ID A0A174G7N3_9CLOT Unreviewed; 2234 AA.
AC A0A174G7N3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Family 6 carbohydrate binding protein {ECO:0000313|EMBL:CUO56435.1};
DE EC=3.2.1.96 {ECO:0000313|EMBL:CUO56435.1};
GN Name=lytB_4 {ECO:0000313|EMBL:CUO56435.1};
GN ORFNames=ERS852407_03208 {ECO:0000313|EMBL:CUO56435.1};
OS Hungatella hathewayi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=154046 {ECO:0000313|EMBL:CUO56435.1, ECO:0000313|Proteomes:UP000095651};
RN [1] {ECO:0000313|EMBL:CUO56435.1, ECO:0000313|Proteomes:UP000095651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608850 {ECO:0000313|EMBL:CUO56435.1,
RC ECO:0000313|Proteomes:UP000095651};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CYZE01000008; CUO56435.1; -; Genomic_DNA.
DR RefSeq; WP_055656677.1; NZ_CYZE01000008.1.
DR Proteomes; UP000095651; Unassembled WGS sequence.
DR GO; GO:0004336; F:galactosylceramidase activity; IEA:InterPro.
DR GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006683; P:galactosylceramide catabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.3630; -; 4.
DR Gene3D; 2.10.270.10; Cholin Binding; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR049161; GH59_cat.
DR InterPro; IPR001286; Glyco_hydro_59.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR022038; Ig-like_bact.
DR PANTHER; PTHR15172; GALACTOCEREBROSIDASE; 1.
DR PANTHER; PTHR15172:SF1; GALACTOCEREBROSIDASE; 1.
DR Pfam; PF07523; Big_3; 2.
DR Pfam; PF19085; Choline_bind_2; 1.
DR Pfam; PF19127; Choline_bind_3; 1.
DR Pfam; PF07554; FIVAR; 2.
DR Pfam; PF02057; Glyco_hydro_59; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51170; CW; 3.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:CUO56435.1};
KW Hydrolase {ECO:0000313|EMBL:CUO56435.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095651};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..2234
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008022316"
FT DOMAIN 551..886
FT /note="Glycosyl hydrolase family 59 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02057"
FT DOMAIN 1727..1785
FT /note="Ig-like"
FT /evidence="ECO:0000259|Pfam:PF07523"
FT DOMAIN 1811..1888
FT /note="Ig-like"
FT /evidence="ECO:0000259|Pfam:PF07523"
FT REPEAT 2132..2151
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 2174..2193
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 2195..2214
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REGION 2085..2132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2085..2103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2109..2129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2234 AA; 245263 MW; 6FF68870CC2461DF CRC64;
