Y7071_DICDI
ID Y7071_DICDI Reviewed; 2454 AA.
AC Q550K8; Q86B02;
DT 10-FEB-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 DDB_G0277071;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0277071;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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).
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 -!- DOMAIN: The tyrosine-protein phosphatase domain is predicted to be
CC catalytically inactive.
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; AAFI02000019; EAL69037.2; -; Genomic_DNA.
DR RefSeq; XP_642924.2; XM_637832.2.
DR AlphaFoldDB; Q550K8; -.
DR SMR; Q550K8; -.
DR STRING; 44689.DDB0231326; -.
DR PaxDb; Q550K8; -.
DR EnsemblProtists; EAL69037; EAL69037; DDB_G0277071.
DR GeneID; 8620793; -.
DR KEGG; ddi:DDB_G0277071; -.
DR dictyBase; DDB_G0277071; dupA.
DR eggNOG; KOG0578; Eukaryota.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_228878_0_0_1; -.
DR InParanoid; Q550K8; -.
DR OMA; FTEILIM; -.
DR PRO; PR:Q550K8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IDA:dictyBase.
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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:dictyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IEP:dictyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:dictyBase.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Hydrolase; Kinase; Nucleotide-binding;
KW Protein phosphatase; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..2454
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0277071"
FT /id="PRO_0000362061"
FT DOMAIN 1730..2034
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 2130..2271
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 31..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2379..2404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 259..307
FT /evidence="ECO:0000255"
FT COMPBIAS 342..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1858
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1736..1744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1760
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 2454 AA; 274128 MW; 6038F1266B93E574 CRC64;
MERSRKHRAL SITPHKQKQY MLDIEDNNVS TSSLTTTTTT TTTTTTTTST THNHESNERS
NQLLESLIVL KEKIKLLDST EKNHCITQGG ITILIQCLCY CGKNSIKNDV IIEICQQLID
NSHDASRLFC KQIISHLYND IECIGISDVL TKIISFYPLR SIFIEDLCIP KLLEIYYKCS
LALSNIKFKV DPSIHINSTP VVQQSQQQLS NSSSSIPTST SSPLQSSSSS SSSSATTAST
ASTTSSTTSN SSPTKTLGKQ QQKQNSQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QKLNIHEFQS IQIPCWDDGV PPPPPQGFTF ENLLTSVPIP RPPLFQQHQQ STTSNNNNNT
IIQQSNTKSG DVTTPTSILS PISTITNNNN NVNSTNITPA PTPNLPSSVT SPISTSTNPP
SNNPKPTSIG QIQSLHYHNP SLYQTPPLFN RNRGNNNNNN NDSNTSSPMD SPLISSTVAS
LNSNNSTAAA TTTTTTTIST PTISTPSITS RVPPLPLSNS INNNNVNQIH PNNTPNSATS
GGSISKVPML SMGGIGGGGG GGSGGGGISK SIVPRLNLPV RVENSTRNTR SSRRRDDASN
STRSHQGELK IETSASKELS DLAIKLGETY MTADLTALIS YKQAIESHKQ SKRSIPSRRY
DIPPISSKNT AALSMVNQQQ SSFSELNLYK VRCNILKTLI SSTSNNLMLL QYGNNPINIL
YSESILLHKG IIPSDKDHLT LFYKLASHWS DYVEYIHRNR WRDVTKGMGL ERKASFRKKL
DLLLWRINSS ISNMLETFTF DDMEYQLCIL SEYMENCPSR ILSSQVVDVC IESLLKVKHS
IFRGPITSDR VKDIHIIHYL LTVFDEIIKQ NKSSPINDLF ISIFLERDET FQFIKQYTIQ
ILTNESIERE FSKCYPNDQN KIRLTEFRCR SIKHFSICVK MLKFKFKKQQ ENKLYNQHNC
NNNNINNINN NNNNNNNNNN NNNNNNNNNN NNNNSNNSGS SGNLANNLNT PTSSQTNSSS
TTTAGTNPTS TSTSSTTTGT NSTTTTTNEN EIPDLLKKME FLLLPQGNGV ILPFLQSNNF
FTHFNVKKQM LKFLNHVFLF KKNPFTKKKL YIDSYISYIY ISFIKLYNNY IFDQATLTLC
RLFLNILISF SVNKNDKISM KFYQLRTMDF LVREVNLEYE IKQNKDQFLK PLSSIPFFAN
SSDDTSSSSS TSSSLSLSTT TTTTTTTTTK TTTTTNTNST TPIKTGGPPT IPKLATPGTK
LNLGLNLSGI TKTDNSSNNN NTSSPPVIPK LSLQPKIDSG SSTSSPSTLI STPSTLASTP
PTTGVSSNPL IKPKFSLNLS SISKGSPAST SSSNLTTTTI SSSSSSSNST TTSLTTVPAS
TIIDSTSSTS TSTTTTTIGS VSTEPPLPAP PKPKFSLNLS SVSKTGQAST STPNLLNLKN
IPTTTNNSNS TTTTTTTTPT GKPQFSLNLS SLSKSSSSTE TVPPSQPNQP ISKPIIKSLN
LGSISKGGST TTTTTTTTPP PINNSNNTIA SNNNEINLPK LSNSPINISS SKPPILIPKL
VLPAIKIRSE EDTKQAGTGV LSSIEQKIDP QDPKFQLVLD NPSQSLTPSD RDSEQMIEPT
ENEIFNENQR YQLERNNRKL YHDRDLHISL LQLIFSLLLN SNQTLEHLYS DQFPIVAKKL
NVPFILHLHI NHQDNEKIIP ELTKRTHEMG PNHFRILKLL FSRLYHSNLF KDLKRVAKGA
YGTVYKGTLG NDEGLEIAVK LMPVPKTIHD RCVLYDIFTE ILIMDTFRSD SRGCHMFDYG
VDGENYWIVM KSYKCSLKEW RLKQTLPFLE LLPLLLNIFT NVLQSVQFLG DHKINHFDIK
CDNFLVHPLK KGTIEEDFWN QPTNDPNFAV CLADWGEAKV YTQDVEGYTT RNRGTEFIKS
PEMLTIAYAS QKTRENFDRR KKVGSNTASD VWSLGCLFYE LLTGDFLFYD DDWVKFFIRV
TQPGQELITP ERKSKVANIP AILDYLDYVF IRDPFYRPTL RDLLTKFIAI KPTILSQWEQ
LKKKLDGHMS NQMNTVEKPK QYYNGGDGTS YKAKSIKFTG HYTPGRFLPH SYNANNPIKV
GSLMVDGDKS TLEMPYEAAE FPEHRFYMDR PSKVASFMYI SSFNPSMNKN MLINEYQITH
IINCTGSPNA FPDHFEYLHL QLHDQPHQDI TQSLSLAFDF IRDAIVHHGK VLICSDKGVS
RSSALAIGYF MDSRSISYFE AFILVRDCRY IISPNTGFVE QLCRWGKQRR NFKGLSEWGG
GETNSTLFQC LCGACSFTLL TPFDNRKYSN PKKCCCTPGS DLDCPNHIIG CSNFLGDMKK
LHGYNNLNYL AWGYTNIINV VGDYERSSIE IVYNNNSNNI NNNNNNNSNN SKSKQQQQQQ
QNQNIQQNND WNLFKCKFCH FLTCAISKST SGVNENLIAV VTNQRTNYFP STLK
