ID   PXI_DICDI               Reviewed;         691 AA.
AC   Q1ZXC8; Q94492;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable serine/threonine-protein kinase pXi;
DE            EC=2.7.11.1;
GN   Name=pXi; ORFNames=DDB_G0289119;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 465-691.
RA   Balding K.M., Corrick C., Parish R.W.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB07588.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAB07588.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
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DR   EMBL; AAFI02000130; EAS66833.1; -; Genomic_DNA.
DR   EMBL; U67923; AAB07588.1; ALT_SEQ; mRNA.
DR   RefSeq; XP_001134516.1; XM_001134516.1.
DR   AlphaFoldDB; Q1ZXC8; -.
DR   SMR; Q1ZXC8; -.
DR   STRING; 44689.DDB0232940; -.
DR   PaxDb; Q1ZXC8; -.
DR   EnsemblProtists; EAS66833; EAS66833; DDB_G0289119.
DR   GeneID; 8626987; -.
DR   KEGG; ddi:DDB_G0289119; -.
DR   dictyBase; DDB_G0289119; pXi.
DR   eggNOG; KOG0032; Eukaryota.
DR   HOGENOM; CLU_398730_0_0_1; -.
DR   InParanoid; Q1ZXC8; -.
DR   OMA; TTMGHNK; -.
DR   PRO; PR:Q1ZXC8; -.
DR   Proteomes; UP000002195; Chromosome 5.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..691
FT                   /note="Probable serine/threonine-protein kinase pXi"
FT                   /id="PRO_0000358891"
FT   DOMAIN          18..263
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          314..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          642..691
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        314..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        137
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         24..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        565
FT                   /note="F -> L (in Ref. 2; AAB07588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        691
FT                   /note="K -> E (in Ref. 2; AAB07588)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   691 AA;  76647 MW;  E7B9161F1DABF4DB CRC64;
     MGKNIIAGSI SSSIHKSYEI GSQIGNGKFA QVHSGTNKST GKKSAIKIMK KSIVEESAII
     KEIEMMTEIN HQNIIKLQEV YETDNEVLLV LELVTGGELF DKIVEREFYT EQDASTLIGT
     VTKVIQYLHS KDIVHCDLKP ENLLYSDNSD QAIIKLCDFG LSQRCGSGSP LRSLVGTLTY
     MAPEISSCTG YGKPVDLWSI GVISYILLCG FPPFDETTGY VLEFPSPEWD NISDSAKSLI
     KGLLNNDPSK RFTIDQTLKH PWIAGTTCGK NSIVGTLKTL REFNTLRRTN GGNTTMGHNK
     QSRSTVFELF PSLTPIKSND ENNNNNNNNN NNNNNNEILD KKSNENENEN ENDKIKINLE
     LNLNNNVNNN NNNNNNTVIL ENNNNNLEKI STTKTTTTTS TINDSINKTK IQLMNSLDFE
     NDSSSSETYS SSSPIENGGG GGDKFTSPEL SSLSIDLGCA SDQLNSDKEK IIEQLKNEKS
     LLQKELLEIK RQSPVPSPSS SFLNNHLQQQ HNNNINNNNN NINNGGSTSI NNGNGTIERQ
     FRPIHMSKDS DSGSYENLLL GTSPFVKNHN NNNINNNNNN FCHSRNSSFG YGNSYNSSNG
     GSGCSSSSDE STGGSFKKDK SKYGVDRICL DLQSEFEKLS LPKETMDKLA SVLSNYKQKN
     QEKSLKVKYE KQKDKYKKLK SQLKKDKSLL K