ID A0A225DP77_9BACT Unreviewed; 694 AA.
AC A0A225DP77;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Alkaline phosphatase {ECO:0000313|EMBL:OWK43202.1};
GN ORFNames=FRUB_02801 {ECO:0000313|EMBL:OWK43202.1};
OS Fimbriiglobus ruber.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Fimbriiglobus.
OX NCBI_TaxID=1908690 {ECO:0000313|EMBL:OWK43202.1, ECO:0000313|Proteomes:UP000214646};
RN [1] {ECO:0000313|Proteomes:UP000214646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP5 {ECO:0000313|Proteomes:UP000214646};
RA Ravin N.V., Rakitin A.L., Ivanova A.A., Beletsky A.V., Kulichevskaya I.S.,
RA Mardanov A.V., Dedysh S.N.;
RT "Genome analysis of Fimbriiglobus ruber SP5, the first member of the order
RT Planctomycetales with confirmed chitinolytic capability.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:OWK43202.1}.
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DR EMBL; NIDE01000004; OWK43202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225DP77; -.
DR OrthoDB; 8198236at2; -.
DR Proteomes; UP000214646; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR Pfam; PF00413; Peptidase_M10; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000214646}.
FT DOMAIN 154..207
FT /note="Peptidase M10 metallopeptidase"
FT /evidence="ECO:0000259|Pfam:PF00413"
FT REGION 284..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 69222 MW; 8F8B95AB232DE08F CRC64;
MSLSSRSVRA VPASANRTVL RVDSLEDRLV PSLTIQFDYS HDTNGFFNDP ARRADLQLAA
DTLASQITTT LPAITPNAAA GNTWNAVFPD PSTGATDETP NLTVPQGTII VYVGGNTLAG
TEAGEGGPGG YQAGGSTAWV SSIVNRGPIG YGSWGGAVTF DMNQNWYFGT DPNARPAGEI
DFFSVATHEL GHTLGIGTST EWSSLVQNGH FVGADATALL GGSSPAVSAD GDHFAENTYS
PGPAGHNIVS MQPILNTTQR VYFSELDYAA LADLGWQVTG QVSTTTSPVT VSPPATTSPP
TTVPPTVPPV TTPGVIPGLA PGASVVPTGS GTTNSVTTSS NTTTPTADAS TSATTSTNTT
TSATDIGLPA GTPASQVAIV SGSGDGSIQV YLVGTNGQMT EVGGPLYPFP GFTGTVRAVA
ADLTGDGTAD IVAGVGPGGG SQIAVLDGRT FTPAAAAFSA YESSFNGGVF LAAGDIGNTG
KDDLIVTPDD GGGARVRILG LSNGQLASVV PDFFGINDPN FRGGARTAVA DVNGDGMPDL
IVVAGTGGGP RVSIINGATL LSGTHQDLVP DFFAFEPTLA NGVYVSAGPV TGGGTDIVFG
AGPGGGPRML VVSAQTLMAE GSADALANPV YDTFVGSTSD RGGVRVAVKN GNVLAGSGSS
PMVQVYTGTS SGSLTLAAST DPLAAATSDG IYVG
//