ID F6FRF3_ISOV2 Unreviewed; 1666 AA.
AC F6FRF3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=PKD domain containing protein {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Isova_1140 {ECO:0000313|EMBL:AEG43914.1};
OS Isoptericola variabilis (strain 225).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN [1] {ECO:0000313|EMBL:AEG43914.1, ECO:0000313|Proteomes:UP000009236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Isoptericola variabilis 225.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002810; AEG43914.1; -; Genomic_DNA.
DR STRING; 743718.Isova_1140; -.
DR KEGG; iva:Isova_1140; -.
DR eggNOG; COG2133; Bacteria.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG3507; Bacteria.
DR eggNOG; COG3828; Bacteria.
DR HOGENOM; CLU_002470_2_0_11; -.
DR Proteomes; UP000009236; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd00146; PKD; 2.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR010496; 3-keto-disaccharide_hydrolase.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR029010; ThuA-like.
DR PANTHER; PTHR40469:SF2; GALACTOSE-BINDING DOMAIN-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 1.
DR Pfam; PF06439; 3keto-disac_hyd; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF18911; PKD_4; 2.
DR Pfam; PF06283; ThuA; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS50093; PKD; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009236};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1666
FT /note="PKD domain containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003339493"
FT DOMAIN 749..828
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 947..1076
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1086..1167
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 473..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1666 AA; 179023 MW; 664430377284D871 CRC64;
MHRRILVASL TAAALVGSTV PGAAYDLQGQ APIAGEVATE ADEESRFRAL VFSKVTNFHH
ESIPAGEALI ESLGAEHDFD VVIDDDASMF TDADLATFDV VIFNNTNSTP ESGDLLDAEQ
RAAFQRYIQG GGGFAGIHAA TASERDWEWY EGLVGAIFSH HPDFSETGGT YPGRIKVLDQ
VHPSTRDLPQ LWERSEEWYN FGTNPTGDVH VLAQIKLRDG IPGMEMGVDH PYSWCQVYDG
GRSWYTAGGH DPSSFQEPEF VSHLLGGIEW AAGVEPGDCG ATVDASFART LLTDDLADPF
ELDVMPDGRV VYIQRTGQFK MIDQETLEVT TIGDLELGLS TARHSDGLTG FALHPNFADN
GWLYAAYSDP DVARVNVSRF TFDFDTSVLD MESEKRMLEF PTWRDVGLAN VHMGGSLQFG
PDGNLYIAQG DNTDFSQSDN YAPIDERPGR APYDAQATSA NTNDLRGKVL RITPTDDGGY
EIPEGNLFPP ETSDPELTRP EIYAMGLRNP FRISVDPISG ALLVGDYAPD ARQPNPERGP
EGLVEWNVID EPGNYGWPHC AGDNKPYIDY DFATGESGEP FDCEGGPVND SPHNTGLQQL
PPAQEAHIWY GYALSEEFPE LGTGGAGPMS GPVYEYDPEL DSDTKFPEYY HGKWTVFEYT
RNFYKTVTLV EEDLQFADER FAPASAGDLL SINPFLDSWD FRGPFEAEFG PDGSLYVIDF
GAGSGAGRGD RNEGAGIYRI DYVGGDRPPS VQASGTPSSG QLPLEVAFSS EGTVHPSGLE
MTYHWDFGDG ATSTEANPTH TYVDAGNHTA LLTVTDSMGR SSVAAVRIAA GNTAPEVAFQ
WPPHGGFYDW GDTFDYEVVV DDAEDGSTAD GTIACEEVDT STFLGHDTHA HPVDNYTGCE
GSVTILPDAG HDVETDLYFV LESSYTDKGA PGVTPLTGSD GLRLNPKRTE AEHFSDASGV
GVYDRDQASG GARIGDITDG DWVRYEPVNL ANIDAVTLGV SSGGLGGTVE FRRDAPDGDL
LGTATVPVTG DYNTVVEVTA ELEDPGETFT LYAVFRNPAW TEGGPDLLAF DWMEFQGAGV
ADQSAPRVTV DASVTEGRAP LAVELTGTAT SPVGQEIVSY EWDFGDGASA TGADAEHVYT
TAGEYLAVLT VTDAEGRKGS AGVRITVGEP LPVCERAGSD EFDGDSLDLG RWCTTLHHDP
DGYQVTGGRL VLPTAHGELN GSQFDAPNLV LQPAPSDPWQ VTTQVTLEPT TGYQQAGLLL
MADSDHFAKA VMMGRPDGTR RMSFFTVAGG QERNQAADFV ALPADFPSTF QLRLSSDGAV
VTAEYSADGE QWSPLGRSYG VGSSDLWHVG VAALSGGGGD STIPVVDAAF DWFRMTTEEP
QQCQAPAPPE GFTALWDGQT LDGWQMVGGG SFAVTGDCTL MSQGGGGMLW YTPEAFGDFH
LSLEYRMNNA SDNSGVFMRF PAPWDWEGAW SSRPDDSVRG YEAQIEDNAG GGDPQKTGSI
YNFASINQVL AKPIGEWNTY EIRAVGQTYE VTLNGEVVNT YTGDGSRALE GHIGLQAHHN
GSDVEFRNIW ISTGEDVEPE PSFEGVRELL VGLVETGAVS PQGETVLTRT LDQAESRCTA
GQVDAAVRLL EAFATQAANP RLVPDAAAQD ELVGAADGLR GWLADQ
//
