ID Q2HA51_CHAGB Unreviewed; 572 AA.
AC Q2HA51;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAQ90968.1};
GN ORFNames=CHGG_02903 {ECO:0000313|EMBL:EAQ90968.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ90968.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ90968.1; -; Genomic_DNA.
DR RefSeq; XP_001229419.1; XM_001229418.1.
DR AlphaFoldDB; Q2HA51; -.
DR SMR; Q2HA51; -.
DR STRING; 306901.Q2HA51; -.
DR GeneID; 4389134; -.
DR VEuPathDB; FungiDB:CHGG_02903; -.
DR eggNOG; ENOG502QRIP; Eukaryota.
DR HOGENOM; CLU_021264_11_3_1; -.
DR InParanoid; Q2HA51; -.
DR OMA; ASGCQKD; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000001056; 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; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 2.
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:SF7; CHITIN BINDING PROTEIN; 1.
DR PANTHER; PTHR46471; CHITIN DEACETYLASE; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 2.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 2.
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:UP000001056};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..572
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004209086"
FT DOMAIN 76..120
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 154..349
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT DOMAIN 406..452
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT REGION 49..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 86..98
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 91..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 409..424
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 423..437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 572 AA; 60225 MW; 8BFA156E8F24E543 CRC64;
MKLSSAILAA SLGLAWAHDD RGQHVPKLLG LRKFVSGLEA RRRAAFDEQP IAARSQHLPA
NQRRSLKGRQ DDDDNEGRCG PGIGACPNGE CCSFEGWCGR GLDYCSAPDC QINYGSGCDA
NQKPGGADTS GVARPKLGSV QYGGAGIYDC ENPGDIALTF DDGPYIYTND LLDKLKSYGA
KATFFITGTN LGKGKINDPA TIYPAIIKRM HAEGHQVASH TWAHQNASQL TNQQFTDHMV
WNEIALNSIL GFFPTYMRPP YSICERNCQS ILSTLGYHII YFDLDTEGYL HDSQQEIQTS
KNIWDDAIDG ANPSSDSYLQ IEHDIHYQTV YNLTDYVLTS LFAAGFRAVT VGECLGDPAT
NWYRTGPTGG VVPSGSVAPT STSTPPTGPT RTTISVAPTR TGASIDGSCG NGVTCAGTEF
GSCCSVFGYC GVGDDFCSVD RGCQPDWGTC GGDGTVPSSS VKPTSSVKPT TSTAKPPTSS
AKPPTSSAKP TSFSTKTTTT TTNKSTPATS TTPKPTQTGL AISTDGRCGP EVKQTCTGSG
LGNCCSPAGK CSSNTISCLA ILGCQVGYGS CV
//
