UniProt: E2C413

Database: UniProt
Entry: E2C413_HARSA

LinkDB:  E2C413_HARSA 
Original site:  E2C413_HARSA

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (10)   
   RefSeq(pep) (10)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (24)   

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ID   E2C413_HARSA            Unreviewed;       334 AA.
AC   E2C413;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=5'-nucleotidase {ECO:0000256|ARBA:ARBA00012643, ECO:0000256|RuleBase:RU361276};
DE            EC=3.1.3.5 {ECO:0000256|ARBA:ARBA00012643, ECO:0000256|RuleBase:RU361276};
GN   ORFNames=EAI_14530 {ECO:0000313|EMBL:EFN77399.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN77399.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN77399.1,
RC   ECO:0000313|Proteomes:UP000008237};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(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         ECO:0000256|RuleBase:RU361276};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361276}.
CC   -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00008389, ECO:0000256|RuleBase:RU361276}.
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DR   EMBL; GL452364; EFN77399.1; -; Genomic_DNA.
DR   RefSeq; XP_011150338.1; XM_011152036.2.
DR   RefSeq; XP_011150339.1; XM_011152037.2.
DR   RefSeq; XP_011150340.1; XM_011152038.2.
DR   RefSeq; XP_011150341.1; XM_011152039.2.
DR   RefSeq; XP_011150343.1; XM_011152041.2.
DR   RefSeq; XP_011150344.1; XM_011152042.2.
DR   RefSeq; XP_011150345.1; XM_011152043.2.
DR   RefSeq; XP_019700025.1; XM_019844466.1.
DR   RefSeq; XP_019700026.1; XM_019844467.1.
DR   RefSeq; XP_019700027.1; XM_019844468.1.
DR   AlphaFoldDB; E2C413; -.
DR   STRING; 610380.E2C413; -.
DR   EnsemblMetazoa; XM_011152041.3; XP_011150343.1; LOC105189741.
DR   EnsemblMetazoa; XM_011152042.3; XP_011150344.1; LOC105189741.
DR   EnsemblMetazoa; XM_025305515.1; XP_025161300.1; LOC105189741.
DR   GeneID; 105189741; -.
DR   KEGG; hst:105189741; -.
DR   InParanoid; E2C413; -.
DR   OMA; WQQSHEL; -.
DR   OrthoDB; 531581at2759; -.
DR   PhylomeDB; E2C413; -.
DR   Proteomes; UP000008237; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium 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: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   NCBIfam; TIGR01544; HAD-SF-IE; 1.
DR   PANTHER; PTHR13045; 5'-NUCLEOTIDASE; 1.
DR   PANTHER; PTHR13045:SF0; CYTOSOLIC 5'-NUCLEOTIDASE 3A; 1.
DR   Pfam; PF05822; UMPH-1; 1.
DR   SFLD; SFLDG01128; C1.4:_5'-Nucleotidase_Like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU361276};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361276};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080,
KW   ECO:0000256|RuleBase:RU361276};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008237}.
SQ   SEQUENCE   334 AA;  38085 MW;  E2039120B2D1E56F CRC64;
     MFSASVRQQS GLRSRFGVRH ILRLSCGASL RFFALPPTMM SNEITIDDFP ALRLKHVFIK
     DEVGLLKRIN AMLQGGANNL QIVTDFDLTL TKQHINGAHV LSSFGMFRKS KQLPTKYSEE
     AKRLYAKYRP MEIDPSLSLN EKANAMRDWM LAAQDLLKGI EFDSHEMEEI AQSCSGILRD
     GTEEIFEKLH NVQVPIVIFS AGLGDMVEAI LRYHNALYDN VKVISNFLKY NGNYLDGFEN
     DVLIHAYNKN ECALEKDYLK ILGEKQNILL MGDTIGDADM VERTEDTKTV LKIGFLYEHV
     EASLDMFMEK FDIVLVDDQT MRVPMEILQS ILQQ
//

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