ID G8BZD3_TETPH Unreviewed; 1885 AA.
AC G8BZD3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase {ECO:0000256|ARBA:ARBA00031935};
GN Name=TPHA0K01270 {ECO:0000313|EMBL:CCE65261.1};
GN OrderedLocusNames=TPHA_0K01270 {ECO:0000313|EMBL:CCE65261.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65261.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE65261.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000192};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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DR EMBL; HE612866; CCE65261.1; -; Genomic_DNA.
DR RefSeq; XP_003687695.1; XM_003687647.1.
DR STRING; 1071381.G8BZD3; -.
DR GeneID; 11533424; -.
DR KEGG; tpf:TPHA_0K01270; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR OMA; AWTDFFI; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000005666; Chromosome 11.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF29; 1,3-BETA-GLUCAN SYNTHASE COMPONENT FKS1-RELATED; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 504..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 539..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 573..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 684..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1367..1388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1454..1475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1481..1498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1569..1588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1608..1641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1653..1673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1809..1830
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 308..420
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1885 AA; 216177 MW; D8F50173D8E225C5 CRC64;
MSGTGGDPNH YQGQSYDDYG QPIYGSDPNQ QQAQQGYGQQ TVADGYYDQN MQADQFMNGQ
VPQGDEYYQN DPHMNGYYDQ PNYGNANGNV DGENFSDFSS YGPPGTPGYD DYGNNMGQYT
PSQVSYGDPN ATGTSTPIYG EGYDPNYVAM TLPNDPYPAW TADSQSPVTI EQIEDVFIDL
TNRFGFQRDS MRNMFDHFMT LLDSRASRMS PDQALLSLHA DYIGGENANY KKWYFAAQLD
LDDEVGFRNM NVAKISKKKR LFKRKKKEQL EEANIEDPEE MLNKLEGDNS LEANDFRWKA
RMNSLTPIEK VRQIALYLLC WGEANQVRFT PELLCFIYKC ALDYLDSPIC QQRTEPMPEG
DYLNRIITPL YRYLRDQVYE IVDGRFFKRE KDHNEIVGYD DVNQLFWYPE GIARIAFEDS
TKLIDLPVEE RYLRLGDVIW TDAFMKTFKE TRTWLHLVTN FNRIWIIHAT VFWMYAAYAA
PTFYTHNYQQ LVNNQPLAAY KWAASALGGT LASFIQLCAV ICEWTFIPKN WAGSQRLSPR
FWFLCIIFGI NLGPIIFVFA YDKIDVYSTA AHAVAAVMFF IAVGTLLFFS IMPLGNLFSN
YRKKDARRYV ASQTFTASFA PLHGIDMWLS YLVWVTVFAA KFSESYYFLI LSLRDPIRIL
STTTMRCTGE YWWGDVLCKQ QTKIVLGLMI ATDFLLFFLD TYLWYILVNV IFSVGKSFYM
GISILTPWRN IFTRLPKRIY SKILATTDME IKYKPKVLIS QVWNAVVISM YREHLLAIDH
VQKLLYHQVP SEIEGKRTLR APTFFVSQDD NNFETEFFPR DSEAERRISF FAQSLATPIP
EPLPVDNMPT FTVLTPHYAE RILLSLREII REDDQFSRVT LLEYLKQLHP VEWDCFVKDT
KILAEETAAF DGDVDDPNKE DALKSQIDDL PFYCIGFKSA APEYTLRTRI WASLRSQTLY
RTVSGMMNYS RAIKLLYRVE NPEIVQMFGG NAEGLERELE KMSRRKFKYL VSMQRLAKFK
PHELENAEFL LRAYPDLQIA YLDEEPPMNE GDEPRIFSAL IDGHCEILEN GRRRPKFRVQ
LSGNPILGDG KSDNQNHALI FYRGEYIQLI DANQDNYLEE CLKIRSVLAE FEELDVEQVN
PYSPGLSYQD QVAKHPVAIV GAREYIFSEN SGVLGDIAAG KEQTFGTLFA RTLSQIGGKL
HYGHPDFINA TFMTTRGGLS KAQKGLHLNE DIYAGMNALL RGGRIKHCEY YQCGKGRDLG
FGTILNFTTK IGAGMGEQML SREYYYLGTQ LPIDRFLSFY YAHPGFHLNN LFIQLSLQMF
MLTLVNLNSL AHESIICIYD RNKPITDILY PIGCYNLSPV VDWVRRYTLS IFIVFWIAFV
PIVIQELIER GVWKATVRFC RHLLSWAPVF EVFAGQVYSS AIFTDLTVGG ARYISTGRGF
ATARIPFSIL YSRFAGSAIY LGARSLFMLL FSTIAHWQAP LLWFWASLSA LMWAPFVFNP
HQFAWEDFFL DYRDFIRWLS RGNNQYHRNS WIGYVRMSRS RVTGFKRKLV GDESEKAAGD
AHRAHRTNLI AGEIIPSAIY CAGCFIAFTF INAQTGVKTT DDDRVNSVVR IIICTLAPIA
VNLGVLSFCL GMLCCSGPLF GMCCKKTGSS MAGFAHGVAV VIHLIMFIVM WVFEGFHFTR
GLLGTITCIQ IQRLIFMCMS TFLLTREFKN DHSNTAFWTG KWYGSGMGYS AWTQPSRELC
AKVIEMSEFA ADFVLGHILL FCQAPLLLIP RIDSFHSMML FWLKPSRQIR PPIYSLKQAR
LRKRMVKKYI SLFVAVLVLF LVVIIAPAVA SNYVADDVAS SLTGAFHNLL QPRNVSNNDT
GYQMSTYLSH YYTHTPSLRT WSTIK
//
