ID   AK1_DICDI               Reviewed;        1352 AA.
AC   Q54DK4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Alpha-protein kinase 1;
DE            Short=AK1;
DE            EC=2.7.11.-;
GN   Name=ak1; ORFNames=DDB_G0292150;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=15987738; DOI=10.1091/mbc.e05-03-0219;
RA   Yumura S., Yoshida M., Betapudi V., Licate L.S., Iwadate Y., Nagasaki A.,
RA   Uyeda T.Q.P., Egelhoff T.T.;
RT   "Multiple myosin II heavy chain kinases: roles in filament assembly control
RT   and proper cytokinesis in Dictyostelium.";
RL   Mol. Biol. Cell 16:4256-4266(2005).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC       protein kinase family. ALPK subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000187; EAL61431.1; -; Genomic_DNA.
DR   RefSeq; XP_629868.1; XM_629866.1.
DR   AlphaFoldDB; Q54DK4; -.
DR   SMR; Q54DK4; -.
DR   STRING; 44689.DDB0220120; -.
DR   PaxDb; Q54DK4; -.
DR   PRIDE; Q54DK4; -.
DR   EnsemblProtists; EAL61431; EAL61431; DDB_G0292150.
DR   GeneID; 8628550; -.
DR   KEGG; ddi:DDB_G0292150; -.
DR   dictyBase; DDB_G0292150; ak1.
DR   eggNOG; KOG0703; Eukaryota.
DR   HOGENOM; CLU_257642_0_0_1; -.
DR   InParanoid; Q54DK4; -.
DR   OMA; NEDRMVY; -.
DR   PRO; PR:Q54DK4; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:dictyBase.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR   Gene3D; 1.10.220.150; -; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR004166; MHCK_EF2_kinase.
DR   Pfam; PF02816; Alpha_kinase; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   SMART; SM00811; Alpha_kinase; 1.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57863; SSF57863; 1.
DR   PROSITE; PS51158; ALPHA_KINASE; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1352
FT                   /note="Alpha-protein kinase 1"
FT                   /id="PRO_0000363922"
FT   DOMAIN          7..127
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   DOMAIN          990..1194
FT                   /note="Alpha-type protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT   ZN_FING         25..48
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          123..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          901..979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1198..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1279..1352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          393..429
FT                   /evidence="ECO:0000255"
FT   COILED          689..781
FT                   /evidence="ECO:0000255"
FT   COILED          1241..1320
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        262..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..934
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..979
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1279..1321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1164..1169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1352 AA;  154085 MW;  1A18FD3142AC0DE1 CRC64;
     MQPVPSDPNY GLLRSLFQDP NNQCCAECNS ANVPYVCIKL GVFICPTCAH FLSTLGFKVR
     PIMGSSFSEE DISRLQSIGN LVSKQFWLAR WTPMDIVMPP PEDPNLESFL RLKYIEKRWT
     SSLSTSDGFS SPNNNNTSNV NNINNNSNHN NNINNNNNNI NNNNNNNINN NNNIINNFSN
     INNISNGMNN ISLNNINNNN NNNNHYNGND IGIPIVHKTQ SQPQPQPQPQ PQPQSQGFSP
     FNSPRSSPKP GRHHLIDDLI SFNPTPVNNS NNNNNNNNNN NNGNNGNPLK FSGGIPQNNN
     NNNNNNTTTT TTTTNNNNKV PFDPFSPIKT FSESGEYQNT NGNQQLSGSG NSLIDILSHP
     TQSKSPSPSG TPHSLSPQHH SSDFKVHLID IPTTQQQLQQ QQLQLQQQLQ QQLQQQQQQQ
     QQQQQQQQSP ISNPFTSNNN SNSEPLVSIL DKHEDLHNHH HHQQQQHHKQ QQQQQQQQQN
     GNNSPLAQFN QIQQQQINNN NPFVEEKQPH QHPHHLQHHR HHSTSSINHG SNGDLASISL
     TLLTPSPSPS PSFNYSGGVS SAPNNSLNNS CNGNNNLNNG MLNFSNLNIG GSTSSACSTN
     SSSNITIANN INSSNNINII NNQNNQNNNN NNNTNNVMIS PSPSPNPFLP TPTSTNQNNH
     IITPIPVNPF TDNLQLNSNN IRQHPQQMYI QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQLQ
     MQQQQQQQMQ QHYQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQHIN
     LSSSAPLQSV NHSPIPLQPQ HSSSQYMNQQ GYQVYPNVGN QPQSPQQIQP QPLQQQIFQQ
     VQQQQPQIPQ QSPQPLQSST DEDQSVLEVL NLKKLFDMNM MDKEEFEHRR RQIIDNLTKT
     TSPIHQQPPQ PPQPVLPVSA PAQVPQPHPP QQQNGPTVPQ QQQQQQQQQQ QQQQQQQQQQ
     QQQQPIPQPS SSSPTPDARL TGTERVIRHR FDAKLGKWVQ TATIVITEPT PFAEGAMRKA
     FRMKDLSAEG PSSQMVAKLF KDSNEDRMVY FKDVEMQTYS KEIAERFNLK SPPKKIDFVP
     AFVMELVERQ GKPFCAVEYF IEGKYEKHNN NFGYKNDYDR NTPQAFSHFS YEDSGCQLIV
     VDIQGVGDVY TDPQIHSADG QGFGKGNLGI EGIKRFFSTH QCNPICHYLG LSSVNPKPAN
     DESGTMPRPP SIGQSYVRPS AFPPNLQQSF SFNFPPLKDH HVLEQLNQQQ QHLQQQQQQQ
     QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQNQQQNQ QQNQQQQQQQ QQQQQQQQNG
     HPPPQTPLPP TPQQKDKPKI EVFGDILRKL VS