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Database: UniProt
Entry: A8RE63_9FIRM
LinkDB: A8RE63_9FIRM
Original site: A8RE63_9FIRM 
ID   A8RE63_9FIRM            Unreviewed;      2314 AA.
AC   A8RE63;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=F5/8 type C domain protein {ECO:0000313|EMBL:EDP10457.1};
GN   ORFNames=EUBDOL_01701 {ECO:0000313|EMBL:EDP10457.1};
OS   Amedibacillus dolichus DSM 3991.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Amedibacillus.
OX   NCBI_TaxID=428127 {ECO:0000313|EMBL:EDP10457.1, ECO:0000313|Proteomes:UP000004090};
RN   [1] {ECO:0000313|EMBL:EDP10457.1, ECO:0000313|Proteomes:UP000004090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10457.1,
RC   ECO:0000313|Proteomes:UP000004090};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Eubacterium dolichum (DSM 3991).";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDP10457.1, ECO:0000313|Proteomes:UP000004090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP10457.1,
RC   ECO:0000313|Proteomes:UP000004090};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806}.
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:EDP10457.1}.
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DR   EMBL; ABAW02000024; EDP10457.1; -; Genomic_DNA.
DR   RefSeq; WP_004800332.1; NZ_DS483477.1.
DR   STRING; 428127.EUBDOL_01701; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   GeneID; 83059832; -.
DR   eggNOG; COG1501; Bacteria.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_001337_1_1_9; -.
DR   Proteomes; UP000004090; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   CDD; cd08759; Type_III_cohesin_like; 1.
DR   Gene3D; 2.60.40.1080; -; 2.
DR   Gene3D; 2.60.40.680; -; 1.
DR   Gene3D; 1.20.1270.90; AF1782-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF00754; F5_F8_type_C; 3.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SMART; SM00635; BID_2; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   PROSITE; PS50022; FA58C_3; 3.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          955..1035
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1025..1195
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          1441..1570
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          1736..1896
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          303..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2248..2284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2259..2284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2314 AA;  253017 MW;  B4FCF9BD92F0AB0B CRC64;
     MFKKVVASGL SLMMVLSSTG YQQLVQVHAE TNMLSKQLSG IKSVEADKSE KNVVWVTFTN
     GYKGKLTFLD NGIFRYNVDP KGEFSEYATP RSSAHKARIQ QYPDDSDKYK HPEATVTNQG
