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Database: UniProt
Entry: A0A1R4FVB1_9ACTO
LinkDB: A0A1R4FVB1_9ACTO
Original site: A0A1R4FVB1_9ACTO 
ID   A0A1R4FVB1_9ACTO        Unreviewed;      2176 AA.
AC   A0A1R4FVB1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Fibronectin, type III domain protein {ECO:0000313|EMBL:SJM59859.1};
GN   ORFNames=CZ771_11340 {ECO:0000313|EMBL:SJM59859.1};
OS   Actinomycetales bacterium JB111.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales.
OX   NCBI_TaxID=1434822 {ECO:0000313|EMBL:SJM59859.1, ECO:0000313|Proteomes:UP000196124};
RN   [1] {ECO:0000313|EMBL:SJM59859.1, ECO:0000313|Proteomes:UP000196124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB111 {ECO:0000313|EMBL:SJM59859.1,
RC   ECO:0000313|Proteomes:UP000196124};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FUHX01000066; SJM59859.1; -; Genomic_DNA.
DR   Proteomes; UP000196124; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 4.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR040853; RapA2_cadherin-like.
DR   NCBIfam; NF012211; tand_rpt_95; 1.
DR   PANTHER; PTHR14340; MICROFIBRIL-ASSOCIATED GLYCOPROTEIN 3; 1.
DR   PANTHER; PTHR14340:SF9; TITIN; 1.
DR   Pfam; PF17963; Big_9; 4.
DR   Pfam; PF17803; Cadherin_4; 2.
DR   Pfam; PF00041; fn3; 2.
DR   SMART; SM00060; FN3; 4.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   PROSITE; PS50853; FN3; 3.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196124};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        89..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1602..1689
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1690..1780
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1782..1876
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1670..1708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1861..1887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2043..2062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..512
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2176 AA;  229147 MW;  2E0E2E873ED7DA0E CRC64;
     MPPRRRRDHG SADDASQQRP TADTPTAPPP IDPADDVGAS PAPARTRAGS RPAPAAGSRP
     AGTSGAGTSA AAASGEDRRE ARRHKRRRAV ASSTSLAVVA GAVVVAAFSY DGEPVADIEL
     HDGGVWVTNS DELMVGRVNY PVQELDGSVT TASDEVDVLQ DGSTVFVVDS GAALLQTLDP
     ATVSTGTGAV TIPRGADLQL GGGTIGMLDP STGALRAVPV EGANYLGDAE AEPAAHLGED
     GQLAVGPDGR THGLSIDDAS VVTVEPGGVD DGSDAPGAPQ GGESASESAS ESPTTEPVAE
     EGDQDEEEAS EQVRTRALAT TPDALDLAEQ VALTSVGDRS VVAVITEDND ELLVYVDDAE
     PIDLTAYDLD LAEVAVQQPG ARSDEVVLAT RDALVHVPLD GGEPSIIRSP REGGPAQPIV
     VGDCVHGAWD GADEGSYLLQ CGNGEPADAP IPLRGSDHAL RLRENHGLVV VNDTLTGTVY
     LPQEDMQLVD NWDDTTPPDG ESEDETDSPD DRLEDVPPDR EEENRPPTAN PDSVGVRAGS
     TTVVEVLAND TDPDGDLLTV TDVEDAGEQI GDISVIEGGR AVQITVPAEA TGRITVPYSI
     TDGRENGESS STLTVEVVPD DVNSAPEVRE GREPRMDLAL GGTATIDVLS SMVDPEGDAM
     VLESAETDSD DVVHFTPDGT LTFVDTGTSS GLKEVTVRVS DGSDTTEVTV PVEVRESTNL
     PPRAVGDFIA VTEGEEVLLD VLANDVDPEG EPLRLGSVTT ADIVEVTPDY DTGQIHLEGL
     TEGTAYLEYV VADAGGADAT GLVRVDVVAP DPDAAPIAVR DTALLPAGGT TLVDVLANDD
     DPAGGLLAVQ QIDVPPDSPL VVSVIDHRLL RISAQTTPTG PQTLTYTVSN GSRSAVGEVT
     VLPILADSAP QPPVAEPDVV DVRAGDYVTI PVLQNDSHPQ GMEFSLDPEL QEVPDGDRGH
     FFTSGDVVRF RAPDTPQTVN AVYSITDENG NGASALITVR VQASSESNAA PIPEPIEVRA
     FGGERIRIQV PVYGIDPDGD SVQLLGADTA PSLGRIVEIG PGYLDYEAYG QSSGTDTFSY
     AVRDRLGAIG SAQIRVAVVP PPISNSRPQA QADSLEVRPG RTVDVDVLRN DTDADGDPLY
     LADAPDGGPF DAMPELAPEA TEQHLIRITA PLTEGRYPLT YRASDRRGGI DSAVATVTVS
     EDAPLLPPIA RDDLVAPADI IGHDVVTIPV LANDEDPDGT ADALTVELID VPEGARVTGN
     NIQVPVLAER QVLTYRVEDP DGLEGFAFID IPGSESTAPV LRTNVRPIEV HSGELVEISI
     YDYVVAPSGR PIRLTDTSQV TATNSDGGSP VVDATTLQFR SAEDYYGPAS ITFEVTDGIT
     ARGSLSSRLT LPITVLSDGV NIPPTFRGGE MDVVPGEGEA ALNLRSAIDD PEDFSELRLD
     FGEDGLPEGL EGRIEGHTLY VAADVDLAPG QTLDVPMTVS DPENDPVPSV IEVHVRPTDR
     DVPSVPDVNI GEVEQGDTVA VDVLDGAFNP FEAEGEPLTI IGAQTERGTA TVDHSLSDVS
     ITPGADHVGP VTVRVTVEDG TGLPTRRAEA RITMNVIGAP GRPTPPRVVD EQDSAVVLTW
     PAPVSNGSPI TGYTVDTAGH RQVCATTTCT ITGLTNAQEY TFTVIATNAV GDSDPSAPSG
     PAMPDVRPER PNAPEAERGD GSASLGWEVP ATRGTPVERY DVQVSPASGS GQISETSTAY
     MWDGLTNGTS YTFRVRAYNQ ADEPSEWSPW SAPVVPAGPP TAPGEPQVQR VDSPIEAQIS
     GSFGEAQGNG APVTGYEVII YQDGNEFSRF ETTGTSFTQD APEGHEYTVA VVAINEVGTG
     PASPRSNSVR SFIKPTAPGR PTATATGTSR EITLDYSAAD PRGDEIVRYE VSTNGGEWRE
     LEGDRITGLD NGSSYQFRVR ACNQYCGDPS PASATQIPYG PMGTPDLRLE YQEPTHWGDP
     AQIDYGWGVP NGNGRPIVSA TVTTGLGTRR DGLAANGYTE NVEWDRTYQA TITVVRDLGN
     GQTDSVTATA SEPVPAQPPR PERSVDIRFV RDGRDEPRQD CDDDNDQCRF LDFTWTNFGD
     YWSQEGPYEV RWINVDDDDE LINSRPFWRN PDQFDFPQED GQYQSSRAVG ADITVRLEIR
     NRDGDVVASD TYDIDP
//
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