ID A0A0J1G4N6_9FIRM Unreviewed; 812 AA.
AC A0A0J1G4N6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|PROSITE:PS50022};
GN ORFNames=RHS_3625 {ECO:0000313|EMBL:KLU70612.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU70612.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU70612.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU70612.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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:KLU70612.1}.
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DR EMBL; JNGB01000038; KLU70612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1G4N6; -.
DR PATRIC; fig|1504536.3.peg.4552; -.
DR Proteomes; UP000036477; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR SMART; SM00710; PbH1; 3.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Reference proteome {ECO:0000313|Proteomes:UP000036477};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..812
FT /note="F5/8 type C domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005251295"
FT DOMAIN 654..786
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 812 AA; 88570 MW; 7524F66958B59FF7 CRC64;
MKKKFLSFML AVALVCSTQA FSTMPYVNAA ETAGVGTAYY ISSRNGDNGN SGTSEGEAWE
TLDKLENVTL GPGDSVLLES GSIFNGFIHL QNVGGTQENP ISISSYGEGN KPVINCNGEG
IWYQDYGKAM DNSGHRSSGY VSSAILLYDV DYVEISNLEI TNKSNDFDYF STNVNKASGR
MDRTGVAGIA KDGGTMEHIY LDDLFIHDIS GNLQDKHMNN GGIQMNVLKP ADENATGIAR
YQDVKISNCY VKDVSRAGIV VGYTYQHDKF NGAALADETV KKYGHTNLVL EGNYVQNAGN
DAIVAMYAYQ PVIQNNVSDT AGVDLDDGYP GYWQSFCAAI WPWKCKDAVF QYNEAFDTVG
EGNGDGQAWD IDWSDGTVYQ YNYSHNNGGG AMLICLNEAY NGTFRYNLSQ NDLKCLITFQ
GNPLAKIYNN VFYVGGDLET AVHHPAAGKR SGAGYLANNI FYNVSTNKNV SDDGWNPGNN
KSFKNNLYYG YSDEGMPGLP EADAITADPK FENPGSAPVT VNEGGKIHDR SAFEGYKIAD
NSPAVNAGVY IPNNATEDFF GNKLTGIVPD IGIHETGIEE SVSLNVYSDR YLIQEQDIRN
VPQGTTAEDF LKNIKASAKA ECKVMKGSEQ VAPDTAVTEE MVLKVVNKAN DQETKTYNIH
VVKVYAEYAT EGMTATAGSF QPNNTTEGNP SYVLDNNMNT IWHTAWSGCD RSEAWISIDM
GKEQSVGMLK YVPRKAGGVN GLITEYEVSV STNGTDWTKA ATGSWENNSE IKYAEFPSVN
ARYVKLWAKD SKSQEAGKVF ASAAEIRLGY EE
//