ID A0A1H3ZRJ5_9FIRM Unreviewed; 1726 AA.
AC A0A1H3ZRJ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=F5/8 type C domain-containing protein {ECO:0000313|EMBL:SEA26011.1};
GN ORFNames=SAMN04515656_10697 {ECO:0000313|EMBL:SEA26011.1};
OS Eubacterium aggregans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=81409 {ECO:0000313|EMBL:SEA26011.1, ECO:0000313|Proteomes:UP000199394};
RN [1] {ECO:0000313|EMBL:SEA26011.1, ECO:0000313|Proteomes:UP000199394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR12 {ECO:0000313|EMBL:SEA26011.1,
RC ECO:0000313|Proteomes:UP000199394};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNRK01000006; SEA26011.1; -; Genomic_DNA.
DR STRING; 81409.SAMN04515656_10697; -.
DR OrthoDB; 197688at2; -.
DR Proteomes; UP000199394; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14256; Dockerin_I; 1.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.60.120.1250; Peptidase M60, enhancin-like domain 1; 1.
DR Gene3D; 3.40.390.80; Peptidase M60, enhancin-like domain 2; 1.
DR Gene3D; 1.10.390.30; Peptidase M60, enhancin-like domain 3; 1.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR042279; Pep_M60_3.
DR InterPro; IPR031161; Peptidase_M60_dom.
DR PANTHER; PTHR44170:SF30; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF13402; Peptidase_M60; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM01276; M60-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS51723; PEPTIDASE_M60; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Reference proteome {ECO:0000313|Proteomes:UP000199394};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1726
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011667997"
FT DOMAIN 192..253
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT DOMAIN 431..524
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 526..615
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 881..1225
FT /note="Peptidase M60"
FT /evidence="ECO:0000259|PROSITE:PS51723"
FT DOMAIN 1415..1574
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1726 AA; 188006 MW; 9FAC3782D1AC5DF4 CRC64;
MKRGLACLMA LVLLFVSVPT SVLAEVITSQ TTHEEAGQEV SQKKASDLLE AEAVDTVNAK
AVGTLEVEIS YPQPRKALTD RAAVSLTNTA GEIVTISLKD VASDKKTASL GSQSIQYKNL
LFDKNAIGDG SMAGSVLYNP SAQDAQVYYT TVNFYDLPVD TYTLTLSDTG LLPVTTTAAI
NTTSKRVEVN AKALLTGDVD GNGAIDDVDY DAVLAKLGTT EVAYDLNGDG TVDIIDLVYL
QEGLSKTVDT TAIQVSETSP VVNPEGVKLE SSAENPVSVK DGAISQLFGA STTATEVVGF
QRQDGQSIST NTPLEIPLVM AETIQASQIR LEPSALGIDH AAKKGEVIVT NEAGNDEIYY
FGTEESTAVL FLTDEPSENT IVIDLKGQTA IKKITIRVTE TTKASSNLVE ISKVEFLNNT
KDKIVEQVSS IPTNVRATPG NESLSITWDA QANVTGYEVK MSFDNPKTGK NETTITPVDG
NALTIGDLTN YVDYTISVQS VNRSDTGNWE SGYSAPIVAT PLPTSVPEAP EAITLSGGYR
QITVNWEKQK NSTGYNVYYR EKGKTEYSKI GGLTATSTVI TDLKDQTEYE IYLRGYNAIG
EGAASPVYRC ETKSIDPPIT SNYKLINCAN GVDEPTAHIT DITYPYLKEG DYENGFDQYD
ITDNDYTSYW NYGGWNAGGW AGTLQGPVVA FDGAYEMDDI VLIRGEGEPS TYTYMTIRWW
DEAGLAHTLK AQEDFTISSK KTTNGKEYYR IQIKDKIKPV KIQINPALYW AGAPNARCRI
SELKFYAYDS LANETDALFV DDLHVELKDS VTMAYVDGLI ERANTPDPDS GEFHPDKDLI
LSELTLAKSI LSETNIDDTV VVDQNVSNAK NGTLGFAMSL NDFQPLGLAA KAGDTINVYV
GTTGSVLPEL VYTQYHPDIK TGWSKTVKLK KGKNEITLAQ IGGEDSERGG ALYIRYPNAT
ATDKEIKVRV AGAVKTPTLN LTGITDAAAA KTKIRSYITE LKAYATSLPS MYEGEDVRYP
WDKTSSIYNA TEIMMDQMLL SVPATAVVEN LTGSEDAQVE QLYQNSLAME QMMNITYTSK
GLSRDAADNL DQWPGSRINV RYTRMFTGAF MYATGQHIGI EYGSVGGMVK GQPHKAQSNG
TMADGQLYGW GIAHEIGHVT DEGDMVYGET SNNILSQLVK TFDEKEGARA NYSAIYQKVT
SGTTGYSSDV FTQLGMFWQL HLAYDDTPNS LDAKDSFYAK LYQGYRRNTQ KTDKDNLLIR
MASDAVQRDL TIYFEKWGLT ANEETLAYVS KYPKEERAIY YLNDDARHKR IQKAPAMAAG
TAVKATLNHT VENGKDSKQI TLNLGVNKNQ DAILGYEIVR NGQSVGFTTN NTYTDVIASM
NNRVLNYEVI AYDNYLNKTE ALALEPIKLQ HDGSVAKTKW TMDSTMTSQG DTLVDEDCSD
SGIAHPALKT LYDEDYANVY QGTKTSNNPS ITINLQERMP VVGFKYTAAV VDGALAENTI
KSYTIQVSED GTTWQDATKG SFTVSVEEPS AIVYFNETDQ EGANQLHTYQ AGYVRLIANG
AAGVSAAELD IVGPPGDNVN LEQSGIGILK SDFTYDPEQA PIKAGSLIFT GSYRGHPGFN
ALLLKDSQGN NVVGKDGQAE SIFMATVPEN GNIGEISQGT WIYWIDVDNL DMNALPDTVR
AELYRVNNME TNEGQRLTSD TFGIALPATI PAIELTGAQT AEDKSI
//
