ID R7YHQ8_CONA1 Unreviewed; 685 AA.
AC R7YHQ8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chitin deacetylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=W97_00373 {ECO:0000313|EMBL:EON61161.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON61161.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; JH767555; EON61161.1; -; Genomic_DNA.
DR RefSeq; XP_007776478.1; XM_007778288.1.
DR AlphaFoldDB; R7YHQ8; -.
DR STRING; 1168221.R7YHQ8; -.
DR GeneID; 19897684; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR HOGENOM; CLU_021264_11_3_1; -.
DR OMA; HEQTAMN; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000016924; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10951; CE4_ClCDA_like; 1.
DR CDD; cd00035; ChtBD1; 1.
DR CDD; cd11618; ChtBD1_1; 3.
DR Gene3D; 3.30.60.10; Endochitinase-like; 4.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR46471:SF4; CHITIN DEACETYLASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 2.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00270; ChtBD1; 4.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 4.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 4.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Reference proteome {ECO:0000313|Proteomes:UP000016924};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..685
FT /note="Chitin deacetylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004449770"
FT DOMAIN 67..111
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 145..342
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 392..438
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 469..515
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 545..591
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 77..89
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 82..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 411..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 488..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 564..578
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 685 AA; 69242 MW; 3289F0D43E9036F2 CRC64;
MHFPSVLVAS AALPALITAH GSEGMPQIFG RRSVAELKAR NIMGPVRGEG SFEKRAGLEA
RQGGNAEGRC GANIGTCAAG YCCSSAGWCG QGKDYCAAPD CQFLYGPGCD ANTVPAGTNT
STVARPLSGN VPYGGAGVFD CVVPGTVAIT YDDGPYIYTD AVLDIFASYG AKASFFITGN
NLGKGQIDNA ANPWAAMIRR MHAEGHQIAS HSWSHQDLSA VSRWERKNQM WKNEMALRNI
LGFFPTYMRP PYSSCTAASG CEADMRELGY HVTNFDLDTD DYNNVTPELQ QNAKNRFSNA
LSGSNPGADE FLAIAHDIHY QTAYNLTGYM LDTLYKAGYR AVTVGECLGD PVANWYRSSS
GSVISSASSS AGPTLSATSS APAASATKAS TDGSCGGTTG QTCLGAAFGN CCSQYGWCGA
TADHCGTGCQ PGFGNCGSNG ASSSAAPTST VASSSSSAPP ASTNKVSVDG SCSGTTGQTC
AGSTFGNCCS QYGWCGSTAD HCGTGCQSGF GNCGSNGASS AVPTSARPSS TSSAPPAGTN
KVSVDGTCSG TTGQTCAGST FGVCCSQYGW CGSTVDHCGA GCQAGFGSCS VGGSGSVASS
SPLISSSAMT APVTTSRASS VAPSATSAPP ATVTKVSTDG NCGAAAGMTC RGSTFGKCCN
ASNRCGNSLS RDCQRGCQKA YGQCL
//
