AFK_PHYPO
ID AFK_PHYPO Reviewed; 737 AA.
AC P80197; Q94706;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Actin-fragmin kinase;
DE Short=AFK;
DE EC=2.7.11.1;
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-49; 225-234; 410-420;
RP 442-454; 471-481; 493-507; 545-574; 629-642; 644-656 AND 659-668, FUNCTION,
RP SUBUNIT, ATP-BINDING SITE, AND SUBCELLULAR LOCATION.
RX PubMed=8896448; DOI=10.1002/j.1460-2075.1996.tb00939.x;
RA Eichinger L., Bomblies L., Vandekerckhove J., Schleicher M., Gettemans J.;
RT "A novel type of protein kinase phosphorylates actin in the actin-fragmin
RT complex.";
RL EMBO J. 15:5547-5556(1996).
RN [2]
RP PROTEIN SEQUENCE OF 42-49; 225-234; 410-420; 442-454; 471-481; 493-507;
RP 545-574; 629-642; 644-656 AND 659-668.
RX PubMed=8389700; DOI=10.1111/j.1432-1033.1993.tb17902.x;
RA Gettemans J., de Ville Y., Vandekerckhove J., Waelkens E.;
RT "Purification and partial amino acid sequence of the actin-fragmin kinase
RT from Physarum polycephalum.";
RL Eur. J. Biochem. 214:111-119(1993).
RN [3]
RP SUBUNIT, AND ACTIVITY REGULATION.
RX PubMed=1324166; DOI=10.1002/j.1460-2075.1992.tb05395.x;
RA Gettemans J., de Ville Y., Vandekerckhove J., Waelkens E.;
RT "Physarum actin is phosphorylated as the actin-fragmin complex at residues
RT Thr203 and Thr202 by a specific 80 kDa kinase.";
RL EMBO J. 11:3185-3191(1992).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1587799; DOI=10.1093/oxfordjournals.jbchem.a123763;
RA Furuhashi K., Hatano S.;
RT "Actin kinase: a protein kinase that phosphorylates actin of fragmin-actin
RT complex.";
RL J. Biochem. 111:366-370(1992).
RN [5]
RP FUNCTION.
RX PubMed=1315751; DOI=10.1016/s0021-9258(19)50427-6;
RA Furuhashi K., Hatano S., Ando S., Nishizawa K., Inagaki M.;
RT "Phosphorylation by actin kinase of the pointed end domain on the actin
RT molecule.";
RL J. Biol. Chem. 267:9326-9330(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2-343 IN COMPLEX WITH AMP.
RX PubMed=10357805; DOI=10.1093/emboj/18.11.2923;
RA Steinbacher S., Hof P., Eichinger L., Schleicher M., Gettemans J.,
RA Vandekerckhove J., Huber R., Benz J.;
RT "The crystal structure of the Physarum polycephalum actin-fragmin kinase:
RT an atypical protein kinase with a specialized substrate-binding domain.";
RL EMBO J. 18:2923-2929(1999).
CC -!- FUNCTION: Has a role in the regulation of microfilament formation.
CC Phosphorylates the actin-fragmin complex on threonine residues, in
CC vitro. {ECO:0000269|PubMed:1315751, ECO:0000269|PubMed:1587799,
CC ECO:0000269|PubMed:8896448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Inhibited by staurosporine.
CC {ECO:0000269|PubMed:1324166}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=190 nM for actin-fragmin complex {ECO:0000269|PubMed:1587799};
CC KM=25 uM for ATP {ECO:0000269|PubMed:1587799};
CC Vmax=83 umol/min/mg enzyme {ECO:0000269|PubMed:1587799};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10357805,
CC ECO:0000269|PubMed:1324166, ECO:0000269|PubMed:8896448}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8896448}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AFK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; U64722; AAB08728.1; -; mRNA.
DR PIR; S36952; S36952.
DR PIR; S72442; S72442.
DR PDB; 1CJA; X-ray; 2.90 A; A/B=2-343.
DR PDBsum; 1CJA; -.
DR AlphaFoldDB; P80197; -.
DR SMR; P80197; -.
DR PRIDE; P80197; -.
DR SABIO-RK; P80197; -.
DR EvolutionaryTrace; P80197; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05124; AFK; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 2.120.10.80; -; 2.
DR InterPro; IPR015275; Actin-fragmin_kin_cat_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR Pfam; PF09192; Act-Frag_cataly; 1.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Kelch repeat; Kinase; Nucleotide-binding; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..737
FT /note="Actin-fragmin kinase"
FT /id="PRO_0000086044"
FT REPEAT 431..480
FT /note="Kelch 1"
FT REPEAT 482..533
FT /note="Kelch 2"
FT REPEAT 534..584
FT /note="Kelch 3"
FT REPEAT 586..635
FT /note="Kelch 4"
FT REPEAT 646..693
FT /note="Kelch 5"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT CONFLICT 506
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="T -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="Q -> K (in Ref. 1; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="S -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1CJA"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 184..200
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1CJA"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 284..302
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 305..322
FT /evidence="ECO:0007829|PDB:1CJA"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:1CJA"
SQ SEQUENCE 737 AA; 80955 MW; D950BD5BAE6764B0 CRC64;
MAGALWEIEK ELFTKLPAPS SAINSHLQPA KPKVPQKKPS KWDPPAEFKV DLSTAVSYND
IGDINWKNLQ QFKGIERSEK GTEGLFFVET ESGVFIVKRS TNIESETFCS LLCMRLGLHA
PKVRVVSSNS EEGTNMLECL AAIDKSFRVI TTLANQANIL LMELVRGITL NKLTTTSAPE
VLTKSTMQQL GSLMALDVIV NNSDRLPIAW TNEGNLDNIM LSERGATVVP IDSKIIPLDA
SHPHGERVRE LLRTLIAHPG HESSQFHSIR DIITLYTGYD VGTEGSISMQ EGFLATVREC
ASFDLDAFER ELLSWQESLQ KCHNLSISPQ AIPFILRMLR IFHDAIHNPS PSSPSPSPSS
SSSTSHPTPA SSSTSSTLPS SIPSSSNTSP PPASSSESLV GVEECAWLKV VVPNEKPAPR
RYHSGVLYEG KLYVFGGVCI KTASNDFYVF DFAKKKWSIV VAQGEAPSPR CGHSATVYGG
KMWIFGGHNN NKQPYSDLYT FDFAKSTWEK IEPTKDGPWP SPRYHHSATL VGASLYIFGG
AEHKSKYHND VYVYKFDANQ WELLNATGET PEPRAGQMTV EWNNSLFTFG GHGGEGGYTS
FVDAHVFEIA TNTFHEVDCS GTFPRTARPL SYVPYYYGSG DKREGAVFSF GGSDGKSPLG
SLYQWNLKTH KWKIIKAWMA VEDNTIGSMA AIASGKLDPI PRYGHCTVLD DTGVISIFGG
SGSLFLDDIV QFDMTES
