ID F6FWE5_ISOV2 Unreviewed; 1351 AA.
AC F6FWE5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=PKD domain containing protein {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Isova_1772 {ECO:0000313|EMBL:AEG44519.1};
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:AEG44519.1, 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; AEG44519.1; -; Genomic_DNA.
DR STRING; 743718.Isova_1772; -.
DR KEGG; iva:Isova_1772; -.
DR eggNOG; COG2133; Bacteria.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG3828; Bacteria.
DR HOGENOM; CLU_257666_0_0_11; -.
DR Proteomes; UP000009236; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 3.40.50.880; -; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR029062; Class_I_gatase-like.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR006311; TAT_signal.
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; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF06283; ThuA; 2.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009236};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..43
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 44..1351
FT /note="PKD domain containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038616812"
FT DOMAIN 186..279
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 975..1054
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1351 AA; 145812 MW; 46B08FDA660E045D CRC64;
MERTGRDRGL RGGTPPRELR RRALAATAGA VLAAGLAVAP VAAAPAADPS PEPTSPSAAQ
GKGQSAGTDG GTRAAAAATL PTDLRVLIFH GDPAAQVDPV EVAADTIGEI AGEHGFAVDV
THDPAAFTTD NLAQYRGVVF LSAEGTELDA DAENALRAFV EGGGGFLGVR DAARAQERSQ
WFTGLIGTRP VGNLPDPADV ANVTASANNP PNETEANLTD GDPGTKWLAF ERTAWLEYEM
SEPVTAVRYA LTSANDFDGR DPQSWTLQAS TDGETWVDLD SRTDEDFPDR FLTRDFAIEN
DTAYTHFRLD ITENAGEPLT QLADWAIYDA SAFEGEEPEI PVQEATVNVV DRHHPANEGL
PVNWTRSDRW LNWSPNPTGE VHTVAQVQEW DYDPGEGANG PFHPVSWCRD YDGGRSFYTG
MGGTAESYGE PEFRDHLAGA LLWSTGVVRG DCQATIGANY TIERLTGTNA PGQLDQIGEP
HGLTIADDGG VFYIGKAACP SGPIVPWENP DVGLGCGTIH RWDPETKETS LLTTLEVMGN
RGSGSELVKN EEGLIGITLD PDFADNGWVY VFWMPHESID RERRVGERTV SRFTYDAEAN
TIDQSTRVDL MAWETQIHSC CHAGGGMAFD DEGNLYIGSG DNNSSGGSNG YSGNNWTQEF
AGISFQDARR TSGNTNDYNG KILRIHPEPD GTYTIPEGNL FPEGEYPADK TKPEIYVMGV
RNISRLAWDS KNDWLTAAWV GPDAFSPDPE LGPAKYETAT IITSAGNQGW PYCMGDRQPY
RDRSNEDASV LTGWYDCDNL KNTSPRNTGL VDIPPARDNM IWYSPGGGGP VFPRDENGIP
SYVDDEATYT QPYLRGGGQA IMDGPTYHRS EVDTESGVAW PEHWDNKWFI GDQSNANNRV
AVTVNPDTVE EAGPPVFVED LRSIIRSGGG SNALQSWMDA KFGPDGALYM LDYAGGFFSL
HPNQKLIRIT YDGGPATPAP AGTATSVQSD PLTVAFTGSS SGGVSWHWDF GDGTTSTEPD
PRHTYARVGQ YDASLTVTYA DGEEVTVDVP VRITCTIPDG RGTVHVGGTD TGVPNDDLGG
CTINDLINDE GDWDGHGAFM EHVNTVLNQL QADGVITGKE KGAITRAAAR SDVGKPGQTG
YRWLFDGTSE SLDGWRQAPG GSFELTADGS LRSQGGLGML WYEAEEFGDF SLKLEYRDVS
AGDHFANSGV FTRFPDPRVP QDERPECGQL TGSEAWVAIY CGHEIQIYDG PGGEPQKTGS
VYNFDPVGLG DAGVTPKGEW NSYEIRVVGQ HYEIVRNGEV INTFDNVPGI SSSRAGDPPT
DLRQFLSGYV GLQNHGNADL IEFRNIRVQE L
//