ID A0A0J1G0D6_9FIRM Unreviewed; 2186 AA.
AC A0A0J1G0D6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=PA14 domain-containing protein {ECO:0000259|PROSITE:PS51820};
GN ORFNames=RHS_5135 {ECO:0000313|EMBL:KLU69042.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU69042.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU69042.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU69042.1};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:KLU69042.1}.
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DR EMBL; JNGB01000116; KLU69042.1; -; Genomic_DNA.
DR Proteomes; UP000036477; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF07691; PA14; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000036477};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..2186
FT /note="PA14 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005251320"
FT DOMAIN 139..287
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 36..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2186 AA; 239387 MW; 54BCB06ED2BB836E CRC64;
MGKRRKKLLS MALVVGMVVS NLSPYTNVLA AEPDNVSTGS AETAELNEDP GDALPPGTAK
AIKETESETE PETEPVSRVE TETEAVREST SQAETIAETN QVETEKETMS ETETQLTEET
EAETARETKN KNAAAVNNVD VNGLFAEYYT TSGSGKNVKL DALKSKGIDY NINYGDLNAK
LMLTTGKDDY AGIRWSGRIR VPETADYTFY GLADNGIRLW VNGEQLFNYW DGESWDILQT
SKGVALEAGK FYDIKVEYFD YSGGAHATLS WSNNKGLKDK STIPSSAFFL PSDYNGIYIG
SIDTSQANLK EGEDFKGDVT VNGFGLDQVE SFEIVKTSGE SLKTPVYAEV TSQKNEEAKI
VIPNMETGTY KLKIKQSNTA VISKGLIIVK PGTEEVPTRT ERPRADWERE SYVNLNGIWE
FDFDADEEGK NAGWYNPDQE FSRSINVPFC WESSLSGISD PDYKGQAWYK KTVRVDKSWE
GRKIFLKFGA VDWKCKLWVN GEEVGEHIGG YSAFEMDVTD HMKAGEDNVI TLWVEDKGSY
GDDSYPALIG KQGRNAPCGY IHTSGIWQTV GMEARSATYL DNAKAVSDID NATVTYDLDV
TTDKDQTLTV EYDFASTVYD MENDVDIPTG SVVEGSQEIQ VESGDNEVEL SPIAIANQKL
WNYDDPNLYQ GTLTVKDMDG NVLDELSTYF GLRKVEAKYY NEDLGVKYIY LNDEPVYMSG
LLDQGFWEEG IYTAPSEDAL KYDILAMKEA GFNMIRKHLK IEDPLQYYWC DKLGMMVWQD
MPHATAMVPS KEGGEALGRK YYEECLDAAM EMNYNHPSIV SVMLFNETWG LYAAYNDNGK
NRNVKASDGK STAEWVEYLY NKTKGAYPNM LIEDMSPCNS DHVQPSDLNT YHMYPKSYDG
TVGDVENRVN NAYVGSENNY KFGFKQDGDP LLNSEYGGVA AYDGDFDISY CFKFMTDVQR
RYEKQSGFVY TEPFDVEYER NGILTYDRQK KIFGYDEIAY GGDMGIQDLV QETYIGIVDS
PVKNVKPGAK IKTKIMAMSW TNDVPENTVV KWRFDGTDIY GNNISTDLAG TLGMEIIPYE
KAEASLSFHA PAQACVGTLT VWIEGPDGAK IAKNFTNIVV ADPSSENKEL VLDNENGSIT
MKAAVNDRRM VTTEGTGSQD YSYTLPENFN LDTLNGLKII AEASSFKGQT GTDKNHSSFS
SAYSQTAEGR ERASDMTVYV NGVEVDTVYL PDNPRDMRGT LSLNAPYNGA TSAGDFGYLV
NLSVSKEKLA EIKAAMGDSK VMKVTYAVKE DAANQNGLRI YNSVYGRYAV NPTIILNPKD
IEKADQVTAV KNIKTDSDNY SVEGVLSGNS SLNVRTGEKE GYVIALANGG SSITVTNKKT
NQVIGDAAEL AAGNHHVKVT LFDEQIRVFA DNNPEAAINV FDRSGFTGGI TVNASGTNPV
ADLVVSPESY EAVKSEIDDT VKDVEITDDF SDADYAKRYE IMGGAWSGNV VNGALNMSAS
DQGDKMIMKD ISMSDGIYEM DIKVTNSSGI NGNAGFLFRS SNYNIGPDGA NGYYAGIGDR
YVQLGRMSQG WKELAKVTVP ELVVGSTHTL RIAVFGSRIQ IYVDDAQVPC VDINDSTYLE
GGAAVRGYRV AATLDNIHVA SIPRYSSTFE KGSDEWEANG NWKTVDGAYT SASKGAYSLI
DSNKIKDVLF AADVKPGTED SVTAMLLRTV SGSAGIRGYQ LVADAENDKV KIVKSENGRT
TVLAETGMRL QAGRTYRLTV EMQGSVIKVY KNDNREALMI AEDSAFTAGQ IGIMNVNGTS
AIDNVAVNNQ FIDGGLMKPA DPKALDEIIA EAQKADAGKY TADSYSRLKA ALDAALDADR
YDQQEIDGAV TAVREALNQL VLKPVDLTVL NSKIAEAKKL DPGRYTADSY AKVKAALAAA
EAVNKKDQAA VDVAAKALGD AIGQLKIKPA DLSVLNQKIA EAKKLDVNKY TADSYAKVKA
ALAAAEAVNK NDQAAVNAAA KNLSDAMAQL KVKPAAPKVP KKNAVYTVNS LVYKVTKSSS
KNGTVKVMKA KKKSYTSISV PKTVKLNGYT FKVTEIYKNA FKNNTKLKTV KIADNVSKIG
SYAFAGCRKL KSVTIGKGLK SIGSKAFYND KVLKSIVIKS TKVSKVYSKA FSGIHKNAYI
NVPNKKASDY KKTFKKGNPA KTVKIK
//
