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Database: UniProt
Entry: Q8XMJ5_CLOPE
LinkDB: Q8XMJ5_CLOPE
Original site: Q8XMJ5_CLOPE 
ID   Q8XMJ5_CLOPE            Unreviewed;      1686 AA.
AC   Q8XMJ5;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Fibronectin type-III domain-containing protein {ECO:0000259|PROSITE:PS50853};
GN   OrderedLocusNames=CPE0693 {ECO:0000313|EMBL:BAB80399.1};
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB80399.1, ECO:0000313|Proteomes:UP000000818};
RN   [1] {ECO:0000313|EMBL:BAB80399.1, ECO:0000313|Proteomes:UP000000818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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DR   EMBL; BA000016; BAB80399.1; -; Genomic_DNA.
DR   RefSeq; WP_011009975.1; NC_003366.1.
DR   STRING; 195102.gene:10489955; -.
DR   CAZy; GH101; Glycoside Hydrolase Family 101.
DR   KEGG; cpe:CPE0693; -.
DR   HOGENOM; CLU_235534_0_0_9; -.
DR   BRENDA; 3.2.1.97; 1503.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd14244; GH_101_like; 1.
DR   Gene3D; 2.60.120.870; -; 1.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR011081; Big_4.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR025706; Endoa_GalNAc.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR040633; Gal_mutarotas_3.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR049314; GH101_dom-5.
DR   InterPro; IPR040502; GH101_dom-6.
DR   InterPro; IPR035364; Glyco_hyd_101_beta.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF07532; Big_4; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF18080; Gal_mutarotas_3; 1.
DR   Pfam; PF17974; GalBD_like; 1.
DR   Pfam; PF21466; GH101_dom-5; 1.
DR   Pfam; PF17451; Glyco_hyd_101C; 1.
DR   Pfam; PF12905; Glyco_hydro_101; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000818};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1686
FT                   /note="Fibronectin type-III domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004317946"
FT   DOMAIN          1601..1686
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
SQ   SEQUENCE   1686 AA;  187828 MW;  00F276EBE357453B CRC64;
     MGRKCMNKKI AAIIAAAVIV GQLPISVLAT PVNEAGDEIN SESAEILTNS DEEAEAYIQN
     YDRPEGITWT KLAGSGSVEV TDGFLSVTNN GDYRIMEDQS PNIKNGELES KFTVGGSQTG
     IIFRATESNY GMINYNSGTG WVIENKNSWE DITGPKLNNG DVVTVKATFV EKHLTVNVSV
     NDGEFETIYD KESDLIPLQA GKVGYRGWGN AKTTKFDYIK YAPMTIDKGP IVSINEVNVE
     TYPRVKPILP SSVTVNHENG MSSIKDVSWN YIPKESYSKP GTFKVEGTVE GTDVKAIANV
     TVSSDLAYYE TNFETEETRG DWQVVQGGGS PSYEEGKVKI PMNGVSIAVD MNSPEVKNFT
     YETDFSVDNN GGRIGLLFRY VSETEWGAVC YDNGSWVWKT GDGKYGNFPG TFTPEPGKTY
     RIKLKVEDTN ITMWVDGEKI GQVAVSNLPD VRGKVGLTGW FGNKNVTLDN LVVEELGGIM
     APEVGPLEEQ SIESDSMKVV LDNRFPTVIR YEWKGTEDVL SGASVDDLEA QYMVEINGEK
     RIPKVTSEFA NNEGIYTLNF EDIGMTITLK MTVNENKLRM EVTDIQEGDV KLQTLNFPNH
     SLASVSSLNN GKTASVLTTG DWNNINEEFT DVAKAKPGVK GKTYAFINDD KFAVTINNNT
     IEGGNRVVLT TENDTLPDNT NYKKVGISNG TWTYKEILQD TTDQGSKLYQ GEKPWSEVII
     ARDENEDGQV DWQDGAIQYR KNMKIPVGGE EIKNQMSYID FNIGYTQNPF LRSLDTIKKL
     SNYTDGFGQL VLHKGYQGEG HDDSHPDYGG HIGMRQGGKE DFNTLIEQGK EYNAKIGVHI
     NATEYTMDAF EYPTELVNEN APGWGWLDQA YYVNQRGDIT SGELFRRLDM LMEDAPELGW
     IYVDVYTGNG WNAHQLGEKI NDYGIMIATE MNGPLEQHVP WTHWGGDPAY PNKGNASKIM
     RFMKNDTQDS FLADPLVKGN KHLLSGGWGT RHDIEGAYGT EVFYNQVLPT KYLQHFQITK
     MSENEVLFEN GVKAVRENSN INYYRNDRLV ATTPENSIGN TGIGDTQLFL PWNPVDEANS
     EKIYHWNPLG TTSEWTLPEG WTSNDKVYLY ELSDLGRTLV KEVPVVDGKV NLEVKQDTPY
     IVTKEKVEEK RIEDWGYGSE IADPGFDSQT FDKWNKESTA ENTDHITIEN ESVQKRLGND
     VLKISGNEGA DAKISQSISG LEEGVTYSVS AWVKNDNNRE VTLGVNVGGK DFTNVITSGG
     KVRQGEGVKY IDDTFVRMEV EFTVPKGVNS ADVYLKASEG DADSVVLVDD FRIWDHPGHT
     NRDGYVFYED FENVDEGISP FYLSPGRGHS NRSHLAEKDI SIDANQRMNW VLDGRFSLKS
     NQQPKEIGEM LTTDVSSFKL EPNKTYEFGF LYSLENAAPG YSVNIKNRDG EKIVSIPLEA
     TGSNYAQDIF TKTKSVTHEF TTGDFAGDYY ITLEKGDGFK EVILDNIYVK EIDKSIESPE
     LAHVNLNTVE HDLEVGQSVP FAINALMNNG ANVNLEEAEV EYKVSKPEVL TIENGMMTGA
     SEGFTDVQVN ITVNGNKVSS NTVRVKVGNP EVEEEEVIVN PVRNFKVTDK TKKNVTVSWE
     EPEKTYGLEG YVLYKDGKKV KEIGADKTEF TFKGLNRHTI YNFKIAAKYS NGELSTKESI
     TVRTAR
//
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