ID   FKS1_CRYNH              Reviewed;        1799 AA.
AC   O93927; J9VWV0;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 3.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=1,3-beta-glucan synthase component FKS1;
DE            EC=2.4.1.34;
GN   Name=FKS1; ORFNames=CNAG_06508;
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=9882657; DOI=10.1128/jb.181.2.444-453.1999;
RA   Thompson J.R., Douglas C.M., Li W., Jue C.K., Pramanik B., Yuan X.,
RA   Rude T.H., Toffaletti D.L., Perfect J.R., Kurtz M.;
RT   "A glucan synthase FKS1 homolog in cryptococcus neoformans is single copy
RT   and encodes an essential function.";
RL   J. Bacteriol. 181:444-453(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
CC   -!- FUNCTION: Alternate catalytic subunit of the 1,3-beta-glucan synthase
CC       (GS). Synthesizes 1,3-beta-glucan, a major structural component of the
CC       yeast cell wall. Involved in cell wall synthesis, maintenance and cell
CC       wall remodeling (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Component of the 1,3-beta-glucan synthase (GS). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Impairs mitotic growth.
CC       {ECO:0000269|PubMed:9882657}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD11794.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF102882; AAD11794.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CP003832; AFR98738.1; -; Genomic_DNA.
DR   RefSeq; XP_012053533.1; XM_012198143.1.
DR   AlphaFoldDB; O93927; -.
DR   CAZy; GT48; Glycosyltransferase Family 48.
DR   SwissPalm; O93927; -.
DR   PRIDE; O93927; -.
DR   EnsemblFungi; AFR98738; AFR98738; CNAG_06508.
DR   GeneID; 23889702; -.
DR   VEuPathDB; FungiDB:CNAG_06508; -.
DR   HOGENOM; CLU_000844_0_1_1; -.
DR   Proteomes; UP000010091; Chromosome 13.
DR   GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR026899; FKS1-like_dom1.
DR   InterPro; IPR003440; Glyco_trans_48.
DR   Pfam; PF14288; FKS1_dom1; 1.
DR   Pfam; PF02364; Glucan_synthase; 1.
DR   SMART; SM01205; FKS1_dom1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW   Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1799
FT                   /note="1,3-beta-glucan synthase component FKS1"
FT                   /id="PRO_0000394217"
FT   TRANSMEM        431..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        530..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        591..611
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        648..668
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1268..1288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1323..1343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1422..1442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1446..1466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1527..1547
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1563..1583
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1605..1625
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1635..1655
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1704..1724
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1762..1782
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        1333
FT                   /note="I -> M (in Ref. 1; AAD11794)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1799 AA;  204372 MW;  E3D5290290DD48EC CRC64;
     MSYPNPPPPP KGSASFSSSS SDPFNQTNQL PYDSQFPPQH AFAHPSAPNP GAGGAGVAPP
     GQGGQYAPYY DNEPEMGGRW EGGGMGRETW ASESGWSQNE PNYPPSDYHG GPGYLPSRAS
     TPTFEGSNAG HRPRDPYPAW TVDANIPLSK EEIEDVLIDL ANKFGFQKDS SRNVYDFLMI
     QLDSRASRMS PNQALLTLHA DYIGGEHANY RKWYFAAQLD LDDAIGAVQN PGLNRVRSVA
     RRGGKTKNPL ATAQEKSLES ATSRWRTAMN NMSQYDRLRQ VALYLLCWGE AAQVRFMPEC
     LCFIFKCADD YYRSPECQNR QEAVPEGLYL RAVIKPLYRF LRDQGYEVVD GKFLRRERDH
     DKVIGYDDVN QLFWYPEGIS RITLNDNTRL VDIPPAQRFM KFDRIDWNKV FFKTYLEKRS
     FFHLLVNFNR IWVLHISVFW FFTAYNAPSI YAPSGSTTAT TPMAWSMTGL GGFVATLIMI
     AATLAEFSYI PTTWNNTSHL TRRLIFLLII LAITGGPSIY IAFFNQTGHV ALILGIVQFF
     CSVVATIAFA TLPSGRMFGD RVAGKSRKYL ANQTFTASYP ALGFYPRVAS FLLWFLVFGC
     KFTESYFFLT LSFRDPMKVM NGMKVQNCHD KYFGNGLCTN QPAFALAVMF VMDLTLFFLD
     TFLWYVIWNT VFSIARSFAI GMSIWTPWKD IFARLPKRIY AKILATDDME VKYKPKVLVS
     QVWNAVIISM YREHLLSIEH VQKLLYHQIQ SDQPGKRTLR APAFFISQSE KGSKAEFFPK
     GSEAERRICF FAQSLTTSIP APIPVDAMPT FTVLVPHYSE KILLSLREII REEDQNTRVT
     LLEYLKQLHP VEWDNFVRDT KILAEESDAF NGGNPFASDE KEEAKKADDI PFYTIGFKSA
     APEYTLRTRI WASLRAQTLY RTVSGFMNYS KAIKLLYRVE NPEVVQLFGG NTDQLERELE
     RMARRKFKFV VSMQRYSKFN KEEHENAEFL LRAYPDLQIA YLDEEPPRKD GGESRIFSAL
     IDGHSEIMPN GRRRPKFRIE LPGNPILGDG KSDNQNHAIV FYRGEYLQLI DANQDNYLEE
     CLKIRNVLGE FEEFKVSTQS PYAAQGHADF AKFPVAILGA REYIFSENIG ILGDIAAGKE
     QTFGTLAARS LSYIGGKLHY GHPDFLNAIY MNTRGGVSKA QKGLHLNEDI FAGMLAFGRG
     GRIKHSEYYQ CGKGRDLGFG TILNFQTKIG TGMGEQMLSR EYYYLGTQLP IDRFLTFYYG
     HPGFHINNIL VMMSVQVFML ALVFLGTLNK QLTVCRYSSG GDILPGQSGC YNLVPVFKWI
     KRCIISIFIV FWIAFVPLFV QELTERGTGR AILRLCKHFL SLSPVFEVFS TQIYMHSILN
     DLTFGGARYI ATGRGFATTR ISFSILYSRF AGPSIYLGMR TLVLLLFITL TVWVPHLIYF
     WITVVGLCVA PFLFNPHQFA IADFIIDYRE FLRWMSRGNS RTHANSWVGY CRLSRTRVTG
     FKRKRLGLPS EKLSSDVPRA PWKAILIGEI IGPICLAILF VICYLFIKSF AVDGQIQPGL
     VRIAIIALGP IVWNMALLIT LFLISVFLGP CLNSYTHQFG ATMAALAHFG AVAGMLVFFE
     LLWFLELWNT SHAVLGIIAV ISVQRCIFKF LIAVFLSREF KHDETNRAWW TGVWFNRGLG
     SHALSQPARE FVVKTIEMGL YSADFIACHL LLALLTIPMF IPYFDRVHAT MLFWLAPNQQ
     IRPPIYSFRQ RSQRRKIVFK YGLLYLIIQG IFIALIVVPI IFKDVAGLTP KSVPFNGII