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Protein

Actin-fragmin kinase

Gene
N/A
Organism
Physarum polycephalum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has a role in the regulation of microfilament formation. Phosphorylates the actin-fragmin complex on threonine residues, in vitro.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inhibited by staurosporine.1 Publication

Kineticsi

  1. KM=190 nM for actin-fragmin complex1 Publication
  2. KM=25 µM for ATP1 Publication
  1. Vmax=83 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei82ATP; via amide nitrogen1
Binding sitei98ATP1
Binding sitei163ATP; via carbonyl oxygen1
Binding sitei165ATP; via amide nitrogen1
Binding sitei232ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi178 – 185ATPSequence analysis8

GO - Molecular functioni

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKiP80197.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-fragmin kinase (EC:2.7.11.1)
Short name:
AFK
OrganismiPhysarum polycephalum (Slime mold)
Taxonomic identifieri5791 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaMyxogastriaMyxogastromycetidaePhysariidaPhysaraceaePhysarum

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000860441 – 737Actin-fragmin kinaseAdd BLAST737

Interactioni

Subunit structurei

Monomer.3 Publications

Structurei

Secondary structure

1737
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 15Combined sources12
Helixi25 – 27Combined sources3
Turni52 – 54Combined sources3
Helixi69 – 71Combined sources3
Beta strandi72 – 77Combined sources6
Beta strandi85 – 92Combined sources8
Beta strandi94 – 98Combined sources5
Helixi103 – 116Combined sources14
Beta strandi123 – 130Combined sources8
Helixi131 – 143Combined sources13
Beta strandi145 – 147Combined sources3
Helixi149 – 153Combined sources5
Beta strandi157 – 163Combined sources7
Beta strandi167 – 170Combined sources4
Beta strandi175 – 177Combined sources3
Helixi178 – 181Combined sources4
Helixi184 – 200Combined sources17
Beta strandi204 – 206Combined sources3
Beta strandi208 – 210Combined sources3
Helixi216 – 218Combined sources3
Beta strandi219 – 224Combined sources6
Beta strandi228 – 230Combined sources3
Helixi244 – 257Combined sources14
Helixi264 – 277Combined sources14
Helixi284 – 302Combined sources19
Helixi305 – 322Combined sources18
Helixi331 – 341Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CJAX-ray2.90A/B2-343[»]
ProteinModelPortaliP80197.
SMRiP80197.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80197.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati431 – 480Kelch 1Add BLAST50
Repeati482 – 533Kelch 2Add BLAST52
Repeati534 – 584Kelch 3Add BLAST51
Repeati586 – 635Kelch 4Add BLAST50
Repeati646 – 693Kelch 5Add BLAST48

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi350 – 365Poly-SerAdd BLAST16

Sequence similaritiesi

Keywords - Domaini

Kelch repeat, Repeat

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
2.120.10.80. 2 hits.
InterProiView protein in InterPro
IPR015275. Actin-fragmin_kin_cat_dom.
IPR015915. Kelch-typ_b-propeller.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
PfamiView protein in Pfam
PF09192. Act-Frag_cataly. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.

Sequencei

Sequence statusi: Complete.

P80197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGALWEIEK ELFTKLPAPS SAINSHLQPA KPKVPQKKPS KWDPPAEFKV
60 70 80 90 100
DLSTAVSYND IGDINWKNLQ QFKGIERSEK GTEGLFFVET ESGVFIVKRS
110 120 130 140 150
TNIESETFCS LLCMRLGLHA PKVRVVSSNS EEGTNMLECL AAIDKSFRVI
160 170 180 190 200
TTLANQANIL LMELVRGITL NKLTTTSAPE VLTKSTMQQL GSLMALDVIV
210 220 230 240 250
NNSDRLPIAW TNEGNLDNIM LSERGATVVP IDSKIIPLDA SHPHGERVRE
260 270 280 290 300
LLRTLIAHPG HESSQFHSIR DIITLYTGYD VGTEGSISMQ EGFLATVREC
310 320 330 340 350
ASFDLDAFER ELLSWQESLQ KCHNLSISPQ AIPFILRMLR IFHDAIHNPS
360 370 380 390 400
PSSPSPSPSS SSSTSHPTPA SSSTSSTLPS SIPSSSNTSP PPASSSESLV
410 420 430 440 450
GVEECAWLKV VVPNEKPAPR RYHSGVLYEG KLYVFGGVCI KTASNDFYVF
460 470 480 490 500
DFAKKKWSIV VAQGEAPSPR CGHSATVYGG KMWIFGGHNN NKQPYSDLYT
510 520 530 540 550
FDFAKSTWEK IEPTKDGPWP SPRYHHSATL VGASLYIFGG AEHKSKYHND
560 570 580 590 600
VYVYKFDANQ WELLNATGET PEPRAGQMTV EWNNSLFTFG GHGGEGGYTS
610 620 630 640 650
FVDAHVFEIA TNTFHEVDCS GTFPRTARPL SYVPYYYGSG DKREGAVFSF
660 670 680 690 700
GGSDGKSPLG SLYQWNLKTH KWKIIKAWMA VEDNTIGSMA AIASGKLDPI
710 720 730
PRYGHCTVLD DTGVISIFGG SGSLFLDDIV QFDMTES
Length:737
Mass (Da):80,955
Last modified:May 5, 2009 - v2
Checksum:iD950BD5BAE6764B0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti506S → G AA sequence (PubMed:8389700).Curated1
Sequence conflicti507T → P AA sequence (PubMed:8389700).Curated1
Sequence conflicti560Q → K AA sequence (PubMed:8896448).Curated1
Sequence conflicti560Q → K AA sequence (PubMed:8389700).Curated1
Sequence conflicti639S → W AA sequence (PubMed:8389700).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64722 mRNA. Translation: AAB08728.1.
PIRiS36952.
S72442.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64722 mRNA. Translation: AAB08728.1.
PIRiS36952.
S72442.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CJAX-ray2.90A/B2-343[»]
ProteinModelPortaliP80197.
SMRiP80197.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKiP80197.

Miscellaneous databases

EvolutionaryTraceiP80197.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
2.120.10.80. 2 hits.
InterProiView protein in InterPro
IPR015275. Actin-fragmin_kin_cat_dom.
IPR015915. Kelch-typ_b-propeller.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
PfamiView protein in Pfam
PF09192. Act-Frag_cataly. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAFK_PHYPO
AccessioniPrimary (citable) accession number: P80197
Secondary accession number(s): Q94706
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 5, 2009
Last modified: April 12, 2017
This is version 83 of the entry and version 2 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

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.