ID A0A0G1T3C0_9BACT Unreviewed; 1910 AA.
AC A0A0G1T3C0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=LamG-like jellyroll fold domain-containing protein {ECO:0000259|SMART:SM00560};
GN ORFNames=UY03_C0040G0002 {ECO:0000313|EMBL:KKU76274.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_64.
OC Bacteria.
OX NCBI_TaxID=1618845 {ECO:0000313|EMBL:KKU76274.1, ECO:0000313|Proteomes:UP000034132};
RN [1] {ECO:0000313|EMBL:KKU76274.1, ECO:0000313|Proteomes:UP000034132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
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:KKU76274.1}.
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; LCOL01000040; KKU76274.1; -; Genomic_DNA.
DR PATRIC; fig|1618845.3.peg.1156; -.
DR Proteomes; UP000034132; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.1190; -; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR Pfam; PF06452; CBM9_1; 2.
DR Pfam; PF09136; Glucodextran_B; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF49344; CBD9-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 105..247
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT REGION 516..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1910 AA; 200666 MW; 5C828A15AA5698E3 CRC64;
MTHSKTRTSK RFRFSLGFFP LCFLLLFIFS LSTFHFQSAS ADITTDLVSH YKLDETSGTT
ATDSAGTNNG TLTNSPTWTT GKLNNALNFD GTNDYVTIGD IFYSDIFTVC AWFKSDVMTG
STGKTIVAKR NSSGITAGTN EWSFSIDAGT LQFISWNSGG GVTHNIGYNT ALTANTWYHG
CAVQSGNGNT GYVYLNGVVD ASASQTSAMI NSASLIQVGV RIAGSDTRYF DGIIDDIRIY
SRALTAADIT QLYSYTGALP PVSTTNSATS LTSTTATLNA TVNPNNLSTT AYFQYGWTSA
YGNTTPAQTL TGSANQNITA SIASLDSNTV YYYRAVALTE SVWNLAESIS RPISGTNNNT
TTFQTLWDDN YLYIAYKVLD SNLINDSTNN WMDDSVELYI DPDNSKSTTY DTYDRQFVKG
YNDSALAAPQ NGTGVLHNTA SIAGGYTVEL AIPWSNLGVA PSANMTLGFD LQQNDDDTGG
DIQNAMGWNS TTGTNYKNTS AFGTLALSSQ TVGTAQSSSS SVSQSSSSSA TAADTTPPIV
SISSPTTNTT YSTSASTIDV SGTASDNVSI SSVTCAVNGS SCGVVSGATF WSITSIPLII
GTNTIIVTAR DAANNTSTDT LTVTRTTTTT SSNVWQRVPI RTKAQQTAGL VGGEGSQFVF
AMNYAPSDSQ IMYLVRDTNS VWKSEDGGAT WGLKDDGIQS RGGVSIVVNP YDKNVVLMAG
SLHATDLTST SVTDGIYRTA DGGSSWTRTR DTHYMRNYWG DMFAFGNTST VYAGTKDQGL
LKSTDGGVTW SSLNLLTSYP VRDIKIHPTD ATTLFVANTN GLYKITGSGG SATKIGTGLF
AVPQSISINQ SSPNTIYVTT GRSGAASPHN LGGVYKSTDG GVNFTRKSNG LDSLLGASNT
NYTKRLAISP VDPNRLYVAF ELSGSPHPFY TINAGENWIQ PIDLDVGDLI SDLIYADSGV
SPRYQINQVI AHPTATTNAF TLNNKACPIK TTNSGSTWTY SGNGLTGSNA EGGSTSFGWD
VNNVNRYVLF FQDSGPYITR DGGSTFIRMD IPAGVSNGRT TPAGALDPTV DSEIVITAVD
SWGSQEIIVT TDEGASWVKK GYSSSFSFIA FDPNNPNVVY ANNYRSTNKG STWGTISKSV
IAMYSGTQTS VYAYSTTGGI TTVSRSDDTG TTWSSPYGTF NAGTVYELSI DPTNKNILYA
ATSQGVYKYN GSSWSQKVNG LTVDGKGSIE TRRIAIDPNN PSVIYAAKYA YLYGPSNGVF
RSIDGGETWS SIIGNLGPEF TAMSLSVNPN SSYVYLGSAS GTWRLPPPGT VTTADTTPPS
VSITSPTTVS TYSTTASTVA LSGTASDTSG ISSVTCAVNG SSCGTVSGTT SWSVSNIPLV
VGTNTIIITA RDSSANGNTS TATLSVTRTT TTTSSSSSSS APLPTLTVTA SKTLSPITID
GALSESVWNL TEPIARTISG TNNNTATFST LWNDTYLYLA YKVLDSNLIN DSTYPWQDDS
VELYLDGQHE RSLTYDGNDR QFVQGYNDTT LAALQNGTGV LHNTTSIVGG YTIELAIPWT
NLGITSPTAN QTLGFDLQQN DDDTGGDVQN ALGWNSTTGA NYKNTSAFGT LALSSQTVGT
AQSSSSSAAS QSSSAQSSVS SPSSSSQSSA TQSSSASSAK FITGDRVITT TDTLNVRSSA
SLTGTALGAQ SLNQAGTIVS GPVSSGGYNW YDVNYDTAPD GWSVENYLEK AVSSSSSSSQ
SSSVPSQSSS SSLSSATSGG GGGGGGGGSG GGGGGIYIPP VSYESTLKTI ASSTKPSAAT
ATTTEFVNPF VSLESVFRPF VQIFTQDLKI GSRSAQVKTL QEKLSADKTL YPEGLTTGYY
GSLTQAAVKR FQKKHNLAAT GSIDLKTRAK LNEIYGSNSS KKLSKNFFSN
//
