ID I4EXP8_9ACTN Unreviewed; 724 AA.
AC I4EXP8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:CCH88161.1};
GN OrderedLocusNames=MODMU_2732 {ECO:0000313|EMBL:CCH88161.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88161.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH88161.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH88161.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; FO203431; CCH88161.1; -; Genomic_DNA.
DR RefSeq; WP_014740753.1; NC_017955.1.
DR AlphaFoldDB; I4EXP8; -.
DR STRING; 477641.MODMU_2732; -.
DR KEGG; mmar:MODMU_2732; -.
DR PATRIC; fig|477641.3.peg.2589; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_11; -.
DR OMA; PYYYNHK; -.
DR OrthoDB; 9803863at2; -.
DR Proteomes; UP000006461; 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 Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCH88161.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT DOMAIN 643..713
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 724 AA; 76418 MW; 81AF04A10E85778F CRC64;
MNAGTDVDAL IARMSWTEKL AQLQVGYRPQ LEDAAELVRG GIGAVFWPRS AEATNELQRV
ALEETPHGIP LLVGLDVVHG QRTTFPIPLA QAASFDPAVA ETDGRVSAAE AASGGVTWTY
APMIDVSRDP RWGRVAEGFG EDTLLNAVFG AAKVRGYQGS DLADPGSILA CAKHYVAYGA
AEGGRDYDTA DVSASRLRNV YLEPFRAAVE AGAATVMASF NTVDGRPVHA SRELLTDVLK
EEWGFTGAVV GDADGVVNLL AHGIAEDLHD ALVQSLSAGL DVEMGGHVIA PDGTTSLTPD
DVTVARVDDA VRRVLRLKVA LGLFDHPYVD RAAEVAAPTA ATRSAAREAA ERCPVLLAND
GTLPLADGPL RVLLTGPYAD STDHLGAWVQ SFAEPAGSLA DALRAERPDL EVTVLPGASF
DGTDPARQEE VARAAAGCDV VLVAVGEPSH LTGEASSRAD LRLPGDQEAL VHAVADTGVP
FAVVLANGRP LVTSDWIDRA PAVLEAWHLG LEAAPAIARV LTGAVNPAGR LPMSFPRSAG
QVPVHYDHDN TGRPATTGGS MQPLSHDIGL QGPANVQEWF TSKYRDLPLG PQFAFGHGLS
YTTFSYGTPV LSRAQLSADE LRGGTAVEVS VEVTNTGQRA GDEVVQLYLR DPVASLAQPV
RRLRGFRRLP LEPGESATVT LSLGWRDLGF WTGRGEEFVV EPGRFELHVG GSLESTQQCD
LVVT
//