ID A0A0V0S530_9BILA Unreviewed; 1606 AA.
AC A0A0V0S530;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 18-JUN-2025, entry version 35.
DE RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
DE Flags: Fragment;
GN Name=NSUN2 {ECO:0000313|EMBL:KRX21796.1};
GN ORFNames=T07_12994 {ECO:0000313|EMBL:KRX21796.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX21796.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX21796.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX21796.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00048329};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00047559};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX21796.1}.
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DR EMBL; JYDL01000036; KRX21796.1; -; Genomic_DNA.
DR OrthoDB; 275301at2759; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046872; DRHyd-ASK.
DR InterPro; IPR046873; HisK-N-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR043969; MAP3K_PH.
DR InterPro; IPR025136; MAP3K_TRAF-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11584:SF394; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 1.
DR PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF19039; ASK_PH; 1.
DR Pfam; PF20309; DRHyd-ASK; 1.
DR Pfam; PF20302; HisK-N-like; 1.
DR Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF25376; Pre-PUA_NSUN2; 1.
DR Pfam; PF25378; PUA_NSUN2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX21796.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 853..1113
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1434..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1484..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1494
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 882
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX21796.1"
SQ SEQUENCE 1606 AA; 181610 MW; 4501E3B2D72130B4 CRC64;
LKIIMHKIIF FPFGKLSIKQ AQSCFAFFFH FVREYFGMDD RFSNFSLLMR QKEVSKKGII
YLVNENIKHF IKNNEHRIKI INAGLRTFSR CSVSDSVPVD FRLVQDGLRY VIPLMSKRLV
NISKDELLKL IKSKESILLK DLSDELHSQL KQIGEGSAAL VCGTENAKCT FQVASWLGRC
SVAPHLDKEN RAHFLFMLDD LQAAYGMNLY VQRQWNRWSG HEIGSCGMNW LVKWKFCFIR
GSIVFEKKAN ITYIIDTIEE VMSRKVTPPG SLVSADSVTG IKPLSRALQV AVVIDLLIKD
GLPIRQLVWD ELQKLDESTN MNMQYIPFEK LDFGEISSLD MFYNADLAIV DVSVSSQRTT
LCYHLGVRES MHQDYNIVLC SFEEKRQPMS FMFMVPFNNY KPLICTTADN ALIAVECSQF
FPGMSSNAIL ASGNNSSFRT KIKKLLKDVQ IDATAHVKEK FLADLRQARQ KCEGGELSVV
LDRLRMRLDD PDVLSVDTVV NMLLSYRDIQ NYNAMVSLVE DVSSLPYDKI HESPAVQFNY
AFALNRRNKD KDRDKALSVT LDSLSSQENQ VPDFLCLAGR IYKDKLAEYR KGFEIQPNEY
AGINLATLLV IAGETFQTSS ELQQIAVILS GLLGRKGSLQ DLKDYWDVAT FFEISVLAEN
YANSCQAAYH MFLLKPPAWF LKSTIGNIKL IKRFRETLNR SMPENQFDYR QFLFWMEFFV
ENTKSDEICT DTRFPVLTME PSKIYIPSYV SVNEESKAIS LWHVEDTNRK NLTQWIFPAE
SIRAVSAARR DERAVYLYVY LNSDDFMLFF PSDNHRKRFL QLVEEITCFE GTKLLASYTE
LQPVLYEYET DANDQRVVLG KGTFGTVYAG RDLNSQRTIA IKEVEIKNHE EVQPLMEEIQ
LHSTLVHPNI VQYLGCEVSD DNRIFRIFME QVPGGSLSLL LRNKWGPLID NETTIAYYAR
QILEGLNYLH SQKIVHRDIK GDNVLVNTYS GQCKISDFGT CKRLAGLNPI ADTFTGTLQY
MAPEVIDQGM RGYGAPADIW SFGCTMIEMA SGKPPFVELG SPQAAIFKVG MFKAHPPIPE
GLSNQAKQLI ERCFEPDPNK RPTAVQLLVD PFFEQIRFRR IAKPALESGY RDSSIRYSSV
SIPESNFSIS SRLSSSSLLA LNELSDSSAI QERHPSSAGH DSAASKFFML RKDSERRDTL
ATIMTEYENQ IIDLWLSSIG SGANSDVAVS ANILRTLLTC MRKYIFDKDS TKVRTVAGNG
HIDPPIFTDE IRCLISSGAT SNTNIRLALY AFQDVMHYVL RQQRIKPHWM FALDNLIRSC
VQCVVEMLLP DAVSNLSVQD SDGSSSYSSV VSAKSPIVPS FGYNDFGFTN SLTKQLRKEL
KDYTAENQRL LGELLKLYTC YQKLLKPLTE HIEQKLTATT IKCAGSSGSN SSGICAAGRS
GKAEEQQQMS RRNSAPATTS SIAAETRKCS LIVEEEGIGG VESSASASSS LLDNSSDDYQ
EGKSWTKDSS LPKNDDDGGR DALVNWLKEL NVDERSIEIL TNHQYTLQDL MEMVTREELL
HIGLKGGVCC RLWRSIVSQR RSFCATTVAA ADEADRRENN NESNND
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