ID L0GVQ7_9GAMM Unreviewed; 1846 AA.
AC L0GVQ7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN ORFNames=Thimo_0605 {ECO:0000313|EMBL:AGA89450.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA89450.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA89450.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA89450.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
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DR EMBL; CP003051; AGA89450.1; -; Genomic_DNA.
DR STRING; 765912.Thimo_0605; -.
DR KEGG; tmb:Thimo_0605; -.
DR PATRIC; fig|765912.4.peg.591; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_232936_0_0_6; -.
DR OrthoDB; 5664384at2; -.
DR Proteomes; UP000010816; Chromosome.
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; cd00146; PKD; 1.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR032109; Big_3_5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR NCBIfam; NF038114; rightmost; 1.
DR PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR Pfam; PF16640; Big_3_5; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF00801; PKD; 1.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50093; PKD; 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 Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1357..1420
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 1176..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1846 AA; 191458 MW; 7AE9C769F4713B41 CRC64;
MLRPDRASAV FVHIHFREQI MNALKRQFFV PSWWRGNRGI ASILVLIAAL MASAGTLAAS
QWTFQGPGPI TAGQQWVPEP ATNPVTGSVN AIAASPNDPD LLYIGGANGG IWKTTNATNP
SPSWTPLSDE LESQSIAAMA LDPTDSTGQT LIAATGRYSG LASLGDDQVG IYYTTDGGVT
WTNSRGTGDN LVYDSARYWG YLTDVAASGD TLLAAMRSWD YLRGGIFRST DGPTGTWTHL
SNGLPDGSAG FVIIDPADPN VLYAGFLGAS GGVYKSTDGG DTWTDITNGI PRTTADSTGF
GISALTKAMG AAVFNDGTTS VLTVALAGTF GNSSSSTTGY AVYRSVNGGP FTAQDYPAGL
RPFSGHFPIA ADRIDPNLVY LAGYGFNGGD GYLFRLDASQ PSGSQATPLA QRPRVDVSPA
ISATKTAFYV WSVSGLPTET PFTIRVDQEE MQVNQVNGYQ TSGGTPYWYF YVTRGINGTT
ATAHARGAPI WPIPLSGNLY GAPHADYTDL TVDANGALLA GNHGGIYRLP EPASPASAAN
LWTALNSDQT VTEIHDIAYD HVSGTLVATM QDLGAAIQNA PDDRVWTSVR GGDGGDVAVV
DIGGGQSIRY VSSQDLSGLA RDVYDASNTL VGSTKISTSV ITDKKSITPV VANAVDPNRL
AFGGGNRVYE SKDQGATIAA LPDPVGVNYY YPYPGSNFKG PMVYGGRLNG LPNPDLLYVG
YYDKVYVRTQ AGGAFAETAQ LPSGAGNVQS IAVDPDDYYR VFATDNDHVF MSDDGGASWS
DITGDIGTTQ LTALVYVPGP APYLAVGSRA GVLASPLSSL GTWTSLKDFP SFVVFDLAYD
ATDDVLAVGC FGSGAYLLTN ASAALSSTTT AVLPADETSG GDRTDGALAE VWSWIGGIGA
QVLSAVIPSA EAGELTQPPG LVSWWRANGD ATDDHDGNDG TLENGATFGA GQYGQAFSLD
GVDDYVNVPD APNLDLTTNF TIDAWVYPNS NTVGRVVGKG RTSVGTGYAL GTDSSGNAQV
SLHDGSVGCS AADIQPLAVG QWSHIAGTFA GTELKIYVNG TLQATETCSF SSIGPSTEPL
NIGREAAGIG RYFDGSVDEV HVYDRALTAA EVHAIYTYTQ AVLMQVDLQE SGASNQQTQA
GWDAQELPHD PDGVGSFSLL LTSAGSTAGI TATLGGDSDG WEARGPGQSS ARGQISGTSL
DDLLEDFVLT RDEDASVSLT GLVVGDEYLF QAWNNDSYTV NTGFAAGAGT VTPSVTGGIV
QSSSNGTITN LYGTQTDSAF GATSLRFTAT SSSATIDLDG NNPNGYLPIN GIRFSQVTSV
APTAAVTGPA SALEGQVIEV VLTATDLSPA NQAVGFTYVI DWDDGSPIQT VDPVAGTGAA
TARHAFADVG TYEVQVTATN QDGVISDQAD NPIQVEVLTP GSLQDQLDAL SLVTFQPIDD
TALQGEVGAV NALAGQASPM DVTIVLGAGP FGPVVLSPPE NVYLNLAGNY TADSLVESGG
STEAPPEIEL AADATLIDGE ASGPAVTVTR GETYVQGDAL TTAAGAPTVL VTGGRLTLSQ
GNIQESTGAD SVAIEVAGSG KVELGFDMVL NVNGEGTFIR SPDREAVEPP KGIDAELNPN
LFSRNGAPVN AIALSSTRIA SSVSPSTFGE PVTFTATIDV EVEEGGVPTG TVSFYDGASL
LGSSVVQPVG YGYQASFATA ALEAGDHDVS AVYGGDDRYI SSRSAVLVQS VDAYAFTGFF
RPVDNPPTMN RAKGGSSIPV KFSLGGDRGL DILAGYPTSQ PISCDDNTPV DDIEEEATSK
SGLKYDPDSD QYIYVWKTLK GWSSTCRQLT VRLADGTAYT ALFSFK
//
