ID A0A077ZBL0_TRITR Unreviewed; 521 AA.
AC A0A077ZBL0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Pkinase domain containing protein {ECO:0000313|EMBL:CDW56010.1};
GN ORFNames=TTRE_0000428401 {ECO:0000313|EMBL:CDW56010.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW56010.1};
RN [1] {ECO:0000313|EMBL:CDW56010.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW56010.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. GCN2 subfamily. {ECO:0000256|ARBA:ARBA00037982}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG806001; CDW56010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZBL0; -.
DR STRING; 36087.A0A077ZBL0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR11042:SF91; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE 2-RELATED; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|EMBL:CDW56010.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..517
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 521 AA; 59613 MW; 221648D5DA5B74E4 CRC64;
MKSSSALQKW TRWDKYFNKQ AQNEQKYVTQ LVVVDVWDWW KHAFVVCFTL ICIPQIFVFI
YVFKKRSDVC AESKSDDSSS VKKKSQESMT DFNSFASVST EAEFTSRYLK DFVPVRCLGC
GGFGTVVESI NKVDEQKYAI KRIPLPNRQY AKERVIREVK ALARLDHPGI VRYYNSWFEE
PPAGWLESSE AAVFNICRTK QCSGGTESQV TNEHSSHAFD DKVLKPKHKI TGSSNTLSTL
ALKQSTLMHM KRPDVDEDAS SDSLEIVFEG SEKKGDQPSI ASRGYGLISK NIDLSFFRFR
RQTKQSKSKK NKELQTVPVG DVFLFIQMQL CREYTLMDWL GEHTEKRDLS MMLDWFKQIV
EAMQYVHDCG MIHRDLKPTN IFFSLTGQVK IGDFGLVKEC LTYEQSDESD PDIGAVSSTV
AHTQNVGTYL YMSPEQETKG PYTFKVDIYA LGLIFVELVI PFATQMERII TLKRLRQMSL
PELIQRSAAM CSFVMKTLSH SPEERPSCKA ILSSPLFTEL L
//