ID A3TK76_9MICO Unreviewed; 627 AA.
AC A3TK76;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Putative 2',3'-cyclic-nucleotide 2'-phosphodiesterase {ECO:0000313|EMBL:EAP98781.1};
GN ORFNames=JNB_01395 {ECO:0000313|EMBL:EAP98781.1};
OS Janibacter sp. HTCC2649.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP98781.1, ECO:0000313|Proteomes:UP000005063};
RN [1] {ECO:0000313|EMBL:EAP98781.1, ECO:0000313|Proteomes:UP000005063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP98781.1,
RC ECO:0000313|Proteomes:UP000005063};
RX PubMed=21075932; DOI=10.1128/JB.01298-10;
RA Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA Vergin K.L., Giovannoni S.J.;
RT "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL J. Bacteriol. 193:584-585(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'-
CC phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001730};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000527};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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:EAP98781.1}.
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DR EMBL; AAMN01000002; EAP98781.1; -; Genomic_DNA.
DR RefSeq; WP_009774590.1; NZ_CH672413.1.
DR AlphaFoldDB; A3TK76; -.
DR STRING; 313589.JNB_01395; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_4_3_11; -.
DR Proteomes; UP000005063; Unassembled WGS sequence.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-EC.
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 CDD; cd07410; MPP_CpdB_N; 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; IPR041827; CpdB_N.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000005063}.
FT DOMAIN 69..313
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 396..580
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 627 AA; 66609 MW; 10FE77165EA7B7D6 CRC64;
MTDSHHHLSQ PTPRWCSCAV PDDAIDRSSS VTRRGVVLGA SAASVLAAAG WPSPAAAAPA
ARDGNVTITV MGTSDLHANV VNWDYYKDAT YSDSAGNTVG LARVASVVKQ IRADRGREHT
LLFDAGDTIQ GTPLGFYYAT VEPTTETGAV HPMAAQMNAL GYDAVALGNH EFNYGLDFLD
HWIEQMDAPV LAANAVHAGT KVPRFRPYTI TTMKVKGRPP IRVGVLGLTN PGVVIWDKAN
VSGKVEVQGL VEAAARWVPV IRGEGADVVI VSAHSGDSGT SSYGGDLPVE NAAALVAQQV
PGIDAILFGH AHVDVPERFV TNVKTGKQVI MSEPKNWGQR LSVFDLQLEF VRGSWQVAQS
HSLTVNTNTV EDDPAFVSIV RDQHAAVVKY MNTPVANSTE AMSAAEACWK DTAILDYVNE
VQVATVTAAI AGTPEASLPV ISIAAPFNRS ASFPAGPVTI RDVAGLYIYD NTLMASVLTG
SQIKDFLEYS AKYFKQVDPG APVDPAAWTN APYPTPTSPT TPDYNYDQFS GVDYSVDISQ
PVGSRITGMS YEGVPVAPDQ KFVVAVNNYR QSGGGGFPHI ASAPVIYNAQ VAIREAIVAY
ASAAGTIDPA SFHVENWRLV RGGVPVF
//
