ID   SPLA_DICDI              Reviewed;        2410 AA.
AC   P18160; Q54R51;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 3.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Dual specificity protein kinase splA;
DE            EC=2.7.10.2;
DE   AltName: Full=Non-receptor tyrosine kinase spore lysis A;
DE   AltName: Full=Tyrosine-protein kinase 1;
GN   Name=splA; Synonyms=DpyK1, pyK1, pykA; ORFNames=DDB_G0283385;
OS   Dictyostelium discoideum (Social amoeba).
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 [GENOMIC DNA] OF 827-2410, AUTOPHOSPHORYLATION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=JH10;
RX   PubMed=8898241; DOI=10.1242/dev.122.10.3295;
RA   Nuckolls G.H., Osherov N., Loomis W.F., Spudich J.A.;
RT   "The Dictyostelium dual-specificity kinase splA is essential for spore
RT   differentiation.";
RL   Development 122:3295-3305(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2074-2410.
RX   PubMed=1972546; DOI=10.1128/mcb.10.7.3578-3583.1990;
RA   Tan J.L., Spudich J.A.;
RT   "Developmentally regulated protein-tyrosine kinase genes in Dictyostelium
RT   discoideum.";
RL   Mol. Cell. Biol. 10:3578-3583(1990).
CC   -!- FUNCTION: Essential for spore differentiation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- DEVELOPMENTAL STAGE: Expressed in vegetative cells and throughout
CC       development with a peak during the mound stage of morphogenesis.
CC       {ECO:0000269|PubMed:8898241}.
CC   -!- PTM: Tyrosine kinase domain is capable of autophosphorylation, in
CC       vitro; however it is also autophosphorylated on serine and threonine
CC       residues.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Tyr protein
CC       kinase family. {ECO:0000305}.
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DR   EMBL; AAFI02000055; EAL65677.1; -; Genomic_DNA.
DR   EMBL; U32174; AAB41125.1; -; Genomic_DNA.
DR   EMBL; M33785; AAA33202.1; -; mRNA.
DR   PIR; T18276; T18276.
DR   RefSeq; XP_639040.1; XM_633948.1.
DR   AlphaFoldDB; P18160; -.
DR   SMR; P18160; -.
DR   STRING; 44689.P18160; -.
DR   PaxDb; 44689-DDB0252636; -.
DR   EnsemblProtists; EAL65677; EAL65677; DDB_G0283385.
DR   GeneID; 8624065; -.
DR   KEGG; ddi:DDB_G0283385; -.
DR   dictyBase; DDB_G0283385; splA.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_229194_0_0_1; -.
DR   InParanoid; P18160; -.
DR   OMA; EIGEPYG; -.
DR   BRENDA; 2.7.12.1; 1939.
DR   Reactome; R-DDI-5673000; RAF activation.
DR   Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR   Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR   PRO; PR:P18160; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:dictyBase.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:dictyBase.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IMP:dictyBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR   CDD; cd12885; SPRY_RanBP_like; 3.
DR   CDD; cd13999; STKc_MAP3K-like; 1.
DR   Gene3D; 2.60.120.920; -; 3.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR044736; Vid30/RanBPM/SPLA_SPRY.
DR   PANTHER; PTHR23257:SF975; DUAL SPECIFICITY PROTEIN KINASE SPLA-RELATED; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF00622; SPRY; 3.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00449; SPRY; 3.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50188; B302_SPRY; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..2410
FT                   /note="Dual specificity protein kinase splA"
FT                   /id="PRO_0000088121"
FT   DOMAIN          822..1004
FT                   /note="B30.2/SPRY 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   DOMAIN          1020..1209
FT                   /note="B30.2/SPRY 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   DOMAIN          1481..1703
FT                   /note="B30.2/SPRY 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   DOMAIN          1734..1798
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          2115..2387
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          29..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1228..1428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1493..1512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1862..2105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..596
