ID D4INK4_9BACT Unreviewed; 478 AA.
AC D4INK4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=5'-nucleotidase/2',3'-cyclic phosphodiesterase and related esterases {ECO:0000313|EMBL:CBK64516.1};
DE EC=3.1.3.5 {ECO:0000313|EMBL:CBK64516.1};
GN ORFNames=AL1_22480 {ECO:0000313|EMBL:CBK64516.1};
OS Alistipes shahii WAL 8301.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=717959 {ECO:0000313|EMBL:CBK64516.1, ECO:0000313|Proteomes:UP000008794};
RN [1] {ECO:0000313|EMBL:CBK64516.1, ECO:0000313|Proteomes:UP000008794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK64516.1,
RC ECO:0000313|Proteomes:UP000008794};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J.;
RT "The genome sequence of Alistipes shahii WAL 8301.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK64516.1, ECO:0000313|Proteomes:UP000008794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK64516.1,
RC ECO:0000313|Proteomes:UP000008794};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929032; CBK64516.1; -; Genomic_DNA.
DR AlphaFoldDB; D4INK4; -.
DR STRING; 717959.AL1_22480; -.
DR KEGG; ash:AL1_22480; -.
DR PATRIC; fig|717959.3.peg.724; -.
DR HOGENOM; CLU_005854_7_3_10; -.
DR Proteomes; UP000008794; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd00845; MPP_UshA_N_like; 1.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119, ECO:0000313|EMBL:CBK64516.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000008794};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 23..478
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5005126485"
FT DOMAIN 34..231
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 311..431
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 478 AA; 52185 MW; 8E1C8B6C8A82F7BC CRC64;
MPTNMKGMFR TGLILLAAAA AACAPRERTL VLLSTNDMHA KIQNFPRLVA AVENCRDTAQ
LVVLVDAGDR WTGNAYVDMA ATPGMPMIAL MNRLGYDVAT LGNHEFDHGQ AFLGRMIDSM
AFEVVCANVT SDTCTFPQLP PYVVLDKDGI RIGFVGVVTN YEGPGHPAGN ASSFEGLEFP
DPQAMAMKYA AELRPKVDLL VLVSHMGDDR DVELLGKETR FDVVIGGHTH VKVDSLVNGT
LLTQTGKYLK NVGVTAVRFR GRKIEGIESR LVPLDGYAPD ASYQAEVDRY YADPELNKPV
GAFAGPADKW GLANWMAASV ADEADADVGF YHIGGVRLDS IPAGGVGAAK VYDLEPFGTE
IATMRMTPAD MRRMILSKYN DEENRKEAHR IDLISTTPYV IVTDAADNAL DVRFPKLREG
KVYEVAVSDY VYRNYKDLNY TDGKLTGTAV AGVLLEELQD DGPLTPDNRP RQKIIRNS
//
