ID H1VLD6_COLHI Unreviewed; 1940 AA.
AC H1VLD6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=CH063_02497 {ECO:0000313|EMBL:CCF41039.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF41039.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CACQ02004456; CCF41039.1; -; Genomic_DNA.
DR STRING; 759273.H1VLD6; -.
DR EnsemblFungi; CCF41039; CCF41039; CH063_02497.
DR VEuPathDB; FungiDB:CH63R_11903; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
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 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 495..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 583..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 613..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1347..1366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1399..1420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1490..1510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1516..1534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1606..1627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1652..1679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1691..1716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1722..1740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1788..1811
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1848..1872
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 349..461
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1921..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1940 AA; 221685 MW; E952F49F994966C8 CRC64;
MSGHPAGSAG GGGHQDYDDG YGQQGRGHGN GTQQTDSYYQ DDQQYYDQNG YDAHGHPQQG
AEGYYDESGY YNADPNNAYH QDGGYYDNNE QYQDEYYNNN GNGNGYYDQD YNQGYAGGPR
RQGSEEDSET FSDFTMRSDM ARATDMDYYG RGDERYNSYD QGGARGFRPP SSQISYGGNR
SSGASTPNYG MDYANMMSAA SREPYPAWTS DAQIPLSKEE IEDIFLDLCA KFGFQRDSMR
NMYDHFMILL DSRASRMTPN QALLSLHADY IGGDNANYRK WYFAAHLDLD DAVGFANMKG
KGLRRKAKNK KKKGEAENDA EALEDLEGDN SLEAAEYRWK TRMNRMSQHD RVRQLALYLL
CWGEANQVRF MPECLCFIFK CADDFLNSPA CQNMVEPVEE FTFLNNVITP LYQFCRDQGY
EISDGVYVRR ERDHDKVIGY DDCNQLFWYP EGIEKIVLED KSKLVDVPPA ERYLKFKDIN
WKKCFFKTYK ETRSWFHLLV NFNRIWIIHL TMFWFYTSAN APSIILGNKY EQEANNQPTK
AQLFSIMGFG GTIAALIQVL ATLAEWAYVP RKWAGAQHLT KRLLFLLLIL VINVAPFVYV
FVLPNPNEKI AEILAIVEFV IALLTFIFYS VMPLGGLFGS YLTKNSRKYV ASQTFTASYP
RLKGNDMAMS YGLWLLVFGA KFGESYVYLT LSFRDPIRYL SIMKLDCMGD ALFGNILCKN
QHYVLLALMT FTDLIFFFLD TYLWYVLVNA LFSIARSFYI GSSILTPWRN VFSRLPKRIY
SKILATGDME IKYKPKVLIS QVWNAIVISM YREHLLAIDH VQKLLYHQVP SEQEGKRTLR
APTFFVSQED HSFKTEFFPT NSEAERRLSF FAQSLSTPIP EPVPVDNMPT FTVLIPHYSE
KILLSLREII REDEPYSRVT LLEYLKQLHP HEWDCFVKDT KILADETSQF NGDNEKNEKD
TAKSKIDDLP FYCIGFKSSA PEYTLRTRIW ASLRFQTLYR TISGFMNYSR AIKLLYRVEN
PEVVQMFGGN SDKLERELER MARRKFKLCV SMQRYAKFKK EEMENAEFLL RAYPDLQIAY
LDEEPPLAEG EEPRLYSALI DGHSEIMENG MRKPKFRIQL SGNPILGDGK SDNQNHSLIF
YRGEYIQLID ANQDNYLEEC LKIRSVLAEF EEMKTENVSP YTPGVKNKMI NPVAILGARE
YIFSENIGIL GDVAAGKEQT FGTLFARTLS QIGGKLHYGH PDFLNGIFMT TRGGVSKAQK
GLHLNEDIYA GMNALLRGGR IKHCEYYQCG KGRDLGFGSI LNFTTKIGTG MGEQMLSREY
YYLGTQLPLD RFLSFYYAHP GFHLNNMFIM LSVQMFMICL LSLGALRHET KSCNYNRDVP
ITDPLYPTGC QNTDALMDWV YRCILSIIFV LLLAFVPLVV QEVTERGVWR AAKRLAKQFG
SLSPFFEVFV CQIYANSVQQ DLSFGGARYI GTGRGFATAR IPFGVLYSRF AGPSIYFGSR
LLMMLLFATV TIWQGLLVYF WISLLALVIS PFLYNPHQFA WSDFFIDYRD FLRWLSRGNS
RSHASSWIAF CRLSRTRITG YKRKALGDPS AKMSSDVPRA AITNMFLGEI LTPLLLVAVT
VIPYLFINAQ TGVEGANNSN VSGDPPKRTN SLIRVGLVAL APIAINAGVL LMMFFMACFM
GPLLSMCCKK FGSVLAAIAH GLAVVMLLVF FEVMFLLESF EFARTLLGMI AVVAIQRFVF
KLIISLTLTR EIKTDAANIA FWTGKWYSMG WHSVSQPARE FLCKITELSM FAADFVLGHF
LLFIMLPVIL IPKVDMLHSM MLFWLRPGRQ IRPPIYSMKQ SKLRRKRVFR YAILYFTMFI
LFMALMIGPA VVGDLIPMDI FKQLDTTSIA LIQPTKYNND NTQQSSKTGT GRDDYSGAYL
TMTPSSSSSA TGNSERVRLF
//
