ID D9TD70_MICAI Unreviewed; 382 AA.
AC D9TD70;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Glycoside hydrolase family 12 {ECO:0000313|EMBL:ADL44708.1};
GN OrderedLocusNames=Micau_1146 {ECO:0000313|EMBL:ADL44708.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL44708.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL44708.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC {ECO:0000256|ARBA:ARBA00005519, ECO:0000256|RuleBase:RU361163}.
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DR EMBL; CP002162; ADL44708.1; -; Genomic_DNA.
DR RefSeq; WP_013284347.1; NC_014391.1.
DR AlphaFoldDB; D9TD70; -.
DR STRING; 644283.Micau_1146; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH12; Glycoside Hydrolase Family 12.
DR KEGG; mau:Micau_1146; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_060511_0_0_11; -.
DR OrthoDB; 2557744at2; -.
DR Proteomes; UP000001908; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.180; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR002594; GH12.
DR PANTHER; PTHR34002; BLR1656 PROTEIN; 1.
DR PANTHER; PTHR34002:SF9; XYLOGLUCAN-SPECIFIC ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF01670; Glyco_hydro_12; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361163};
KW Glycosidase {ECO:0000256|RuleBase:RU361163};
KW Hydrolase {ECO:0000256|RuleBase:RU361163, ECO:0000313|EMBL:ADL44708.1};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361163};
KW Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..382
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038849438"
FT DOMAIN 272..382
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 249..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 39456 MW; C650038B0A4A2D63 CRC64;
MKRPLRALAA AGLLAAGTLV AVALGGTASA DTQICEQYGS TTIGGKYVVQ NNRWGTSAQQ
CINVTSTGFS ITRADGSAPT NGAPVAYPSI FVGCHYTNCS PGTNLPVQVK NISSAPSSIS
YNYVSGAIFN ASYDIWLDPS PKRDGVNQME IMIWLNRQGS IQPIGSPVGT ASIAGRTWEV
WRGSNGSNNV ISYLSPSAIP SFSFDAMAFI NDTRNRGAIT NDWYLTSIQA GFEPWQGGVG
LAVNSFSQSV NTGSNPPPTS APPTTSAPTT PPPSGGASCT VTYKAANVWN NGFTADVTVK
NTGSGTINGW TLNYNLPSGQ TVTNAWNATV SQSGSAVTAR NAGYNGTLAP GASTSFGYQA
TLNGSYSAPS SFTLNGSTCA RG
//
