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Database: UniProt
Entry: K1WN25_MARBU
LinkDB: K1WN25_MARBU
Original site: K1WN25_MARBU 
ID   K1WN25_MARBU            Unreviewed;       373 AA.
AC   K1WN25;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Putative endo-beta-1,4-glucanase D {ECO:0000313|EMBL:EKD13722.1};
GN   ORFNames=MBM_07923 {ECO:0000313|EMBL:EKD13722.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD13722.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD13722.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD13722.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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DR   EMBL; JH921448; EKD13722.1; -; Genomic_DNA.
DR   RefSeq; XP_007295812.1; XM_007295750.1.
DR   AlphaFoldDB; K1WN25; -.
DR   STRING; 1072389.K1WN25; -.
DR   GeneID; 18763858; -.
DR   KEGG; mbe:MBM_07923; -.
DR   eggNOG; ENOG502QVJU; Eukaryota.
DR   HOGENOM; CLU_038296_0_0_1; -.
DR   InParanoid; K1WN25; -.
DR   OMA; MWRTELI; -.
DR   OrthoDB; 2728405at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.1160; -; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR041524; GH131_N.
DR   PANTHER; PTHR34612; GH131_N DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34612:SF6; GLYCOSIDE HYDROLASE 131 CATALYTIC N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF18271; GH131_N; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          337..373
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          266..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   373 AA;  38745 MW;  7D198700889102B7 CRC64;
     MRFSVSYFAA LVGAASSSII WDGRFNTFAS STDLNNWSWS NQVGPYQYYI QHHQHGSSAV
     TSYVNLSPSF KNAADSGSTQ GAKFTLDSTA YWNGQPMRRI ELIPQTTAVI ATGKVWYHFS
     MMRSATNAPS TYREHQINFF ESHFTEMKSG WISGAAGTSN PALQWFVGGT SKWSTTWDAG
     VWHNVAYEID FSAKTVAFWH STGAAPLALT VAAVSASTAS NGADWHLGVL ELPVSGQADA
     NEDFYFSGVY IESGSLTTSV AGPGGGGGGV VVSSSSPASP GSSSSSSSSS SSTSARSTSS
     STSAASSVVA TTARPTSLST TSSVGVTTSS APAAGGGAIP KYAQCAGLTW TGSGTCVAGT
     TCKYSSDYYS QCL
//
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