ID A0A0V0U685_9BILA Unreviewed; 1345 AA.
AC A0A0V0U685;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 18-JUN-2025, entry version 34.
DE RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN Name=Map3k5 {ECO:0000313|EMBL:KRX46830.1};
GN ORFNames=T05_6440 {ECO:0000313|EMBL:KRX46830.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX46830.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX46830.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX46830.1};
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:KRX46830.1}.
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DR EMBL; JYDJ01000051; KRX46830.1; -; Genomic_DNA.
DR Proteomes; UP000055048; 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 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:KRX46830.1};
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:UP000055048};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 592..854
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1170..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1240
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1345 AA; 151250 MW; 8AEDE6873DBE7A0B CRC64;
MSRKVTPPGS LVSADSVTGI KPLSRALQVA VVIDLLIKDG LPIRQLVWDE LQKLDESTNM
NMQYIPFEKL DFGEISSLDM FYNADLAIVD VSVSSQRTTL CYHLGVRESM HQDYNIVLCS
FEEKRQPMSF MFMVPFNNYK PLICTTSDNA LIAVECSQFF PGMSSNAILA SGNNSSFRTK
IKKLLKDVQI DATAHVKEKF LADLRQARQK CEGGELSVVL DRLRMRLDDP DVLSVDTVVN
MLLSYRDIQN YNAMVSLVED VSSLPYDKIH ESPAVQFNYA FALNRRNKDK DRDKALSVTL
DSLSSQENQV PDFLCLAGRI YKDKLAEYRK GFEIQPNEYA GINLATLLVI AGETFQTSSE
LQQIAVILSG LLGRKGSLQD LKDYWDVATF FEISVLAENY ANSCQAAYHM FLLKPPAWFL
KSTIGNIKLI KRFRETLNRS MPENQFDYRQ FLFWMEFFVE NTKSDEICTD TRFPVLTMEP
SKIYIPSYVS VNEESKAISL WHVEDTNRKN LTQWIFPAES IRAVSAARRD ERAVYLYVYL
NSDDFMLFFP SDNHRKRFLQ LVEEITCFEG TKLLASYTEL QPVLYEYETD ANDQRVVLGK
GTFGTVYAGR DLNSQRTIAI KEVEIKNHEE VQPLMEEIQL HSTLVHPNIV QYLGCEVSDD
NRIFRIFMEQ VPGGSLSLLL RNKWGPLIDN ETTIAYYARQ ILEGLNYLHS QKIVHRDIKG
DNVLVNTYSG QCKISDFGTC KRLAGLNPIA DTFTGLCTLQ YMAPEVIDQG MRGYGAPADI
WSFGCTMIEM ASGKPPFVEL GSPQAAIFKV GMFKAHPPIP EGLSNQAKQL IERCFEPDPN
KRPTAVQLLV DPFFEQIRFR RIAKPALESG YRDSSIRYSS VSIPESNFSI SSRLSSSSLL
ALNELSDSSA IQERHPSSAG HDSAASKFFM LRKDSERRDT LATIMTEYEN QIIDLWLSSI
GSGPNSDVAV SANILRTLLT CMRNYIFDKD STKVRTVAGN GHIDPPIFTD EIRCLISSGA
TSNTNIRLAL YAFQDVMHYV LRQQRIKPHW MFALDNLIRS CVQCVVEMLL PDAISNLSVQ
DSDGSSSYSS VVSAKSPIVP SFGYNDFGFT NSLTKQLRKE LKDYTAENQR LLGELLKLYT
CYQKLLKPLT EHIEQKLTAT STATTAIKCA GSSSSNSSGI CAAGRGRKAE EQQQMSRRNS
APATTGSIAA ETRKCSLIVE EEGVGGVESS ASVSSSLLDN SSDDYQEGKS WTKDSSLPKN
DDDDALVNWL KELNVDERSI AILTDHQYTL QDLMEMVTRE ELLHIGLKGG VCCRLWRSIV
SQRNSTAATT VPATDEADRR ENNND
//
