ID D8LLR2_ECTSI Unreviewed; 2004 AA.
AC D8LLR2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=PK {ECO:0000313|EMBL:CBN74693.1};
GN ORFNames=Esi_0037_0120 {ECO:0000313|EMBL:CBN74693.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN74693.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBN74693.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; FN648564; CBN74693.1; -; Genomic_DNA.
DR STRING; 2880.D8LLR2; -.
DR EnsemblProtists; CBN74693; CBN74693; Esi_0037_0120.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG1989; Eukaryota.
DR InParanoid; D8LLR2; -.
DR OrthoDB; 5476031at2759; -.
DR Proteomes; UP000002630; Unplaced LGUn.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22967:SF57; AUXILIN, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR22967; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00220; S_TKc; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 14..299
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 533..702
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 1484..1545
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1735..2001
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 307..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2004 AA; 207054 MW; 1FCD91F64844C14E CRC64;
MGNMPVVDVG TRKVRVKRLL SEGGYAHVYK AVDEVNKKDF ALKMVRIPRS RSGQLANEEV
AEMAVVEQSV VRSLPNNHPN IVKFHDAGIS KADNEIRYFI LSEYCPSNVL KKMSGAADQG
SLLPETEVLL IFRDTLMAVL YLHSRDPPIA HRDLKVDNLL VGRDGLIKLC DFGSCSTQHK
AYLSPKELQL ANEDIRRNTT AAYRSPEQVD LFQGHVVSEK VDIWALGVIL FKLAFFQTPF
EDNKGNVDAG AILKGLGDKK IPQEKRYSAG LVSLIRCCLV VDPARRPTIG QVLKLCEELK
VKGSLPDWPG LNSLPRTPPL SSSSPFSPRP WDALGGDASG SSVNSIPGEG AVGGGGVGAS
GGGGGVTGGG GSGGSGGGGG AISGHSRRVS RDVVGADHRE GLSASLRGAG ARAVGEGGGD
AGVGGAGGRS ANSRSPDIGA SSDIPRNPDL MRNGLPRPNS RRSGPMAGLM APGPSSIDGS
GYGQTGGGGG ESGGGVLSSP RRSQRVTRSH TGSGDAKWMA RVGDGMRSKW YKLLGGETQR
KRLWVLKTTS QNSTGPKPKY VGKIVAALWE KELTMDSVFT LLLDRPLSES PVVAMKALIT
LMKVLQQGPP HVLSECTTYA PTVEDIGQMW GPDHVDTSDS AIAEGVDAAA TAGGDSSGGL
GGSGSGVGGG SAVDPALSLL ILRFATMIVQ KIRFHQHHPE YGDYWSPDTG NDTDTTPTTY
DNPVSERLPQ QPRDEARTLQ AFMLLTKGAK DAGPSTRSAL LPLMAESYLT YFATTRVLLT
VSDKYCTGQL RLKARPDQLV SLSQKYETDL KIMRELYKRA DEVEEVAIMK RTPRLPVVSP
LSEGGAKKFR EMSRKTSRQS TFGRASSKME ALKTLHDEER RFVDSDDDSS SDGAPGGAGG
NGGWAGGRGA KNLRLEVKGD GDGDDGSEWG NYYSWQGPDS RAPSSGQAKD GTFGVRRQSN
QSEGEGGRNL GPWATDSSGA PPGGGGGGGG QASFPSHPSP LAGAGEERTS ETRWRKQANG
ASATDAAGSS SRRTGRSLSA RDLRAAAALD GGGGGGGGGH TASPSRMPPE KGKGAGGSRR
KDEVSGRRKS SNEGNGDNGH QAAAAAASAA AAAPMLSDFD TLTLGGSERP VTPVGEESQT
TYQLPAAAAA AAAGGGEGGS KKQLALRRER THPPPLPPRR DNEGSPTHSG VAERGGSQQQ
DPSGAAAAVS GVAPPPLPPR ITYGWAGAAG VVATSQQVDP PAGAAAASGG GGGGPGRSNA
SSPPPPDPPS LAGDRGASSA SAAVTAGASV GGGGVVRANS GPVRRKERGD GPSSPRKRAT
ERGGGDAPSS LLVQQQQPSA TGPSSPRLIK GGFGPANPLS WTAKDNASGT GGNTSFSHTN
TEKKRPASGV GAGAAGAGVE PSASTAATGS SALSKTSPSL VVPAATGTGA RGKSAAAAAA
AAATGGGSAV AAGTSAQQAV PAAGASAATA AGAGAGAGGG AANAAGRVAV AKYEYVAQGP
EQLSFRVGDI VQLHTEKINA KGWGLGQANG KVGWFPGDFV EMRPTPSERK SRSSSSKTSG
ASRNRRQHPH PTPAAATGGG GGGGGAASSA APQGAGGASK GPPPPPYPGR NQRASRGQSG
GTGAGGGGGG ERRRSSATSQ TATAAAAGAG AGAGANKINP ELYETSNAWG TAREKEREEG
IGGREPEQLP EHVFAIQMAK NQPWRDRLTP GGKIAHDDLL AFFKASRMVL DFDEIELKSV
IGSGAFATVF RGIYRYRIGR PGEAGGDKKI EVAVKKLVGG GGGPMEKTLK DFKTECVLLS
RLKHRNIIAL VGATTHPVTC VMQYCSRGNL MVLLDDRSVE LTFKLKKQMM LDVATGMQYL
HSQNPVIIHR DLKSLNVLID ENWVTKVTDF GLSRFKATSV SEKMTGQAGT YHWMAPEVIN
SQHYTEKADV FSYGIILWEI FTRAIPYGGM QPVQVVAAVL GRRERPRIPS QCPQALSQLM
QACWSHDPDQ RPCFDDVVPW LESL
//
