位置:首页 > 蛋白库 > KARG_ARTSF
KARG_ARTSF
ID   KARG_ARTSF              Reviewed;         356 AA.
AC   Q95V58;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Arginine kinase;
DE            Short=AK;
DE            EC=2.7.3.3;
GN   Name=ARGK;
OS   Artemia franciscana (Brine shrimp) (Artemia sanfranciscana).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Anostraca; Artemiidae; Artemia.
OX   NCBI_TaxID=6661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen T., MacRae T.H.;
RT   "Cloning and characterization of arginine kinase cDNA from brine shrimp
RT   (Artemia franciscana).";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine;
CC         Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, ChEBI:CHEBI:456216; EC=2.7.3.3;
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC       ProRule:PRU00843}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF426741; AAL25092.1; -; mRNA.
DR   AlphaFoldDB; Q95V58; -.
DR   SMR; Q95V58; -.
DR   GO; GO:0004054; F:arginine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR   GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.135.10; -; 1.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR   InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11547; PTHR11547; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF48034; SSF48034; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..356
FT                   /note="Arginine kinase"
FT                   /id="PRO_0000211995"
FT   DOMAIN          9..91
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          119..356
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         64..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         280..284
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         309..314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  39976 MW;  0E1CA699FC9C86A1 CRC64;
     MVDAGTLEKL EAGFQKLQAA TDCKSLVKKY LTREVFDQLK TLKTSLGATL LDVIQSGVEN
     LDSGVGIYAP DAESYTLFAP LFDPIIEDYH IGFTKNDSHP PSDFGDVNTL GDLDPDNKFV
     ISTRVRCGRS LQGYPFNPCL TEAQYKEMED KVSSTLNGLD GELKGTFYPL TGMAKEVQQQ
     LIDDHFLFKE GDRFLQAANA CRYWPTGRGI YHNDAKTFLV WCNEEDHLRI ISMQKGGDLK
     AVYARLVNAV NEIEKRIPFS HHDRLGYLTF CPTNLGTTIR ASVHIQLPKL AADRKRLEEV
     ASKYNLQVRG TRGEHTEAEG GIYDISNKRR MGLTEYQAVK EMYDGIAELI KLEQSA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025