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..644
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..749
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1228..1406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1414..1428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1863..1881
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1916..1930
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1939..1977
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1984..2005
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2015..2086
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2087..2104
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2243
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         2121..2129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         2142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        2074
FT                   /note="D -> R (in Ref. 3; AAA33202)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2261
FT                   /note="V -> L (in Ref. 3; AAA33202)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2282
FT                   /note="M -> K (in Ref. 2; AAB41125 and 3; AAA33202)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2410 AA;  264919 MW;  768EC59E9E05C229 CRC64;
     MNSKNDLFIG FFFFFYNYYY YYNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNIYIIVIIG
     LDPQQNHPSL KIPPPPSPTS PYVRRHARQH SRSNSSNSPG ELTGGVEIIQ QQNSINTQTS
     PPTSTSPNTV PPPPPTNTTT SSTTITRNSN NINNSNGGII NSSSGSNINN SSSSGVINTN
     INNSGGNISP TSNSLPSSNN NILYTSSGSN SGNNNNNNNT INISSGSSGI NNSSNSNINN
     NNNNNSSSSS GIHASGSLTA IPTNTNSNSS IFHSSNSVNR INKSNYSADS LVLPPNRISQ
     VPQSQTQPQL QISPSTSFSS QQQQQQQLQQ QLQLQQQLQQ QIQQQQQIQQ QQNLHFTYSK
     TFTSGQPNTL VNLSSPPPQS KHLHVSSDHS FFNEVLTPTP VIHNSTNQNN QLLFGDSDPL
     SFLEYNNFIN RYQPALKNNQ PVSSYRQQQQ IQHQIQLQQI QQQQQQQQQI QQQQLQQQQQ
     IQQQQIQQQQ QQIQQQQQQQ QQQQQQQQQL QQIQPPPTIQ PPPQQTTPTL RGNRSSGNLS
     GLNSFSLKQS TDSLTPPPNS QQSTVSSNST PIAATPISPL TAPTSPPPPP PPPTNFNSKF
     NNNNNNNINN SSNNNTTVPP SPPPIIVLPK SPSSRSPRPA SAPVPSAPFL VNNRVINTSS
     SSNISTNNTD LNLSSSSSSS PPLNISTASP SKSEDSPPTV SPSYKQQQQQ QQQQQQQQQQ
     LNNSSNSSYS PKPRSPSVSS PPPSSISPNS SPIGSPNISF HHHQQHQIPP PPPVLSNTNN
     NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NTNHTNKKEG DSSWFNMSFK FFKKKLVPSN
     EYRWDLRKSN SLTLNIEDKS RCSYRLPTSG SKGIAKSTQP FSSSFTYFEL FITNGNGDKI
     CFGLTTNDHP IEVYPGNYQG SYGYSGDGKC YFGTNEGRVY GPSFSSGDVV GCGYDSSSKT
     LYFTKNGVYL GVAAQKVNLI GLYPTVGLQN PGESVVINFF GPFSYRGAPE KPSKQSTIKD
     SGGSSIIPSE DLIPKEEFEV CRWSEKKNYH GKHVVVRNRT AFLPLDSPKD TIGGVRATQP
     FGEGFCYFEV IIDQLDKGQL SIGLANLEYP TFYHVGWMPR SYGYHNDDGR KFRWREEPGV
     NEGESYGSSY KKGDIIGCGL SFTSREIFFT KNGMYLGTAF SNVYGVFYPS VAFNEPGISI
     TGVFGPPFKF SQVTLMLKNV NSTSILVPNG NNNNNSNNNN NNNNNNIIGN GKITTTTTTS
     TSPSSINNNE DISSNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNSNSSNT NNNNINNTTN
     NNNSNSNNNN NNNNSNSNSN SNNNNINNNN NNNNNNNNIY LTKKPSIGST DESSTGSLGG
     NNSSGNNNSS SGSIGNNSSI IKQRSPPHSI NGPLMLPPSS TNNNNNIYSS YNSTTAGSST
     TILPTLNHPI FGNTTSNNNS SSTLSVGGNN NLLGRHCQSL PITASTNHTL SSSLGVSFSS
     PSSSPKTSPR KIVNSSEDLG FVQTFQDQDG QPPSAWRRCG KSIKTKDDIT LTIIKKKTSV
     AMADRPFSSN SSSTICYFEV YLEGHDKKGS ITVGLSHSTY PFIKHIGREP KSYGFSSEGE
     KYGGSEIGEP YGPFFFFDGD SIASSCVIGC GINTSTRDIF FTKNGHYLGV AFSRVTSDPL
     YPSISFRGVV GGLCVATFPG GHFRFNIEDL PGISPSVWTE ALGPDRQGSG FKNWAPNDVA
     IWLESFNYGQ YRKNFRDNNI SGRHLEGITH AMLKNDLGIE PYGHREDIIN RLNRMIQIWN
     DKSPDSYPKI AIDSSDKIRW PASGGSSGGI NISGGVVIGS SSGSDDGITE ISSSSKNIRP
     YKSYTQKEIE DRNRRSTISG GEKKNKYYID NQMDPHQIGS MDSDGLLPDF GQGPPDEKNS
     SKTLSNEQIR YLQQRKDEPP IAISSTGNGG SVSSTGGSSG FLTFPSSNSL THPPQRDKPT
     QEFTHLPPIT SNYKGITNTG QPHKSFDQPL ELFPRHSAFS NNGNNGNNNN NNNNNNIKAN
     QQQQQQSSYQ QSQTQQQQQH ITSTSTSTTN KWIDPFGGWE TQSSLSHPPS RPPPPPPPPP
     QLPVRSEYEI DFNELEFGQT IGKGFFGEVK RGYWRETDVA IKIIYRDQFK TKSSLVMFQN
     EVGILSKLRH PNVVQFLGAC TAGGEDHHCI VTEWMGGGSL RQFLTDHFNL LEQNPHIRLK
     LALDIAKGMN YLHGWTPPIL HRDLSSRNIL LDHNIDPKNP VVSSRQDIKC KISDFGLSRL
     KMEQASQMTQ SVGCIPYMAP EVFKGDSNSE KSDVYSYGMV LFELLTSDEP QQDMKPMKMA
     HLAAYESYRP PIPLTTSSKW KEILTQCWDS NPDSRPTFKQ IIVHLKEMED QGVSSFASVP
     VQTIDTGVYA
//