TSUA_DICDI
ID TSUA_DICDI Reviewed; 2247 AA.
AC Q55FT4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable serine/threonine-protein kinase tsuA;
DE EC=2.7.11.1;
DE AltName: Full=Tsunami;
GN Name=tsuA; ORFNames=DDB_G0267962;
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 DISRUPTION PHENOTYPE.
RX PubMed=15473840; DOI=10.1146/annurev.cellbio.20.011303.132633;
RA Manahan C.L., Iglesias P.A., Long Y., Devreotes P.N.;
RT "Chemoattractant signaling in dictyostelium discoideum.";
RL Annu. Rev. Cell Dev. Biol. 20:223-253(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-34.
RX PubMed=18708585; DOI=10.1101/gad.1694508;
RA Tang L., Franca-Koh J., Xiong Y., Chen M.-Y., Long Y., Bickford R.M.,
RA Knecht D.A., Iglesias P.A., Devreotes P.N.;
RT "tsunami, the Dictyostelium homolog of the Fused kinase, is required for
RT polarization and chemotaxis.";
RL Genes Dev. 22:2278-2290(2008).
CC -!- FUNCTION: Plays a role in chemotaxis and seems to be involved in
CC polarization. {ECO:0000269|PubMed:18708585}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18708585}. Note=Localized to the microtubule
CC network.
CC -!- DISRUPTION PHENOTYPE: Null cells have small aggregation territories and
CC express early gene. {ECO:0000269|PubMed:15473840}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000003; EAL73434.1; -; Genomic_DNA.
DR RefSeq; XP_647449.1; XM_642357.1.
DR AlphaFoldDB; Q55FT4; -.
DR STRING; 44689.DDB0229382; -.
DR PaxDb; Q55FT4; -.
DR EnsemblProtists; EAL73434; EAL73434; DDB_G0267962.
DR GeneID; 8616256; -.
DR KEGG; ddi:DDB_G0267962; -.
DR dictyBase; DDB_G0267962; tsuA.
DR eggNOG; KOG0597; Eukaryota.
DR HOGENOM; CLU_230695_0_0_1; -.
DR InParanoid; Q55FT4; -.
DR OMA; IDWMIHY; -.
DR PRO; PR:Q55FT4; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:dictyBase.
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; ISS:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0043326; P:chemotaxis to folate; IMP:dictyBase.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:dictyBase.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:dictyBase.
DR GO; GO:0007228; P:positive regulation of hh target transcription factor activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IC:dictyBase.
DR GO; GO:0060176; P:regulation of aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0031272; P:regulation of pseudopodium assembly; IMP:dictyBase.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045193; Fused-like.
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 PANTHER; PTHR22983; PTHR22983; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Kinase; Microtubule;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..2247
FT /note="Probable serine/threonine-protein kinase tsuA"
FT /id="PRO_0000362034"
FT DOMAIN 5..257
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 271..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2106..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 323..350
FT /evidence="ECO:0000255"
FT COILED 437..532
FT /evidence="ECO:0000255"
FT COILED 818..889
FT /evidence="ECO:0000255"
FT COILED 963..990
FT /evidence="ECO:0000255"
FT COMPBIAS 536..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 34
FT /note="K->R: Not able to complement the aggregation defects
FT of the tsuA-cells."
