ID A0A3D9L8F1_9MICC Unreviewed; 2051 AA.
AC A0A3D9L8F1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Fibronectin type III domain protein {ECO:0000313|EMBL:REE02595.1};
GN ORFNames=C8E99_0368 {ECO:0000313|EMBL:REE02595.1};
OS Citricoccus muralis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Citricoccus.
OX NCBI_TaxID=169134 {ECO:0000313|EMBL:REE02595.1, ECO:0000313|Proteomes:UP000256727};
RN [1] {ECO:0000313|EMBL:REE02595.1, ECO:0000313|Proteomes:UP000256727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14442 {ECO:0000313|EMBL:REE02595.1,
RC ECO:0000313|Proteomes:UP000256727};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUL-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:REE02595.1}.
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DR EMBL; QREH01000001; REE02595.1; -; Genomic_DNA.
DR OrthoDB; 5241356at2; -.
DR Proteomes; UP000256727; 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; 3.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.40.2810; -; 1.
DR Gene3D; 2.60.40.3440; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR041690; Cadherin_5.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040853; RapA2_cadherin-like.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF14; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR Pfam; PF17963; Big_9; 5.
DR Pfam; PF17803; Cadherin_4; 1.
DR Pfam; PF17892; Cadherin_5; 1.
DR Pfam; PF00041; fn3; 3.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS50853; FN3; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000256727};
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 1485..1571
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1572..1665
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1669..1763
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 377..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2051 AA; 212587 MW; EBC6851249F401C2 CRC64;
MGNKRKQLKS VATPVAFSAI GALVATGAFL YPGFDTADLE LHDSGVWVTH NSGGYVGHLN
HESTILDGGF RPPMEGVELH QEDATALMLD PASGALTSID TTSMVAGDQI MLPATQDFAL
GASVISASNP SEGTVYAGTV DPSPQISTDE PLYEAEGAVT STTTVEGEVL VADLGQDTVV
TFGAEDDQPG ALVETGRDGV EGLSGLQEPQ LVAVGDVPVV VDPASGTLSW PGHSVQDERL
VGAVPQPSGP EAERLALSTE RDLFTVALSN GGIQTMSVTP PTDTSAGSTT PAGADGGVAA
TAPVRVAGCL HAASAVTGHY VQDCDGEERD QIVPIPDLQS GAELVFRVNR DVVVLNDTMS
GTNWMVLDQM KVVANWDDLE PPKGEGEETE EESDEVTQET ALPERQEENR PPVAEDDSFG
VRPGRTTQLP VLFNDSDPDG DVLTASLEGD QPPVGTVQEI IDGIGMQIVV PESASGRAEV
TYAADDGRGG TDTAQISLRV VPDSENRGPT QERKAVLRVP AGESVTSQVL TDWIDPDGDD
LQLVGALAEE PDTVRTRPDG QLTFQDNTGE AGRRDIQVSV SDGRETTTGT VQIEVLERGS
VHPPITQADH VTVQAGQEIT FYPLENDTDP LGGQLRLAQV AAAENAEIDY SAAGGSVQWS
SDVADTYYVE YLAANEYDSA PGLIRVDVVK SEESSGLPVA VRDIALLPAG GQTLVNVLGN
DTDPTGGVLL VQGVQDATTE SGASAPLKLA VEDFNHIRVV DTGGMTGPAT FTYSVSNAQG
TAQGEVTVVP LPEPEVMQPP IAVADTANVR VGDVVTIDAL ANDTHPNQEE LTLVPELERQ
VAEDRGIGFV SDGKVRFRAG SEPGRATLAY TVRAPDGQEA SATVEITMVP MDRESNNPPV
PLSVSARVLS GESVAVPIPL DGIDPDGDSV TLEGVQSPPS QGSVRMEKGR MIYTASGAAT
GSDVFTYSAV DRLGARATGT VTIGIAQPLS TNHPPVALDD SVEVRPGRTF TTNVLANDAD
PDGDQVALVQ GRFAPSQPEV PVDIVDGRVR VVTPETEGFL NIGYTIADPA GATATANLSI
RVDEEAPLMP PIARDDLVGV EEIDGREQIS VSVLDNDEDP DGAVEELELG VDEAAQTAGA
RVESSNVVVP VQSAAQVIMY SVTDVDGGVG RAFILVPGND HRAPWLTTTD PLRVVAGEEL
RVDLTDHIGV RDGRTPRLTD DSSASATPAT AAFTVGSATE VRFTAPADYA GGASVNVTVT
DGEDGSDPNG LVSTLSIPII VEPRPDENNP PTVQSSSLQI EQGGDPVTLD LSPLATDPDG
DELTFSRGQV SGEFAAELDG TELTVTPSSN AERGTAGTVA FTVSDGEAEP VTAEITVDVV
GTSRELPRAL DDEIPDARSG EPVTVNVLEN DINPFEGEAP LTVTAAQVVT GEGTAATDGS
TVTVTPGQDY SGRMQVTYTI QDLTADPTRE VQGNITVIVK GRPDVPGVPR IESVDDQTVE
LSWAAPPDNG DPITGYTVTD TTTGSTQQCS STACSITDLE NAVEHRFTVT ATNGVGESDD
SGLSAPAIPD VRPEQPAPPT VDAGDGLVTV QWTPPVNRGS AITDYRVQLS PAPPGGGLRS
AGAGTSLSWD GLTNGVDYQF RIQAVNQADE PSEWSGWSVA ATPAGKPLAP GTPSAVRDTS
AVDGGVVRLI WSAANDNGAA LRDYTVTAHS GSSSQSRTVG AGTTSMNWSG LDKSTAYTFS
VVARNAEGTS PSSGRSAAVT PYGLPGAVSG LTTSPTGANR ELDISFSGAA SNGSPVSYQY
SLGSGWASLG TSTSSTITVP ANGSTYQLSV RATNAAGAGD SRTVSTQVAY GPFAMPTIRA
TPQVGSVKFT WSPTNTSTIG NGRSVTVTPK VDSTTVDNNG SFTTARTREA TSSTLTIQVC
VTGTSTCETV TQSGTSLAIP DPSVSITRGG SAASYARCST GEFTDCWLTD KTFSNFDPGT
TIEYTCTAVG SSTTERPGEV FTFGEYSTTV GSNGSASLSD TTCIAHDGHR QIWLDLTSHG
IESNRLQGPG D
//
