Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P51541

- KARG_LIMPO

UniProt

P51541 - KARG_LIMPO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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-KW
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.5 Publications

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MVDQATLDKL EAGFKKLQEA SDCKSLLKKH LTKDVFDSIK NKKTGMGATL
60 70 80 90 100
LDVIQSGVEN LDSGVGIYAP DAESYRTFGP LFDPIIDDYH GGFKLTDKHP
110 120 130 140 150
PKEWGDINTL VDLDPGGQFI ISTRVRCGRS LQGYPFNPCL TAEQYKEMEE
160 170 180 190 200
KVSSTLSSME DELKGTYYPL TGMSKATQQQ LIDDHFLFKE GDRFLQTANA
210 220 230 240 250
CRYWPTGRGI FHNDAKTFLV WVNEEDHLRI ISMQKGGDLK TVYKRLVTAV
260 270 280 290 300
DNIESKLPFS HDDRFGFLTF CPTNLGTTMR ASVHIQLPKL AKDRKVLEDI
310 320 330 340 350
ASKFNLQVRG TRGEHTESEG GVYDISNKRR LGLTEYQAVR EMQDGILEMI

KMEKAAA
Length:357
Mass (Da):40,239
Last modified:October 1, 1996 - v1
Checksum:iD4AE7B46EE5A9DF1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09809 mRNA. Translation: AAA82169.1.
PIRiS52098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09809 mRNA. Translation: AAA82169.1 .
PIRi S52098.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 29, 2014
This is version 75 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