ID A0A1Y4N2Y8_9FIRM Unreviewed; 1620 AA.
AC A0A1Y4N2Y8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|PROSITE:PS50022};
GN ORFNames=B5F09_09545 {ECO:0000313|EMBL:OUP75254.1};
OS Erysipelatoclostridium sp. An173.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=1965571 {ECO:0000313|EMBL:OUP75254.1, ECO:0000313|Proteomes:UP000196550};
RN [1] {ECO:0000313|Proteomes:UP000196550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An173 {ECO:0000313|Proteomes:UP000196550};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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:OUP75254.1}.
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DR EMBL; NFKR01000021; OUP75254.1; -; Genomic_DNA.
DR Proteomes; UP000196550; Unassembled WGS sequence.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06564; GH20_DspB_LnbB-like; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 2.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR Pfam; PF00754; F5_F8_type_C; 3.
DR Pfam; PF07554; FIVAR; 3.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR PROSITE; PS50022; FA58C_3; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000196550};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1620
FT /note="F5/8 type C domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012711977"
FT DOMAIN 24..164
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 166..321
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1206..1356
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 1560..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 724
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 1620 AA; 179821 MW; 74970613B9B691B0 CRC64;
MKLKKKSLAA VLTFTMLFSS LFSIIPVKAE VTDGTNLALN KTVTVSAEYG GNLAKEYLTD
GDEETRWSTE ADVTQWAYVD LGQEFEMNKF QMIWESDSVY AKDYNIYVSN NVDDWGEPVI
TKTDNNTKTS EDILTTKVSG RYVKLEITRM QGYPNVSCRE FKIFNTDEKY QDPTTNVALN
KTAVASSQEA DSVKAANAVD GDTTSRSSRW GSAIGNGPDW IYVDLGESLN VNVVKVFWEN
RKATAYKIQI ANTESRPSEG DWQTVKEFSD HPASIDEKIV LDQVYKARYV RLYIDSHTSQ
DPDGGVAWNT VSIYELEVYG GNPDTKPPIS EVLNGIEVKT PEKGDQKLEV TLPEIEGYTV
SYNGTDFEQV VDDDLTIYQP VVDKDVKVSF KVTDTDTNDY RFKEVNVTIP GKYSSDESDN
SAPNVLPELA EWKGGNGDFV IDGSTKIVYQ DDALKATAEA LANDYEELTD KSLEVTKGTA
DNGDISLALT SDKSQGLQDE GYLMEISNNS VAITAQTTTG AYWATRTILQ SVKQTGDIPC
GITRDYPLYE IRGFILDVGR KTFTMDFLKQ VVKQMSWYKM NDFQVHLNDN LIPIENLEDP
MTAYSAFRLE SDVKKGGNGG LNQQDLTSTD LFYTKEEFKS FIKESRTYGV NIVPEIDTPA
HSLALTKVRP DLRHGTNGRE NDHLALRDKY DESLSFVQSI FDEYMKTDDP VFDQQTTVHV
GADEYNADKE AYRKFSDDML KYVQDTGRTA RIWGSLTQCF GTTPVRSENV QMNLWNFGYA
NMDQMYEQGY DLINCNDGNY YIVPNAGYYY DRLYDSTLYN LPINSIGGVT IPAGDEQMIG
GAFAVWNDMT DYLENGISQY DVYDRIENAI PLFGAKLWGI NDNSLEEANQ IRNQLGGAPG
TNFDYQVPTD ENGVIAHYKL DDLSGLTAGT NADITSVDGR NALQLNGKES YVTSPIVTAG
LGNDLRVKVK RTSSGSDEQI LFESDYGSIK AIQKDTGKVG FSREGRDYSF SYELPVNEWV
ELEFKNEINV TKLYVNGQLI DTLGDDEQVE GRPLVATTMF PLERIGSQSN AFVGYVDDIR
LSTEKEFNST MSLDYAMITA QSILENTEND ELQALVAEGK KVIDQFAPEA AVITDLTTKI
NDVLNTIEYK KADYSRVDKY LALVAEDLSI YTDASINNLN QVINSIRRDL PLAMQDIVDG
YEANLAKALA QLELKSQLNI NYVDNKLLTA SASSYQKDGS NPSNVLDDNP ATMWHTDWNI
TTLPHWIALE SQTPISINGL TYVPRQTGTN GNVTSYAIEV SDDGNDWRVI KEGKLPSDSS
TKIIGFDEVT TTHVRLVYRE AENDNGSAAE IKLHRGDVPA DLTGLQAAIE AAEAIENIGY
TGASWQNLQD TIADAKALLN SVNPDPNDVE IAKRNLSAAT MKLVLKVDSR QLESLVDSFK
DYNEDDYTPE SWANFKAALD AAKAVINNSD ATKDDVNKAY QDLLDASSLL VEVNHKEGLE
SLINKAESFD SSKYTVESWA KLAEALKYAK EVFNNEQATK EEIATAVLNL ETAINGLKEI
EGSEGQNPSD PSTPSVTPKP GTDDDKGQSA KTGDNSPVLA LVSISTLALA GMWLARRKED
//
