ID A0A3N4ZBT7_9MICO Unreviewed; 2040 AA.
AC A0A3N4ZBT7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Fibronectin type III domain protein {ECO:0000313|EMBL:RPF22932.1};
GN ORFNames=EDD34_3611 {ECO:0000313|EMBL:RPF22932.1};
OS Myceligenerans xiligouense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Myceligenerans.
OX NCBI_TaxID=253184 {ECO:0000313|EMBL:RPF22932.1, ECO:0000313|Proteomes:UP000280501};
RN [1] {ECO:0000313|EMBL:RPF22932.1, ECO:0000313|Proteomes:UP000280501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15700 {ECO:0000313|EMBL:RPF22932.1,
RC ECO:0000313|Proteomes:UP000280501};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) 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:RPF22932.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RKQZ01000001; RPF22932.1; -; Genomic_DNA.
DR Proteomes; UP000280501; 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; 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; PTHR46957; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR46957:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR Pfam; PF17963; Big_9; 5.
DR Pfam; PF17803; Cadherin_4; 1.
DR Pfam; PF00041; fn3; 2.
DR SMART; SM00060; FN3; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000280501};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1467..1553
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1556..1650
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1652..1749
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1750..1839
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 387..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2040 AA; 213387 MW; 551DD92EAB58FB0E CRC64;
MSLVSRLMEN KRAVASAGVV TIFSGALLGL ALWYDGEATA EVVLNDSGIW VTRVSHGELG
RYNFEAGSID GVMATNSTTF DISQDGGRVL FDNDGASEAS PVDPAHLRLG GTLTLPAGAQ
VASGGAASAV YDGDTGRLWV LPFDGAPAFD EEKLDPTAEI GQGGTLAVGT DGTVYVATAA
EGGELTIVPT SGRGTPGEVE TERVSVQEGA DLQVSAVGDR PVVLDPTAET LIIPGGDRIR
VEGFAEAQLQ QPSGESDTVA VAVTDALISQ PLDGGDALKQ PASGSPAAPV QVGGCTYGAW
STTGDVIRDC PGTDSDDRQT LEGLSPGAVL EYRTNRGRII LNDVIGGNLW LPTEEYRKVD
DWDLKDNEDD EGEETDSQET VFEQVDQTVA DRDKPNKQPR PEDDDLGVRA GRTTVLNVLG
NDVDPDGDVM TASVLDGPDG STGVTVDRVL DGAALQADVP ADATGTITFT YQVDDGRENG
TAEADVTLTV RPPEENKAPE LMADDVSGPV LKAAQGGTAT INVLPYFKDP DGDDLFLSTA
TTKDPNDEVR SRPDGTLEFL DGGGATGRKI VDITVSDGEG AIAKGLVNVQ VESDNQPPIP
VQDHVTTLVG DPVTVRPLAN DSDPDEDRLR LVEVGDAESV EITPNHTAGA FRFVSEKPGS
YDIPYYVSDG PNPTVTGLVR VDVLEPPDDA GKPVVVSDQA LLPKGGEGLV DVLANDTDPA
GGVLVVQELD VPEDSGLTVA VLDHQVLKIT ENRRLESTVT IGYTVSNGEA AADGQVHVVP
IPTSERLRPP EAGADEVDVH VGDTVTIPVL KNDSHPDGLP IELATDLVEE PAADLGEGFV
SEEVVRFKAG DEAGVAHAVY EVSDPNGQRD SAQITINVRD DEKNAAPQLP DVTARVLSGG
TVRIDVPLDG IDPDGDYVML SDISGAPTMG RARITDGFID FEASPDAVGT DTFTYSATDT
RGAVGIGTVR VGIAPLPETN QKPVAQDDET LVRPDRTVAI DALANDTDPD GDEIGLVESL
FGSTGDLDPA VVDDQVIVTA PSEAGEHPFY YGIQDSYKAR AQAAITVKVS RDAPLLPPVA
NDDVLSIPDV VGKDAVTVDV LANDVDPDGV AADLEVSLGS DAGAATLTDD GGITVPMEPD
LQIITYTVTD MDGLESSAFI RVPGDSLTPH LKPGLDPLEA ISGEPLEIDL NEYVVVEEGL
EPRITEESTV SAVEGSVEVT GLAGMTYVSK KDYIGPASVS FEVTDGDSPE DPDGRKATLT
LPIEVRARDN QPPEITGSPV LEVPAGDEGA VDLAAYVRDP ENDELTFDVE GGGDGLAASV
QGSTVTAQAE PSVTKGASQT IPFTVTDGHT DPVRGDLTVQ VVASNRPLAV TGDDVVDGAH
EGVAENVAVL VNDTNPFPET PLELFGVPVV ETGSGTATYS GDQVVVTPDE GFHGAMRVKY
TVQDATKDPD RQVDGVVNLT VLGKPEAPRA PRVEEVRSET VVLTWDEPNN NGAPIESYTV
TSSQQDEQQC PTTTCTFSGL TNNVTYTFTV QAENEVGLGE ASAPSQEARP DEKPDQPAPP
ELDFGDQALD VTWVNRTYTD RSPIDCVNLE ISPAPPSGPI QKECLQGTST TWEGLENGTA
YTVRVQAENK APDPSEWSDP SAPEVPAGPP EQPAAPTATR VNTNLGGQVE VSWTAPANNG
DAIKDYDLDI LQGGSVVRTL PDIAGTSQTV QNLDTDKSYT FQVTARNKAG NSERSPQSNA
VLPHGTPDRP GTPSAQLGSN TSGQADVSWG AIGDFRGTGG YYEVRANQAN PKGPITGTSY
TYQGLSNGTA YTFSVRACNA QGACSAWSGE SSPAVTPYTV PGTPGVTWHR SGNGQGGYFT
VRGPGSDGGR AVQRIEWRAS GSWSNSGTIQ QGGWPTNITV GNNGYDRTYT LQARACNVAG
CGSWASATGT TVSAPDPQAT VVHGSRVNNS DCRHSSCARY KVNYSDFPQG SHRVECWSGT
NPTTPGWHNI IDGSTSPGGA GETRTFGGTG SIELRCFYGH PGTTVGVVID GKDVYSRSTW
//
