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P51541

- KARG_LIMPO

UniProt

P51541 - KARG_LIMPO

Protein

Arginine kinase

Gene
N/A
Organism
Limulus polyphemus (Atlantic horseshoe crab)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-arginine = ADP + N(omega)-phospho-L-arginine.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei185 – 1851ATP
    Binding sitei225 – 2251Substrate
    Binding sitei229 – 2291ATP
    Binding sitei271 – 2711Substrate
    Binding sitei314 – 3141Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi122 – 1265ATP
    Nucleotide bindingi280 – 2845ATP
    Nucleotide bindingi309 – 3146ATP

    GO - Molecular functioni

    1. arginine kinase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP51541.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine kinase (EC:2.7.3.3)
    Short name:
    AK
    OrganismiLimulus polyphemus (Atlantic horseshoe crab)
    Taxonomic identifieri6850 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataMerostomataXiphosuraLimulidaeLimulus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi225 – 2251E → A: Reduces catalytic activity by 99.9%. 1 Publication
    Mutagenesisi225 – 2251E → D or Q: Reduces catalytic activity by 99.7%. 1 Publication
    Mutagenesisi271 – 2711C → A, D, N or S: Decreases affinity for phosphoarginine and ADP and reduces catalytic activity by 99%. 1 Publication
    Mutagenesisi312 – 3121R → G: Reduces catalytic activity by 20%; when associated with V-314; D-315; A-317 and V-319. 1 Publication
    Mutagenesisi314 – 3141E → D: Reduces catalytic activity by 98.3%. 1 Publication
    Mutagenesisi314 – 3141E → Q: Reduces catalytic activity by 99.7%. Reduces catalytic activity by 99.8%; when associated with Q-225. 1 Publication
    Mutagenesisi314 – 3141E → V: Reduces catalytic activity by 20%; when associated with G-312; D-315; A-317 and V-319. 1 Publication
    Mutagenesisi315 – 3151H → D: Reduces catalytic activity by 20%; when associated with G-312; V-314; A-317 and V-319. 1 Publication
    Mutagenesisi317 – 3171E → A: Reduces catalytic activity by 20%; when associated with G-312; V-314; D-315 and V-319. 1 Publication
    Mutagenesisi319 – 3191E → V: Reduces catalytic activity by 20%; when associated with G-312; V-314; D-315 and A-317. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 357357Arginine kinasePRO_0000212000Add
    BLAST

    Proteomic databases

    PRIDEiP51541.

    Interactioni

    Subunit structurei

    Monomer.5 Publications

    Structurei

    Secondary structure

    1
    357
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1916
    Helixi26 – 305
    Helixi33 – 397
    Helixi50 – 5910
    Turni60 – 623
    Beta strandi70 – 723
    Helixi74 – 774
    Helixi79 – 8911
    Helixi107 – 1093
    Beta strandi118 – 12912
    Helixi137 – 1393
    Helixi142 – 15615
    Helixi161 – 1633
    Beta strandi166 – 1705
    Helixi175 – 1839
    Helixi193 – 1975
    Turni202 – 2076
    Beta strandi209 – 2124
    Beta strandi216 – 23823
    Helixi239 – 25416
    Turni263 – 2653
    Helixi272 – 2743
    Beta strandi280 – 2856
    Helixi288 – 2925
    Helixi294 – 30310
    Beta strandi306 – 3105
    Beta strandi322 – 3276
    Beta strandi331 – 3333
    Helixi335 – 35521

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BG0X-ray1.86A2-357[»]
    1M15X-ray1.20A1-357[»]
    1P50X-ray2.80A2-357[»]
    1P52X-ray1.90A1-357[»]
    1RL9X-ray1.45A1-357[»]
    1SD0X-ray2.30A1-357[»]
    3M10X-ray2.35A/B1-357[»]
    4GVYX-ray2.09A1-357[»]
    4GVZX-ray2.96A1-357[»]
    4GW0X-ray2.45A1-357[»]
    4GW2X-ray2.16A1-357[»]
    ProteinModelPortaliP51541.
    SMRiP51541. Positions 2-357.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51541.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 9183Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini119 – 356238Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 685Substrate binding

