ID R7GAD5_9FIRM Unreviewed; 1423 AA.
AC R7GAD5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|PROSITE:PS50022};
GN ORFNames=BN631_00364 {ECO:0000313|EMBL:CDE23728.1};
OS Amedibacillus dolichus CAG:375.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Amedibacillus.
OX NCBI_TaxID=1263076 {ECO:0000313|EMBL:CDE23728.1, ECO:0000313|Proteomes:UP000018093};
RN [1] {ECO:0000313|EMBL:CDE23728.1, ECO:0000313|Proteomes:UP000018093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:375 {ECO:0000313|Proteomes:UP000018093};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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:CDE23728.1}.
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DR EMBL; CBIN010000291; CDE23728.1; -; Genomic_DNA.
DR Proteomes; UP000018093; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06564; GH20_DspB_LnbB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS50022; FA58C_3; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018093};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1395..1413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..181
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 957..1102
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT ACT_SITE 566
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 1423 AA; 162134 MW; 58C94970CF1D2563 CRC64;
MMKKLSGGIL VALVINMIFS FIFQSTIIAN DGVDEVENEK LINIAMNEKA IATASSEWND
DKSASKVRDG IVSKDSRWVS KYENGVEKPE WVKIDLGDVY SIDEVRINFE AAYASEYTIS
SSLDDESYDV IKTVTDGKVG ENIQADLESK KARYVKLDLT KQGREDKKYG FSIYEIEVYD
YSKTEEIPMT AEMWAQQLES IPPIISADGS KIELPKIDSD IYEVSLFGSD NQQVVAMDGR
IIQPLQDMKV NLLYKIQNKK DSTDFATTSK DVSIVIPGKY KMSENDNLRP QVIPGIREWK
GYTGNFTLLD DSKIIVTDES LTETATTIQS YFKEMLGINI AIGNGVSKKG DVVLTLDNAN
ELGNEGYYLN IDDIITISAP STKGILYGGI TVTQILYQSS NRITAPKGLV RDYPKYEVRS
GMIDVGRVYI PLEYLKEITM YMSWFKLNEI QVHINDYWGA SGYTAFRLES DVYPEIVSKD
GYYSKDDYRK YQQDMLKYGV DVITEIDTPY HAESFRAIEG VKMLKKGALD IRDPFSYEVV
ENLIDEYLDG PNPAIISDNF HIGTDEYDQK YPEEMRKWTD HFINYVNNKG KNSRLWGSLG
GGSASNGFEG TTPVSNEATM NIWAPYWSDV KEMYKAGYDI INTCGGWLYI VPAGNAGYPD
RLNIQELYDK FDVNNFEPNR KVGNGSAIMP VAHPQTKGAE FAIWNDNTSF NIGFSEFDLF
DRIKDAILIT SEKTWYGEKT EGQTSEQFMQ RVNLYSDKVP LANPGRYVPS KGTTIVEYDS
ESAKKDTLID ISGNGNDAII YDASIKDDFI NFDEKSSYMK LPMQSIGYPY TMSMDLMINE
YDENSILFTG KDGTLYANID GTGKIGYERL HGRFIFDYTL PKNKLINLTL VCDENDLYLY
IDGVLVSNGA LIEKPIKGKE QKSSTFVLPC EEVFKDINVS LANFKIYNYA MSKDEIAKLY
NVTGYSENLA LNKEVTVSSY YSEDTLPKNL TDGNDSTRWG SKYKNGVEKP EWVVIDLGDT
YLIDEIRISW ENAYASGYTI QGSIDGKTYT DIINVTDGNG SLDVLKELGD QPARYLKIDM
HTQGREDKKY GFSIWEVEVY ENPNTQVKRV SSNALDVLKT YTRGYEKGNF PVEIYDEWET
TFKEYYQRAE KEKLNEFEKV NIITDITNKL NRVDEILLRE ALVDKEILRK EYEQAVSLNA
DDYVEESYLE LQKQLEEAKE VLDNPASTQI EVDNMLDSLR NSVQTLLPIS RIIISEDGLV
EIEGNLPQDV ILKVEEIDPN IIQDDIINEY DIHELYKFEL YRNGEIYIPI NEIKVKINST
KDYLQKNPKV ISYNNEKETK FIEFKYDGKS FDFKTDTLSS YGIITRKEST EEILPKPIEP
ENEDSLPNTG DNSKIMLYQM LFILSGVAFI FALKNIRNQD DKK
//
