ID M2QSU1_CERS8 Unreviewed; 330 AA.
AC M2QSU1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carbohydrate-binding module family 12 protein {ECO:0000313|EMBL:EMD40103.1};
GN ORFNames=CERSUDRAFT_81386 {ECO:0000313|EMBL:EMD40103.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD40103.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD40103.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD40103.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445793; EMD40103.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QSU1; -.
DR STRING; 914234.M2QSU1; -.
DR HOGENOM; CLU_072648_0_0_1; -.
DR OrthoDB; 1331412at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd12214; ChiA1_BD; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR006616; DM9_repeat.
DR PANTHER; PTHR31649; AGAP009604-PA; 1.
DR PANTHER; PTHR31649:SF1; NATTERIN-3-LIKE; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF11901; DM9; 2.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00696; DM9; 2.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT DOMAIN 2..48
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT REGION 47..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 36990 MW; 5B37E10BB8F0A77A CRC64;
MVYQWEPSTP YGSGAVVVYE GVKYQIIQPH TSEPGWEPPA TPALWARLPE EVPDNQDPFR
DNCNPGYQPS YEQPQAPPPQ PPYGGPGVEE KRWTEVQEQQ VEIDHEERKK KWWELDDDRK
KQLEVGGGLL AGIAAIGAGY YAYHEHEKSE DEKKANVWAL QNWLHEAEAR TRRYYEQGPS
GPANWVLTDG LNIPQGAIQG GEQQGQPLFI VRGFHEGSIQ IGKVSPAYSK GAVIGYGHKE
IQLPKYEVLC GDMRALQWVP SSGRVHLERL GARPVEGGHE ADGTPLFVAQ AETHDSIIPG
KASEKLSGAF VTFRDTEKEV DEYRVLCYNY
//
