ID E4X460_OIKDI Unreviewed; 568 AA.
AC E4X460;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643};
DE EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
GN ORFNames=GSOID_T00001175001 {ECO:0000313|EMBL:CBY23849.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY23849.1};
RN [1] {ECO:0000313|EMBL:CBY23849.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000815};
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|ARBA:ARBA00006654, ECO:0000256|RuleBase:RU362119}.
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DR EMBL; FN653024; CBY23849.1; -; Genomic_DNA.
DR AlphaFoldDB; E4X460; -.
DR InParanoid; E4X460; -.
DR Proteomes; UP000001307; Unassembled WGS sequence.
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 CDD; cd07409; MPP_CD73_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; IPR029052; Metallo-depent_PP-like.
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 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; PS00786; 5_NUCLEOTIDASE_2; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 18..568
FT /note="5'-nucleotidase"
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5003192283"
FT DOMAIN 33..250
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 352..531
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 568 AA; 63044 MW; 423C0BC15EF2A14B CRC64;
MVFERKVLLL LLAAVLGDDN DSSEARAETF KLTIVHTNDV HAHFVESDAY GNACKEGGPC
YGGAARRATL INEIRANRQN PVLLLDAGDQ SQGTPWYNTY KGAAAANFIS VLGYDAFIIG
NHEFDRGVEN FIEHFIGNIS SGNEFPILSA NIDAKNEPSL IGKFDKTLTI DIEGLKIGVI
GYTTEETPEI SDTGNLIFNN VVKTVQEEST RLRSENADIL IGVGHYGLSE DKAMASQVDL
DVIIGGHSHS LLYSDQLDID PIDAEKSKGP YPTWEKNVYG NDLPICHAFE YGKYLGIVDL
EFHLIDGKYV LQKDLVQGAP RILDQKIEKN KVVLAEIEEW KVAVDRLTEE PIGYAMTFLD
GDRTSCRRRE CTMGNWAADA VVHHQNRLYS SGSDAAPTAC HIAMLGSGGI RASISAGKIN
YGQMLTVFPF DGFFDSIVVN GSIFRQTVET GVRRYVDSID SNPGEFLQFS GVKVVYDMEK
ESFSRVSDLK VRTRNETTGE LVYTDLEDEK EYCFVSSDFL AVKGGDGYDL LRNGSTNCLS
RQTLKVLWKS FKKRPCNSAH KKTPWHRY
//
