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Ankyrin repeat-containing protein kinase A (EC 2.7.11.1) (Ankyrin repeat-containing protein kinase 1)

 ARKA_DICDI              Reviewed;        1460 AA.
Q54HC6;
25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
20-JUN-2018, entry version 90.
RecName: Full=Ankyrin repeat-containing protein kinase A;
EC=2.7.11.1;
AltName: Full=Ankyrin repeat-containing protein kinase 1;
Name=arkA; Synonyms=arck-1; ORFNames=DDB_G0289555;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[2]
SUBCELLULAR LOCATION, FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH
14-3-3 PROTEIN, AND DISRUPTION PHENOTYPE.
PubMed=14597204; DOI=10.1016/j.ydbio.2003.07.012;
Aubry L., Lee S., Ravanel K., Firtel R.A.;
"The novel ankyrin-repeat containing kinase ARCK-1 acts as a
suppressor of the Spalten signaling pathway during Dictyostelium
development.";
Dev. Biol. 263:308-322(2003).
-!- FUNCTION: Involved in the development of the fruiting body.
Overexpression phenocopies the spnA null phenotype.
{ECO:0000269|PubMed:14597204}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:14597204}. Membrane
{ECO:0000269|PubMed:14597204}. Nucleus
{ECO:0000269|PubMed:14597204}. Note=Localized in the subcortical
region of the cell with some enrichment in cell protrusions. In
developed cells, colocalized with spnA. May translocate to the
nucleus in response to a regulatory signal.
-!- DEVELOPMENTAL STAGE: Not detected during axenic growth. Induced
during aggregation with 2 peaks, one at 8 hours at the end of
aggregation and one at 15 hours during later morphogenesis.
Preferentially expressed in a subclass of prestalk cells.
{ECO:0000269|PubMed:14597204}.
-!- DISRUPTION PHENOTYPE: Null cells show weak and late developmental
defects. {ECO:0000269|PubMed:14597204}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AAFI02000143; EAL62663.1; -; Genomic_DNA.
RefSeq; XP_636166.1; XM_631074.1.
ProteinModelPortal; Q54HC6; -.
STRING; 44689.DDB0229363; -.
PaxDb; Q54HC6; -.
PRIDE; Q54HC6; -.
EnsemblProtists; EAL62663; EAL62663; DDB_G0289555.
GeneID; 8627199; -.
KEGG; ddi:DDB_G0289555; -.
dictyBase; DDB_G0289555; arkA.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
InParanoid; Q54HC6; -.
PRO; PR:Q54HC6; -.
Proteomes; UP000002195; Chromosome 5.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0030863; C:cortical cytoskeleton; IDA:dictyBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007275; P:multicellular organism development; IMP:dictyBase.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
CDD; cd00204; ANK; 1.
CDD; cd00029; C1; 1.
Gene3D; 1.25.40.20; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR004182; GRAM.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF12796; Ank_2; 1.
Pfam; PF02893; GRAM; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00248; ANK; 5.
SMART; SM00109; C1; 1.
SMART; SM00568; GRAM; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
ANK repeat; ATP-binding; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Kinase; Membrane; Metal-binding; Nucleotide-binding;
Nucleus; Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
CHAIN 1 1460 Ankyrin repeat-containing protein kinase
A.
/FTId=PRO_0000354055.
TRANSMEM 1293 1313 Helical. {ECO:0000255}.
DOMAIN 653 724 GRAM.
REPEAT 814 843 ANK 1.
REPEAT 852 883 ANK 2.
REPEAT 887 920 ANK 3.
REPEAT 924 955 ANK 4.
REPEAT 959 988 ANK 5.
DOMAIN 1112 1375 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 499 551 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 1118 1126 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 467 667 Interaction with 14-3-3 protein.
COILED 1425 1460 {ECO:0000255}.
COMPBIAS 19 26 Poly-Ser.
COMPBIAS 111 123 Poly-Ser.
COMPBIAS 124 128 Poly-Asn.
COMPBIAS 218 223 Poly-Asn.
