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Database: UniProt
Entry: P18160
LinkDB: P18160
Original site: P18160 
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   29-OCT-2014, entry version 119.
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 (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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,
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=JH10;
RX   PubMed=8898241;
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;
RA   Tan J.L., Spudich J.A.;
RT   "Developmentally regulated protein-tyrosine kinase genes in
RT   Dictyostelium discoideum.";
RL   Mol. Cell. Biol. 10:3578-3583(1990).
CC   -!- FUNCTION: Essential for spore differentiation.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC       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
CC       threonine residues.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Tyr
CC       protein kinase family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 3 B30.2/SPRY domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00548}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00184}.
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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   ProteinModelPortal; P18160; -.
DR   STRING; 44689.DDBDRAFT_0215670; -.
DR   PRIDE; P18160; -.
DR   EnsemblProtists; DDB0252636; DDB0252636; DDB_G0283385.
DR   GeneID; 8624065; -.
DR   KEGG; ddi:DDB_G0283385; -.
DR   dictyBase; DDB_G0283385; splA.
DR   eggNOG; COG0515; -.
DR   InParanoid; P18160; -.
DR   OMA; RWIVEDE; -.
DR   BRENDA; 2.7.12.1; 1939.
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: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:0018108; P:peptidyl-tyrosine phosphorylation; IDA:GOC.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR013320; ConA-like_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF00622; SPRY; 3.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00449; SPRY; 3.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF49899; SSF49899; 3.
DR   SUPFAM; SSF56112; SSF56112; 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; Complete proteome; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN         1   2410       Dual specificity protein kinase splA.
FT                                /FTId=PRO_0000088121.
FT   DOMAIN      822   1004       B30.2/SPRY 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   DOMAIN     1020   1209       B30.2/SPRY 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   DOMAIN     1481   1703       B30.2/SPRY 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   DOMAIN     1734   1798       SAM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00184}.
FT   DOMAIN     2115   2387       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND    2121   2129       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   COMPBIAS     23     52       Poly-Asn.
FT   COMPBIAS    162    320       Ser-rich.
FT   COMPBIAS    213    219       Poly-Asn.
FT   COMPBIAS    235    245       Poly-Asn.
FT   COMPBIAS    321    352       Poly-Gln.
FT   COMPBIAS    447    514       Poly-Gln.
FT   COMPBIAS    515    648       Pro-rich.
FT   COMPBIAS    601    610       Poly-Asn.
FT   COMPBIAS    631    759       Ser-rich.
FT   COMPBIAS    706    720       Poly-Gln.
FT   COMPBIAS    777    813       Poly-Asn.
FT   COMPBIAS   1229   1246       Poly-Asn.
FT   COMPBIAS   1275   1306       Poly-Asn.
FT   COMPBIAS   1309   1317       Poly-Asn.
FT   COMPBIAS   1320   1358       Poly-Asn.
FT   COMPBIAS   1422   1426       Poly-Asn.
FT   COMPBIAS   1852   1855       Poly-Ser.
FT   COMPBIAS   2021   2036       Poly-Asn.
FT   COMPBIAS   2041   2046       Poly-Gln.
FT   COMPBIAS   2050   2059       Poly-Gln.
FT   COMPBIAS   2088   2103       Pro-rich.
FT   ACT_SITE   2243   2243       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10028}.
FT   BINDING    2142   2142       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   CONFLICT   2074   2074       D -> R (in Ref. 3; AAA33202).
FT                                {ECO:0000305}.
FT   CONFLICT   2261   2261       V -> L (in Ref. 3; AAA33202).
FT                                {ECO:0000305}.
FT   CONFLICT   2282   2282       M -> K (in Ref. 2; AAB41125 and 3;
FT                                AAA33202). {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
//
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