CHIA1_ASPNC
ID CHIA1_ASPNC Reviewed; 1257 AA.
AC A2QUQ2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Endochitinase A;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase A;
DE Flags: Precursor;
GN Name=ctcA; Synonyms=chiF, cts1; ORFNames=An09g06400;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP INDUCTION.
RX PubMed=17561995; DOI=10.1186/1471-2164-8-158;
RA Guillemette T., van Peij N., Goosen T., Lanthaler K., Robson G.D.,
RA van den Hondel C.A., Stam H., Archer D.B.;
RT "Genomic analysis of the secretion stress response in the enzyme-producing
RT cell factory Aspergillus niger.";
RL BMC Genomics 8:158-158(2007).
RN [3]
RP INDUCTION.
RX PubMed=23449598; DOI=10.3114/sim0009;
RA van Leeuwen M.R., Krijgsheld P., Bleichrodt R., Menke H., Stam H.,
RA Stark J., Wosten H.A., Dijksterhuis J.;
RT "Germination of conidia of Aspergillus niger is accompanied by major
RT changes in RNA profiles.";
RL Stud. Mycol. 74:59-70(2013).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
CC -!- INDUCTION: Highly expressed in germinated conidia. Expression is
CC induced by tunicamycin and DTT. {ECO:0000269|PubMed:17561995,
CC ECO:0000269|PubMed:23449598}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; AM270210; CAK40432.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QUQ2; -.
DR SMR; A2QUQ2; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; A2QUQ2; -.
DR EnsemblFungi; CAK40432; CAK40432; An09g06400.
DR VEuPathDB; FungiDB:An09g06400; -.
DR HOGENOM; CLU_009107_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 1L.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1231
FT /note="Endochitinase A"
FT /id="PRO_5000220487"
FT PROPEP 1232..1257
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429822"
FT DOMAIN 28..339
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 364..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT LIPID 1231
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1257 AA; 122094 MW; F6087E3251015C19 CRC64;
MVFKPLTIAA AIAGLTPFVS AFDAQAKSNV AVYYGQGYGQ QRLSHFCQET SLDIINIGFI
NTFPDQGAAG WPGSNFGNQC DGLTYEVDGV STKLLSGCHQ IAEDIPICQA AGKKVLLSLG
GASPDNQQIL SDASAVRFAD FLWGAFGPQT EEWVSNDGPR PFGEVVVDGF DFDIEHNGGF
GYATMVNRFR ELFALVPERT FYISGAPQCP IPDPQLSDAI AQSPFDFVWV QFYNTAGCAA
SDSINGVSTG FNFDDWVDVI KRGANPDAKL YVGLPAGPGA AGAGYYLTPE EVYPLVDVYM
NLYPETFGGI MLWEATASDE NTFSGLTFAD VIKDILVAVD PSPPVPSPSS SSVIASSTPV
ASSTPVASSA PASSTPISSG SPVPSSSAVS SSPAVSSTTE SSSTQVVSGS VSASSSPITS
SPVASSTPVA SSAPSATSSA VASSSPIAPS SPVASSSAIA SSSAIASSSA IASSSAIASS
SAIASSSAIA SSSAIASSSA IASSSAIASS SAIASSSAIA SSSAIASSSA IASSSPVAPS
SPVASSSPAV SSSAIVSSTP AVSTPVASSI PVISSPAIAS GSAIASSSHV ASSSTPAASS
SPAVSSSPVA SSSPALSSSP SASASSTPII PSSTASSAVV SSSPTPSSSV VRSSSLLSSS
SPALSSTRTP SNPVIPSSSA ISITPSSTPV RSTSSVAPGK SSSAPVIPKP SSTVIATFTS
SSGSLPSSSA PAGSGVPSSS TLPHPSSTSL LSSSPVSSAE PVSSSSAVGT SVGSSSNVVT
GVSTRSSSSV VPSGTPIPPV SGTATESVTS SSSGSGSPTV PSSINTSSTD ASSSSSASSV
EPTSSGSVIT SVTSSSASRV SSSSSSVVIT NPSVPSDSSS SSGSELSTTS STESTSSASS
QTGAPTTSVS LGSSEAASTS TSGAAASGSG AQDSTKPTDH ASTLSPSYST PLASASGQTG
SPTTVPAGIP TGNGSGLAPI TSSITSAQAV PSVTSSGLES EPEPTITTTV IVTSYIDICP
EGFTTITTTY TTTYCPATVS ATATATAAVT NPPGAPAQTT SPSVPEGWTT TVTVCTHCAP
TPTTVTLTLP ATNRPSALAS STSAPNSPED WTTTVSVCTD CGPTPTTVTV TIPVGAATGV
DALTASPSGS QPAGESSPGQ SAPTAPASTA PTTTETVIVV PSQSSTSQPV ILGTGSVRAS
STFHIQPSQS GSRVPVAPSG TAAGVSPVFT GAASRVSRLQ HGAGAVSAFA LFLLAAI
