ID I3KK00_ORENI Unreviewed; 1489 AA.
AC I3KK00;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 65.
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=MAP4K4 {ECO:0000313|Ensembl:ENSONIP00000021445.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000021445.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000021445.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR RefSeq; XP_005475451.1; XM_005475394.3.
DR STRING; 8128.ENSONIP00000021445; -.
DR Ensembl; ENSONIT00000021464.2; ENSONIP00000021445.2; ENSONIG00000017004.2.
DR GeneID; 100703199; -.
DR KEGG; onl:100703199; -.
DR eggNOG; KOG0587; Eukaryota.
DR GeneTree; ENSGT00940000155063; -.
DR HOGENOM; CLU_001831_2_0_1; -.
DR InParanoid; I3KK00; -.
DR OMA; ACEDSVE; -.
DR OrthoDB; 2904475at2759; -.
DR TreeFam; TF105138; -.
DR Proteomes; UP000005207; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
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; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 25..289
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1176..1463
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 302..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..750
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..926
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1032
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1489 AA; 168124 MW; 06DEA68804274762 CRC64;
MANDSPAKSL VDIDLASLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ LWLVMEFCGA GSITDLVKNT
KGNSLKEDWI AYISREILRG LAHLHAHHVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR
ALFLIPRNPP PRLKSKKWSK KFFSFIESCL VKNYTQRPPT EQLLKHPFIR DQPNERQVRI
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EESSEQEGEP SSIVNVPGES TLRRDFIRLQ
QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE QQKEQRRRLE EQQRREREMR
RQQEREQRRR EQEEKRRIEE MERRRKEEEE RRRAEEEKRR ADREQEYIRR QLEEEQRHLE
ILQQQLLHEQ AMLLEYKWRE LEEQRQAQKL QRQLQQEQAY LLSLQQNQNL DSSKTAQQQT
PKPPQNPEPD RVKPLQAPEQ ETTKQPQNTD SEKTRPSPAS SLEKTTESRL PVADLQGPAP
DSEPVREADE RYRKNIQGSP QSAQTKPQQP PVPPRSESSY PNGNSASEAM HRPVEPQVRS
HLAALKSSSS VASSNSSTAT PPVVSRSHSC TEPLTPSFEN LHLQNSHESR HHLPSSSSPL
SSSSSTPART DPHPHPQPRQ YEPAPSAEVP PRVPVRTTSR SPVLPRRDSP HHLGNAAHSS
HAAQHNAASA AEPRLLWERV EKLVPRTTSN SGSGGSSSSS SSSNSSSQPG SHCGSGERFR
ARSSSKSEGS PLQRPENAGK KPEERRDVLR PNRSADLTAL AKELRAVDDV RPLNKVTDYP
SSSSEESDTT DEDDDEEVDQ EAGEESTSGP EDSRAVSSRL SNGETESVKT MIVHEEGESD
AGTTPCKDST LIVRQSAGDN RKRTGPGPGQ TQTPGMHAGF APSPGSVSLQ GLAHHTPSPH
HHHHHHHHHP IQHSDRNGFA GRIHHLPDLI QQSHHSSPSS SASNSPSSSS LASPSSMSPQ
SPLDKLGILT ESQSSNNMQK HKSSSSFTPF IDPRLLQVSP STGSALNNVG YGNDARLAEA
LRADPSRKGS VVNVNPVNTR PQSDTPEIRK YKKRFNSEIL CAALWGVNLL VGTESGLMLL
DRSGQGKVYP LINRRRFQQM DVLEGLNVLV TISGKKNKLR VYYLSWLRNK ILHNDPEVEK
KQGWTTVGDL EGCVHYKVVK YERIKFLVLA LKNSVEVYAW APKPYHKFMA FKSFGDLVHK
PLLVDLTVEE GQRLKVIYGS CSGFHAVDVD SGAVYDIYLP THIQTSIQSH AIIILPNTDG
IELLVCYEDE GVYVNTYGRI TKDVVLQWGE MPTSVAYIRS NQIMGWGEKA IEIRSVETGH
LDGVFMHKRA QRLKFLCERN DKVFFASVRS GGSSQVYFMT LGRSNLLSW
//
