CHIA1_EMENI
ID CHIA1_EMENI Reviewed; 961 AA.
AC G5EB30; C8V7G5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Endochitinase A;
DE EC=3.2.1.14;
DE AltName: Full=Chitinase A;
DE Flags: Precursor;
GN Name=chiA; ORFNames=AN8241;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP GLYCOSYLATION, GPI-ANCHOR AT GLY-936, SUBCELLULAR LOCATION, INDUCTION,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18420434; DOI=10.1016/j.fgb.2008.02.008;
RA Yamazaki H., Tanaka A., Kaneko J., Ohta A., Horiuchi H.;
RT "Aspergillus nidulans ChiA is a glycosylphosphatidylinositol (GPI)-anchored
RT chitinase specifically localized at polarized growth sites.";
RL Fungal Genet. Biol. 45:963-972(2008).
RN [4]
RP IDENTIFICATION OF GPI-ANCHOR.
RX PubMed=19940384; DOI=10.2323/jgam.55.381;
RA Cao W., Maruyama J., Kitamoto K., Sumikoshi K., Terada T., Nakamura S.,
RA Shimizu K.;
RT "Using a new GPI-anchored-protein identification system to mine the protein
RT databases of Aspergillus fumigatus, Aspergillus nidulans, and Aspergillus
RT oryzae.";
RL J. Gen. Appl. Microbiol. 55:381-393(2009).
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.
CC {ECO:0000269|PubMed:18420434}.
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 Evidence={ECO:0000269|PubMed:18420434};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18420434};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18420434}. Secreted, cell
CC wall {ECO:0000250}. Cell tip {ECO:0000269|PubMed:18420434}.
CC Note=Localizes at the germ tubes of conidia, at hyphal branching sites
CC and hyphal tips.
CC -!- INDUCTION: Expressed specifically highly during conidia germination and
CC in the marginal growth regions of colonies.
CC {ECO:0000269|PubMed:18420434}.
CC -!- PTM: O-glycosylated but not N-glycosylated.
CC {ECO:0000269|PubMed:18420434}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; BN001302; CBF74186.1; -; Genomic_DNA.
DR EMBL; AACD01000145; EAA58979.1; -; Genomic_DNA.
DR PIR; JW0067; JW0067.
DR RefSeq; XP_681510.1; XM_676418.1.
DR AlphaFoldDB; G5EB30; -.
DR SMR; G5EB30; -.
DR STRING; 162425.CADANIAP00004295; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EnsemblFungi; CBF74186; CBF74186; ANIA_08241.
DR EnsemblFungi; EAA58979; EAA58979; AN8241.2.
DR GeneID; 2869070; -.
DR KEGG; ani:AN8241.2; -.
DR VEuPathDB; FungiDB:AN8241; -.
DR eggNOG; KOG0516; Eukaryota.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_009107_2_0_1; -.
DR InParanoid; G5EB30; -.
DR OMA; DTVYPTD; -.
DR OrthoDB; 923272at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051286; C:cell tip; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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 1: Evidence at protein 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..936
FT /note="Endochitinase A"
FT /id="PRO_0000429818"
FT PROPEP 937..961
FT /note="Removed in mature form"
FT /id="PRO_0000429819"
FT DOMAIN 28..339
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 338..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..933
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 936
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000269|PubMed:18420434"
SQ SEQUENCE 961 AA; 96840 MW; 66263B3325C533E2 CRC64;
MAPKLFTFVS ALSGLASLAS AFHAEAKSNI AVYYGQGVNQ PRLAEFCAET SYDIINIGFI
NSFPEQNPLT GLPGSDFGNQ CWADTFVVDG IASQLYSHCP NIAEDIPKCQ AAGKKVFLSL
GGATPTYWFD TIDASTKLAD FLWGAFGPVT DAWTVADKPR PFGNAVVDGF DFDIEFFGSK
GYANMIKRFR RRFGEVPDQT FYISAAPQCS IPDEQLSVAI KNAVIDFVWV QFYNTPGCSA
RDFVLGTKNG FNYDSWVEVI KAGANPNAKL YVGLPASGAA ANLGYYLTPE EVKPLVKKYM
DKYPETFGGV MLWEATQARN NQIDGVGYNE KIREILYDLD PNHPPPTTSP TPTPTPSTTT
TSTTSTTSTT SATSTTSTTS TTSTTSTTPT TSTTSTTSTT TPTPSPSPST ASSSTTETVT
PSPKPSPSES STTSETSSLP STSTPVVSET PSETKTPTSS SAPPLSSSSP VGGSSSTASS
STSTPSETPS ASSTRAVSET STHISTSTSS GPETSLTGSS TSVPATSSSV PSSAISPSST
PVISETPRPP VTSSSSSTFV SSTSTSTDCS ESSTAIGTHS SSSISETPSA STPAASPSTS
PETTKTLTVF PTPGSSVSTG TTSASTLSSS VPATSGGHTE TSTVSTSSAN QTPSASTSKP
LIPTNSASST STGSVTSTPS APGVPSSSAG SDETATTSTT DSEPTSTSSG SVTAKPTTTE
PATTTTIIVT SYTSICPTGF TTITTTITST YCPGTASATA TAIAPTTDVP GSGSGSSPAQ
PTITADIPEG WTTTVTVCTV CAATPTTVTL TLPPATTTEE STSAQPTGEV PSSDGSGSGE
VSTTTVVVVP APTGNAGDGV PAPGANVGEE YTAAPGSATT SKPLIGGGAS GAHTAYPYAS
STFHIIPSAS AHVPVPSGSG SSPSGTQGGA SPTFTGAGSR YDVVKGVPAL VALALSLLAV
L
