ID A0A0V1D0X8_TRIBR Unreviewed; 906 AA.
AC A0A0V1D0X8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN Name=MAP4K5 {ECO:0000313|EMBL:KRY55096.1};
GN ORFNames=T03_1138 {ECO:0000313|EMBL:KRY55096.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY55096.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY55096.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY55096.1};
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=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 -!- 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. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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:KRY55096.1}.
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DR EMBL; JYDI01000060; KRY55096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D0X8; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06613; STKc_MAP4K3_like; 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; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF18; HAPPYHOUR, ISOFORM A; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR038172-
KW 2}; Kinase {ECO:0000313|EMBL:KRY55096.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR038172-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transferase {ECO:0000313|EMBL:KRY55096.1}.
FT DOMAIN 57..324
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 567..875
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 340..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT BINDING 63..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY55096.1"
SQ SEQUENCE 906 AA; 102728 MW; FF58EBCC9A57B510 CRC64;
KNTDQVQSCH RLSEPLFREY NKTKVDADNT AKLLIGTLYL CRRCVMDFNR RNPSDDYELL
QRVGSGTYGA VYKARHIVSG EFAAVKVIKL EPGDDFSVIQ QEIVMMKECK NPNIIAYYNS
YLRRDKLWIV MEYCSGGSLQ DIYHMTGPLQ ELQIAFVCRE TLKGLQYLHG MGKIHRDIKG
ANILLTENGD RILALQPRLL PQLASGDHLS APHIGDEFFK KIIIARMMAP EVAAVERKGG
YNQLCDVWAV GITAIELAEL QPPLFDLHPM RVLVLMSKPN YKPPSLRDKI RWSPAFHEFV
KQSLTKNPKK RPTPEKLLTY SPFLQGKLTN RLTRDLLDRV NNSGQTSTAE VQNYELEDDE
PGPSRAPKEI HSKRSSSVQP EVVNRIRPSV STQNNCKPVP VIDSPFSVQE TESISDILRR
WGIVDRCSSD DRQANAARHV GRDRNKKAPQ IDEQQKQPTT SDATLSNARY DEGQTLQVNG
SGTPPDLLLG HTLNRLLLGD EETVQLQGCY SSSGSDSESY LPPVPPDRRR SKEHRSRANV
RQSAFGLPPT PKVVMGACFS KIFNQCPLNI QCSASWIHSV TKEQHILIGA SEGIYSLNLN
ELHEATLRRV CFRPCSWMYV YKDTLMAIQG RTTHLYRHSL ISLHSANLTN RLSSLPLDRL
PAKILPRRLA ISCRVANTKG CTRCCVALNP FHGHRFLAVA ISTGILLMQW YEPLQKFLRI
KLVECTMPSL IPVFEMFIPV EHQYPVIFIE IISYRPSGKH VVFDYIDLNI TETSFSKPHL
LNLPLLDVSA VQQLQKDVVL VAHGDKVKLV NFKGKLKSSR YAPAEFEFPF KIERIDSVLA
FHKYGMQGRS FIDSKITQDI EDKSQEYRVI GSDRLIVLES HRQVDSTQSD NQNAVNLYIL
SGHEKY
//