GenomeNet

Database: UniProt
Entry: A0A6H5K6D0_9PHAE
LinkDB: A0A6H5K6D0_9PHAE
Original site: A0A6H5K6D0_9PHAE 
ID   A0A6H5K6D0_9PHAE        Unreviewed;       426 AA.
AC   A0A6H5K6D0;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643};
DE            EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
GN   ORFNames=ESUBFT_2520_3 {ECO:0000313|EMBL:CAB1106799.1};
OS   Ectocarpus sp. CCAP 1310/34.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Ectocarpales; Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=867726 {ECO:0000313|EMBL:CAB1106799.1, ECO:0000313|Proteomes:UP000485383};
RN   [1] {ECO:0000313|Proteomes:UP000485383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bft15b / CCAP1310/34 {ECO:0000313|Proteomes:UP000485383};
RX   PubMed=20520714; DOI=10.1038/nature09016;
RA   Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA   Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA   Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA   Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA   Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA   Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA   Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA   Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA   Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA   Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA   Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA   Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA   Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA   Yamagishi T., Van de Peer Y., Wincker P.;
RT   "The Ectocarpus genome and the independent evolution of multicellularity in
RT   brown algae.";
RL   Nature 465:617-621(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 pyrimidine 5'-nucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00008389}.
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:CAB1106799.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CACKRE030001653; CAB1106799.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6H5K6D0; -.
DR   Proteomes; UP000485383; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 1.10.150.340; Pyrimidine 5'-nucleotidase (UMPH-1), N-terminal domain; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006434; Pyrimidine_nucleotidase_eu.
DR   PANTHER; PTHR13045; 5'-NUCLEOTIDASE; 1.
DR   PANTHER; PTHR13045:SF0; CYTOSOLIC 5'-NUCLEOTIDASE 3A; 1.
DR   Pfam; PF05822; UMPH-1; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000485383}.
FT   REGION          326..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  46005 MW;  32D7889941E9EDC6 CRC64;
     MGPIHGSAAV GAKVESIRTA LREQHDHPAH GLQVIMDFDL TMTAPGSEQC HHMFETSPAL
     PEKLRRRLAP FFTGEIELTT REAWWEGFHD VLIDAKVTKE QVAAVAGGAD LALRDGTAEL
     MLLLRERGVP LLVVSAGITD IVAETLSRNG LLLDNVTVRA NTMHFGEDGK LERFRESTPV
     HSRQASRDHL SLLSRNKNKT AEREKAYFDS NSHRRRLLIV GDKPGDADVN SGFAPDDQCL
     KIGFFDHSHE HPHPDLPPLP IPTAVTMSSA APVAAASNGL AGETTATLEG LGFLRGANRL
     VLRTTQSTME STAAAAVQGS GAFQLSTSAE QERIRGRPGS QGGGEIFVSE RGQEQQQQPE
     TTAVVEELLR AYRDRFDVVA CGGHSMDLVA DFVRHFVGAG GNSAVAGADA EATRHEARQS
     ASPRKR
//
DBGET integrated database retrieval system