ID C6VTQ4_DYAFD Unreviewed; 2135 AA.
AC C6VTQ4;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE SubName: Full=Fibronectin type III domain protein {ECO:0000313|EMBL:ACT92997.1};
GN OrderedLocusNames=Dfer_1756 {ECO:0000313|EMBL:ACT92997.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT92997.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT92997.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
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DR EMBL; CP001619; ACT92997.1; -; Genomic_DNA.
DR RefSeq; WP_015811251.1; NC_013037.1.
DR STRING; 471854.Dfer_1756; -.
DR KEGG; dfe:Dfer_1756; -.
DR eggNOG; COG1749; Bacteria.
DR eggNOG; COG3386; Bacteria.
DR HOGENOM; CLU_231939_0_0_10; -.
DR OrthoDB; 505641at2; -.
DR Proteomes; UP000002011; Chromosome.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 2.60.40.650; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR046540; DMFA2_C.
DR InterPro; IPR025141; DUF4082.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR InterPro; IPR032812; SbsA_Ig.
DR Pfam; PF13205; Big_5; 1.
DR Pfam; PF17957; Big_7; 1.
DR Pfam; PF20254; DMFA2_C; 1.
DR Pfam; PF13313; DUF4082; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
DR PROSITE; PS50853; FN3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002011};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1498..1592
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1517..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2135 AA; 227062 MW; 77ABE1EB73EC43CD CRC64;
MLRKLHYSIR FFIALIFLLG VAGIPVVAQN AIVTENTLPG SPPSEWDVDG SGDLSIQGFA
TDISYNRGET AVFKIKTDAT GYTVKIYRLG YYQGNGASFK GDATITASSL PQTQPTCLTN
PTGLVDCGNW EESARWDIPT SAVSGIYIAK LQRTDTPEGE DPRASHITFV VRDDASTADL
FFQTSDATWQ AYNVYGDNDN GRSLYTGVNG IGKASKVSYN RPFLTRTGGG GGGAYEDFLF
NSEYPMIRFL EKNGYDMSYT TNIDTDRRGE LILNHKVFMS VGHDEYWSQA MRNNVAAARN
AGKHLAFFSG NEVYWRTRWE NSISTGEADR RTLVCYKEGA EGENQCNGKC DTSSPEWTGL
WRSGCEYTGS GGCNPENELS GQISWDGTTG TIQVPSNYKN LRFWRNTSVA QLSDGSSETL
TANTLGYEWN PEQENYRSSY PAGRILLSRS VVAGKIHHLS LYKHSSGALV FGAGTVQWTW
GLDDQHDRGN EPVSRTMQQA TINLFADMGV QPATLQTDLT AASESDDDTA PTVAITAPAE
AGNVPVGSVA TITGTAADGK VIAGVEVSTD NGVSWRLATG TNAWTFTWVP SQQGAATIRA
RSFDDSGNIS EVAITNVNVS EPEPLPCPCT VFLPTDVPDG NVHNDGGRAI QLGMKFRSAV
AGFVTGVRFY KHPSNTGTHI GQLYSNAGVL LAEATFVNET ESGWQQVQFG APVAISSNTT
YVISYHSSQG YYSAMDSYFQ VPKQTGALKG LANEEDGKNG IYIYSATPAF PNSNYESSNY
YVDIVFETES GPDTAPPTVT MTSPGANATG IHINNNITVR FSEGIDAATV SGASVVLSSG
GQEVPANITY DAGSLTVTID PASALGYATV YTLLVKGGGA DPRIKDVAGN ALAEDFSFSF
TTQNAPGPSP NDGPGGPILV LSAGANPFSR FPVEILRAEG LNAFAAKDIS EISGNPALLD
AYDVIVLGEI GLSGDNINAL TAWVNAGGTL IGLRPAAGLA SLFGISPAGG SLSDRYLKVN
TATGPGVGIV DESIQFHGTA DLYTLAGATS IATLYSDATN ATINPAITLN NVGPNGGKAI
AFTYDLARSI VYTRQGNPAW AGQERDNQSG PIRSDDLFFP DWIDLNKVAI PQADEQQRLL
ANLILLGNLH KKPLPRLWYL PRGLKAAVIM TGDDHGSGGT IGRFDDYISR SAANDQQAVD
NWTAIRGTSY IYPNTPITNA QASAFQAQGF EIGVHLNTNC SNFDETSLRG FFNTQLAQMT
NNFPGLSPTI TLRTHCIAWS DWATMAKVEL ENGIRLDANY YYWPGSWVAD RPGMFTGSGI
PMRFADLDGS LIDVYQAATQ MTDESDMSYT KHITTLLDNA LGSRGYYGVF TANMHTDASG
STGSDVIITE AQARQVPVIS ARQMLTWLDG RNNSSFGALS WTGNTLNFTI SAAAGSGSMQ
AMVPTEAQNG HLVGITVDGN TVSYSTQVIK GISYAFFPAN NGSYVATYEV TETNQAPQIS
NVTVTQPVAG SATITWTTDE PADSRVDYGT SGDALTQNSA TTTPTTSHSV TLTGLLPGTT
YHFRVTSADE LAASSTSPAS SDAPLSFTTA PNADPACFED LTAAHFSEGT TGTGTLVTAG
GVTLKPIIVE DFTNLPPTEQ WQSFPWDGGG SSTISDGQLV VNGARFNTEP VGNTLSPGTS
IEFVATFGAS TFQHIGLGAG NNTDMYNSAG TWIMFSTGAS GAMQARVNLN NSPEDVNLGG
GLIGTPHLYR IEWNATNILF YVDGTLVHTS SKVISTPMRF GISDYHMGAP GVSIDWVRIT
PYVPSGSFTS RVYDAGGIKT WQTANWTTTL PEGTSVQLLQ RQGNVAEPDD SWSAFTSIPG
SGSTVGGSSR YIQYRADLST SNTAVTPVLQ SVAIHCADPV VTCNAGTEQV ALSANAITNT
CPVTTVNLSS LVTGTLPEGV LAVFYTTADH QEGTQVADPL AAPASGTYYA FYFDTHNSCF
NTANSTAIVT ATATDCTIPT DLRPYLVMDH VEFTADAVTN PLSLRVRNTK VGSNATARIY
VQIYKPVPGA TIALTGQAAV DWVQESENAN YYEFYTDVDI PYAPTGGYVI TATLTIPAAA
TNGAYDFKAS IKDNSGGEDP ASYTNNNVVI GVSKQ
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