ID A0A2A9EVE9_9MICO Unreviewed; 2042 AA.
AC A0A2A9EVE9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Fibronectin type III domain protein {ECO:0000313|EMBL:PFG42139.1};
GN ORFNames=ATJ88_0790 {ECO:0000313|EMBL:PFG42139.1};
OS Isoptericola jiangsuensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=548579 {ECO:0000313|EMBL:PFG42139.1, ECO:0000313|Proteomes:UP000224130};
RN [1] {ECO:0000313|EMBL:PFG42139.1, ECO:0000313|Proteomes:UP000224130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21863 {ECO:0000313|EMBL:PFG42139.1,
RC ECO:0000313|Proteomes:UP000224130};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG42139.1}.
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DR EMBL; PDJJ01000001; PFG42139.1; -; Genomic_DNA.
DR Proteomes; UP000224130; 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; 2.60.40.2810; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
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; PTHR44170:SF30; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF17963; Big_9; 4.
DR Pfam; PF17803; Cadherin_4; 1.
DR Pfam; PF00041; fn3; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR SMART; SM00060; FN3; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS50853; FN3; 4.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1490..1576
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1579..1671
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1675..1767
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1768..1860
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 383..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..401
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2042 AA; 212195 MW; AD45EF4E8CECFBC1 CRC64;
MRADLAVDDA NVTARHHLGG EVSILTRLRA DRRTSISTAV VLAFSGGVAV AAMLYDGEAT
ASVDLDDSGV WVTKESSGLV GRFNTEAKAL DGTLLAGSAS FDVQQQAGDV LVADGGNSSV
SVVDVARLKY ASTTLLPAGA AVASGGGHVA ILDPEDGRLW TTTVERLPGF DATETDPTVE
LDAAAKIVVS PGGTAFAVVP ETDTLWTFAP GEDPASTELD GLLAAGDDVV LTTVGDDVVV
LDRTGARLRL PGGDVVTVPD AQGARLQQPG RDTDAVAYAT VSALVMQPLD GGSATTRRAS
GTPAAPVQLG GCLYGAWSGT GQILRDCAGT DADLDRTLDG IDADTRLEYR VNRNAVVLND
LSAGTLWMAL DEYEKVDDWE VQRPEEGDGE DENADDDTPE LVDNTIVDRE RQDPPEANDD
RFGVRPGRAT VLDVLANDLD PDGDVITASF DGDQPDDMTI QEVLGGKALQ AVVPQDATGR
ASFRYTVSDG RGGEDTAEVA VKVVPWEENS APEQTGEPVL KVQQGGSADI RVLPFFRDPD
GDDAYLATAS STVKGDEVRA YPDGLVEFQD DGSATGRKKV DLVVVDGQGD AVEGTLWVDV
IGDTPEPPIA VGDHVVVPAG EPVTVEPLKN DSDPNGDTLR LASVSEAAPA EITPNYDAGT
FTFVASEPRS YDILYQVSDG PSSTTGVVRV DVLDPDDAAG PPVVVADTGL LPAGGSTLVD
VLANDVDPAG RVLVVQSVEV PDDAGVTVAV LGHQMLKVTE SRRISEPVVM EYTVTNGEES
ATGQVRILPV PAPEKLQPPH ASPDEVTVHT GDYVNIPVLA NDTHPDGLEL ILDDELEQGV
DPSLGEVFVA EDMLRFRAGA EDGTAYAIYK VSDANGQEDS AQVTIHIRGG EDNAAPVPHD
VEARVISGGT VRVRVPLDGI DPDGDSVRLV NLVRPPTKGL AQIVEGRYVD FRATRGTSGQ
DTLTYAVQDS RGETAVGTIR IGIAAPSTKN HPPVVEDDSV TVRPERRVAV PALRNDSDPD
GDQIGLVPGA LEAEPPLDPE VSQDRIVLET PGDEGTYSFY YAVEDSWGAR AMGTVSVQVA
EDAPLLAPVA RDDVVLPDAV TPTTTEVSIV ALENDEDPDG SADELTVTVD SPQAVVDADG
VVTVTLTDER QLLTYTVTDQ DGLSAKAFLQ VPPLHRAEAQ AADEPEDLGP APRLKDGFVA
LEVLSGETLK IDLTDAVVVA EGGTVAISDA GSVSAVAGKA DIVDAQHLTF VSDPDYVGPA
AVSVQVTDGL EDADGESRTA LVQVPINVLP PENLPPEPGS PSGQVAAGEE SSVDLSRYAT
DPNPEDVLSF ALGSVPEGLS ASVTGDVVSV QAAPEISKGS SFSIPFTVSD GVNPPVDGTI
AVEVAASTRP LPRANPDTVE GAHQGVAVTV PVLENDVDPF APEGLEIVGT NVETGVGEAT
FDGADTVVVS PGASFVGTMV VVYRIQDVTK DPDRQVEGRI TLTVLGVPEA PAAPLVEEVR
SETVVLSWTP PVNNGAEITG YTVTSSQGDT FQCATTTCTL DGLTNNVTYT FTVVATNEVG
DSKASPASAE ARPDEKPDPP AAPTLVFGDK SLEVTWENAT YTDRSPIQAV NLEISPALPS
GETQKVGLTG NRIVWEGLQN GTAYKIRVQA ENLAPDPSEW GAWSASEIPA GVPDAPAAPT
ATRVDTPLGG QVNVSWTAPY NNGDAIKAYS VDVYAGGSKV QTVETSSTSY AFTGLDTKST
YTFDVKANNK AGWGATSARS AGVTPYGRPL TPSAPSASID AGDVVVTWAA ADGNGSPITG
YTVTASNGSR TTTTGGRSVK FTSLPDGQNV TFTVTATNAG GTSDASPASN AVKPFSAPSA
PSVSWTKTSA TDGRFTVSGP GSWNGQSGTV HWSMSGSESK SGTGTGNVGV SGGYGKSYTL
QARACNDAGC SAWRSASGST DAPPDPRIWT SDSGIVFKVS GCDTNNCTRV RVHSNADVPS
GTYSFRCWND RNGPSNFSTQ TAYLASGGYA DLYCVVGIMN GANVWATVDG KSWTFEKRAW
PR
//
