ID A1DAT9_NEOFI Unreviewed; 586 AA.
AC A1DAT9;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Capsule polysaccharide synthase Cps1, putative {ECO:0000313|EMBL:EAW19979.1};
GN ORFNames=NFIA_095990 {ECO:0000313|EMBL:EAW19979.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW19979.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027694; EAW19979.1; -; Genomic_DNA.
DR RefSeq; XP_001261876.1; XM_001261875.1.
DR AlphaFoldDB; A1DAT9; -.
DR EnsemblFungi; EAW19979; EAW19979; NFIA_095990.
DR GeneID; 4588331; -.
DR KEGG; nfi:NFIA_095990; -.
DR VEuPathDB; FungiDB:NFIA_095990; -.
DR eggNOG; ENOG502SICP; Eukaryota.
DR HOGENOM; CLU_019940_2_0_1; -.
DR OMA; QITHAMP; -.
DR OrthoDB; 2724691at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR CDD; cd06434; GT2_HAS; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR47844:SF1; EXOSTOSIN-LIKE 2; 1.
DR PANTHER; PTHR47844; SYNTHASE CPS1, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G02500)-RELATED; 1.
DR Pfam; PF13641; Glyco_tranf_2_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REGION 463..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 66332 MW; 118DDD816712372A CRC64;
MYGLLAFITL PWVIAHPRLF MVAAAAAAYF MHSTGRTLQD VHADITSRVA GILPEDLRRD
DVFCDPMTVV FLHLFVFRYL RLLVHLISFW LFYHPTPVPK NPTLFPSDCT IILPTVDPEN
RDFEECIISC LRNKPGAIII VTVGDQLTKL TKDIIAPYKR RFPSTEISVR TADEANKRRQ
TKITVLLDDH VFWPTERFLP TILAPFEDPK VGIVGTNKRV RRTNTGFNIR SFWNMLGALY
LERHNFEIRA TNAIDNGVFV VSGRTSAHRS EILKNPEFMA EFTNERFFFG LFGPLNADDD
NFITRWDVRH GWKVKIQYCP DAMIETTLGT YPKFLSQCLR WVRTTWRSNS ASLFTDRTVW
YTQPWCVYAV YWTSFVNFAL FYDGALAYTL LKSPLGTADN LKYLAAWIFC TKMVKLTPYF
LREPQDLVML PGYFAFAYFH SLIKLYAGLT FWETNWGGRN LSAVNNQPGG GPDDDDDADD
SSDDSVDGGV QLPPTPPSLR RRQTAGSSSA GRGGNASGSN RVQSRTSTVG TKAPRKTQAQ
PRTRVSSSST SSTSSSTSSK WQRCPGCRKL HSDSGTVCQV RDVWGR
//
