ID H0V4V8_CAVPO Unreviewed; 391 AA.
AC H0V4V8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=N-acetylaspartylglutamate synthase {ECO:0000256|ARBA:ARBA00012938};
DE EC=6.3.2.41 {ECO:0000256|ARBA:ARBA00012938};
GN Name=RIMKLA {ECO:0000313|Ensembl:ENSCPOP00000004663.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000004663.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000004663.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000004663.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + N-acetyl-L-aspartate = ADP + H(+) + N-
CC acetyl-L-aspartyl-L-glutamate + phosphate; Xref=Rhea:RHEA:40035,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16953, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:76931,
CC ChEBI:CHEBI:456216; EC=6.3.2.41;
CC Evidence={ECO:0000256|ARBA:ARBA00000622};
CC -!- SIMILARITY: Belongs to the RimK family.
CC {ECO:0000256|ARBA:ARBA00007854}.
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DR EMBL; AAKN02053622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02053623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003462549.1; XM_003462501.3.
DR AlphaFoldDB; H0V4V8; -.
DR STRING; 10141.ENSCPOP00000004663; -.
DR Ensembl; ENSCPOT00000005239.3; ENSCPOP00000004663.2; ENSCPOG00000005184.4.
DR GeneID; 100713055; -.
DR KEGG; cpoc:100713055; -.
DR CTD; 284716; -.
DR VEuPathDB; HostDB:ENSCPOG00000005184; -.
DR eggNOG; ENOG502QT4M; Eukaryota.
DR GeneTree; ENSGT00390000014577; -.
DR HOGENOM; CLU_054353_3_1_1; -.
DR InParanoid; H0V4V8; -.
DR OMA; EKHGVMV; -.
DR OrthoDB; 4026633at2759; -.
DR TreeFam; TF332035; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000005184; Expressed in frontal cortex and 8 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0072590; F:N-acetyl-L-aspartate-L-glutamate ligase activity; IEA:Ensembl.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF1; N-ACETYLASPARTYLGLUTAMATE SYNTHASE A; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT DOMAIN 115..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 343..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 42603 MW; 430F9F1525981346 CRC64;
MCSQVWLLTD RRLSEDYPQV QILRALRQRC SEQDVRFRAV FMDQLAVTVV GGHLGLQLNQ
KALTTFPDVV VVRVSTPSVQ SDSDITVLRH LEKLGCRLVN SSQSILNCIN KFWTFQELAG
HGVPMPDTFS YGGHDDFSKM IDEAEPLGYP VVVKSTRGNQ GKAVFLARDK HHLSDICHLI
RHDVPYLFQK YVKESHGKDI RVVVVGGQVI GSMLRCSTDG RMQSNCSLGG VGVMCPLTEQ
GKQLAIQVSN ILGMDFCGID LLIMDDGSFV VCEANANVGF LAFDQACNLD VGGIIADYSM
SLLPNRQTGK MAVLPGLSSP REKKEPDGCA SAQGVAESVY TINNGSTSSE SEPELGEVRD
SSANTKGGPP PVLPEPGYNI NNRIASELKL K
//
