ID A0A4U3L1Q6_9BACT Unreviewed; 1109 AA.
AC A0A4U3L1Q6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carbohydrate-binding protein {ECO:0000313|EMBL:TKK68810.1};
GN ORFNames=FC093_08935 {ECO:0000313|EMBL:TKK68810.1};
OS Ilyomonas limi.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Ilyomonas.
OX NCBI_TaxID=2575867 {ECO:0000313|EMBL:TKK68810.1, ECO:0000313|Proteomes:UP000305848};
RN [1] {ECO:0000313|EMBL:TKK68810.1, ECO:0000313|Proteomes:UP000305848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17mud1-8 {ECO:0000313|EMBL:TKK68810.1,
RC ECO:0000313|Proteomes:UP000305848};
RA Chhetri G.;
RT "Panacibacter sp. strain 17mud1-8 Genome sequencing and assembly.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR602324-1}.
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:TKK68810.1}.
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DR EMBL; SZQL01000006; TKK68810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U3L1Q6; -.
DR OrthoDB; 9816308at2; -.
DR Proteomes; UP000305848; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002324; Cyt_c_ID.
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; IPR029010; ThuA-like.
DR PANTHER; PTHR40469:SF2; GALACTOSE-BINDING DOMAIN-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF06283; ThuA; 1.
DR PRINTS; PR00606; CYTCHROMECID.
DR SMART; SM00606; CBD_IV; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF46626; Cytochrome c; 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; PS51007; CYTC; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602324-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602324-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602324-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000305848};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1109
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020897387"
FT DOMAIN 701..784
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 850..935
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 988..1108
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 411..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 864
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
FT BINDING 868
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
FT BINDING 913
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
SQ SEQUENCE 1109 AA; 123407 MW; 5A0F361F77800981 CRC64;
MRTIVCIASL LFIIAFAACN NSDTRKVLVF TKTKGYHHES IPAGIAAIEK IGKEQHFEVD
TTTDAGEFND DNLKQYKAVV FLSTTGNILN SDQQVALQRY MEAGGGFMGI HAAADAEYKW
GWYNKLVGAY FKSHPQDPNV RKATVVVTDT ANPAMKGLPQ QWERTDEWYN YKNIEPDIHV
LARLDEDTYE GGENGRNHPI AWYHTVDGGR AFYTGGGHTT ESYSEPLFLQ HLAGGIQYAM
GPDSVKLDYS KAYATKAPEE NRFTKVILTN DLNEPMEIAV TPSNYVYVIE RSGNFYAYNP
KANTTKLVYK FGVMPDSKQA FGNGLLGMTI DPDFATNKYV YFFYTPNKEP IHQNISRFKM
IGEDSLDVAS EKVIIQVPLD PEVSAHTGGS LAWDKNKNLF ISTGDNTVPF ESDGYAPLDE
RPGRKTFDAQ RSASNPADLR GKVLRIHPEA DGSYTIPAGN LFAKGTAGTR PEIYTMGCRN
PYRIAINQET STLYWGEVGP DAGEDSRHGP RGYDEFNQAK KPGYYGWPYF VGNNRAYHDS
DFATKQIGAL FNVNGAVNTS PNNTGMQQLP PATAAMIYYP YSFYDTFPDL GEGGRTAIAG
AFYHYNKSKA KPNSIPEYYD KALFVMDWMR NWIFALRFDE NENYKRMEAF MPLTGDFRRP
IDMDITPDGV MYVLEYGSVY GADNDDARLV RIDYNGGNRA PIAKISANDS IGLVPLKVSF
NSNNSYDNDE DDQLKYEWKF EGDKVGSTEP NPTYTFNNKG VYKVILKVTD PSGLSSVDTM
EVKVGNTMPQ IAINTTSNST FYFDNTALNY NVDVKDKEDA NIDAKKIQVK LEYVPEDAGT
WKPSPGAHGT WTTTGKDLIM MSDCKACHQF DTTVIGPAFT AVAQRYQNKP GEIPRLANKI
ITGGSGVWGE HYMNAHPQLS KDQTTAIVKY ILSLTQQQTT NNLPASGTVP LKAPAGKGGT
YVLTAAYTDA GSGVVPLTNT NELILRPAKI EAEDADVLSN IRRDNNDLGS IHNKSYFVLK
GIDLKDIKSV TYNYSSRNIG ATLEVHADSP KGAIISTLNY EPTGDWNKFK QVTTSIQDPG
GKHNLYFVFK KDTEPNRDMF SLDWLKFNK
//
