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Protein

Arginine kinase

Gene
N/A
Organism
Limulus polyphemus (Atlantic horseshoe crab)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionKinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.3.3 3034
SABIO-RKiP51541

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

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

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

Family and domain databases

Gene3Di1.10.135.10, 1 hit
InterProiView protein in InterPro
IPR000749 ATP-guanido_PTrfase
IPR022415 ATP-guanido_PTrfase_AS
IPR022414 ATP-guanido_PTrfase_cat
IPR022413 ATP-guanido_PTrfase_N
IPR036802 ATP-guanido_PTrfase_N_sf
IPR014746 Gln_synth/guanido_kin_cat_dom
PANTHERiPTHR11547 PTHR11547, 1 hit
PfamiView protein in Pfam
PF00217 ATP-gua_Ptrans, 1 hit
PF02807 ATP-gua_PtransN, 1 hit
SUPFAMiSSF48034 SSF48034, 1 hit
SSF55931 SSF55931, 1 hit
PROSITEiView protein in PROSITE
PS00112 PHOSPHAGEN_KINASE, 1 hit
PS51510 PHOSPHAGEN_KINASE_C, 1 hit
PS51509 PHOSPHAGEN_KINASE_N, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiKARG_LIMPO
AccessioniPrimary (citable) accession number: P51541
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 28, 2018
This is version 85 of the entry and version 1 of the sequence. See 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

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