ID A0A166YIP5_9PEZI Unreviewed; 652 AA.
AC A0A166YIP5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Chitin binding protein (Polysaccharide deacetylase) {ECO:0000313|EMBL:KZL77701.1};
GN ORFNames=CT0861_06331 {ECO:0000313|EMBL:KZL77701.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL77701.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL77701.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL77701.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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}.
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:KZL77701.1}.
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DR EMBL; LFIV01000006; KZL77701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166YIP5; -.
DR STRING; 708197.A0A166YIP5; -.
DR OrthoDB; 2474766at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.30.60.10; Endochitinase-like; 3.
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; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00270; ChtBD1; 3.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 3.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 3.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..652
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007882793"
FT TRANSMEM 535..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..123
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 157..349
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 417..463
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 485..532
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT REGION 46..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 89..101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 94..108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 436..450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 505..519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 652 AA; 71984 MW; 5B47ABAB69EF3986 CRC64;
MRWFPVLLAT LAGLEAAQAH RDGPHVKLAV PHRRRVEDLR QKRNAFEPWN PPTVANKPRG
HRRNHLSPRQ TTAIAVGDNS RCGGTYGRCA DGYCCSASGW CGQTASYCSS PDCQISYGPA
CDGNQKPSGA DTSGDARPLK GSVPYGGVGI YNCVNDGDVA ITYDDGPYIY TAAMLDAFKA
HGAVATWFIT GNNIGKGMIN VAYSDVIQRM VADGHQIASH TWSHENLDQM TQEQRKNQMV
YNEIAFQSIL GFYPTYMRPP YSICGQDCQA QMLELGYHIT YFDLDTQGYL HTDPSQIAFS
VGLWDQAMQA RSPCNGSYLH IEHDIHQQIA TTLTNHILDS VVANGWNAVT VGTCLGDPPE
NWYRGNVPSY NFKITPVSAP VCSSTATSNS LLNLTGSAVL TGTSATSTSI ALAISLDAAC
GSVSGQTCQG STFGDCCSQY GYCGKTEFHC GAGCQSGFGK CTTSDSSSST AVNSGTVSAL
LVSLTGSCGA NNGNATCAGS IFGNCCSQYG YCGSDIDFCG TGCQSDFGSC GESIFWIHVY
FVFCIHVYFI LCYNVSVVFC DYRYVQFTFK NHVFFVQYHN HIYFIIQHHV QFVFENHIYF
IQYHIYFIIQ HHVQFVFENH IYFIIQHHVQ FVFKNHVYFI QYYIYIIIKH HF
//
