ID Q4WLF4_ASPFU Unreviewed; 1378 AA.
AC Q4WLF4;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=AFUA_6G13720 {ECO:0000313|EMBL:EAL89210.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL89210.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL89210.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
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., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:0000256|ARBA:ARBA00000822};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL89210.1}.
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DR EMBL; AAHF01000006; EAL89210.1; -; Genomic_DNA.
DR RefSeq; XP_751248.1; XM_746155.1.
DR STRING; 330879.Q4WLF4; -.
DR EnsemblFungi; EAL89210; EAL89210; AFUA_6G13720.
DR GeneID; 3508563; -.
DR KEGG; afm:AFUA_6G13720; -.
DR VEuPathDB; FungiDB:Afu6g13720; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002846_2_0_1; -.
DR InParanoid; Q4WLF4; -.
DR OMA; HICTANC; -.
DR OrthoDB; 11640at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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; cd00035; ChtBD1; 1.
DR CDD; cd02878; GH18_zymocin_alpha; 1.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR PANTHER; PTHR47700:SF2; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1378
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004246169"
FT DOMAIN 297..342
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 361..409
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 504..842
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 982..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 146163 MW; CCB483447DEFC4D4 CRC64;
MSPFFLYAST ILLFLSACVH TFSPAQNLAL AQYPPHSSCP VACSKAGLNP SNWTFIHDSH
SLRLCNATSL FDINIYTPVE GPKARISLRA CGAAALDANS ATPQTLTAGS ASLSSCDVSS
QSIKTTRDVQ FLQWAGDKTR DFSANAVSAA TELSRLLQEG DNCDQGIFLS QSKDVIVGVY
IGSDIQRASA VDILQNFGNS APSGPVKASQ LAAQACENGN KTAQTLGVFA DATGNLASVL
NALQVWDKGQ CLTGADNQQV WSNTPINVLN RHTTVRSDNT TIAARLKTKV LPRDTCTYVQ
AIANDGCWSL AQRCNITQAE LQQYNSDPNF CNDIAVGQYV CCSPGSLPDF SPQPNPDGSC
ATYSIQTNDT CSAIAAANSM TVTQLESRNS DVWGWSGCQS LYIGQVICLS TGTPPMPAPI
ANAVCGPQVP NTTAPANMSD LASLNPCPLN ACCDIWGQCG ITTDFCIADP ADTGAPGTAQ
PGTNGCISNC GMDIVGNGSP PSEFMRLGYY EAWNFQRPCL HMSTYKIPPL LTVCHQHFAF
GGITYDYQID MSAVQGQFQQ FRSLTGTKRI VSFGGWAFST QPSTFNILRT AFVVNNNLDG
VDFDWEYPGA PDIPGIPAGS PDDGPNYLAF LQELRSILPS GKTISIAAPA SFWYLKAFPI
AEISQVVDYI VFMTYDLHGQ WDYNNAFSDP GCPGGNCLRS QVNKTETVQS LAMITKAGVP
ASKILVGMAL YGRSFQMTEA GCYTADCTYT GPMSGATPGE CTDTAGYLSN YEIEQIIAGG
GVQQYSSDDG DILVYNQTQW VSWMNPSTYW DRLAWVQGLN FGGTSDWAMD LNQTFADADA
SNIVYISPDI WSEPDPTVAC YPPCTFVFPP WSLSTPTTIS RPPVTMTLEE TWPLIESLNG
NITTTGYTTG TTVTTITLPP VTTDLIQVWN YEWTDTEIVT VYITSSVPFP PILLTEDSPP
TQTQISTGTP FWYTYSPDPY PPYTGPSQTS SPTSIIPPPP PPPGSPGSVH VTQGPPSPTP
RPGNNPKNGH ICTANCIPEP PCLICGCIGP GCRGGGHCIG RGCSSGGGSN GGGDDTNSCS
TSHTADICTE YISSYSSTGM DSSSTITQTA CRTTTACEVL GTTITTTITT NCPACTLDPP
APDYTTMAPD PSNTLTWTIP AGDTTITGDP ASPTPSFISC DFYGEDPDRG ITSQYCVCSG
STFAPSSNTI VTPPNSCAYT TLPTNTVAVT TLTVTTTDTA ICSACTAVGL SETCTSLPNC
TPIPATTTTT TTTTSKPAPT KTSATCQITG WADLSEVVGS GGPGQVWTLP FCSASLRQNT
HPVNRPQSTT TNTVSLWATK MDLHWVVSRV IPSICIGRLW TVNLSDCLKT SCGLPPGM
//
