ID J0L2W6_9LACO Unreviewed; 519 AA.
AC J0L2W6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=2,3-cyclic-nucleotide 2-phosphodiesterase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FD00_GL000748 {ECO:0000313|EMBL:KRN11343.1};
OS Liquorilactobacillus mali KCTC 3596 = DSM 20444.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1046596 {ECO:0000313|EMBL:KRN11343.1, ECO:0000313|Proteomes:UP000050898};
RN [1] {ECO:0000313|EMBL:KRN11343.1, ECO:0000313|Proteomes:UP000050898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20444 {ECO:0000313|EMBL:KRN11343.1,
RC ECO:0000313|Proteomes:UP000050898};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRN11343.1}.
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DR EMBL; AYYH01000002; KRN11343.1; -; Genomic_DNA.
DR RefSeq; WP_003691547.1; NZ_BACP01000057.1.
DR AlphaFoldDB; J0L2W6; -.
DR PATRIC; fig|1046596.6.peg.819; -.
DR OrthoDB; 9801679at2; -.
DR Proteomes; UP000050898; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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:SF6; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE_3'-NUCLEOTIDASE; 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}.
FT DOMAIN 4..239
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 325..481
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 519 AA; 58550 MW; CE66F9A1B5A2E33B CRC64;
MKVRILSTSD VHGYIFPTNF SSRIDSHPFG YLKAAQVIKK IKEETANDEV VIYIENGDFL
EGSPISEYTY QTRKTKKYNQ KYCQMTNFLG ADAGVLGNHE FDYGLVYIKE TLKNRKYPVL
GANISGKMAQ SIIDQPYRII EKAGIKVAVL GLTTQYVPHW EKAGNIEEVT FSSALETAKK
YVPILKKQAD VVVVAYHGGF EKSLDTGKLT ERLTGENEGY ALLSEVPGID ALVTGHQHRK
IAQLVNGIPT TQPGYRAENV GQIVIELDND KKIISASAEL INTTEKPVNQ ELESLLTDWR
HDVEDWLDMP VATVEGDMQI YDHVDARLYG HAYLDLINRI QMDATRTDIA GSALFNDEVS
GYDTQITIRD ILNSYVYPNT LVVERISGAD LKAALERCAS FFELQADGSV SMTNGHNVVK
SQLYNYDYYS GIDYTFDLTK PLGQRVVRIL YHNQVLEDTD RIDVAISQYR AVGGGEYPMF
NMDKSIRVYE DDMPKLIAKY LRDRKVIKAE QPNNLKIIK
//
