ID L5M7A2_MYODS Unreviewed; 127 AA.
AC L5M7A2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Adenosine 5'-monophosphoramidase HINT1 {ECO:0000256|ARBA:ARBA00039810};
DE AltName: Full=Desumoylating isopeptidase HINT1 {ECO:0000256|ARBA:ARBA00042634};
DE AltName: Full=Histidine triad nucleotide-binding protein 1 {ECO:0000256|ARBA:ARBA00042358};
GN ORFNames=MDA_GLEAN10002295 {ECO:0000313|EMBL:ELK33578.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK33578.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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:0000256|ARBA:ARBA00024472};
CC -!- SIMILARITY: Belongs to the HINT family.
CC {ECO:0000256|ARBA:ARBA00025764}.
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DR EMBL; KB104016; ELK33578.1; -; Genomic_DNA.
DR RefSeq; XP_006759406.1; XM_006759343.1.
DR AlphaFoldDB; L5M7A2; -.
DR GeneID; 102774946; -.
DR KEGG; myd:102774946; -.
DR CTD; 3094; -.
DR eggNOG; KOG3275; Eukaryota.
DR OrthoDB; 5472065at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01276; PKCI_related; 1.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR23089:SF33; ADENOSINE 5'-MONOPHOSPHORAMIDASE HINT1; 1.
DR PANTHER; PTHR23089; HISTIDINE TRIAD HIT PROTEIN; 1.
DR Pfam; PF01230; HIT; 1.
DR PRINTS; PR00332; HISTRIAD.
DR SUPFAM; SSF54197; HIT-like; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT DOMAIN 19..127
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT MOTIF 111..115
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PIRSR:PIRSR601310-3,
FT ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 113
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601310-1"
SQ SEQUENCE 127 AA; 13852 MW; E724E081DEEAA137 CRC64;
MMADEIAMTQ AAQPGGDMIS GKVIHKEIPA KIIFEDNQCL AFHNISPQTP THFLVIPKKH
ISQISVAEDD DENLLGHLTI VGKKCAADLG LKKGYHMVVN EDTDGGQSVY HVHSHVLGGR
QMNWPSG
//