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Database: UniProt
Entry: A0A0J1G4N6_9FIRM
LinkDB: A0A0J1G4N6_9FIRM
Original site: A0A0J1G4N6_9FIRM 
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
//
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