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Protein

Arginine kinase

Gene
N/A
Organism
Limulus polyphemus (Atlantic horseshoe crab)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei185ATP1
Binding sitei225Substrate1
Binding sitei229ATP1
Binding sitei271Substrate1
Binding sitei314Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi122 – 126ATP5
Nucleotide bindingi280 – 284ATP5
Nucleotide bindingi309 – 314ATP6

GO - Molecular functioni

  • arginine kinase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.3.3. 3034.
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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi225E → A: Reduces catalytic activity by 99.9%. 1 Publication1
Mutagenesisi225E → D or Q: Reduces catalytic activity by 99.7%. 1 Publication1
Mutagenesisi271C → A, D, N or S: Decreases affinity for phosphoarginine and ADP and reduces catalytic activity by 99%. 1 Publication1
Mutagenesisi312R → G: Reduces catalytic activity by 20%; when associated with V-314; D-315; A-317 and V-319. 1 Publication1
Mutagenesisi314E → D: Reduces catalytic activity by 98.3%. 1 Publication1
Mutagenesisi314E → Q: Reduces catalytic activity by 99.7%. Reduces catalytic activity by 99.8%; when associated with Q-225. 1 Publication1
Mutagenesisi314E → V: Reduces catalytic activity by 20%; when associated with G-312; D-315; A-317 and V-319. 1 Publication1
Mutagenesisi315H → D: Reduces catalytic activity by 20%; when associated with G-312; V-314; A-317 and V-319. 1 Publication1
Mutagenesisi317E → A: Reduces catalytic activity by 20%; when associated with G-312; V-314; D-315 and V-319. 1 Publication1
Mutagenesisi319E → V: Reduces catalytic activity by 20%; when associated with G-312; V-314; D-315 and A-317. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002120001 – 357Arginine kinaseAdd BLAST357

Proteomic databases

PRIDEiP51541.

Interactioni

Subunit structurei

Monomer.5 Publications

Structurei

Secondary structure

1357
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 19Combined sources16
Helixi26 – 30Combined sources5
Helixi33 – 39Combined sources7
Helixi50 – 59Combined sources10
Turni60 – 62Combined sources3
Beta strandi70 – 72Combined sources3
Helixi74 – 77Combined sources4
Helixi79 – 89Combined sources11
Helixi107 – 109Combined sources3
Beta strandi118 – 129Combined sources12
Helixi137 – 139Combined sources3
Helixi142 – 156Combined sources15
Helixi161 – 163Combined sources3
Beta strandi166 – 170Combined sources5
Helixi175 – 183Combined sources9
Helixi193 – 197Combined sources5
Turni202 – 207Combined sources6
Beta strandi209 – 212Combined sources4
Beta strandi216 – 238Combined sources23
Helixi239 – 254Combined sources16
Turni263 – 265Combined sources3
Helixi272 – 274Combined sources3
Beta strandi280 – 285Combined sources6
Helixi288 – 292Combined sources5
Helixi294 – 303Combined sources10
Beta strandi306 – 310Combined sources5
Beta strandi322 – 327Combined sources6
Beta strandi331 – 333Combined sources3
Helixi335 – 355Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5J99X-ray1.70A1-357[»]
5J9AX-ray2.00A1-357[»]
ProteinModelPortaliP51541.
SMRiP51541.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51541.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 91Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd BLAST83
Domaini119 – 356Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd BLAST238

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 68Substrate binding5

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.
InterProiIPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERiPTHR11547. PTHR11547. 1 hit.
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.
RefSeqiNP_001301013.1. NM_001314084.1.

Genome annotation databases

GeneIDi106471713.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09809 mRNA. Translation: AAA82169.1.
PIRiS52098.
RefSeqiNP_001301013.1. NM_001314084.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5J99X-ray1.70A1-357[»]
5J9AX-ray2.00A1-357[»]
ProteinModelPortaliP51541.
SMRiP51541.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP51541.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi106471713.

Enzyme and pathway databases

BRENDAi2.7.3.3. 3034.
SABIO-RKP51541.

Miscellaneous databases

EvolutionaryTraceiP51541.

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERiPTHR11547. PTHR11547. 1 hit.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 82 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.