ID A0A369RZ87_9METZ Unreviewed; 609 AA.
AC A0A369RZ87;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643};
DE EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643};
GN ORFNames=TrispH2_008242 {ECO:0000313|EMBL:RDD39621.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD39621.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD39621.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD39621.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD39621.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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:RDD39621.1}.
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DR EMBL; NOWV01000128; RDD39621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369RZ87; -.
DR STRING; 287889.A0A369RZ87; -.
DR Proteomes; UP000253843; 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; 2.
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; 2.
DR SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 2.
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:UP000253843}.
SQ SEQUENCE 609 AA; 69674 MW; 561A62C101F0C4AB CRC64;
MKYCFVNNAA TDSVMESLTE SQWAATSQEL EKRIMAETLS AALSNQLRKL LQQSPMHCRV
IDGTLAKLKS IAKGGPRKLQ FVTDYDRTLT CLEHNGEITS TTFDVIYANP LIDKEIRDKI
IATRMQYIST FTSRQGAEEL MAFLDRYNIP ILIFSAGIGD IILEGFRQRS VFRKNMEVLS
NMMKFNDDGL LVGFQGDIIH ARNKARASEY HSSYFERIKE RDNIILMGDV EGDLQMADGI
DYSRNKVTIG FLNGQVDELL DTYMALYDIV IVGDESMESV NQLLLTMFDH AQLPWAHISS
NATHLQIRRQ LPGNTSKRNH GEQFFRTIIQ SAVYCRDVDG TIAKLQMIAK DGTDKFQFIT
DYDWTLTYRM YKGEIAATSF GVIDSNPLVD KKIRDAAESL RDYYYGIEIS DKYTFEEKTA
YMATWWKEAE KLMVSANIYR NDLSKLLKVS SIRLREGTDE LMATLKRHNI PVLILSAGLG
DIIREGFHQQ SMFYENMEIL SNMMIYSDDG SLIGFQEDVI HSFDKTRASE HNSSYFKKNK
ERYNLILMGD TEGDLNMADG IDYLRNQVSI GFLNTKVNEL LDSYKAKYDI VIAGDQNMDF
VNKLLKAIF
//
