ID F6FQL9_ISOV2 Unreviewed; 1678 AA.
AC F6FQL9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=PKD domain containing protein {ECO:0000313|EMBL:AEG44915.1};
GN OrderedLocusNames=Isova_2195 {ECO:0000313|EMBL:AEG44915.1};
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:AEG44915.1, 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; AEG44915.1; -; Genomic_DNA.
DR STRING; 743718.Isova_2195; -.
DR KEGG; iva:Isova_2195; -.
DR eggNOG; COG2133; Bacteria.
DR eggNOG; COG3291; 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:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.120.200; -; 2.
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; 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; PF17957; Big_7; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF18911; PKD_4; 1.
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; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009236};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1678
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003335914"
FT DOMAIN 749..832
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 947..1068
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 1348..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1678 AA; 179763 MW; 13E679A2A680CF7E CRC64;
MTERPRPRRG RSVAAVTVGA LAFTLAPTTI AAAAPTAPAT PLAQTVEEEH KVLIFTETTQ
YRHSEAITQG TPVLEAAFAE AGIASDHTED SSVFNDADLA QYDALVMFQA SGDPWTAEEK
AALERYQQAG GGIVAIHNAT DMRGNYAWWD EMIGSLMPGH AATGSSPGLL GTVRVEDRTH
PSTEHLPQRW ERADEWYNFS TNVRGDAHVL ATMDESTYEP GSNAMGYDHP ISWCKHYDGG
RAWMTGMGHF GAHYTAEPEF VQHIVGGVQW AAGLVEGDCG GTDWGQFEKI ALDSNTSAPF
AMDIAPDGRV FFTELVRGQI RVYDPRTQTT TTALEIPVYS GGEDGMLGIA LDEDFENNGF
LYQYYSPASE DDTDPASFFN RLSRFTVTGD EPGATVIDPE SEVVILEVPA RRLPDEPGHT
GGGLIIDHRT GDLYLGVGDD VNPHSEPSGG YAPISEREGT FHDARETSAN TNDLRGKILR
IHPEDDGTYT IPEGNMFPEA EDTEDKTLPE IYAMGFRNPF RFTIDPETGD LGVADYSPDN
GSDNLATRGP AGIAEWNLVK EPGFFGWPLC MGDNEPFRDV DYTTNPVTVG DFFDCDAPIN
DSVRNTGLTE LPPAQPADLW YGYQRSSVPG AINAGGGLAP MGGPFYQFDP ELDSDTKFPE
YYHGKPFFYE WARNQMFSID LKDPRAGAGE SDVEKVNRFL PTEQFLAPID SKFGPDGSMY
VLDWGGGFGR HNPDSGLHRI DYVSGSRSPE AVATATPDSG TVPLEVTFDG TGSSDPEGDQ
LEYAWDFDGD GTVDATEATA THTFTENGVY DVRLTVTDTA GKTGTATVPV AVGNTRPEVS
FDLPPTGAFF DFGDTISWDV SVTDAEDSPD GSEIDDSRVI IQAALGHDAH AHPSEPLYGR
TGSVATNLGG GHGEDMNVFY VLDARYTDDG GDGVPALTGS DTSLVFPKIR EAEFHTDSEG
TTTVPSRDVE GRGSVISGAD GAWASYDPVN LHEIDALTLR VAAATAGTIE LRRDAPDGEL
LATAEVPQTG LTTFTDVRVD VEDPGESFTL FAVFPGSGER RLNFIEANGK GVSETTRPEV
AITAPEAGVE LEQGEITVAA DATDAENEIT QVEFFVDGSS IGVDTQAPYE AAWTVTEDGY
YELTAVATND RGLSTTSRIV VAQVGDPFDG LKTFTNARGE FEHLGANRYL ITSGGANMWQ
GTDEYSALYR EGVDDTWSVT VRINSQQNSH SSAKAGIIVR NDVTAPGSSP GYAALGIRPS
GGFEWLRGNE SGQLSTSSSA GTTAYPAWVR LVRYGDLYYA YWSADGKDFR QIGQPVTLPG
AASVQDVGMF VTAHSASATS AVEFQDFTFD DDPADPSAPD PGDTPPECDV EGDPDGGVRK
PSDEFDGEGI DGCRWDSIVR YDADHVTVAD GRLQITTQPG DINGSANDDP KNFILQRAPE
GDWVAETRFA APLQHQWQLA GLLAYADDDD YVKLDVVAKN APGAATLLGA ELVSEQGGAF
GAGGNRQIDL AGEPSSGFWH LRLEKVGDTY QGSVSEDGEE WVSLGDPVTH DVPLTSIGLM
AIGPKQTSPV VVGFDWFRLT TADDEEPVAV GVQAVAECVG KQAVVTVRVS NDDAEPAEVL
VETAYGSKTY PDVAPGDTPL HKFRPKADSV EAGTVSVTAT IGDRTSTVEA EYDAVSCG
//
