ID R6FRR7_9CLOT Unreviewed; 1953 AA.
AC R6FRR7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Fibronectin type III domain protein {ECO:0000313|EMBL:CDB14750.1};
GN ORFNames=BN542_02856 {ECO:0000313|EMBL:CDB14750.1};
OS Clostridium sp. CAG:221.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262780 {ECO:0000313|EMBL:CDB14750.1, ECO:0000313|Proteomes:UP000018176};
RN [1] {ECO:0000313|EMBL:CDB14750.1, ECO:0000313|Proteomes:UP000018176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:221 {ECO:0000313|Proteomes:UP000018176};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDB14750.1}.
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DR EMBL; CBDC010000030; CDB14750.1; -; Genomic_DNA.
DR Proteomes; UP000018176; 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; cd14254; Dockerin_II; 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; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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 Pfam; PF13402; Peptidase_M60; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM01276; M60-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
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; 1.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1953
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039351129"
FT DOMAIN 254..315
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT DOMAIN 493..586
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 620..735
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 996..1380
FT /note="Peptidase M60"
FT /evidence="ECO:0000259|PROSITE:PS51723"
FT DOMAIN 1600..1770
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 53..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1953 AA; 217865 MW; DB4047F9BC89A175 CRC64;
MKNKKIVSYT LAATLATSIV PNADSEVVSA TENNSVENNA DENLKENVEV EIENTEKIQD
QDADKSDEST DEVKNESDVV EDEIKDNTIE EKSLEDDEEV VKSEEISKAK EKEEKIEVKK
AEGKVVGKLE VDMNFPLPLA DTSNLGISLN LKNSNKELIG KVDINDILNG NLNSGVTYTV
EKLNSKKQPL EQGDSIYYIR VVFEGLERGN YSVDIDGEGY INTTVDNIDI VDYSKRIKLG
TSINEMISNE NYNPVFLAGD VNNDFVIDMK DYKLVFDAIG SKDSKYDLNR DGSVDIADLS
YVNSNIGKTK GQVEIVDLEK ILDPENIDID TKDLKGAENI KDILTSADTV VNLGRADGEA
PSADKPLTIS MGLDTTKNGT LRTANSEGVE MESVVIKGSA VEGEDASIPS QGYITYTDVD
GNTETVPFNE ENLKRSGASN DVVIDLGSQV AVKQISINVT GNRGNKKISQ IAKIEFLNNV
YKEVPKPDMN IPTIKSLETS TNLHDERITI SWEPQANVTS YEVMYQKLNE SGQVISTKKL
QTNKTNLNIL DKDIKPYDLY RVSIQSLSGE WSSGYLTEKD VPTAFDGKAD NVDADFNPID
SYYNGDKGSV SEIQVIPLNS PEPPRNLTTN QGYKSFTVSW EQHSQARDFD IYYRKVGDSN
KNWIKANDNH KEVIEGSSDI TNPDKSKLVR SHSYTVNNLD DNATYEVRVT ATNHLGTSEM
SKSYIASTTS VTPPSMQEYK LINRPTSENE IGTTHIVDVR NKKDENGWAS QDDYLHYDSK
YALVDGDFTT EWKVDNWDTG ASYGADRGSE ITFDDTYTIG SIGIGRTLQS GHYMGLYKVK
VTYWDENDNK NVVYTESINE KWSNGNSYYM VKLNEPIRAK KIKVDTSGYG GSTQIISELK
FYEYDTLSDD IKNLYEDDLR LVLKKSVTQD VLNELAKRLD TPDAISGEYH PDKDVLKKEL
DTAQKLFDDK EVSEKITTLD ASIRTNNEGP SLGMGNSYQS LGSVARPSVD DKGTSKQIVV
YMGSSDPNTR VDIVFLQNYG LPGSYMSKVQ TVSPGRTEIT IPSIISADVE KGGQVMARVT
QGSTTANVQI RLSGVTEIPN LNVNNMINDT TKEKEVKDKI RNYISELKTY MNDINTLYPS
EVSDKDKINN VYLYDEQTSP LNTTDIEGDR FTLTLPASEI LKGIESGLEG NTEAQVNRVY
DALLAWEQEV KVGFAKKGVF EEVQDFNGNG EIDDEDRAYF RKHRAPLTRL NIKYQRMMMG
AAAYASNHHI GVGFSSSQYI QGVPYKFDEN GKVTNADSAH LYGGLIGHEM GHVMDIGDRL
YPETSNNLMT AITGTMLNEN SPYFDSFKKV YEKVTSNTIG LSTDRTVVLN MLWQPYLAYE
DNITYEMLFT DVDADLTNDS YFAKLNRAYR EMSEEERVNG DRDQWLIRLT SKVVGKDLTD
FYEAHGIIAN ETTLAYVSKF PKETKKIQYI NDEARRQRIA GTADMEEGTT LSASFADGIT
TGSYVDSKEV KINLSVDKSN DRILGYEIYR NGEPCGFIER DKANSQTVYT DTVENINNRV
VEYKAVAYDY NLNPTNEVQL GTVKIRHEGG VDKKSLIISS NTISLHEESN DIHSCDGNED
LKHALDNDKS TVYEGRMLTK DEYNSSIHTA EMNPNNNPYV ILDTTEMKTL VGIKYTAPTT
KSGFIFKSTS IADNALKKYK IEVSKDGASW TTVKEGTLNL DPQNPTETIY FDAEGVTGGN
QLSSYNARYV KITALDTKNF AASELDLITP PGDNIEIGLS DDNITYTNGI GVLKNDYEYQ
ADNPDTNENE RKFIPAGSVI ITGEYRGNPA FNVPLVLNEK EQHIADKYQG ILLAQVPDNG
NLEEVAEGTW IYWVNPEDAT KFKEDNKKIF AELYRTDAAD ALEGGQRLVS DTFKIDVPKE
LPEITLSASS RSVNEVKAID IKTDILNAIK ENR
//