CHIA1_ASPFU
ID CHIA1_ASPFU Reviewed; 888 AA.
AC Q4WEP7;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Endochitinase A1;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase A1;
DE Flags: Precursor;
GN Name=chiA1; Synonyms=chi1; ORFNames=AFUA_5G03760;
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).
CC -!- FUNCTION: GPI-anchored chitinase involved in the degradation of chitin,
CC a component of the cell walls of fungi and exoskeletal elements of some
CC animals (including worms and arthropods). Required to reshape the cell
CC wall at the sites where cell wall remodeling and/or cell wall
CC maturation actively take place such as sites of conidia formation (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- ACTIVITY REGULATION: The cyclic peptide natural product argifin acts as
CC a specific inhibitor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000011; EAL85930.1; -; Genomic_DNA.
DR RefSeq; XP_747968.1; XM_742875.1.
DR AlphaFoldDB; Q4WEP7; -.
DR SMR; Q4WEP7; -.
DR STRING; 746128.CADAFUBP00005116; -.
DR EnsemblFungi; EAL85930; EAL85930; AFUA_5G03760.
DR GeneID; 3505591; -.
DR KEGG; afm:AFUA_5G03760; -.
DR VEuPathDB; FungiDB:Afu5g03760; -.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_009107_2_0_1; -.
DR InParanoid; Q4WEP7; -.
DR OMA; DTVYPTD; -.
DR OrthoDB; 923272at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IMP:AspGD.
DR GO; GO:0001896; P:autolysis; IMP:AspGD.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell membrane; Cell wall; Chitin degradation;
KW Chitin-binding; Glycoprotein; Glycosidase; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..863
FT /note="Endochitinase A1"
FT /id="PRO_0000429816"
FT PROPEP 864..888
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429817"
FT DOMAIN 29..338
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 338..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT LIPID 863
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 888 AA; 88628 MW; EDB4FADAF7281D98 CRC64;
MVSSKLSFVA TAVAALAPLA SAFDASSRSN LAIYWGQGPN QLRLSHFCQE TSLDIINIGF
INYFPDMSPG HWPGSNFGNQ CDGSVYVTND GVVTKLLSGC HQIMEDIPIC QAAGKKVLLS
IGGAYPPDQS ILSEDSAVAF ATFLWGAFGP VAEGWEGPRP FGDVVVDGFD FDIEHNGGFG
YATMANTFRQ YFNQVPERKF YLSAAPQCII PDAQLSDAIF NAAFDFIWIQ YYNTAACSAK
SFIDTSLGTF NFDAWVTVLK ASASKDAKLY VGLPASETAA NQGYYLTPDE VESLVSTYMD
RYPDTFGGIM LWEATASENN QIDGAPYADH MKDILLHCDP SPPVTSSSAI PSSTPVTTPS
PSSSAVPSST PAVSETPSPS SSAVPSSTPV ASSTPVVPGT SASSSPVSSS SAVASSTPVV
PGTSASSSPV SSSSAVASST PVVPGTSTSP STPVIPGTSA SSSPVSSSSA VASSTPVVPG
TSASSSPVSS SSAVASSTPV VPGTSASSSP VSSSSAVASS TPVVPGTSVP SSTPAIPGGS
SSSSEAVASS TPLVTLTLTV SPTPAPSSSE SSSTDLSSST QTDVGTAPSQ PAGPSTTATA
TTSSSSSSTD ESSTTVGSGN GNGSGSTTTT AATDSITAAP TATSSATATG ATSEPVTITT
IIVTSYIDIC PTGFTTVTTT YTTTYCPGTN TATATATVTN PPSGPGGAGS QTTAPTVPEG
WTTTVTICTQ CAAKPTTVTL TLPVTETGST STDAVPAPPA ATGEGSNPTQ PSGASPTGGN
GSFSEEPVPP PAVTQVSTST EIVTLVRPTS SRPLILGTGT VHPSSTLAVK PSAKPSGQNS
GSSSHVPIPP SYTQEAVSPL STGAASRVTG LGHGLVLTVL TLSAFFVL
