CRF1_ASPFU
ID CRF1_ASPFU Reviewed; 395 AA.
AC Q8J0P4; O42800; O74682; Q4WRI5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Probable glycosidase crf1;
DE EC=3.2.-.-;
DE AltName: Full=Crh-like protein 1;
DE AltName: Allergen=Asp f 9;
DE Flags: Precursor;
GN Name=crf1; ORFNames=AFUA_1G16190;
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 [MRNA].
RC STRAIN=ATCC 42202 / AF-102 / Ag 507;
RA Banerjee B., Kurup V.P.;
RT "Expression and characterization of an allergen from Aspergillus fumigatus
RT cDNA.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rodriguez-Pena J.M., Guillen M.V., Perez R.M., Nombela C., Arroyo J.;
RT "Identification of a protein related to the Saccharomyces cerevisiae CRH-
RT protein family in Aspergillus fumigatus.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-292.
RC STRAIN=ATCC 42202 / AF-102 / Ag 507;
RX PubMed=9482698; DOI=10.1159/000023889;
RA Crameri R.;
RT "Recombinant Aspergillus fumigatus allergens: from the nucleotide sequences
RT to clinical applications.";
RL Int. Arch. Allergy Immunol. 115:99-114(1998).
RN [5]
RP PROTEIN SEQUENCE OF 63-76; 183-186; 195-201 AND 204-216, 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 [6]
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 Secreted, cell wall.
CC -!- PTM: The GPI-like anchor contains a phosphoceramide lipid group. The
CC anchor position has not been determined.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CRH1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC61261.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA11266.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF062651; AAC61261.1; ALT_FRAME; mRNA.
DR EMBL; AY169706; AAN87849.1; -; mRNA.
DR EMBL; AAHF01000004; EAL90947.1; -; Genomic_DNA.
DR EMBL; AJ223327; CAA11266.1; ALT_INIT; mRNA.
DR RefSeq; XP_752985.1; XM_747892.1.
DR PDB; 6IBU; X-ray; 2.25 A; A/B=22-266.
DR PDB; 6IBW; X-ray; 2.80 A; A/B=22-266.
DR PDBsum; 6IBU; -.
DR PDBsum; 6IBW; -.
DR AlphaFoldDB; Q8J0P4; -.
DR SMR; Q8J0P4; -.
DR STRING; 746128.CADAFUBP00001522; -.
DR Allergome; 3113; Asp f 16.0101.
DR Allergome; 3127; Asp f 9.0101.
DR Allergome; 68; Asp f 16.
DR Allergome; 79; Asp f 9.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblFungi; EAL90947; EAL90947; AFUA_1G16190.
DR GeneID; 3510010; -.
DR KEGG; afm:AFUA_1G16190; -.
DR VEuPathDB; FungiDB:Afu1g16190; -.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_027506_3_2_1; -.
DR OMA; PMNVRIG; -.
DR OrthoDB; 1209387at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; 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:0019863; F:IgE binding; IDA:AspGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 3D-structure; Allergen; Cell membrane; Cell wall;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Glycoprotein;
KW Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..370
FT /note="Probable glycosidase crf1"
FT /id="PRO_0000045432"
FT PROPEP 371..395
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000045433"
FT DOMAIN 45..230
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 271..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 370
FT /note="GPI-like-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 29..30
FT /note="EK -> AE (in Ref. 1; AAC61261)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="Y -> C (in Ref. 1; AAC61261)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..124
FT /note="WEV -> LVR (in Ref. 1; AAC61261)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="T -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:6IBU"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 103..114
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6IBU"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:6IBU"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:6IBU"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:6IBU"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:6IBU"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 233..246
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:6IBU"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:6IBU"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6IBU"
SQ SEQUENCE 395 AA; 40284 MW; 3250D8966F75000F CRC64;
MYFKYTAAAL AAVLPLCSAQ TWSKCNPLEK TCPPNKGLAA STYTADFTSA SALDQWEVTA
GKVPVGPQGA EFTVAKQGDA PTIDTDFYFF FGKAEVVMKA APGTGVVSSI VLESDDLDEV
DWEVLGGDTT QVQTNYFGKG DTTTYDRGTY VPVATPQETF HTYTIDWTKD AVTWSIDGAV
VRTLTYNDAK GGTRFPQTPM RLRLGSWAGG DPSNPKGTIE WAGGLTDYSA GPYTMYVKSV
RIENANPAES YTYSDNSGSW QSIKFDGSVD ISSSSSVTSS TTSTASSASS TSSKTPSTST
LATSTKATPT PSGTSSGSNS SSSAEPTTTG GTGSSNTGSG SGSGSGSGSS SSTGSSTSAG
ASATPELSQG AAGSIKGSVT ACALVFGAVA AVLAF
