ID A0A077Z968_TRITR Unreviewed; 1383 AA.
AC A0A077Z968;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=TTRE_0000444801 {ECO:0000313|EMBL:CDW56173.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW56173.1};
RN [1] {ECO:0000313|EMBL:CDW56173.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW56173.1}
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; HG806015; CDW56173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z968; -.
DR STRING; 36087.A0A077Z968; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR CDD; cd20813; C1_ROCK; 1.
DR CDD; cd05596; STKc_ROCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.730; Single helix bin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF73; RHO-ASSOCIATED PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01206}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDW56173.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 78..340
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 343..411
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 950..1018
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 1128..1238
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1237..1292
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT COILED 429..681
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 714..832
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 907..1008
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1076..1103
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1383 AA; 158835 MW; 1569F10220D781D2 CRC64;
MAELTQADLE DALVQLSGKL LNPRSSINVD CLLDALSALV GDCDFPALRR IKNIENFLLR
YQTSVHEING TRMRSSHFKL IKVIGRGAFG EVQLVRHKFT GKVYAMKLLN KFEMIKRADS
AFFWEERDIM AYADPQWIVK LYYAFQDAKY LYMVMEYMPG GDLVNLMANY DVPEKWAKFY
TAEVVLALDA IHSMGYIHRD VKPDNMLISA LGHVKLADFG TCVRMGADGM VRCSTAVGTP
DYISPEVLRS QGSEGVYGRE CDWWSVGVFL YEMLVGETPF YANSLVATYS KIMNHQSSLT
FPDDVLISTS AKDIICKFLS DRSVRLGRNG VSEIKSHPFF VNDEWDWDTI QNTRPPVVPD
LSGDDDTRNF DNIEKETTPQ ESFQVPKAFA GNQLPFIGFT YSREFSPLGY MSLTRKNIQH
SDAQISNLAD QLQQGISLME QNEEKHRNEA AKFAIMENRG EAMLRDYYDL ERALASTRLE
LKEMQRKLEQ EVEARQHVET LLQEARTAYA YLEEADNKNQ SESSLDMERQ ISELNERLRL
QSEGEEKLRD LLANFQATCS TQEEALHELR AKHDILMDQC TDAQQNLKMV QDQLEEERAI
SRQHIQAVQI TKEKNESLQA ELDLLTTRHQ QLMEESRQLS DKKRALEKDF SMAELELKSA
RQKYEQELAA QQSELNAKRI IGEADRPESA LIQGTHYMLL IALPQAKDER YQIIAELEQR
LRDEEASRER LEEKLIEVER EKKVLSLDSD HFKEQVHQLV GDSESLRMKI SELNSQVEQE
MEKRNLVEGE LSVASDALKA MKFKESNLQK EIAHLKQKCT QLEDSMAELR RFRSVSQSQL
RDVEEQLETQ QYFSSLYKSQ SRELKDELVC KDQELNSVKI HLNRQSQMLR DQQEADRSAR
RIAEDSLSDV EKARAMLEIE MKQLINRHKQ EITGKEATID TLKEKEAMYL KNIEDLRKAQ
ESLNVDLESA NKELSRKTSM STSTDEQIQQ LKKLLEKEQQ LKKSAIDKLT EVMQMKSTSA
GKKGSRADDR FVARCSCESP ASPRFQEKRK YDIMVTRFQK EISDLQASLY EEGQSKLRMM
LELECKEEEL ELVQQKLHTL LSETCSVDSV SMAGDAVDFS NGDSLEHRLE SSVWIPHKVS
AKKKGWKKHY AVLFNRKIFI YANEADKQTS NASLILDVEK FYHVRHVTNA DVRFAEEKEI
PRIFQIIYAG EGESRLVGEV QPTESPNPWQ DVMSHKGHDF IAISFHSPTS CDICSKQLWN
VLKPPPALEC KRCHVKIHKD HLEKHDKDVA PCRVNYDPML ARDLLVMVSS ADDCKVWVSR
LRRCLENCRK TSDAKTSRSS GSSSHKDSLR LPYKPYTANR SATAPCTKKG SSACPLPVTA
SHY
//
