ID A0A0F4ZL77_9PEZI Unreviewed; 833 AA.
AC A0A0F4ZL77;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN ORFNames=TD95_000828 {ECO:0000313|EMBL:KKA30608.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA30608.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA30608.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA30608.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:KKA30608.1}.
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DR EMBL; LAEV01000350; KKA30608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZL77; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000033483; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd09630; CDH_like_cytochrome; 1.
DR Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR015920; Cellobiose_DH_cyt.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR47190:SF2; CELLOBIOSE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_2G17620); 1.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF16010; CDH-cyt; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000033483};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..833
FT /note="CBM1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002482954"
FT DOMAIN 796..832
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 833 AA; 89276 MW; B2DF228E1C42790A CRC64;
MSLVILFFAY LGLCLAQYTA TKYTDENTGI IFNAWSAPDG ATSGYLTIGI ALPQDALDTD
ANEFIGILKC ASPNGKGTGW CGISIGGPMT QNLLLTIYPQ HEDILTSFMY ATGYVMPEAY
TGDAFITQIS SNITDDGYEL IYRCQNCLSW NQNGQESSAS TSSGSVIIGW CHGYDSPTNA
ECPAELSLVQ HNTQGIFAAA FNSEAVDPSY TSWTALATST VTGNCGGSSA TVTATATSST
ALSTTVTGVP IPTETFDYIV IGSGAGGIPL ADRLSEAGKS VLLIEKGPPS SARWGGTIKP
DWLADSNLTR FDVPGLCNQI WVDSEGIACR DTDQMAGCVV GGGTAVNAGL WWKPYSLDWD
YIFPEGWKAD DMQAATDTAF NRIPGTTIPS EDGTLYLQQG FDIISSALNN SGWTSVNALE
SPDAKNHTYT HTPYMFSHGE RGGPMATYLV SASARDNFKL WTGTSVKRVI RQGGHVTGVE
VEPYIPGGYS GVVNVTAGSG RVVLSAGTFG SAKILLRSGI GPSDQLAIVK SSTDGPTMID
SKSWIPLPVG SNLEDHTNTD IVVSHPDVEF YDFYAAYQSP ITSDKELYLN ERSGILAQSA
PNIGPIFFDE IEGADGVVRQ LQWTARVEGG HGFTSNTSMV LSQYLGRGSK SRGRMTITRS
LNTIVSDAPY LKDKEDVLAV IQGIKNLKAA LDKVEGLNYT YPAPGTSVED FVNEMVVSYS
NRRSNHWIGT NKMGTDDGRF GGSAVVDTNT KVYGTDNLFV VDASIFPGMV TTNPTSYIVT
VAEHAAGKIL ALPETKGLSK YSQCGGERWN GDSYCEEPYT CTYQNDFYWQ CLD
//