     GVYTISAGDV TVTFNQQALM SVKSGNKVVL QETSPLSIGD RSVVQTLAKN DNENYYGGGT
     QNGRFVHTGK TINIANESGW NDGQVSSPNP FYWSTAGYGV LRNTFADGKY DFGETNSETA
     TATHDEGEFD AYYFVSDGAN GAEVSQDILQ EYFKVTGNPA LLPEYGFYEG HLNCYNRDAW
     ADGEQKADPS KGNKTWVTTN PDGTEFKQTE AGGTGYEIKE NLQSESLMGK GPTTKNNVPS
     GVTTPEQFSA KAVLDRYVEN DMPLGYFLPN DGYGCGYGQN GYKVTGGVEA DGSSNAERTA
     AIDANVANLK EFTDYANSKG VDTGLWTQSQ LSPDSNNNTS WHLLRDFKKE VKNGGITTLK
     TDVAWVGQGY SMQLDGVKTA YDTITTEVNK RPNIISLDGW AGSQRFNSVW TGDQAGGNWE
     YIRFHIPTYI GQSLSGNPNI GSDMDGIHGG APLIATRDYQ WKTFTPQMLN MDGWGTYTKA
     PHAFADPYKS TSRMYLKLKG QLLPYIYTSA ASASNLNTKN GDTGLPMIRA MFLEFPNDDY
     AYSKNMQYQY MFGDAFLVAP VYQNTELNEE TGADIRNDIY LPKGETWIDY FTGEQYRGGT
     VINNFDAPLW KLPLFVKNGS IVPMYEENNS PDKINRANRI VEFWPEGEST YTAYEDDGKS
     ITNKTEKDED YGVIDNISYG NHSELTYKSV VNEEKKQATL TAEKVNVTGS YDGYSAEKNT
     TFVVNVSKKP TKLTAKNGSS TLKNVEVNSK AEFDAKTPNA GEAVFFYDAN PTIETYANEH
     ETKIKEMVKD VKVAPKLYVK FAKTNATENA QQLVIDGFVN DGNLPNDGEN ASLDAPKNIE
     YKPSSDSIAL TWDEVEGATS YDVEADGIVY SMLEKPAYTH SGLNYLEKHT YRVRSVNKDG
     HSEWSELKEV STLDDPYRNV PKGMTVSYDQ GNTPAAYAGK FEYMVDGDDV TEYSSADAGV
     FNGKSFTIDM KKIYSINKLD YVFRQDGSNG TIKKFKLSYS NDGVNWKKYK DGEEINLTPT
     TQWPLGDKNK LNTQNVNARY ATVDLEQFKA RYIKVELVET AGGFLQAYEI RPYHVDKDKG
     VMPGDFEANG IINDNDEVWL DSHNPEAAGA RKGGAFYESD ANKFDLNENG IFDAYDIAVL
     TTQLNGGVKE KTNASGVLSA VPSKQNVKAG ETFTVDIYGS GLKNVYAFDF ELSFDKGALS
     YSDDDFVVKT TAKTRNQKVY EYLHHEETDE KDRVYATITN LGNQTSLNGD MKLATVTLKA
     NKELDLSNLQ LSHGLVVGSS LNYVNGLDPV KPNEPSDMVE KRLVAHEDIV KAKAKSNGPV
     GDGNDIWASL DQNNSTYTNS NYGNAANAHP QVYTFELKDK MSLSKVGVRP RSANHYGQLG
     SFKVFVSDDK NTWTPVSDKV TVNATTADSE GYTSVELPKG TSAKYVKLEL EPATADGNCV
     ATSEVAIYSA ASVKPTSIVF EKDTMELHIG HLTPVKAIVA PEDAANKLYE VTSDNSKVKV
     ITSSDANGYY YSLLALEKLN DGEVVTLTAT SKADPKLKDT MTVTVTDKAF VDDLNAAIAE
     AEKVVNEKDL YTSASVDVVE KALAAAKEAV KNGDQATVDK AEIDLLNAIA GLEFKGSDDT
     RPDSTNHIDE GQMEVISVTN YADSDIKDHI IDNNADSIWH SSYGQGAKLP VDAVIDLGAV
     YQLEQVDYLP RQSSSNGHIT HYRIEVSTDN KTFTPVVEGY LPNNGYELDN KEVAKMIKFA
     PVEAQYVKFI ALGTIGDSGK NNDRYASIAE LDFYGTTNAA VTNVAFENDA MEMVIAEQKQ
     LKAITTPSNS TEQLVWSSDK EDVVSVDQNG VATAKAAGTA TITVKKATDA NISASMTITV
     KALDKSVLEA KIKEVSEFKA TVKDEKVVAY LTEEIAKAQA VVDNAGATES DVTQAVEALT
     SAKDTAVKAI DVLNRFAAVK ALDLSKFDPA GQEELLALIS EVEELAKEPI TNLDVLTEKV
     AKLEELSGKL LPLDVTTLEN LIKVAEGIEL DKYVDNDAKD AFSAALNKAK EVAANPKTLA
     EIKAAETALK DAEGKLVLKA TTATKDALKD LYDEFAKLDL ENYSNKHQEQ IRDMMDRIQS
     ALKDEQLSED DAKALLSEAA KVYAELPAIS PLPDPNNPGN GQNPDGNNGA GQKPNGDSTN
     TGDTTNAALY SMLLLASAGG VALIGMKKKK ANKE
//
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