FT /evidence="ECO:0000269|PubMed:18708585"
SQ SEQUENCE 2247 AA; 252890 MW; 2771228FE0CD4691 CRC64;
MDDDYKLIGQ IGEGSFGKVY KYRKKFTGQL VACKVISKKG KNEEDILSLR QEIDILKNLS
HPNIIQFISC FENKNEFTLV TEYADGDLSQ IISEEKTLSV DLIQSICYQL VIALNYLHYK
KVIHRDIKPQ NILITSGGQI KVCDFGFAKT ISSNSILLTS LKGTPLYLAP EIIQEQPYDY
KADLWSLGII LYQILVGSPP FSANSLADLV HMTLESNIEI PKELNKYPDL VSLFRQLLCK
NPDKRIGWPD LLYHPFVKSY NGAHVINNNN LNYNNNNNNN NNNNNNNNNG NRPITSAGGN
YLNDNSSSPS ISSPIQSLPL ISADSLINSL NNNINNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNGNI NTNGYYQPLQ SPTSQNFVNG IPIPILNGIS NPFSVYNNNN
NMNNNNNNKF NPTSPKHHQT LQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQIP
PPQSPKTPKV LSPKAVGISI QQQQQQQSQQ QQMQQQQQQQ QQQQQQQQQQ QIPPQSPKVP
QSPRVAPPPQ SPRVLSSPRI AHSPKNSPRQ TNPTSPSPSP RRNSLKSQQT PSLTNLNQAL
VNPSSSSSSL NSSIPTSSST NKQIPPLSSN LNQVNLSNNI NDNNNIINNN SNNNSNNINN
NINNNNNNNS NNINNNINNN INNINNNNNN NSNINNINNI NNNNNINSSN NNSSNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNI INSSNNNINN INNSNNNINN SNNNININNS
NNNINGNRPT SGGNNDLILN NMLMNNISLS SSIESIASNN NSILVQQQLQ QQQQQIQQQQ
QQIQLLQQQQ QIQIQQQQQI QQQQQLQIQL MQQQQQLNII QQQNSVVQNG MVVSVLNKKA
PPTPITRPQT PTSFRPQTPQ YRTCTPRTPQ PINTPASRNN FQSNVLPSWP NLYYQQLNVN
DPHQLQQLQQ QQQQLQLQQQ QQQQQQQQLP LSSSQQQIHY YNQMNHNGNS QNERLDEISE
ASESLESLEF WRFHESISFK SEENASKLRS DKQFLHKIIS HLSASSFSMI ERLPIGLILR
TFSNIMKYGT LTIQSSNNTT LQSTRTPPQT PPLYPSFNNN GNNSNNNNNS NNSGGGNNSS
EIYKFSNFQI LVNVLSNILA TTLHITNGNG NSGIIGSTSS NGMVLLNNPY TNLLDCLNTI
TMFLETFQPS LSVLFNVNGL NERHGSSSTP NQSSPCPTSP NGGSSNISIN NINGGKRIHS
QPQQSNQTQQ INTQLMFLSI LNHLTKNIFI YNQGIQIAVI KIISRLFSRL GENPYLFGEI
YRKIIEQTDI LQNICSYFLL LLNQSYQSSS SSTISNTSSL SSSSTSPPTS SSSSTSSSTT
TPLSSSTTTA ATATATTSAA TTSTATNSSQ QQQQQPIPSS IEVEVEIVLQ CFHNILYTSP
QHAFEFPLEP KRNYQTNTSI QTYLMNYYQA CVIIGDGLSS EIIINLLLCS ISSYPHLRKI
ILQLSLHCLR GSKLFAESIS KEEKSLIYPI NQNNNNNNNN NNNNQNKNNN NSNSNPSTPN
LQFQNSYNSP YNTINNNKPR SFFDYLSIKN INQSNNNNNN NNNNNNNNNN NNNNNLNTES
TIEFNQEQKS LVLLILSAIL IHSKESIDWM IHYDLVDLSI RYFQNTDIRI SSSASYFLSG
FLTVSINYEK EFDNFNNNLN NSNNNLIRPT SPNSNNLIIN GTNSLIDNQL TIIIDSIIQV
IPIKNIRKLF SAKRVEGNTM RDLEGGCFGK PNIGMLDGVV CILLRMLKRG GQEFLETMLE
SGIWEALCHQ ISSTTSEIEL SPHGIIHSLR VIYEVLSSDT DHIPYLVKNN LLTSLCNLLD
SGHLERIKEW PSLQMGSVSG ISALANQIFF ILYLPLSSNA KDRIGDPMIE LIRHIMLAQE
LVRNIIMLLP QIPSDSIDLP LGLLSNIILE DSKFANQFIE FGGLEPNTAQ LILNPDRISP
STLVDSLIIF SQLARISQDN YKAMHRSDLY GLLKKLLAHP EATVRAKTCN LIGNMFKYNG
YFYQHFQKSG ILPILISRCI DVDLNTRKFA CFALGNAAFH SSDLYDELDD SIPILKKLLN
NEYPFSGQQQ QQQSQQQQQS QQQQQNDLLL QIEEDEKTRS NVIGALGNLV RNSSQLCQKM
IDSGILDALT SYLDEYKSHT NILKSVLFSL GNFSVYEQCR YILIEDYDLD STLDDLFEYL
KQNQQQIDPT IIKYINRIKK ILRSPST
