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Endochitinase A1 (EC 3.2.1.14) (Chitinase A1)

 CHIA1_ASPFU             Reviewed;         888 AA.
Q4WEP7;
09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
25-APR-2018, entry version 72.
RecName: Full=Endochitinase A1;
EC=3.2.1.14;
AltName: Full=Chitinase A1;
Flags: Precursor;
Name=chiA1; Synonyms=chi1; ORFNames=AFUA_5G03760;
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
A1100) (Aspergillus fumigatus).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=330879;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
PubMed=16372009; DOI=10.1038/nature04332;
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
Machida M., Hall N., Barrell B.G., Denning D.W.;
"Genomic sequence of the pathogenic and allergenic filamentous fungus
Aspergillus fumigatus.";
Nature 438:1151-1156(2005).
-!- FUNCTION: GPI-anchored chitinase involved in the degradation of
chitin, a component of the cell walls of fungi and exoskeletal
elements of some animals (including worms and arthropods).
Required to reshape the cell wall at the sites where cell wall
remodeling and/or cell wall maturation actively take place such as
sites of conidia formation (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Random endo-hydrolysis of N-acetyl-beta-D-
glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
-!- ENZYME REGULATION: The cyclic peptide natural product argifin acts
as a specific inhibitor. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
class III subfamily. {ECO:0000305}.
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EMBL; AAHF01000011; EAL85930.1; -; Genomic_DNA.
RefSeq; XP_747968.1; XM_742875.1.
ProteinModelPortal; Q4WEP7; -.
SMR; Q4WEP7; -.
STRING; 5085.CADAFUBP00005116; -.
EnsemblFungi; CADAFUAT00002927; CADAFUAP00002927; CADAFUAG00002927.
GeneID; 3505591; -.
KEGG; afm:AFUA_5G03760; -.
EuPathDB; FungiDB:Afu5g03760; -.
HOGENOM; HOG000159794; -.
InParanoid; Q4WEP7; -.
KO; K01183; -.
OMA; FDFIWVQ; -.
OrthoDB; EOG092C4MM9; -.
Proteomes; UP000002530; Chromosome 5.
Proteomes; UP000002530; Unassembled WGS sequence.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
GO; GO:0004568; F:chitinase activity; IMP:AspGD.
GO; GO:0001896; P:autolysis; IMP:AspGD.
GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
InterPro; IPR001223; Glyco_hydro18_cat.
InterPro; IPR001579; Glyco_hydro_18_chit_AS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00704; Glyco_hydro_18; 1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS01095; CHITINASE_18; 1.
3: Inferred from homology;
Carbohydrate metabolism; Cell membrane; Cell wall; Chitin degradation;
Chitin-binding; Complete proteome; Glycoprotein; Glycosidase;
GPI-anchor; Hydrolase; Lipoprotein; Membrane;
Polysaccharide degradation; Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 863 Endochitinase A1.
/FTId=PRO_0000429816.
PROPEP 864 888 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000429817.
REGION 170 174 Inhibitor binding. {ECO:0000250}.
REGION 230 232 Inhibitor binding. {ECO:0000250}.
COMPBIAS 346 752 Ser/Thr-rich.
ACT_SITE 174 174 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10053}.
BINDING 34 34 Inhibitor. {ECO:0000250}.
BINDING 124 124 Inhibitor; via amide nitrogen.
{ECO:0000250}.
BINDING 125 125 Inhibitor. {ECO:0000250}.
BINDING 207 207 Inhibitor. {ECO:0000250}.
BINDING 312 312 Inhibitor. {ECO:0000250}.
LIPID 863 863 GPI-anchor amidated glycine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 780 780 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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