ASND1_MACFA
ID ASND1_MACFA Reviewed; 643 AA.
AC Q4R5D4; Q4R4W1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Asparagine synthetase domain-containing protein 1;
GN Name=ASNSD1; ORFNames=QnpA-19512, QtrA-13028;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex, and Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AB169610; BAE01691.1; -; mRNA.
DR EMBL; AB169783; BAE01864.1; -; mRNA.
DR AlphaFoldDB; Q4R5D4; -.
DR SMR; Q4R5D4; -.
DR STRING; 9541.XP_005573760.1; -.
DR eggNOG; KOG0573; Eukaryota.
DR Proteomes; UP000233100; 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; 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..643
FT /note="Asparagine synthetase domain-containing protein 1"
FT /id="PRO_0000324761"
FT DOMAIN 2..184
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 285..601
FT /note="Asparagine synthetase"
FT REGION 367..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT CONFLICT 20
FT /note="R -> K (in Ref. 1; BAE01864)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="Q -> H (in Ref. 1; BAE01864)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="I -> V (in Ref. 1; BAE01864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 72181 MW; B78253BD76C1459E CRC64;
MCGICCSVNF SAEHFSQDLR EDLLYNLKQR GPNSSKQLFK SDVNYQCLFS GHVLHLRGVL
TTQPVEDERG NVFLWNGEIF SGIKVEAEEN DTQILFNYLS SCKNESEILS LFSEVQGPWS
FIYYQASSHY LWFGRDFFGR RSLLWHFSNL GKSFCLSSVG TQTSGLANQW QEVPASGLFR
IDLKSTAISR CIILQLYPWK YISRENIIEE NVNSLSQISA DLPAFVSVVA NEAKLYLEKP
VVPLNMMLPQ AALETHCSNI SNVPPTRETL QVFLTDVHIK EVIQQFIDVL SVAVKKRVLC
LPRGENLTAN EVSKMCDRKA NVAILFSGGI DSMVIATLAD RHIPLDEPID LLNVAFIAEE
KTMPTSFNKE RNKQKNKCEI SSEEFSKDDA AADDDSPDKH VSVPDRITGR AGLKELKAVS
PSRIWNFVEI NVSMEELQKL RRTRICHLIQ PLDTVLDDSI GCAVWFASRG IGWLVAQDGV
KSYQSSAKVV LTGIGADEQL AGYSRHRVRF QSHGLEGLNK EIMMELGRIS SRNLGRDDRV
IGDHGKEARF PFLDENVVSF LNSLPIWEKA NLTLPRGIGE KLLLRLAAVE LGLTASALLP
KRAMQFGSRI AKMEKNNEKA SDKCGRLQII SLENLSIEKE TKL