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Database: UniProt
Entry: A0A0V1D0X8_TRIBR
LinkDB: A0A0V1D0X8_TRIBR
Original site: A0A0V1D0X8_TRIBR 
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
//
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