COMPBIAS 226 251 Poly-Asn.
COMPBIAS 270 302 Thr-rich.
COMPBIAS 444 460 Poly-Asn.
COMPBIAS 462 471 Poly-His.
COMPBIAS 569 590 Poly-Ser.
COMPBIAS 1457 1460 Poly-Asn.
ACT_SITE 1231 1231 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 1139 1139 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SEQUENCE 1460 AA; 161727 MW; 551CB02BD6FA6A3A CRC64;
MSIKLPLSNI NSGGNSNNSS SSNSTSNNNI NINIGNGIPT NIEKMTFEDS ETQKLNIKQQ
SNNNTSTSVC VSSIHSSSPI SSPTSHQVNK SSGSLPPVIK RSPTTTHHHN SSGSNSSSSS
SGSNNNNNQI KTSNGMNKPN PTGFLFGSKP RENSQNKIDD NKGVNLAVST SNSSNNFHKS
HSESNIININ APPVETVNME EIYNNIPSSI SMENIRENEN NNNSSNNNSN NNNNNNNNNN
NSNNINNVNG NKSSLASSTS SISSLSSVST LSTSNAATNT NTNANTTSTT KTTSTVRSTS
PTQFKPRVEF DENNPNAIIL SRQRCKSISS PSDFRLNPPS NVHMPTSSLS TSTSTTNVNG
LLLPNGVGGV SMSFTPSGLP MTPPTNSSQV DTLQMSTESI TIQPSSLDSS SESVSDGLQS
VSGSPVTASP SPTISNNTNA TTTNNNNNTN TNNNNNNNNN QHNHHHHQHS HSQQHDVYQI
KKENFPSSPT SPTLLPSETH DFSSEYSSNP GGKCAICRKP LWSFPISDKS RRCRDCSLVV
HRACVPLATE CPSAKKSPSK LSVPNGNQSN SSSSSSSSSS SSSSSNSSSS NTKGHSRTPS
SPSVSSIPGF QLTSNASQNL HVNSHTLSLL VNGATIDSNH YKRNKKSLEA GARDFHFIFR
GCGIPLDEFP LDSYVCGLYS YFAHGRLYLT ESYVCFYDGF VFDRTKERTK IIKVSNIASI
EKRSSGLNPS AIKIKTFDDQ SFIFTHFMHR EVAFDDLEGL LIHQESLHFA HSIVANNFPG
MNEAIRGQTK RLLSRARLDG HYQIHSKIRC PMPSKEILLM SAIKNNNLDM VVTLLNYYCQ
VNSDEINSVD SKGYTPLHNA VFSECSDQIF MHLLNQKEVR VRERNMDGNT PLHYFCQKFK
SPECQRIVQA MIEKGANINE QNYNGETPLH KAIFNHSVRL LMVYILLKNN ANVNIVNNAG
ESPLHYAVRL GRLDVAKMLL AAGADPTIIS LRDRKTALAL AVDYDVCPEI SDLLRRLDTI
TTSLEMYELE KFQASLVVEE LQKENVVARL DEKLLDKIGC TDKEERRKFL SLKSNRLLIH
HPARTQGAKI ILKEMETMDI KNGKLIISET ELEYTEKIGS GASGKVFKGI YRGRVVAIKV
LKSADDEMTR EDFLKEFGVL ASLESHTIVG LYGVVLEPKI CLVMEYCSNG SIYHSIRKNP
PSWERFFSFV QQMLAGINAL HQSTPQVLHR DIKTLNFLVN HNNKVKVADF GLSRFNTESN
QETLNKTRGT SVYCAPEVFE GKEYNERSDM YSMGIVMWEI VYCVVYGCYM IPYQEYNKMF
NAFQVALLVN SSKRVLRPTI PIGVPQVLKD LIYCLWDHDV SSRPTATEAM TALAVCEKEY
KQNKAQWELV ITKKEPTPLP RVAPLPAFPG YRQFYEQNLD IKPIPEEEQI YQEAMEKQRR
NQEASANRNQ KNKELLNNNN


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