ID D3E6W7_GEOS4 Unreviewed; 1289 AA.
AC D3E6W7;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Glycosyl hydrolase family 32 domain protein {ECO:0000313|EMBL:ACX66440.1};
GN OrderedLocusNames=GYMC10_4213 {ECO:0000313|EMBL:ACX66440.1};
OS Geobacillus sp. (strain Y412MC10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX66440.1, ECO:0000313|Proteomes:UP000002381};
RN [1] {ECO:0000313|Proteomes:UP000002381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Brumm P., Mead D.;
RT "Complete sequence of Geobacillus sp. Y412MC10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACX66440.1, ECO:0000313|Proteomes:UP000002381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y412MC10 {ECO:0000313|EMBL:ACX66440.1,
RC ECO:0000313|Proteomes:UP000002381};
RX PubMed=23408395; DOI=10.4056/sigs.2605792;
RA Mead D.A., Lucas S., Copeland A., Lapidus A., Cheng J.F., Bruce D.C.,
RA Goodwin L.A., Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C.S.,
RA Tapia R., Land M., Hauser L.J., Chang Y.J., Kyrpides N.C., Ivanova N.N.,
RA Ovchinnikova G., Woyke T., Brumm C., Hochstein R., Schoenfeld T., Brumm P.;
RT "Complete Genome Sequence of Paenibacillus strain Y4.12MC10, a Novel
RT Paenibacillus lautus strain Isolated from Obsidian Hot Spring in
RT Yellowstone National Park.";
RL Stand. Genomic Sci. 6:381-400(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902}.
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DR EMBL; CP001793; ACX66440.1; -; Genomic_DNA.
DR STRING; 481743.GYMC10_4213; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; CBM66; Carbohydrate-Binding Module Family 66.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR KEGG; gym:GYMC10_4213; -.
DR HOGENOM; CLU_265085_0_0_9; -.
DR Proteomes; UP000002381; Chromosome.
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; cd18622; GH32_Inu-like; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR010496; 3-keto-disaccharide_hydrolase.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR42800; EXOINULINASE INUD (AFU_ORTHOLOGUE AFUA_5G00480); 1.
DR PANTHER; PTHR42800:SF1; EXOINULINASE INUD (AFU_ORTHOLOGUE AFUA_5G00480); 1.
DR Pfam; PF06439; 3keto-disac_hyd; 2.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACX66440.1}.
FT DOMAIN 1163..1288
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 1289 AA; 141840 MW; 2F173DBC16C97817 CRC64;
MFGLILPISR VVKNPKRGGY MKLPQDVHTM LLRTLSAITM SLLLATSVIP ASAASVIQEA
NAALKGEGEN DIFESVSNVN TNLEGWQLKG KGKMEQTAEG LRLSSDSSEN AAAISSTRAD
DFVYEADVMI TDMQADASLV FRSSVDGWSS YMLQIVPSAG LVRLKDAREG DGRLKVEKAV
ALSRGDIVHL KVKVVGSNIK VYWGSQYEPM IEVDDTAYST GYLGLHVWDG SALFQNIKVS
EWKGNLFGPA ATSGDWQPDI KGLKGSASKG LEAYRIYKNA AADYVLEGNI TLGGQAEAGF
YWRGNDQGTE GYEAVFRRED DQVRVTLETS DGKVIGASSR TYPSLPTSAH HVEIHVSEDS
IQIAVDGYEP AAIRVSDSSY AGGSIGMKVK SGTAYFQDVY VTPMADYYTE EYRPQYHYSP
IRGSASDPNG LVYFEGEYHL FHQDGGQWAH AVSRDLVHWN RLPIALPWND LGHVWSGSAV
ADTTNASGLF GDSGGKGLIA YYTSFNPDRP GGNQKIGLAY STDHGRTWTY SKERPILIEN
PGKQGEDPGG WDFRDPKVVR DEANNRWIMV VSGGDHIRFF TSDNLVDWTL TDRFGYGEYI
RGGVWECPDL FQLAVDGSGQ RKWVLMISSG ANPNTQGSDA EYFIGDVTPD GKFMNDHTAG
NVLRTDWGKE FYASMSFSDL PDNRRIMLAW MTNWDYPFSF PTSGWKGQLT IPRELSLRTT
SEGIRLHQSP IAELETLRKT VIHVNNRQVT ETSQNVLKGI QAGAFEIEAE VEIPTDSSEL
EFGFRLREGG GQQTVVGYNN SAHHMFIDRS ASGTTDFSSL FSTEHKALLH PVDGVVKLRI
YVDESSVEVF GNDGNIVFSD VIFPDRARRG MSFYTLGGQV KLKSLKVHEL DSVWRPLDPS
EPGSRILLDS YELDLSRGQT ESLYAAVDRV PGNGKKPLVW TSSHPDTVRI VSSDETHAVL
KAANAGEAVI TASTPNGKIS ASTRVLVSSG TFKTNLTGWK PDLKASKWVL TEHGIRGSHS
SDANYMAQER AGDFTFEGDM RLGEAGGAGS MLFRASGDGR SGYYLNLDPG LKSIRLFYMV
EGRFEERQVL ASVPGFIQGG RTYHLRIEAK GPHIQVDVDG KKVIDVMDGT FAEGHFGVNV
FGGQASYQNV YVRHPSEARL TKTSFTNEAV NKAIHTEKSV NGEPVTVKES TGTGNLLWVW
VPTGEEGTYS IRTPEGKALD VDTGQNRIQL YTYLGYNNQR WRVERQEDDT VTIRSVHDGR
ALAVKADGSG LELNEPDAAS DRQRWRLGL
//
