ID A0A416EQW4_9FIRM Unreviewed; 716 AA.
AC A0A416EQW4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=SH3b domain-containing protein {ECO:0000259|PROSITE:PS51781};
GN ORFNames=DWZ56_03520 {ECO:0000313|EMBL:RHP35579.1};
OS Lachnotalea sp. AF33-28.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=2292046 {ECO:0000313|EMBL:RHP35579.1, ECO:0000313|Proteomes:UP000285302};
RN [1] {ECO:0000313|EMBL:RHP35579.1, ECO:0000313|Proteomes:UP000285302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF33-28 {ECO:0000313|EMBL:RHP35579.1,
RC ECO:0000313|Proteomes:UP000285302};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC {ECO:0000256|ARBA:ARBA00010646}.
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:RHP35579.1}.
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DR EMBL; QUEE01000002; RHP35579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416EQW4; -.
DR OrthoDB; 9765879at2; -.
DR Proteomes; UP000285302; Unassembled WGS sequence.
DR GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06414; GH25_LytC-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR34135; LYSOZYME; 1.
DR PANTHER; PTHR34135:SF2; LYSOZYME; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF01183; Glyco_hydro_25; 1.
DR Pfam; PF08239; SH3_3; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49478; Cna protein B-type domain; 1.
DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
DR PROSITE; PS51781; SH3B; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000285302}.
FT DOMAIN 484..547
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT REGION 121..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 77116 MW; F3250677553C0A98 CRC64;
MKEKLTSLLA KMAPYKIPIL CGVLVVVLGV TAVIAVPIAM NAGTDGTQAV AGANTDPTED
TQVENIQESP RQLADFNLAE PMKVINPTTV HSVGVIGATE APTEAEEPVE VEHKVIEKEK
LPEVDKAPVN DAADPGDGAD DAGNAADVDI SDIAKGDYES QGMSLGIDVS HHQGSINWQQ
VKDSGIEFAM IRVGYRSRDT GTIYEDRQAA ANMKGALAAG LKVGVYFFSQ AINEYEAVEE
ASWVVNYVSK YQITYPIVYD CEYIGQYRTA AAGVTKSQRT DYAIAFMETV KSAGYSPMMY
ASKNGYANNW ETDRLSNRYK IWVAQYPGSV NPVTDKSSYT GKHQMWQYTS KGSVPGISGN
VDMNVAYFKY TGTPDASVTN VKFVVKDNSG KAVKGATVQM AGATTNSAIT DETGTAVFTY
VPFGDYTVTV SGVPNGYKKT GKIVQVNFSK YQAEYVDSTS FVLEPGQDDS TTFPVGDETF
TRVNKQVKVT ASTLNVREFN NTSSRVLGKV TKNTVLKCTA TGSGSWIQVE YNGQTGYVSR
DYVTFVDESS SCVNGHTKDT PTYTKVDDKT HKVTYICKVC KEEIKDAAVT ENHTWDDGKV
TTAAICGKDG VKTYTCTKCG ATKTEVIPAP GKTHKWEKQS DGTYKCTVCG EVKEDVTDSS
TETETESTEE SSSETESSTA PTQSTEPSST EPVTEAPTES STPAESTTSN VSGNSL
//
