ID D8LIK7_ECTSI Unreviewed; 2319 AA.
AC D8LIK7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Ca2+/calmodulin-dependent protein kinase kinase beta and related serine/threonine protein kinases {ECO:0000313|EMBL:CBN80046.1};
GN Name=CAMKK {ECO:0000313|EMBL:CBN80046.1};
GN ORFNames=Esi_0022_0166 {ECO:0000313|EMBL:CBN80046.1};
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:CBN80046.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBN80046.1, 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).
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DR EMBL; FN648398; CBN80046.1; -; Genomic_DNA.
DR STRING; 2880.D8LIK7; -.
DR EnsemblProtists; CBN80046; CBN80046; Esi_0022_0166.
DR eggNOG; KOG0585; Eukaryota.
DR eggNOG; KOG0698; Eukaryota.
DR InParanoid; D8LIK7; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000002630; Unplaced LGUn.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004690; F:cyclic nucleotide-dependent protein kinase activity; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00143; PP2Cc; 1.
DR CDD; cd14008; STKc_LKB1_CaMKK; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24346:SF77; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE KINASE 1; 1.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00481; PP2C; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; cGMP {ECO:0000256|ARBA:ARBA00022535};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW Kinase {ECO:0000313|EMBL:CBN80046.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002630};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:CBN80046.1};
KW Transferase {ECO:0000313|EMBL:CBN80046.1}.
FT DOMAIN 320..428
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 569..923
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1872..2258
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1839..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1949..2010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2044..2092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2077..2091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2319 AA; 244269 MW; 7D29058BBF74FEAA CRC64;
MNSGYHGVGS GGGGSGGEHG SPGDSPRARA AVEHGQQSLD SPGGNSLITF GSSPSTTDDE
VTDFLLESSD GVSFHPENDG GGGGSGGGGG GRAENTGNRS SSPGGSKIGA LSKREIEDFF
RDTSSSSSSS SSSSFSSPCS SSSSSVPREL DDDGRSCSVG EAIPGTATAG GLDSGDGGPV
VGKGEVTPGK KRHHRHDGDK GGGGSRRRRH HHHHHHQRER LPPLPPHMRS LPKKDQRYMQ
ANLALRKGLG AVVGLNFDTL TAELQLKMMK PMTITRYTKS VRVATTVAAS TVVDVASIDI
DDMSVWEPFR MFVLMKEIPL LANLPMLSLH ALQQTLRHQT FSAGDYIVRQ GEDGDVFYMI
VKGTVDVLET SMDPETDMER TKLLVQMFEG HYFGELALIY GEPRNASVRA TEEVRCVCIT
KEDFRSCMNE KRFQEVLEEV AYQRAFYREQ RAQQLEEEQE KQQRGRGKQP RRLIRSRSSV
SPSSRSPGGE DGGGRRGGRP ADSGTGRPGG RGRWTAAEVR GASPTRSLTP PCGQSASSSS
HSLRRSSFRE TVKVVKRKLN NGTIIINKYR IICELGKGSY GSVHLCRDGE TGMEYAMKVM
DKRKRGGIRS RQGQGGHQHL AETLRREVAV MKKLRHPNIV TLWEVIDDPK AQQLYMIQEY
VADGPLLPEG VVVSPMDTEE ARDKFLGCIR GLHHLHQHGV VHGDIKPQNL LVAKDGTVKI
ADFGAAVMLQ SQASAGNNNS SGETEDEEVS KMKGKLISTP AFTPPELFGA STTVSPACDV
WAMGVTLYQM VYGTLPFWPP SGNHSELEIM VTHRELSFPS PSSSSPSSVA ALEGAGGIGI
RVRGGAAGAG VGYGGAGGSG GGLVAAAAAA VADEPDLKNG TRTLSSGVLT NLEAYDPMVG
YLRLEKDPEH PKNLKAAISH PWVTVEGSIP PEGLEALKEP GGKDGELQVT DGELLDAWTI
FPATPTPRGR DVSYSPRSPS PSWRGSRWAH RAPPRRTGEF FPSQERYVDG GWRCGSPGSQ
APSVPSPAAA TPAGTLNHLV TPTATGNITQ FGWPRGVRRK SYSGGGGGGC SYGDGNGSKP
NATAAGGTPM RASAGGGNFD EVESGNNGFN ISRGGGGSSG GGGGGGRRSR WGAPGPFLGG
WTRTASPAPQ RQQQRHDSLP SNLHIDVDHI NHGGGSRSNH GSRRPSGDRT EGGECPARAG
GAEGGTVSSC DLQPAPGIAT SDGGFFCGPG GVMFPLSKQL STGSTTGGSP SPRPSSYFDH
STTTLSSGLG SAAAADAHFA AWDPHGDGDA GRIFHQNRTR SPRQQRQQLQ QQLRNLHQKG
HNRRRPGLRQ KEVRSFVSRL GERHHRQLGR CMTYPLVHGE EVEIQEGSLE ALSVRSPEVP
SSKLARDSQA ETNVKAPLCT TTAASSTFSL LRPARTSTLP FSPAPREPHA HHRGRRRSSK
TTPSPLSTLG ASSSWSRVDA SSSDHTTVTQ EDGGIIVDSP KITPPSPAAL AASGTASREK
GEEGGAGGGG GSAVCERCLD ARDAPPLPPP SPSCGFRGSF LSEEGGDGDE EGATVAVGMM
LPEKAWRVKK EEGEGVATGK IEEEEDEDGD EVVPSRADHD HFVQSFLMSR FVGQRGGIRR
ISDAGLRHAG LDAASWLRRR PRRSSTGGIG GSFAVRGSLC VQDSSESELN AYDDEEQEFC
EDWQGAVSVD PDAIELTLPP RTASSITEGL SFVGFEPLEL EDVPQEAVQA RTWGDQANLT
VGVRYGHSAE IGSRRVMEDR TVAVADIFKA DATPSFRSRS EGYFPSSTIL SRNSSSPGSG
GQDDAARRRF FPAGAVAQAT PGAVATVAVG DPAAASTGVV VPADTDTGGL AATKEEKETT
EGRGGASGQE QKQRSPPMSP SPSTPLCAAF FGVYDGHDGD VVAEALQKGL HKLIAKQKCF
TDSISAAIEH GCYEMDTACL DAQFRVLGRD RSRSPSPSPS PSPSRSRSPS RSTGGETLSA
GRERGRGDDG GGGGGGGGGS HDAVGSGAPA AASARAPAAA AAAASSPRGG GGGGCGACGS
MSENQGGEGG DEVEDCGGGV GKPLAPRRRP REASSASDVR SRLSGTSPGM TGGATAVVAV
ATKVGKQTVI YVGNVGDCRA VLCRRGVAID LTSDHRPSRD DERARVKEAG GYISRDRLNG
ILGVTRAFGD IAFKEYPPPP PDGDMWRGQQ LISKPETRSF LILAWDGVWD LVSSQQVVSY
VHRRLLKHRD VQRASRELCK TLGKMSGSDN CSCVIVCLNQ VSVTPTAYSP GPVCRRRHHH
RQSASLSDAH NDLAASERGF SWSAAGSSSV SPAKRPSFV
//
