ID   Q081B0_SHEFN            Unreviewed;       572 AA.
AC   Q081B0;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=5'-nucleotidase {ECO:0000313|EMBL:ABI72155.1};
DE            EC=3.1.3.5 {ECO:0000313|EMBL:ABI72155.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sfri_2309 {ECO:0000313|EMBL:ABI72155.1};
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI72155.1, ECO:0000313|Proteomes:UP000000684};
RN   [1] {ECO:0000313|EMBL:ABI72155.1, ECO:0000313|Proteomes:UP000000684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI72155.1,
RC   ECO:0000313|Proteomes:UP000000684};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00006654, ECO:0000256|RuleBase:RU362119}.
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DR   EMBL; CP000447; ABI72155.1; -; Genomic_DNA.
DR   RefSeq; WP_011637764.1; NC_008345.1.
DR   AlphaFoldDB; Q081B0; -.
DR   STRING; 318167.Sfri_2309; -.
DR   KEGG; sfr:Sfri_2309; -.
DR   eggNOG; COG0737; Bacteria.
DR   HOGENOM; CLU_005854_7_0_6; -.
DR   OrthoDB; 9803927at2; -.
DR   Proteomes; UP000000684; 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   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; 5'-NUCLEOTIDASE-RELATED; 1.
DR   PANTHER; PTHR11575:SF46; PROTEIN USHA; 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:ABI72155.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000684};
KW   Signal {ECO:0000256|RuleBase:RU362119}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|RuleBase:RU362119"
FT   CHAIN           17..572
FT                   /evidence="ECO:0000256|RuleBase:RU362119"
FT                   /id="PRO_5005142365"
FT   DOMAIN          47..264
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
FT   DOMAIN          375..522
FT                   /note="5'-Nucleotidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02872"
SQ   SEQUENCE   572 AA;  60718 MW;  41F74E56E2CA5E0C CRC64;
     MTNMLIKGLV ATAVLAALTG CGSDDDNTAV VAPTTCAEAG ADCKIFTVLH TNDNHGRFWS
     NSDGEYGMAA RKTLIDQIRA EVSANGGESL LLSGGDINTG VPESDLQDAL PDFIGMNEIA
     YDAMAVGNHE FDNPLAVLDS QRSVANFPML AANIYKADGT RYFDAYKVFD VNGVRVAVIG
     LTTEDTAKIG NPEFIKDLTF TDPTTEAAKV IAEIKAADTA DLIFATTHMG HYADAQNGSN
     APGDVTLARA LAAGDLSAII GGHSQNPVCM EPDTNDYAEF APGDACTPDM QNGTYIMQAH
     EWGKYVGRAD FEYFNGELHL ASYKLIPVNL KKTVEDAEGN KTKVLVADEI TADADLKALL
     SYYQERGQGQ LDEIIATTDA LLDGERANVR NMQTNLGRLV AEAQRTKVGA DIGVMNSGGV
     RASIQAGDIS YRDVLTVQPF GNMVTLSTMT GAEVTEYLNT VASFQRGAGA YAQITGVKMT
     VDCTAQTVAI SEINGKDYSA TDSYSFTVPS FNAAGGDGYP VLDPIQTGYV DAEVLYTFFK
     DKGTIAAADY APIGDIVYEN SNSPLGCEVT AN
//