ID A2RBJ4_ASPNC Unreviewed; 1324 AA.
AC A2RBJ4;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Contig An19c0010, genomic contig {ECO:0000313|EMBL:CAK47332.1};
DE EC=3.2.1.58 {ECO:0000313|EMBL:CAK47332.1};
GN ORFNames=An19g00090 {ECO:0000313|EMBL:CAK47332.1};
OS Aspergillus niger (strain ATCC MYA-4892 / 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 {ECO:0000313|EMBL:CAK47332.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK47332.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
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., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.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).
CC -!- FUNCTION: Might have a role in sequestration of chitin oligosaccharides
CC (breakdown products of fungal cell walls that are released during
CC invasion and act as triggers of host immunity) to dampen host defense.
CC {ECO:0000256|ARBA:ARBA00037375}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; AM270415; CAK47332.1; -; Genomic_DNA.
DR CAZy; GH55; Glycoside Hydrolase Family 55.
DR EnsemblFungi; CAK47332; CAK47332; An19g00090.
DR VEuPathDB; FungiDB:An19g00090; -.
DR HOGENOM; CLU_002540_4_1_1; -.
DR Proteomes; UP000006706; Chromosome 4ER.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 2.
DR Gene3D; 3.10.350.10; LysM domain; 3.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR34997; AM15; 1.
DR PANTHER; PTHR34997:SF1; LYSM DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
DR PROSITE; PS51782; LYSM; 2.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycosidase {ECO:0000313|EMBL:CAK47332.1};
KW Hydrolase {ECO:0000313|EMBL:CAK47332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 1106..1152
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 1255..1303
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1324 AA; 144675 MW; 8F33CE51E6ADA7A7 CRC64;
MNEGRLAHPQ FNQYSFKAGA STVQAEAAPA LNYEDASTHN AAKNATKRSG RKGDQTYTYS
IPPELAEAAR LVAEASPQPV PTDYGVDISL VVSKYRKYDN NDTNVPKQKY VEPNGLDGYV
HTGQPEDSPE IHTELKKRAT TDFWLTQMGD SGSSPYAPDG YKVWRNVRDY GAKGDGITDD
TAAINKAISD GGRCGAECGS STIYPAFVYF PAGKYLVSSP IIQYYNTEFY GNPFDYPTIL
AASSFVGLGV ITSDVYTGDD TEWYINQNNF LRSIRNFKMD ITRTDPNAYV CAIHWQVAQG
TSLENIEFYM MQDGLTTQQG IYMENGSGGF LTNLTFVGGN FGYVYAFSQR CTPLSDLPSG
HTLATQFTST SLTFMNCKTA LQVHWDWAWT MQDVVVENCT NGIVIVGGAG GPKSTGQSVG
SLILVDAVIA HTQTGIVTTL LAENSTSFLL QGVVFIEVDT AILDSAQGKT LMAGGSNVPV
FSWGFGRVVT TGAESTFYNG QDIPRTNRSV PLTTIGYIEP NFYLRRRPTY RDIGMSQVIN
VKDWGAAGDG KTDDTAVLNS ILDRAANMSS IVFFPYGVYI IRDTLRVPVN SRIMGQVWSQ
IMATGPKFQD EQNPHIAVQV GQVGDRGIVE IQSLMFTVSG PTAGAVLMEW NVHQVIQGSA
GMWDSHFRVG GATGSQLQAD ECPKGSGVVL PACKAASLLL HLTSQSSAYL ENIWLWVADH
DLDLQDQAQI DVYSARGLLV ESQGPTWLYG TASEHNVLYQ YQVSQARDLY MGMIQTESPY
FQNVPPAPSP FSPGLFPNDP TFSDCDSDSQ TCPVSWALRI IDSTSVYSMG AGIYSWFSAY
SQDCLDTESC QQHAVGISQS TNTWLYNLVT KGIAEMVTPT NEHPTLSADN VNGFMSSILA
WVRLANTTIG ARKFPGFQLY QPKWLDGLTD TCKTALSQKI LCHPYLEMKF SNPGIGQYID
NNTLADEVCD QGCGESLQMW TTNVANSCLN QTIDDTDPVA AGGYIYAGYN LTCLRDPHTK
KYCPDVLSHF TIVDSVRSMT LAEMCSYCFT TSLEMRQASP YAAYTDVDKD ALETVNAECG
LSGPTDLHKP LYTEDEVDRP ICMSGITHTT SEGDTCDLLA YKYHVASAVI QLANPMLVND
CSELIPGRQL CMPLSCDTQY TLQDNDTCLS IEWAQPIGFG EVRRYNPWLN VDCTNLQTTR
QVHGSVLCLS PQGGSHNVTG TGSPCPGISD GYTNVVQYAP TNSTIAKGTT CYCGKWYTVQ
QGDSCATICI KQGIPSSLFL AVNPSLSTSD CDTSLQVGYT YCVGPDTHWD DTDNFWGEFA
CEAY
//
