase:RU361209};
KW Transferase {ECO:0000256|RuleBase:RU361209}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT CHAIN 18..470
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005109744"
SQ SEQUENCE 470 AA; 52917 MW; 8161E1AEE6A82B68 CRC64;
MFRSIIVIAV CIRLVLGKIN PIEVRGKHFY DSVSNAPFFI RGIDYQPGGS SDFTEDKDPL
SDTSVCARDI PLFQNLGINA VRVYSLNPDL NHDKCMTMLA SAGIYLILDV NSPLTNQHLN
RYEPWTTYNP VYLEHVFKVV EQFSSYNNTL GFIAGNEIIN DKRSAERTPP YIKQLVIDIK
GYIKAHSSRV IPVGYSAADD LKYRVSLSKY LECEDQGNHD SSVDFYGVNS YQWCGDQDFQ
SSGYDKLVDA YKDYSKPVFF SEFGCNEVTP RKFGEIPTLY SDKMYHTFSG GLVYEFTQET
NNYGLVSVDE ETSDVYLLED FDALKNQYTK TPHPTVADLR IIQEKVTSRA AKNNPNCYNK
YTNLDITAKV VPKMAAEFIR KGVKCERGKY VDLDKADLVC NSKYFDAKGN PLSKIPKFSI
VNEINSVKLT EPESKNSNSA STLMLSTTNL IIGCSMALGL ILDVVSVICF
//
