ID A0A2Z4G841_9BACT Unreviewed; 923 AA.
AC A0A2Z4G841;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=PKD domain-containing protein {ECO:0000313|EMBL:AWV97369.1};
GN ORFNames=DJ013_03955 {ECO:0000313|EMBL:AWV97369.1};
OS Arcticibacterium luteifluviistationis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arcticibacterium.
OX NCBI_TaxID=1784714 {ECO:0000313|EMBL:AWV97369.1, ECO:0000313|Proteomes:UP000249873};
RN [1] {ECO:0000313|EMBL:AWV97369.1, ECO:0000313|Proteomes:UP000249873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1504 {ECO:0000313|EMBL:AWV97369.1,
RC ECO:0000313|Proteomes:UP000249873};
RA Li Y., Qin Q.-L.;
RT "Complete genome sequence of Arcticibacterium luteifluviistationis SM1504T,
RT a cytophagaceae bacterium isolated from Arctic surface seawater.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR602324-1}.
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DR EMBL; CP029480; AWV97369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4G841; -.
DR KEGG; als:DJ013_03955; -.
DR OrthoDB; 9816308at2; -.
DR Proteomes; UP000249873; Chromosome.
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; 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; 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; 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 PANTHER; PTHR19328; HEDGEHOG-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR19328:SF13; HIPL1 PROTEIN; 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 PRINTS; PR00606; CYTCHROMECID.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS50093; PKD; 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:UP000249873};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..923
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016317605"
FT DOMAIN 474..559
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 634..719
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 179..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 648
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
FT BINDING 652
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
FT BINDING 697
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR602324-1"
SQ SEQUENCE 923 AA; 101682 MW; 4FA000BE66E9040B CRC64;
MKYLFSALVF MLMLNACTSS STNDPNEKPE DNRFTEVELA RGLDEPMEMT FLPDNKILIV
ERKGGLKLVN ETTKETASAG WVEVNTKYTN KEGNVREAEE GLMGVVLDPN FKENNWIYMY
YADPETAKHV LARWEFKDDY LVDESKKVIL EVPTQRQECC HTGGGMTWDA QGNLFLTVGN
NTVNPRSGAS NLNEAPGHEN EDDQRAPGNS NDLRGKILRI HPESDGTYTI PEGNLFPVGT
EKTRPEIYTM GHRNPWRPTL DSKTGYLYWG EVGPDASKDS IWGPMGYDEF NQAKKAGYFG
WPYLIGNNRP YNRYNSEDGT YGEAFDPNNL VNESVNNTGI RELPEAVPAF LYYPYGPSPE
FPLMGTAGRS ATGGPVYRQA DFKDAARPWP AYYEGKWLIT EFMRGWIIAV TMDENGDYVS
MEKVLPEKNF SGAMDMDFGP NGDLYVLEYG TAWFKGNDNS RLVKLEYNAG NRKPVVAASS
DINSGKIPLT VNFSGEGTTD YDGDKLSYEW KISKDGVEEG TVSGETASYT FENSGDYVVE
LTVTDSEKAT NSTSFSITAG NEAPAISLSL DKENKTFYYG ERELPFEVKV TDAEDGSTEN
GISADEVAVT FDYVPAGYDP IEMAANHATA DAMASFAVGK NLIEASDCIS CHQFDTKSIG
PSYKAVSERY PNNKKNRELL VDKVINGGSG VWGEHGMSAH PDLDKADASR MVDFILSMSS
TGGTPSLGLS GVVKPIKPDY EFEEGSFVLR AAYKDKGGSG VKPLLKENVV VLRSPDMKPH
AAEFKKSVEV LTASGNSFYA VGDKSYIGYK NIDLSGVKNI MVYIQNSERS GTKGGTVELH
LDSPDGAVIS TSEDIPTNTP RGARRPPAGV SMKDWRRQNS SKATLNVPAN AAGFHDVYLV
FRNADATSND YLMKLDEVSF SNK
//
