ID A0A0N1D8L2_9MICO Unreviewed; 1572 AA.
AC A0A0N1D8L2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Cell surface protein {ECO:0000313|EMBL:KPG87040.1};
GN ORFNames=AEQ27_03770 {ECO:0000313|EMBL:KPG87040.1};
OS Frigoribacterium sp. RIT-PI-h.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1690245 {ECO:0000313|EMBL:KPG87040.1, ECO:0000313|Proteomes:UP000037934};
RN [1] {ECO:0000313|Proteomes:UP000037934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-h {ECO:0000313|Proteomes:UP000037934};
RA Tran P.N., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-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:KPG87040.1}.
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DR EMBL; LHOZ01000042; KPG87040.1; -; Genomic_DNA.
DR RefSeq; WP_054145444.1; NZ_LHOZ01000042.1.
DR PATRIC; fig|1690245.3.peg.3244; -.
DR Proteomes; UP000037934; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; 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; cd00110; LamG; 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; 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 InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
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; SM00060; FN3; 1.
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; SSF49299; PKD domain; 4.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS50853; FN3; 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:UP000037934};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1572
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005868924"
FT DOMAIN 456..556
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1012..1101
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1099..1181
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1187..1268
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1272..1360
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1572 AA; 160247 MW; 8A26C23FF91824E5 CRC64;
MGRTVSSRLR LPAIVAASSV LLSVLIGVQP AQADSAPADP TSPSTPATVT ADALPTPQID
GSVFSQVIVG NTVYAAGKFT KARPAGSAPG VNEVPRSYLL AYDITSGALS TTFAPVIDGQ
VKALAASPDG KRLYIGGAFT KVNGVAKYRL AALDPATGTL VTSWNPGTNA TVNAIAAVGP
NVYVAGVFSS IGKDTRTKAA AVTASNGTNL AWAPQIAGGD VLAMVASPDG SKIVLGGSFS
SVNGSSQPGY GLAMVDSTSA ANLPFQANDV IRNGGGQAAI YSLSATANGV YGSGYTFGGG
GRLEGAFKST WGGDLVWVED CHGDTYSVAA NSTAVYIAGH PHYCGNIGGQ PQTDPWTFQR
AMAFSDSATQ TVTNDPMGYY NFAGNPAPSI LNWFPDFGTG SYTGQNQGPW SVAANDKYVV
YGGEFPTVNG KAQYGLTRFA VSSIAPNKEG PVYSGALFEP TLVSLESGSV RVAWQSNWDR
DNANLAYQVY RDGNLTTPVY STTASSTFWK RPSIGFVDKG LTPGSTHDYR VRATDPLGNT
VLGDTVSVTV STTAPSPYQQ QVSADGATSL WRLGEKSGST VYDSIAFDDQ QAQAGVTRGA
SGQASTDSDG SSTFSGTDTG LSSTTSAITA PQTFSVQAWF RTTSTTGGKI VGFGSNRTGL
SGSYDRHLYM DPQGRVSFGV YPGSSRIITS PTALNDGQWH QVVGTLSSAG QSFYVDGKKI
ATDAGTTSGQ DYTGFWRIGG DNNWNGAPYF QGDIDDVSIY PTALSGKQVD GQWVASGRAS
RLPKAPTDAY GARVFQDDPE AYFRLDGDGG SVAADSSPVG TDGLVSGGVT TGDAPAISSG
SGHSARFDGS SGGVSTTTSY DAPNTYSLET WFNTTTTSGG KLIGFGNQQT GYSGNYDRHV
YMEQDGRLQF GIWTGQMNLA SSTASYNDGR WHHMVATQGP DGMKLYVDGA QVGSNQATGS
DGFRGYWRLG GDSSWNSGSG YWAGSLDEAA VYARPLDATT VAQHYALGAD KPNASPTAAF
TSSTTGLGAT FDGSTSVDGD GSVASYAWDF GDGSAAASGV KPSHTYAAGG TYTVTLTVTD
DRGAVGTSTA SVTVTAPRVN QAPSASFAST VDHLVVAVDG TASTDPDGSI ASYRWDFGDG
TAAATGSTAN HTYAVAGTYT VTLTVTDDEG ATGTSTGTVT VAPAPPANVA PTASFSSAST
GLAVSTDASA SSDPDGTVAG YAWTFGDGGT ATGKTASHSY AAAGTYTVTL TVTDDKGASG
SSTGTVTVAP IPNAAPTASF TTATDKLAVS TDGRASSDSD GTVATYAWDF GDGGTATGST
AKHDYATGGT YTVTLVVTDD KGATGTRTST VTVTAPPVVT AVAQDGFGRS ASNGWGSADV
GGAWTRTGQA SQYAVAKGVG TQYLGAAGWS TSMALTGVSA TDSDLRTSVS LDKAATGGGT
FVYVTGRKVA TNSEYRATLR YRSDGRVVVA LNAYKGTSTN VTLVNETLVP GTVTPGAKVN
VRLEVSGSGT TTIRAKVWID GTTEPTAWTV STTDTFAGLQ APGSVALAAY ASGSATNAPQ
TVSFDDLSVF KP
//
