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P51541

- KARG_LIMPO

UniProt

P51541 - KARG_LIMPO

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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

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
Complete GO annotation...

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
Complete GO annotation...

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.

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.

Miscellaneous databases

EvolutionaryTraceiP51541.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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: April 16, 2014
This is version 73 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

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