    Sequence similaritiesi

    Belongs to the ATP:guanido phosphotransferase family.PROSITE-ProRule annotation
    Contains 1 phosphagen kinase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 phosphagen kinase N-terminal domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di1.10.135.10. 1 hit.
    3.30.590.10. 1 hit.
    InterProiIPR022415. ATP-guanido_PTrfase_AS.
    IPR022414. ATP-guanido_PTrfase_cat.
    IPR022413. ATP-guanido_PTrfase_N.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    [Graphical view]
    PfamiPF00217. ATP-gua_Ptrans. 1 hit.
    PF02807. ATP-gua_PtransN. 1 hit.
    [Graphical view]
    SUPFAMiSSF48034. SSF48034. 1 hit.
    PROSITEiPS00112. PHOSPHAGEN_KINASE. 1 hit.
    PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
    PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P51541-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDQATLDKL EAGFKKLQEA SDCKSLLKKH LTKDVFDSIK NKKTGMGATL    50
    LDVIQSGVEN LDSGVGIYAP DAESYRTFGP LFDPIIDDYH GGFKLTDKHP 100
    PKEWGDINTL VDLDPGGQFI ISTRVRCGRS LQGYPFNPCL TAEQYKEMEE 150
    KVSSTLSSME DELKGTYYPL TGMSKATQQQ LIDDHFLFKE GDRFLQTANA 200
    CRYWPTGRGI FHNDAKTFLV WVNEEDHLRI ISMQKGGDLK TVYKRLVTAV 250
    DNIESKLPFS HDDRFGFLTF CPTNLGTTMR ASVHIQLPKL AKDRKVLEDI 300
    ASKFNLQVRG TRGEHTESEG GVYDISNKRR LGLTEYQAVR EMQDGILEMI 350
    KMEKAAA 357
    Length:357
    Mass (Da):40,239
    Last modified:October 1, 1996 - v1
    Checksum:iD4AE7B46EE5A9DF1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09809 mRNA. Translation: AAA82169.1.
    PIRiS52098.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09809 mRNA. Translation: AAA82169.1 .
    PIRi S52098.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BG0 X-ray 1.86 A 2-357 [» ]
    1M15 X-ray 1.20 A 1-357 [» ]
    1P50 X-ray 2.80 A 2-357 [» ]
    1P52 X-ray 1.90 A 1-357 [» ]
    1RL9 X-ray 1.45 A 1-357 [» ]
    1SD0 X-ray 2.30 A 1-357 [» ]
    3M10 X-ray 2.35 A/B 1-357 [» ]
    4GVY X-ray 2.09 A 1-357 [» ]
    4GVZ X-ray 2.96 A 1-357 [» ]
    4GW0 X-ray 2.45 A 1-357 [» ]
    4GW2 X-ray 2.16 A 1-357 [» ]
    ProteinModelPortali P51541.
    SMRi P51541. Positions 2-357.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P51541.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P51541.

    Miscellaneous databases

    EvolutionaryTracei P51541.

    Family and domain databases

    Gene3Di 1.10.135.10. 1 hit.
    3.30.590.10. 1 hit.
    InterProi IPR022415. ATP-guanido_PTrfase_AS.
    IPR022414. ATP-guanido_PTrfase_cat.
    IPR022413. ATP-guanido_PTrfase_N.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    [Graphical view ]
    Pfami PF00217. ATP-gua_Ptrans. 1 hit.
    PF02807. ATP-gua_PtransN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48034. SSF48034. 1 hit.
    PROSITEi PS00112. PHOSPHAGEN_KINASE. 1 hit.
    PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
    PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residues."
      Strong S.J., Ellington W.R.
      Biochim. Biophys. Acta 1246:197-200(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Heart and Skeletal muscle.
    2. "Transition state structure of arginine kinase: implications for catalysis of bimolecular reactions."
      Zhou G., Somasundaram T., Blanc E., Parthasarathy G., Ellington W.R., Chapman M.S.
      Proc. Natl. Acad. Sci. U.S.A. 95:8449-8454(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH ARGININE; NITRATE AND ADP.
    3. "Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights."
      Yousef M.S., Fabiola F., Gattis J.L., Somasundaram T., Chapman M.S.
      Acta Crystallogr. D 58:2009-2017(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH ARGININE; NITRATE AND ADP.
    4. "The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase."
      Pruett P.S., Azzi A., Clark S.A., Yousef M.S., Gattis J.L., Somasundaram T., Ellington W.R., Chapman M.S.
      J. Biol. Chem. 278:26952-26957(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANTS GLN-225 AND ASP-314 IN COMPLEX WITH ARGININE; NITRATE AND ADP, MUTAGENESIS OF GLU-225; ARG-312; GLU-314; HIS-315; GLU-317 AND GLU-319.
    5. "The role of phosphagen specificity loops in arginine kinase."
      Azzi A., Clark S.A., Ellington W.R., Chapman M.S.
      Protein Sci. 13:575-585(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH ADP.
    6. "The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants."
      Gattis J.L., Ruben E., Fenley M.O., Ellington W.R., Chapman M.S.
      Biochemistry 43:8680-8689(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-271 IN COMPLEX WITH TRANSITION STATE ANALOG, MUTAGENESIS OF CYS-271.

    Entry informationi

    Entry nameiKARG_LIMPO
    AccessioniPrimary (citable) accession number: P51541
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3