ID A0A1L8HGQ6_XENLA Unreviewed; 1405 AA.
AC A0A1L8HGQ6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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.L {ECO:0000313|Xenbase:XB-GENE-6486487};
GN Synonyms=LOC108708403 {ECO:0000313|RefSeq:XP_018102555.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018102555.1};
RN [1] {ECO:0000313|RefSeq:XP_018102555.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018102555.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018102555.1};
RG RefSeq;
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_018102555.1; XM_018247066.2.
DR STRING; 8355.A0A1L8HGQ6; -.
DR PaxDb; 8355-A0A1L8HGQ6; -.
DR GeneID; 108708403; -.
DR KEGG; xla:108708403; -.
DR CTD; 108708403; -.
DR Xenbase; XB-GENE-6486487; map4k4.L.
DR OMA; LEKRNGW; -.
DR OrthoDB; 2904475at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 108708403; Expressed in egg cell and 19 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06636; STKc_MAP4K4_6_N; 1.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_018102555.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777,
KW ECO:0000313|RefSeq:XP_018102555.1}.
FT REGION 308..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..872
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1080
FT /note="Polar 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 1405 AA; 160661 MW; BC8274C204D9C0CD CRC64;
MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ LWLVMEFCGA GSITDLVKNT
KGNTLKEDWI AYISREILRG LAHLHAHHVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR
ALFLIPRNPP PRLKSKKWSK KFFSFIEGCL VKNYMQRPPT EQLLKHPFIR DQPNERQVRI
QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES TLRRDFLRLQ
QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE QQKEQRRRLE EQQRREREAR
RQQEREQRRR EQEEKKRMEE MERRRKEEEE RRRAEEEKRR VEREQEYIRR QLEEEQRHLE
ILQQQLLQEQ AMLLEYRWRE MEEHRQAERL QRQLQQEQAY LMSLQHDHRP QQQPPLQQQP
QPQQPPLPQQ ERSKQSYHTQ EPKPHHEQAE RIREAEERLR KANQGSPEAQ ANQPGRVLEP
SVPSRSESFL NGNSEPAQPA MHRPVEPQVQ WSHLASLKNN VSPVSRSHSF SDPSPKFAPQ
LLRSQDSHQT SRSEVQSQSS DPKSETSEPT QRVWARSDSD EVPPRVPVRT TSRSPVLSRR
DSPLQGSGQQ NTQTGQRNST SNIEPRLLWE RVEKLVPRPG SGSSSGSSNS GSQAGSHPGS
QSGSGERFRM RSSSKSEGSP SQRHENTAKK SDEKKDAVRQ AKAPGEVDLT ALAKELRAVE
DVRPLHKVTD YSSSSEESGT TDEEDDDMEQ EGANESTSGP EDARAMSSLN LSNGETESVK
TMIVHDDVES EPAMTPSKEG TLIVRQSTVD KKRANQLESN GFASRIHLLP DLLQQSHSSS
TTSSPTSSQP TPTMSPQTPQ DKLTANETQS ASNTLQKHKS SSSFTPFIDP RLLQISPSSG
TTVTSVGTYM RTLEANLKNT NFILVGFSSE ALRPDAMRQD PTRKGSVVNV NPTNTRPQSD
TPEIRKYKKR FNSEILCAAL WGVNLLVGTE SGLMLLDRSG QGKVYPLINR RRFQQMDVLE
GLNVLVTISG KKNKLRVYYL SWLRNKILHN DPEVEKKQGW TTVGDLEGCV HYEVVKYERI
KFLVIALKSS VEVYAWAPKP YHKFMAFKSF GELVHRPLLV DLTVEEGQRL KVIYGSCAGF
HAVDVDSGSV YDIYLPTHIQ SSIQPHAIII LPNTDGMELL VCYEDEGVYV NTYGRITKDV
VLQWGEMPTS VAYIRSNQIM GWGEKAIEIR SVETGHLDGV FMHKRAQRLK FLCERNDKVF
FASVRSGGSS QVYFMTLGRS SLLSW
//
