ID A0A127W501_SPOPS Unreviewed; 712 AA.
AC A0A127W501;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'-nucleotidase/3'-nucleotidase {ECO:0000313|EMBL:AMQ08632.1};
GN ORFNames=AZE41_17625 {ECO:0000313|EMBL:AMQ08632.1};
OS Sporosarcina psychrophila (Bacillus psychrophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ08632.1, ECO:0000313|Proteomes:UP000071057};
RN [1] {ECO:0000313|EMBL:AMQ08632.1, ECO:0000313|Proteomes:UP000071057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ08632.1,
RC ECO:0000313|Proteomes:UP000071057};
RA Yan W.;
RT "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL Submitted (MAR-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; CP014616; AMQ08632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127W501; -.
DR STRING; 1476.AZE41_17625; -.
DR KEGG; spsy:AZE41_17625; -.
DR OrthoDB; 9801679at2; -.
DR Proteomes; UP000071057; Chromosome.
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 InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR11575:SF24; 5'-NUCLEOTIDASE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF00395; SLH; 3.
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; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362119};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362119}.
FT DOMAIN 526..588
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 589..647
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 650..712
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
SQ SEQUENCE 712 AA; 76656 MW; 5547B13776D6BA96 CRC64;
MLLLSSIAIT PVMAAETPVA ATGDFSMTVL HTNDTHANLA TTAERAALVK KIREEKPYNV
LLDAGDVFSG TLYFNEFEGQ ADLAVMNYLG YDAMTFGNHE FDLGSSAEGH KALVDFIKGA
KFPFISANTD FSADPLFDGL QSKTVEAKAE DGKIYNGIIK EVNGEKVGIF GLTTEETKDI
SSPEKVIFTN YIVEAKEAVA AFEKAGVNKI IALTHIGYND SDNVDNDLLL AKNVPGIDII
VGGHTHVKLD EPFVVNKDTE PVLIVQANEY NKFLGQLDIT FDDKGVIKDY SGVLHAVGGE
NAAVDAGAAE LIKPFSDKVK ETMEKPTGAT AGVFLSGLRD LGGVRAGETN LGNIITDGML
AKAKEIAPST VIAFQNGGGI RTSIPQGPIT YGQAISVLPF GNTLALMELS GAELKSVFER
SVEKYPEEDG GFLHVSGMKL IFNPAAEIGN RVISMAIDGK EIEADKTYKI TTNVFTAQGG
DNYEVLKKAY ADGRASEPGF SDWENFADHM KSIGTINSGI EGRILAKVPY SDVAYDSWAY
PYVSDLYYRG ILKGTDATYG PEKEMTRAQA ASWIVRALDL KADGSAPFND IENYAADTKA
EIVAAYENGL IKGVNGKFMP SEKVTRAQFA LMLERAYENY TGKKYTAAAK APYADFGNYG
SEAVNAISML HELGITTGSD GKFMPGQSTS REHAAKIVSN FIYNVKQAKK AE
//
