ID   HINT3_BOVIN             Reviewed;         182 AA.
AC   Q2YDJ4; Q8MJJ8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Adenosine 5'-monophosphoramidase HINT3 {ECO:0000250|UniProtKB:Q9NQE9};
DE            EC=3.9.1.- {ECO:0000250|UniProtKB:Q9NQE9};
DE   AltName: Full=HINT-4;
DE   AltName: Full=Histidine triad nucleotide-binding protein 3;
DE            Short=HINT-3;
GN   Name=HINT3; Synonyms=HINT4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Huang C.-H., Chen H., Peng J., Chen Y.;
RT   "A novel member of the histidine triad protein family with differential
RT   polyadenylation (Bovine HINT-4).";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exhibits adenosine 5'-monophosphoramidase activity,
CC       hydrolyzing purine nucleotide phosphoramidates with a single phosphate
CC       group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP
CC       and NH2 (By similarity). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-
CC       acetyl lysine methyl ester)) generated by lysine tRNA ligase (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NQE9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+);
CC         Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57890, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q9NQE9};
CC   -!- SUBUNIT: Forms dimers to octamers and even larger oligomer (By
CC       similarity). Interacts with CALM1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9CPS6, ECO:0000250|UniProtKB:Q9NQE9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQE9}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9NQE9}.
CC   -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
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DR   EMBL; AF398236; AAM90584.1; -; mRNA.
DR   EMBL; BC110193; AAI10194.1; -; mRNA.
DR   RefSeq; NP_776766.1; NM_174341.2.
DR   AlphaFoldDB; Q2YDJ4; -.
DR   SMR; Q2YDJ4; -.
DR   STRING; 9913.ENSBTAP00000002542; -.
DR   PaxDb; Q2YDJ4; -.
DR   PRIDE; Q2YDJ4; -.
DR   Ensembl; ENSBTAT00000002542; ENSBTAP00000002542; ENSBTAG00000001956.
DR   GeneID; 281817; -.
DR   KEGG; bta:281817; -.
DR   CTD; 135114; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001956; -.
DR   VGNC; VGNC:29856; HINT3.
DR   eggNOG; KOG4359; Eukaryota.
DR   GeneTree; ENSGT00510000047616; -.
DR   HOGENOM; CLU_056776_4_2_1; -.
DR   InParanoid; Q2YDJ4; -.
DR   OMA; CRIAGRQ; -.
DR   OrthoDB; 1496385at2759; -.
DR   TreeFam; TF353069; -.
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000001956; Expressed in semen and 109 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.428.10; -; 1.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   SUPFAM; SSF54197; SSF54197; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..182
FT                   /note="Adenosine 5'-monophosphoramidase HINT3"
FT                   /id="PRO_0000324326"
FT   DOMAIN          49..158
FT                   /note="HIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           143..147
FT                   /note="Histidine triad motif"
FT   ACT_SITE        145
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQE9"
FT   BINDING         76..77
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P49773"
FT   BINDING         145..147
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P49773"
FT   CONFLICT        164
FT                   /note="R -> K (in Ref. 1; AAM90584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="F -> V (in Ref. 1; AAM90584)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   182 AA;  20470 MW;  39CA8A1A2C5C7CEF CRC64;
     MMEEEECGLG KSCARSEPVA AAQPAGSPGE TPAVAAESPE LANYSSKCVF CRIAAHQDPG
     TELLHCENED LVCFKDIKPA APHHYLVVPK KHFENCKYLK KDQIELIENM VTVGKAILER
     NNFTDFENTR MGFHVSPFCS IAHLHLHVLA PADQLSFMSR LVYRVNSYWF ITADYLIEKL
     RT