ID A0A1G0XC91_9BACT Unreviewed; 583 AA.
AC A0A1G0XC91;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Coagulation factor 5/8 type domain protein {ECO:0000313|EMBL:OGV31326.1};
GN ORFNames=A2523_17020 {ECO:0000313|EMBL:OGV31326.1};
OS Ignavibacteria bacterium RIFOXYD12_FULL_36_8.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798454 {ECO:0000313|EMBL:OGV31326.1, ECO:0000313|Proteomes:UP000177243};
RN [1] {ECO:0000313|EMBL:OGV31326.1, ECO:0000313|Proteomes:UP000177243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:OGV31326.1}.
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DR EMBL; MHBA01000058; OGV31326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XC91; -.
DR STRING; 1798454.A2523_17020; -.
DR Proteomes; UP000177243; Unassembled WGS sequence.
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; cd08982; GH43-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..583
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009569310"
FT DOMAIN 337..489
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 497..583
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 583 AA; 67913 MW; 5348014B9CC200D4 CRC64;
MIKSFLVLIV LFISAEPAAQ NPNQKTWCNP MDIGYRYNWE QINDKISYRS GADPVIVNHK
GTDYLFVTIS GGYWESKDLL NWRYIEPSKW PLEDNCAPAA LSVRDTMYIF QSTFQQRPIF
YTTEPETGKL KFFNRWMPLL PDTIGPWDPA IFYDKDTDRW FMYWGSSNVY PIYGRELDHS
QRLIYKGDIK KLLYLHPEIH GWERFGFNHA SPIKPFIEGA WMTKHNGKYY LQYGAPGTEY
NVYANGTYVG DDPLGPFTYA PYNPISYKPG GFMCGAGHGN TFQDNYGNYW NTGTPWIAIN
WNFERRIAMF PTFFDKDDQM HANTRFGDFP HYLPSKTLTN KDELFTGWMV LSYKKPAVAS
SVMDTFRVAN VTDENPRTFW VANTNGNAEY VTIDLQKVYN VKAVQIHFVD YKSDIFDNDL
SRVYTQYKFF ASSDGNNWNV IVDLSKIKQD RPNGYFELDR PINARYVKYE NVYMPTPNLA
VSDIRVFGNS NGNMPETPKD LKVVRDKDER NAFIKWDKVE GAVGYNILWG IKKDKLYQTY
QVWADQKEEL ELRALTVGQD YYFAIEAFNE NGVSKVSKIV YLK
//
