ID A0A0Q8AGI1_9MICO Unreviewed; 1783 AA.
AC A0A0Q8AGI1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Cell surface protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASD56_02120 {ECO:0000313|EMBL:KQZ85184.1};
OS Microbacterium sp. Root166.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736478 {ECO:0000313|EMBL:KQZ85184.1, ECO:0000313|Proteomes:UP000051650};
RN [1] {ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|Proteomes:UP000051650};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ85184.1, ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|EMBL:KQZ85184.1,
RC ECO:0000313|Proteomes:UP000051650};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ85184.1}.
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DR EMBL; LMGL01000001; KQZ85184.1; -; Genomic_DNA.
DR RefSeq; WP_055960672.1; NZ_LMGL01000001.1.
DR STRING; 1736478.ASD56_02120; -.
DR OrthoDB; 9802683at2; -.
DR Proteomes; UP000051650; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00146; PKD; 4.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003952; FRD_SDH_FAD_BS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029865; KIAA0319-like.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR46182; FI19480P1; 1.
DR PANTHER; PTHR46182:SF2; FI19480P1; 1.
DR Pfam; PF13385; Laminin_G_3; 2.
DR Pfam; PF18911; PKD_4; 4.
DR SMART; SM00282; LamG; 2.
DR SMART; SM00560; LamGL; 2.
DR SMART; SM00089; PKD; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF49299; PKD domain; 4.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
DR PROSITE; PS50093; PKD; 4.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000051650};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..1783
FT /note="Cell surface protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006333527"
FT DOMAIN 615..787
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1016..1096
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1104..1189
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1406..1486
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1490..1577
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 1783 AA; 183745 MW; 8DEEAADAB7582BBE CRC64;
MGVFAESGNG RKRSAIAAIT TSIALIIGSL AFTAPAANAD VSPPEGDPPT VTGDALPTVQ
INGIVWDQEI VGNVVYAAGS FSSARPAGAA AGTNETPRSN LLAFNLTTGA LITSFAPTIN
AQVRQVEASP DGTRLYIVGD FTTVNGSNRN RVAAFELPSG ALSSFNPNSN GTTIGVDATN
TTVYIAGTFG RVGGQDRFGA AAINRDGSLQ PWAPVLEGRQ GRVVVVSPDG AKVVIGGNFQ
TLNNSSNPGY GLAMVSAADG SLLPFATNNV IRNAGNDAAI LSLKSSGDDI YGTGYVFGEG
GNLEGSFRSS WATGDLTWVN DCHGDLYDVH PFGDTVYQAG HPHYCGSLVG GFPQSDPWTF
YRGTAVTRDV ERITPYGLNL GYYDFGGNPA PKLLHWYPTF NAANVSGAWQ GPWTVTAGGD
YVVFGGEFTR VNNTGQQGLV RFAVPSKSTN AQGPILWNTA WQPTALALSG GSIRVSWPLN
YDRDSEFLKY EVLRNNVVIK TFENVRSKSP DWGLPPMAFV DTSVTNGTSY TYQIRATDAQ
NHSITGATVS VTASGTTTAS AYRSAVLTDT PLSYWPLDDS SSTVSYDWAG ASDLAVRGGV
TRETEGAILG EPRASSDFNG NSDGFASTTN AIAGPNSFGL EAWFKTTTNS GGKIIGFGNS
STGTSSNYDR HVYMEPSGQI TFGVYPGSSQ TISSGSTFND GQWHHMTAGM SENGMILYID
GVRVAQRTDI TSAQPYNGYW RVGGDSPWSG NAFFDGQIDE VAVYGAPLTK QQTAAHYNAS
GRTLVGSTPP ADAYGAAVYD LEPALYWRLG ESSGSVAEDA SGSNQRGTYF GAVAKGTTGA
LTGVSNTAAT FAGGQVISQN SFTNPRSYSL EAWFKTSTTT GGKLIGFGNS SDGNSSGYDR
HVYMTPDGKL IYGVWVGFGD TLQTSDSYND GQWHHVVATQ GAEGMRLYVD GALKGTNGQT
NAQDYTGYWH VGGDVTWGPG DWEFDGTIDE VAVYLGPISP TDVAAHYGLG STGEPANVPP
TADFTAVPTK LKVDVDASAS DDPDGTITGY SWNWGDGSPA GSGETATHTY GSAGNYTVTL
TVTDDDGATA TEQTVVNAVA NQAPTASFTS AVNGRTVNAD ASGSNDGDGT IASYSWNWGD
GTATETGVTR SHTYAADGGY TITLTVVDNE GASTTTTAAV NVTAPVGAVT YASDAFNRTV
ASGLGTADVG GAWQLANPAS NYLVNGSAGT FVQTAGGVQR YAYLPSVAST DTALDVDVAL
PQRPVGGSAY YTMFARRVGT VDYKSRVIVA ANGAVTVQLQ QTGAVLTNVG TSLNLAAGEA
LHVRTEATGV SPTTIRVKVW KVGTTEPAAW TSSTTDSTAA LQAAGHIGLG VYLGGSVSNV
PFQTRFDNLW AGSTAGGPNP PANAAPVAAF TATPNGLSAT VDASTSTDSD GTIASYAWEY
GDGGTATGVT PTAHEYASAG TYSVKLTVTD DDGATGTITK PVTVTAGGPV NQNPVAAFTA
TPTNLTVSVD GSASTDDGTI ASYAWKFGDG STGTGATASR TYAAGGTYTV ELTVTDNLGA
TNTITKPVTV VAPAGAPFAL DDFGRAAGAL GAAPTGGTWT QNLGPASIAI DNGAAKFTTL
AAGQTLTATL NTATATSTDL TFSFSAPAVP AGGRVYISAL GRVVGAEDYR ARWLIGTNGA
VQAQLSRGGT VIVWQDLAGV TLTPGVKYNV RVQVFGTSPT TLRSKIWAQG TTEPAAWQLS
TTDATAGLQV AGHTGISTYA GSTLSNVPFS ILFDDYRAAG VTP
//
