ID A0A1G5NRK4_AFIMA Unreviewed; 511 AA.
AC A0A1G5NRK4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'-or 3'-nucleotidase, 5'-nucleotidase family {ECO:0000313|EMBL:SCZ39409.1};
GN ORFNames=SAMN03080610_02445 {ECO:0000313|EMBL:SCZ39409.1};
OS Afifella marina DSM 2698.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Afifellaceae; Afifella.
OX NCBI_TaxID=1120955 {ECO:0000313|EMBL:SCZ39409.1, ECO:0000313|Proteomes:UP000199347};
RN [1] {ECO:0000313|EMBL:SCZ39409.1, ECO:0000313|Proteomes:UP000199347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2698 {ECO:0000313|EMBL:SCZ39409.1,
RC ECO:0000313|Proteomes:UP000199347};
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; FMVW01000005; SCZ39409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5NRK4; -.
DR STRING; 1120955.SAMN03080610_02445; -.
DR OrthoDB; 9803927at2; -.
DR Proteomes; UP000199347; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000199347};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 25..511
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5011330352"
FT DOMAIN 46..229
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 307..461
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 511 AA; 54197 MW; 9188550FB70F0F97 CRC64;
MASTLRWFAA FVIAFSLQPS FAAAKDVSVT FLLVNDADQM AGSSEMRGGY ARIGAVVARE
RAERDHVIFA HAGDAISPSL MAGFDEGAHI ITLLNIIKPD VFVPGNHEHD FGPEVFARRM
GEAEFPVLAA NLRDEDGNRI GAIADTRMIE ADGVKIGIVG LTAEDSYQKS SPGTLEIAPA
LATGEDAAEA LRAKGADFVV AVAHAGREVD RALFQSRAFD LILSGDDHDL MVFFDGKTAM
AESKEQGEYV TAVDVRMGIE EKDGTRTLSW WPEFRPIDTA GVIGDSAVQA KIDEFQADLS
KELDVAVGKT KTGLDSRRAT LRTEEAAIGN LVADAMRAGT AADVAITNGG GIRGNRTYEP
GATITRRDIL TELPFGNVTV KLEISGAAIL EALEHGLGDV ENASGRFPQI SGMRVTADLT
KPAGERVEAV EIGGRPLDPG AVYTLATNDF MADGGDGYVA LTKGHALING RDGRLIANDV
MAFVRSAGEV APRPEGRITF LKGDAARAPK D
//
