ID A0A0Q8PUQ0_9ACTN Unreviewed; 1424 AA.
AC A0A0Q8PUQ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Secreted glycosyl hydrolase {ECO:0000313|EMBL:KRB74906.1};
GN ORFNames=ASE03_19795 {ECO:0000313|EMBL:KRB74906.1};
OS Kitasatospora sp. Root187.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB74906.1, ECO:0000313|Proteomes:UP000051829};
RN [1] {ECO:0000313|EMBL:KRB74906.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB74906.1,
RC ECO:0000313|Proteomes:UP000051829};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB74906.1, ECO:0000313|Proteomes:UP000051829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root187 {ECO:0000313|EMBL:KRB74906.1,
RC ECO:0000313|Proteomes:UP000051829};
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:KRB74906.1}.
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; LMHX01000004; KRB74906.1; -; Genomic_DNA.
DR STRING; 1736486.ASE03_19795; -.
DR Proteomes; UP000051829; Unassembled WGS sequence.
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; cd14490; CBM6-CBM35-CBM36_like_1; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR033801; CBM6-CBM35-CBM36-like_1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF07705; CARDB; 1.
DR Pfam; PF00754; F5_F8_type_C; 3.
DR SMART; SM00231; FA58C; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50022; FA58C_3; 3.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000313|EMBL:KRB74906.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000051829};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1424
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006352644"
FT DOMAIN 16..166
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 167..306
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 482..634
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 386..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1424 AA; 145965 MW; 998E0D08ACABD74C CRC64;
MPRLVATAAT ISLLALAGPL LPTAASAAGG PNLAAGKAVA ASSSTGGQAV GNINDGNQST
YWESSNGSLP QWVQVDLGAA AGVDEVVLKL PAAWGSRTET LAVQGSADGT SFNTLTSSAR
YSFDPGAANT VKIGFPAVTT RFVRLAISAN TGWPAAQISE LEVHGATGTS ANLAQGRNLT
ASSYSQTYTA NNANDGSRSS YWESANNALP QWIQLDLGSS VAVNKLVLKL PAGWEKRTQT
LAVQGSSNGT DFTDLAASTG YVFDPATGNA VTVDFGTATT RYIRLNVTAN TAWPAAQLAE
LEAYGPTAGD TQAPSAPANL AYTQPSPGQI KLTWGAATDN VGVTGYDIFA DGELLTSVGG
GVLTYTDTRP DSATVSYFVR AKDAAGNQSG NSNTVTRTGA AGDTQAPSAP ANLAYTQPSS
GQIKLTWGAA TDNVGVAGYD VYANGALRSS VAGNVLTYTD SQPDSATVSY YVKAKDAAGN
QSASSNTVLR SGSTGGTNLA AGKAITASSS IFTFVAANAN DNDVTTYWEG NSNSYPNTLT
VPLGSNAAVD SVVVKLNPAS AWGPRTQTIE VLGREQSASG LASLVAAKSY AFDPASGNTV
TIPVGATVAD VQLRITANSG SGGGQAAEFQ VIGTPAPNPD LAVTGTTATP ASPVETDVVT
LAATVKNVGT LPSAATAVDL FLGSTKVGTA QVGALAAGGT STVSVNAGAQ NAGSYQVSAK
VDPANTVVER DESNNGYTAP AALVVSQVAS SDLLAAPVSW SPGNPATGNA VTFSVALKNQ
GTVASAAGAH GITLTVADQS GAVVKTLTGS YSGAIAAGAT TAPVSLGSWT AGNGKYTVQT
VIANDANELP VKQANNTSSQ SLFVGRGANM PYDMYEAEDG VLAGGAALVG PNRTVGDLAG
EASGRRAVTL NSTGASVEFT TKAPTNTLVT RFSIPDAAGG DGIDSSLSVY VNGSFLKTID
LTSKYAWLYG SETGPGNSPS AGGPRHIYDE ANVLLGTTVP AGSRIRLQKD AGNTSQYAID
FVSLEQATAT PNPDPARYTV PAGFTHQDVQ NALDKVRMDT TGTLVGVYLP TGDYQTAAKF
QVYGKPVKVI GAGPWFTRFH APATQSNTDI GFRAEATANG STFAGFAYFG NYTSRIDGPG
KVFDFSNVAN TVIDNIWVEH MVCLYWGANT DSMVIKNSRI RDTFADGVNM TNGSTDNLIS
NNEARATGDD SFALFSAIDG GGADEKNNVF ENLTSILTWR AAGVAVYGGY ANTFRNIHIA
DTLVYSGITI SSLDFGYPMN GFGTDPTNLQ NISIVRAGGH FWGSQTFPGI WVFSASKVFQ
GIRVSDVDIV DPTYHGIMFQ TNYVGGQPQF PVKDTVFTNV SISGAQRSGD AYDAKSGFGI
WVNEAAEAGQ GPAVGNAVFN NLRLSGNVQN IRNTTSTFTL TVNP
//
