CAS1_CRYNH
ID CAS1_CRYNH Reviewed; 959 AA.
AC Q8X226; J9VW11;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Probable O-acetyltransferase CAS1;
DE EC=2.3.1.-;
DE AltName: Full=Capsule synthesis protein 1;
GN Name=CAS1; ORFNames=CNAG_07937;
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].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=11703667; DOI=10.1046/j.1365-2958.2001.02651.x;
RA Janbon G., Himmelreich U., Moyrand F., Improvisi L., Dromer F.;
RT "Cas1p is a membrane protein necessary for the O-acetylation of the
RT Cryptococcus neoformans capsular polysaccharide.";
RL Mol. Microbiol. 42:453-467(2001).
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: Probable O-acetyltransferase required for the O-acetylation
CC of the capsular glucoronoxylmannans (GXM) involved in virulence.
CC {ECO:0000250|UniProtKB:P0CM56}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. CASD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF355593; AAL35100.1; -; Genomic_DNA.
DR EMBL; CP003832; AFR98667.1; -; Genomic_DNA.
DR RefSeq; XP_012053554.1; XM_012198164.1.
DR AlphaFoldDB; Q8X226; -.
DR EnsemblFungi; AFR98667; AFR98667; CNAG_07937.
DR GeneID; 23890742; -.
DR VEuPathDB; FungiDB:CNAG_07937; -.
DR HOGENOM; CLU_008003_0_1_1; -.
DR Proteomes; UP000010091; Chromosome 13.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR InterPro; IPR012419; Cas1_AcylTrans_dom.
DR Pfam; PF07779; Cas1_AcylT; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Oxidoreductase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..959
FT /note="Probable O-acetyltransferase CAS1"
FT /id="PRO_0000307853"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 114
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT ACT_SITE 349
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT ACT_SITE 352
FT /evidence="ECO:0000250|UniProtKB:Q96PB1"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 959 AA; 107298 MW; 8A301556CF5DF8B4 CRC64;
MPNSSNSRSQ ATAAKLNPLW YTYACATLVA AVVLGNILRW AFLELPDSYH CSALLNTGKW
LDPGTWTNWQ PEGCFQLPLS AQSWQRCLAS PTVNTHQALH SYYDKRTALF VGDSTVRQLY
FATARKVGKA SKAWESEGEK HTDRSLLVSD PLGGPSLELE FWWDPYLNSS KTIGLLSGRG
LAPSSLLVMG SGLWYLRNPS SGGLASWGAM IHDTFEFIKK NQGSPQAALI NPWDNMLLGS
GLTLPGLLPQ QSPKFVDSSR EVEARSLFSR ASSASHRPAD FSISDAIVYL PISTPVHEKL
SSSRAETIFH TDVEAMNADL YARLTHPDPP PVVIPSVFNQ LLVDDETEDG LHFSDKIMDK
QAELLLSWRC NDVMRHEGAT GACCKRYDWV TPIQGLILAV LILWAPLGTF ITPRLPPNSP
IHDYLPSPSI APALSTFGLA VGYLFLADRT HVFQKEQKDY DAVVFGVITF AAFVAGLLTI
KNSGKDLGFL NRDITDEWKG WMQIAILIYH FFGASKISGI YNPIRVLVAS YLFMTGYGHF
FFYYKKADFG FQRVVMVLVR LNLLSVVLPY TMNTDYAFYY FAPLVSWWYL IIYATMAFGS
KYNDRPAFLL AKLFTCAGLV TLFMHFPWLM EDVFKVLNTV FNIQWSAKEW SFRVTLDLFI
VWAGMLCAYG FVKFKEYQIS DRPWFPTMHT ATLIGSVLGM IWYFWFELHL ANKFVYNEYH
AVVCIVPIIS FIFLRNASPV LRSSTSKIFC FIGQCSLETF ILQFHGWLAS DTKAVLLAVP
STQWRPVNLV ISTICFIWLS YRVSGATGEI TEWLVGKKKA LPLPATSAGP STSTSRQATS
PTLTTASAMQ AVVEGPQDGA KGGIPESIPM MNQADKDIGG LTPMEDETLE RRDSWPTWMA
STAASLTGRT AEGYAPLTRQ WKDQTVLSVI QNLGDLMKKH TSVKIAVILF GLWVLNWIY
