ID A0A1Y0G297_9GAMM Unreviewed; 923 AA.
AC A0A1Y0G297;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Cartilage oligomeric matrix protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBR65_21890 {ECO:0000313|EMBL:ARU29872.1};
OS Cellvibrio sp. PSBB006.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1987723 {ECO:0000313|EMBL:ARU29872.1, ECO:0000313|Proteomes:UP000196143};
RN [1] {ECO:0000313|EMBL:ARU29872.1, ECO:0000313|Proteomes:UP000196143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB006 {ECO:0000313|EMBL:ARU29872.1,
RC ECO:0000313|Proteomes:UP000196143};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP021382; ARU29872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0G297; -.
DR KEGG; cell:CBR65_21890; -.
DR OrthoDB; 5291933at2; -.
DR Proteomes; UP000196143; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 4.10.1080.10; TSP type-3 repeat; 7.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF119; RE20510P; 1.
DR PANTHER; PTHR10199; THROMBOSPONDIN; 1.
DR Pfam; PF02412; TSP_3; 19.
DR SUPFAM; SSF103647; TSP type-3 repeat; 8.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51234; TSP3; 18.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000196143};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..923
FT /note="Cartilage oligomeric matrix protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012372335"
FT REGION 27..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 93757 MW; B3B3BE52CAC3A6D9 CRC64;
MKNFSIYLLL IAILGLTACG GDDGFPQNGN GSGGSASSVP TSSSSSASSS LPPIDPGELP
DQDGDGISDI TDNCPLIANT DQADDDADGI GNACDNDTDG DNVVNLLDNC PTTGNPAQVD
TDNDGIGDAC DTDLDNDNIP NDEDNCPLVA NADQADQDDD GIGDVCDSDS DGDGIPNASD
NCPTNANADQ LDTDSDDIGD VCDTNTDTDG DGIDDGEDNC PLISNSAQED TDNDGIGNPC
DDDHDNDGVT NDTDNCPNTP NADQADLNND GVGDVCDNDT DGDGITNTLD NCPLVANPDQ
LDTDNDTLGD ACDDDRDGDG ISNTTDNCPS IANLNQMDSD GDGIGDVCDT DRDGDGIDNT
ADNCPNTANP DQTDTDGDGT GDLCDDNTDS DNDGIDDASD NCPLIANDDQ ADLDNNGVGD
ACDTDIDGDG VLNPVDNCPL VANTDQADLD GDGQGNACDT DLDGDGVAND TDNCPLLTNA
DQTDTDDDGI GDLCDTDLDG DGIINTLDNC PLAANADQLD TDNDGLGDAC DANTDSDDDG
IDDASDNCPL IANTDQADAD SDGIGDACDN DLDGDGVVNA SDNCPTTANA DQTDTDADGI
GDLCDPLTDS DDDGIDDALD NCPLVANPLQ TDTDGDAIGD SCDTDTDNDG VLNDSDNCPL
VANPGQEDGD GDDIGDACDT DSDGDGITND LDNCPLVANA DQLDADGDNI GDVCDDDLDG
DGVTNALDNC PINNNPSQAD IDGDGIGDAC DPVENVACGP GLLFEPVLGA STSVDTGLRG
VLCIGCGVLN PANLVNTLDD AAVMSTPVAV AASVWASVED TAMTYTGNQR VGFLVSLPVG
VLDLSLLNSL EITTYLDGVA QESSASGGLL GLQLLNLTGD ATRQMVIMET TADFDEAEIE
KAAVLGALSN LNVYAMCVAP PPL
//