ID A0A1Y4F7G2_9FIRM Unreviewed; 1790 AA.
AC A0A1Y4F7G2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|PROSITE:PS50022};
GN ORFNames=B5F54_02140 {ECO:0000313|EMBL:OUO75751.1};
OS Anaeromassilibacillus sp. An250.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaeromassilibacillus.
OX NCBI_TaxID=1965604 {ECO:0000313|EMBL:OUO75751.1, ECO:0000313|Proteomes:UP000195568};
RN [1] {ECO:0000313|Proteomes:UP000195568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An250 {ECO:0000313|Proteomes:UP000195568};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OUO75751.1}.
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DR EMBL; NFJK01000002; OUO75751.1; -; Genomic_DNA.
DR OrthoDB; 1839554at2; -.
DR Proteomes; UP000195568; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.90; AF1782-like; 4.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR049174; Beta-AFase-like.
DR InterPro; IPR012878; Beta-AFase-like_GH127_cat.
DR InterPro; IPR049046; Beta-AFase-like_GH127_middle.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43465; DUF1680 DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_1G08910); 1.
DR PANTHER; PTHR43465:SF2; DUF1680 DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_1G08910); 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00754; F5_F8_type_C; 3.
DR Pfam; PF07554; FIVAR; 4.
DR Pfam; PF20736; Glyco_hydro127M; 1.
DR Pfam; PF07944; Glyco_hydro_127; 1.
DR SUPFAM; SSF49478; Cna protein B-type domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS50022; FA58C_3; 3.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000195568};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1790
FT /note="F5/8 type C domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011007918"
FT DOMAIN 576..728
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 813..980
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1055..1209
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 1071..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1628..1666
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1071..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1790 AA; 194972 MW; C182A27787007E50 CRC64;
MIQKKVRNLL SVVLALLLCL GSLTPAFAAK NNVQADPDAE LSVLDMANVD TLSGYLYERS
QKNYDRLESD PYLLPSVLEG DPNWPGDYQG RALLGIISEA KANQDRAPQN LEAMMQALPD
KLLDGCFFNE TLNPDMINEQ LMAGHSWFLR AMCELYEWNQ DPRALEIIEG LVNKLLIPAK
DGFARYPIIE GGQGGGESGE IIGEEAGWKL STDTGCVFIM LDGATHAYQI TKNEELRSVI
EIMIEKFMQE DVRTLKFQTH ATLSATRGIL RFYGATHEQK YLDYAVQRME EYVSSGMTET
YMNYNWYQRP EWTEPCAIID SYIASMELFR YTQDVKWLEL AQKILLNGMG AGQRSNGGFG
TDTCCGVTSD SLDVSSYEAT WCCTMRGGEG MGKALGYQYM TDAQGRLYVL QYSNNRLTFA
SGGGETVLQQ TSGYPENGDV QFAVESSTAS ELTMRLFIPS YVDLTTLRLT VDGMETEANV
ENGFLEISFD PTTVDEIALH FDIPVIRNVT MPAEDHMFGY TYSKGFALLG WFNGPGTDVE
GEQNLPFEER TLKPIYEAFH LSQSDRSATS IQVVDTPNKD MSISTGAAVS ASSSYEADGW
GISGLVDGAY TNGWSSMPGR NQTEDSTEWV QVDLGGVCSI QEILLYPSDN LDGAMMPVDY
EVLVSVDGNE WTPVKQVEGD TVTSKPRAIL FDEPVEAGYI RVVGTKLRLA NETDGYLMQI
GELEVYSDDV VMLQIASNDP MAYAAVRING GDEKILPYTG AFREGQELTI EPVILNEADY
GFFSWGGDVS SDEETISLTM DSDHSLVLNQ ALAISENLAL HAAVNAKNTI ESPPDWSTSN
LTDGVLLTPG DVSGSKGYTS SATTNPDVSA DPYWVEVDLG ENTEFNRVHL YPRSDYFAAD
GSTCSFPEDF TISVRKDGED TYTVIGTYHD VVAPEYYRPA VYTFDEMQDA RYIRVTVNRI
GKLAADTTTN YMFQLSEMGV YRIDEAQDTY QLYLEGTPGG KISVNNELVS LPYSQEYAKG
DRVTIEAIET TGTFIGWEGS QTGTDSEVYL IMNSDQSVRA NFQYGNMVPN SSMTAEASSE
TNPQHDYDGP ASFAIDGNIQ TLWHSRYDPQ QDPLPVDITL RFDTVRQINQ FVYVPRQTPG
QNNGIITKYR LEIQAADGTW TQVSEGDWAL DMAEKTVEFS PTEAQAVRLT AMEGYGGFAS
AAELRVYEVP TVYTVSGCVL AGETGVDVGG IPVYLYTAGN PDQAIDLTTT DEEGNFAFTD
VKAGDYLVQV NAVEGAYLAS TVAVTVSDGD VTDADLTLRG KPELTVTFPK TVKLSIGGEE
QTIANLLGKY SADVMADTEL ELTFTPRVDG REIAGVTVNG EAVAVEDFDI NEFVYNLTML
NVDTTIELGF TLVDKQNLRA AIEIAEGRAG EADAAVPSVK EKYEAALQAA KDVEAKKTAT
QDEINTAWSD LIDALHYLSF VAGDKSQLDI PMEIADSINR DLFTPDSLDA LDEAYAAAEE
LLDDEEVLEA DITAAVDALY DAIYGLVYRA DITELEALVT KGDSIVANAD QYIQNDAWTS
FETSLEEAKT VLANENATQD AVDTAAEDLA AAISALRLIP DKDALEALIG EAEAINTNKY
TAKSVAAMKA ALSTAKAVLN DAEATEEEVA DAVEALENSI DGLVEKSTST SSKNSGSTSA
NVGNAYGAAG VVSASQSVAA NAYVVSDTTV NFTLKRGSAY CFKMTVVNGN AMTPGFTVGN
GEVLKTQFVA KIGNDYYYRV YAIGTPGQST GVYTTLPGNA PVKHCAVTIG
//
