ID   ASND1_BOVIN             Reviewed;         640 AA.
AC   Q0V8E4; Q3SYU4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Asparagine synthetase domain-containing protein 1;
GN   Name=ASNSD1;
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 [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BT026275; ABG81431.1; -; mRNA.
DR   EMBL; BC103382; AAI03383.1; -; mRNA.
DR   RefSeq; NP_001029852.1; NM_001034680.2.
DR   AlphaFoldDB; Q0V8E4; -.
DR   SMR; Q0V8E4; -.
DR   STRING; 9913.ENSBTAP00000052455; -.
DR   PaxDb; Q0V8E4; -.
DR   PRIDE; Q0V8E4; -.
DR   GeneID; 539672; -.
DR   KEGG; bta:539672; -.
DR   CTD; 54529; -.
DR   eggNOG; KOG0573; Eukaryota.
DR   InParanoid; Q0V8E4; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01991; Asn_Synthase_B_C; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00733; Asn_synthase; 2.
DR   Pfam; PF13537; GATase_7; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Asparagine biosynthesis;
KW   Glutamine amidotransferase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..640
FT                   /note="Asparagine synthetase domain-containing protein 1"
FT                   /id="PRO_0000324759"
FT   DOMAIN          2..184
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   DOMAIN          286..602
FT                   /note="Asparagine synthetase"
FT   ACT_SITE        2
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        237
FT                   /note="Y -> C (in Ref. 2; AAI03383)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   640 AA;  71009 MW;  A5D90A726DF17F3E CRC64;
     MCGICCAVSF SVEHFSRDLK EDLLCNLKRR GPDSSKQLLR STVNYQCLFS GHVLHLRGLL
     TAQPVEDERG NVFLWNGEIF SGIKVEAEEN DTQIMFHYLS SCKNESDILS LFSKVQGPWS
     FIYYQASSHS LWFGRDFFGR RSLLWHFSNL GKSFCLSSVG TQASGVTDQW QEVPASGIFR
     IDLKSASISQ SVVLKLYPWK YSSGGDDIRE CVHNSLTEIS ADLPTFVLVA ANEAKLYLKD
     PVVPLNMALP QAAFETHCSS ISRSPLTRET LRVFLTDGHT KEVVQQFIGV LSTAVKRRVL
     CLPRDENLAP SEVLKTSNRK ANVAVLFSGG IDSMVIAALA DHHIPLDEPI DLLNVAFMTK
     EKTIPVNFNK KGRKQANHCE MPSEEFSKHA AATAAASPGE QLSVPDRVTG RAGLKELQAA
     NPSRIWNFVE INVSLEELQR LRRTRISHLI QPLDTVLDDS IGCAVWFASR GAGWLVTQDG
     AQPYQSSAKV VLTGIGADEQ LAGYSRHQVR FLAHGLEGLN KEIEMELGRI SSRNLGRDDR
     VISDHGKEAR FPFLDENVVS FLNSLPVWEK ANLTLPRGIG EKLILRLAAV ELGLTASALL
     PKRAMQFGSR IAKMEKNNEK ASDKCGRLQI ISLENLSVEN