MKCKKQGQRA LSWILVTAMM VPSVSVPTIA YAETNQRIAT YVGQVPEQLK DDASVKADQF
GKAYDTVAVT SKGVRYDVEV VPQELVYYID NYSSGPLDGT TPAYEAVKEL TGTKLKNDAA
DAVYVEGSWG FHNQNVKTKG NVTTEDKAVS GIYNDQDKLL TYTLPLDAGT YEITTAHYEW
WPDQGRTLDI TAQIDDGTPV SLGTTGALIV NQETRVTGDV TLDKAGEVTL RIQDTKNKGA
ILSWLAVAEK DSALVPFDTA LEETDGGLTN RGASVISDAG RGNVVEVTAG WNNQNGGHAE
IKDAAALFGR KEFTLLANVK VEDTDTNEDN RNKKAAFSIG TENQNIHIFT QSGKVGYGDS
KAGGGISAGN TALEHIIADD WNAMAVSYSE KDGANGSVTV YLNGEKAGEI PDLGFKLSGM
SNITAALGRS FATNFLLNGL YDDIVVTSEA MSEEAAAAET KTRMMEPLLS ELKRAVTEAN
AYLDTEDPGN EALKQAVTEA EALLAGGNAS REAVLAATAK IRNILPVYDA VITIKGSDVD
AAALMTNGLT YKGWGLLSCN GTSNLLMDYK AEAPEKYWEM IHTLFEGEHP LISHVKIEMG
NDGNTSTAAD PATIRYEGED ADVSRSPGWQ LAADAKSVNP DVKVSVLRWR SPNWTNGNTN
TEKVYEWYRD TIFDAYEKYG IMADYIAAGV NEANYNDAIK ISAPMTKAFT KLVEEESDFP
DYMEEDAQDA YHRIQFVAAD EIDSWGIVTD MYNSKDQKGG TWDSVDAVGI HYVTGTDQNV
RDLAQKYNKE IWYSEGCATF GMTSQAERRT DSYVAMGGNQ SPLAMVDGYL NSFVFSNMTH
YIFQPAIGGF YDGLQYAHKD LVSAREPWAG YVRYDEALYM TAHFTQFSKS GWAADEDNSN
GIWLGIPQAS NSYAGDNNKN EHLSNEAGKP SYMTLAAPDK SDFSVVAVNN SPKKLNYQIK
AEDMNLDENQ KLEIWQTKAD EYMEFKGEVA ANSAGMYTVS VDAGAIATFT TLDYHQNDGD
RALTLPEHTS LSDKAVLDTD EDGKMGEGCT GVTDNTILYA DDFEYDEEGT VTVNTANGPE
QQDYLSSRGN EPRYMMDTHG AWVVEKEDDG NQRLGQILPA AVSEWNGGDP ETIVGDYRWM
NYKASVDVQA DNGYALLGIR QQTGMNSDNS GYNLLIQNGT WKMRKGGSTL LEGSMPEKQG
DSCRIALEGR GNAILAYVDG ELAGSYIDTD KPYLMGRVFL GSAWAETYFD NLKVEKIPGY
IPYATAFYDD HDDEVQYSND WRLTGPGNGS ADNWYRTTSY NKKSGDSTYV TFDGRGTGFM
LVGENGGGVK ADIYVDGVKK AENAENNSSS KRYSTIVLDG LTSGDHTFKV VVKSGTLVID
GVYILGEVLP GGSIEALKAL AAECETYREA DYTADHWKVF ADALTAAQAV IGNETESTQL
EIDTAAIRLQ EAKEALLRLD QPVEIIDDRL PEYLAVVEGE TVKDDILPAE VRVKLANGTE
STAKIQWANN EEDSFSAPYK TVRLKGTVEG GKDLQAVIPV EVVPEDTLYY IDSFSAAPGD
GTTPVYEAVR ALLGDQLKNE KADQISDGTK WGFNKTGVVT KPDTDLTDKY SSGFYMEGGN
PVLYYLPLEA GAYSLTVGVN EWWEPRSMKA VVLADGKELA AENLTLSGKG SQDEKTLSFT
LEKADTVTLR VEKVSKNDPV ISWLAVAKQP EVLDISGVKV ERLPDRTEYR IGEKLDTTGM
VVTATMSDAT RVELEEDQYT VSTLNSGTPG EKEITVSAAG KSGTVYTDTF RVVVTEEGTE
YYTTKIKVTG KPDKMKYYTG DELDTAGMVV KAHQKASPSN AERDIEISDY VTEYDFSKAG
KATVEVIYED ENSDGERIEF TDSFTVTVED EPVEPEYYTT RIRVDKKPKK VVYKVGEEFN
PEGMKVMDIQ KASPGNATRA VEIPLEELDY QYDFSTSGNK KVKVVYMGTD KNQEEKEFQA
AVDVSVADEA EEGFYTEMIQ ITSQPDQTVY RVGDMFAPAG MAVTAYRINR ETGERVEELT
RDYKVSPALF MISGDIKVTV SYTGIDKNGD AKVFQDSLWV TVRPASSSDS SGSSDTAETR
PVPKPSSTMD GGSWKQDGGS WQYTKPNGQP ARNEWGRING SWYFFKSDGR MAANEWMMDA
DVWYFVDESG AMYENRWMEY GGNWYYLGQS GAMYGNRWLE YNGVWYYLNA DGTMAKDTVT
ADGYRVGSDG KWVK
//
