ID A0A1H4DXF7_9BACI Unreviewed; 529 AA.
AC A0A1H4DXF7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=5'-nucleotidase {ECO:0000313|EMBL:SEA77276.1};
GN ORFNames=SAMN05421743_10841 {ECO:0000313|EMBL:SEA77276.1};
OS Thalassobacillus cyri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Thalassobacillus.
OX NCBI_TaxID=571932 {ECO:0000313|EMBL:SEA77276.1, ECO:0000313|Proteomes:UP000198584};
RN [1] {ECO:0000313|EMBL:SEA77276.1, ECO:0000313|Proteomes:UP000198584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM7597 {ECO:0000313|EMBL:SEA77276.1,
RC ECO:0000313|Proteomes:UP000198584};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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DR EMBL; FNQR01000008; SEA77276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4DXF7; -.
DR STRING; 571932.SAMN05421743_10841; -.
DR Proteomes; UP000198584; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000198584};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 25..529
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5011327906"
FT DOMAIN 42..271
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 344..494
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 529 AA; 57230 MW; B7AD9A6BA150A5D9 CRC64;
MFQMRKIIPA FLLSLALLST SVSAAPDANE PYKERYIPVQ LLGMNDFHGQ LDVYRTIGDR
KAGGAEYLAA YLKQYEQDNK NTLLVHAGDV VGASSPVSSL LQDEPTIEIL NELGFDVGTV
GNHEFDEGVA EMKRLIDGGT HEETGDFEGA SFPYTVANVK DKETGEPILP PYVIKKVNGM
PIGFIGVVTT DTKNIVLPSG IEGVEFTDET TAINNAAAQL KEKGVESIVV LAHVPASSKP
DGTSASGEVV EFAPKIDDEV DVIYGGHNHA YANTVVDGKL IVESYSYGTA FSDVDLMIDP
KTKDIVSKEA SVVTTFHDAI EPDAEVKEMV NNYSKEVEDL VQEVIAQAAE PITNAPDASG
ESALGNLVAD SQRAFMQTDF AFMNPGGIRS DLDEGPITWG ELYTMLPFGN NLVKMTLTGN
QIKAVLEQQW SGSYPRILQV SGLNYTWDDN APNGEKIVAM TDSNGNPIDP EQQYTVTVNN
YIATGGDGFT VLKEGTNQET GPLALDAMIE YLKQEENIEA PALNRIDVK
//
