CRF2_ASPFU
ID CRF2_ASPFU Reviewed; 443 AA.
AC Q4WI46;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Probable glycosidase crf2;
DE EC=3.2.-.-;
DE AltName: Full=Crh-like protein 2;
DE Flags: Precursor;
GN Name=crf2; Synonyms=utr2; ORFNames=AFUA_2G03120;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP PROTEIN SEQUENCE OF 100-104 AND 242-251, AND GPI-ANCHOR.
RX PubMed=11545413;
RX DOI=10.1002/1522-2683(200108)22:13<2812::aid-elps2812>3.0.co;2-q;
RA Bruneau J.-M., Magnin T., Tagat E., Legrand R., Bernard M., Diaquin M.,
RA Fudali C., Latge J.-P.;
RT "Proteome analysis of Aspergillus fumigatus identifies
RT glycosylphosphatidylinositol-anchored proteins associated to the cell wall
RT biosynthesis.";
RL Electrophoresis 22:2812-2823(2001).
RN [3]
RP STRUCTURE OF GPI-ANCHOR.
RX PubMed=12626404; DOI=10.1093/glycob/cwg004;
RA Fontaine T., Magnin T., Melhert A., Lamont D., Latge J.-P.,
RA Ferguson M.A.J.;
RT "Structures of the glycosylphosphatidylinositol membrane anchors from
RT Aspergillus fumigatus membrane proteins.";
RL Glycobiology 13:169-177(2003).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group. The
CC anchor position has not been determined.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; AAHF01000008; EAL87409.1; -; Genomic_DNA.
DR RefSeq; XP_749447.1; XM_744354.1.
DR AlphaFoldDB; Q4WI46; -.
DR SMR; Q4WI46; -.
DR STRING; 746128.CADAFUBP00001971; -.
DR PRIDE; Q4WI46; -.
DR EnsemblFungi; EAL87409; EAL87409; AFUA_2G03120.
DR GeneID; 3506821; -.
DR KEGG; afm:AFUA_2G03120; -.
DR VEuPathDB; FungiDB:Afu2g03120; -.
DR eggNOG; ENOG502QVQI; Eukaryota.
DR HOGENOM; CLU_040459_0_0_1; -.
DR InParanoid; Q4WI46; -.
DR OMA; CYDPPSG; -.
DR OrthoDB; 1209387at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:AspGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..416
FT /note="Probable glycosidase crf2"
FT /id="PRO_0000245543"
FT PROPEP 417..443
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000245544"
FT DOMAIN 21..306
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 350..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 168
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 416
FT /note="GPI-like-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 443 AA; 46710 MW; 9BDAF2E67421CFE2 CRC64;
MVRIGSSLLL ATLAATTVSA ASDPPKCSQD SHCPEEWPCC SLYGQCGTGA YCLGGCDPLM
SFSLDSCTPE PICQGKTYKD WSNLDNLASN TKYLGDASKS DWVYSGYPKV EDGNLLLTMP
KNSVGTLIAN NHYIWYGKIT AKIKSSRGAG VVTGFILLSD TKDEIDYEFV GADLTNVQTN
YYFQGVLDYN HGGNASVSGG NTFGDWHEYT IDWKPDAITW SVDGEVKRTL KKESTYNETS
KQYMYPQTPS RMQLSLWPAG QASNAPGTIA WAGGEIDWDS EDIKDPGYYY ATFGEITVEC
YDPPSGADIK GTKAYIFKDK AGLESSVQIT NNKTVLASFG ATGLDMDVGA SSSASGSANK
TSSSANTVPS GNGGSGNEPG NSHSGSSGSG TSTSDGSGSS TGFSQGSETS ASSNKNAAPS
QNERVLNGSF FAVLVAVVAL VTL
