ID   AFK_BADPO               Reviewed;         737 AA.
AC   P80197; Q94706;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   02-SEP-2026, entry version 115.
DE   RecName: Full=Actin-fragmin kinase;
DE            Short=AFK;
DE            EC=2.7.11.1;
OS   Badhamia polycephala (Many-headed slime mold) (Physarum polycephalum).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC   Myxogastromycetidae; Physariida; Physaraceae; Badhamia.
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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; 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   AlphaFoldDB; P80197; -.
DR   SMR; P80197; -.
DR   SABIO-RK; P80197; -.
DR   EvolutionaryTrace; P80197; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd05124; AFK; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 1.
DR   InterPro; IPR015275; Actin-fragmin_kin_cat_dom.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011498; Kelch_2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   PANTHER; PTHR46228; KELCH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46228:SF2; KELCH REPEAT PROTEIN (AFU_ORTHOLOGUE AFUA_4G14350); 1.
DR   Pfam; PF09192; Act-Frag_cataly; 1.
DR   Pfam; PF01344; Kelch_1; 1.
DR   Pfam; PF07646; Kelch_2; 1.
DR   Pfam; PF24681; Kelch_KLHDC2_KLHL20_DRC7; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PDBsum; 1CJA; -.
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        358..397
FT                   /note="Low complexity"
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   HELIX           28..30
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   HELIX           120..122
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           326..328
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
//