ID A0A093BPW4_CHAPE Unreviewed; 285 AA.
AC A0A093BPW4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=M959_10931 {ECO:0000313|EMBL:KFU89961.1};
OS Chaetura pelagica (Chimney swift) (Hirundo pelagica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes; Apodidae;
OC Apodinae; Chaetura.
OX NCBI_TaxID=8897 {ECO:0000313|EMBL:KFU89961.1, ECO:0000313|Proteomes:UP000031515};
RN [1] {ECO:0000313|EMBL:KFU89961.1, ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M959 {ECO:0000313|EMBL:KFU89961.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000031515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25504712; DOI=10.1126/science.1251385;
RG Avian Genome Consortium;
RA Zhang G., Li C., Li Q., Li B., Larkin D.M., Lee C., Storz J.F., Antunes A.,
RA Greenwold M.J., Meredith R.W., Odeen A., Cui J., Zhou Q., Xu L., Pan H.,
RA Wang Z., Jin L., Zhang P., Hu H., Yang W., Hu J., Xiao J., Yang Z., Liu Y.,
RA Xie Q., Yu H., Lian J., Wen P., Zhang F., Li H., Zeng Y., Xiong Z., Liu S.,
RA Zhou L., Huang Z., An N., Wang J., Zheng Q., Xiong Y., Wang G., Wang B.,
RA Wang J., Fan Y., da Fonseca R.R., Alfaro-Nunez A., Schubert M., Orlando L.,
RA Mourier T., Howard J.T., Ganapathy G., Pfenning A., Whitney O., Rivas M.V.,
RA Hara E., Smith J., Farre M., Narayan J., Slavov G., Romanov M.N.,
RA Borges R., Machado J.P., Khan I., Springer M.S., Gatesy J., Hoffmann F.G.,
RA Opazo J.C., Hastad O., Sawyer R.H., Kim H., Kim K.W., Kim H.J., Cho S.,
RA Li N., Huang Y., Bruford M.W., Zhan X., Dixon A., Bertelsen M.F.,
RA Derryberry E., Warren W., Wilson R.K., Li S., Ray D.A., Green R.E.,
RA O'Brien S.J., Griffin D., Johnson W.E., Haussler D., Ryder O.A.,
RA Willerslev E., Graves G.R., Alstrom P., Fjeldsa J., Mindell D.P.,
RA Edwards S.V., Braun E.L., Rahbek C., Burt D.W., Houde P., Zhang Y.,
RA Yang H., Wang J., Jarvis E.D., Gilbert M.T., Wang J.;
RT "Comparative genomics reveals insights into avian genome evolution and
RT adaptation.";
RL Science 346:1311-1320(2014).
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; KN126477; KFU89961.1; -; Genomic_DNA.
DR RefSeq; XP_009996393.1; XM_009998091.1.
DR AlphaFoldDB; A0A093BPW4; -.
DR GeneID; 104389139; -.
DR KEGG; cpea:104389139; -.
DR CTD; 51251; -.
DR OrthoDB; 531581at2759; -.
DR Proteomes; UP000031515; 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 CDD; cd07504; HAD_5NT; 1.
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:UP000031515}.
SQ SEQUENCE 285 AA; 32591 MW; 4123134DE5565562 CRC64;
MPEFQKKTVH IKDPGRVEEI ICGLIKGGAA KLQIITDFDM TLSRFSYNGK RCPTCHNIID
NSKLITEECR KKLLQLKETY YAIEIDPALT IEEKYPYMVE WYNKSHALLI EQGLQKDKFA
EIVRESDVML KEGYENFFDK LSEHNIPVFI FSAGIGDILE EVIHQAGVYH SNVKVVSNFM
DFDENGLLKG FKGELIHVYN KHDGALKNTE YFKQLKDNSN IILLGDSQGD LSMADGVANV
EHILKIGYLN DKVDELLEKY MDSYDIVLVK DESLEVANSI LQKIL
//
