ID A0A1I4ECT7_9PORP Unreviewed; 576 AA.
AC A0A1I4ECT7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=F5/8 type C domain-containing protein {ECO:0000313|EMBL:SFL03565.1};
GN ORFNames=SAMN05216357_11142 {ECO:0000313|EMBL:SFL03565.1};
OS Porphyromonadaceae bacterium KH3CP3RA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae.
OX NCBI_TaxID=1855396 {ECO:0000313|EMBL:SFL03565.1, ECO:0000313|Proteomes:UP000198708};
RN [1] {ECO:0000313|EMBL:SFL03565.1, ECO:0000313|Proteomes:UP000198708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH3CP3RA {ECO:0000313|EMBL:SFL03565.1,
RC ECO:0000313|Proteomes:UP000198708};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
CC -!- SIMILARITY: Belongs to the peptidase C25 family.
CC {ECO:0000256|ARBA:ARBA00006067}.
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DR EMBL; FOSU01000011; SFL03565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4ECT7; -.
DR Proteomes; UP000198708; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..576
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011504613"
FT DOMAIN 333..484
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 492..576
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 576 AA; 66182 MW; B53B7BC6A76A0A0B CRC64;
MNNKNLSVVI AGIACMVSFS TIAQNTRMRT YCNPVNIDYT YMIYNSDKDI SYRSGADPAV
VEFRGEYYMF VTRSMGYWHS TDLQSWNFIE PEKWYPQGSN APAAHNYKDS VLYVMGDPSG
AMSVLYTDNP KRGDWKAVPA ILHNLQDPAL FIDDDGSAFV YWGSSNLHPI RGQRLNKNHR
FIRYGEVDSL FNKDMDKHGW ERFGENNSDT IPGYIEGPWM TKHNNKYYLQ YGAPGTEFNV
YADGVYIGDH PLGPFEYAPN NPVSFKPGGF MNGAGHGSTV KGPQDLYWHF ASMALSYNVN
WERRLCMFPL HFDNDDLMWT DTYFGDYPRY APSEPGKAGE FAGWMLLSYK KPVTVSSSVG
DHTAEKLTDE QVKTYWLAGD NSDSQWATID LQKPGLVYAV QINYFDHESD MYGRIPGLRH
RYVVEGSLDG RDWRVLIDKS NSFRDNPNDY VELPEPERIR YLRYRNIEVP TPHLAISDIR
VFGIGEGKKP NPVTGFHVQR EEDRRDAMIT WNAQKDVQGY NVRWGIAPDK LYSSWLIYDD
NQLLLKALTT DQEYYFTIEA FNENGISTPL KPIHVK
//
