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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//