ID A0A077ZBB9_TRITR Unreviewed; 1855 AA.
AC A0A077ZBB9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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_0000593501 {ECO:0000313|EMBL:CDW57642.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW57642.1};
RN [1] {ECO:0000313|EMBL:CDW57642.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW57642.1}
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: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR EMBL; HG806193; CDW57642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZBB9; -.
DR STRING; 36087.A0A077ZBB9; -.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20809; C1_MRCK; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR CDD; cd05597; STKc_DMPK_like; 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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF66; SERINE_THREONINE-PROTEIN KINASE GENGHIS KHAN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 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; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDW57642.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW 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..361
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 362..432
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1128..1178
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1197..1324
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1351..1641
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1707..1720
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 485..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..484
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 515..676
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 726..753
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 787..821
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 921..983
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 488..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1855 AA; 209185 MW; 29C74621D668D286 CRC64;
MPIAPGDQRL KELEKLFLSG PLFGETASVE TLLDVLICLF DECCNSTLRK EKDIANFVEH
VKPIVHKAKA LRLQRDDFEL LKVIGRGAFG EVRTNEKRTV FFLSAQVFKV AVVRLRNTGK
IFAMKILNKW EMLKRADTAC FKEERDVLVF GDRRWITNLH YAFQDEKNLY LIMDYYVGGD
LLTLLIKFDD HLPEEMARFY IAEMVLAIDS VHRLGYVHRD VKPDNVLLDI NGHVKLADFG
SCLKLQPDGT AQSNVAVGTP DYISPEILRA MEDGKGRYGA ECDWWSLGIC MYEMLYGETP
FYAESLAETY GKIMDHMEML EFPEEPTVSE EAKHLLRSLI CPAEQRFGKN DLKDFEMHPF
FKGIDWENIK EAEAPYKPEI SSPTDTSNFE VEDSDFMPCD TKPPNVSAPF TGHHLPFIGF
TYTHNSKLSD SQSLAALIVR SESGAEDEIN ITDMVTVEAY ERRIKRLENE RTDLERKLRE
ATRLVQSQFH GDEGNSATKA GPSEVTSPDT DIVAVAQMKD ELQILRKRVA EYEAVVSSRK
DSAAEEWEKK YRELQKKHRQ LITDRSSLED QISKLSEESN EKKYQLKEAI KYRDAARQDF
AEASDKITEL MNEKQKLLRA SREREDECNV LQQKSDAMRV ELLKMEKLKR SLEFKLEESQ
AECSRERRLR EDVEANQVAL QIELESVRKG KAISGNGPTS PENARKMVEH VEEELQMERD
RHSRQVSVIE TQLSDAKMEV ESLRSQLQTL VCRTDEERAA LIANHEEAIG DLHIAVERER
ELRLETQNQL EMENNGLKEN IHAMEGQIAG LEKQLALMNE KYNFAMILDS QLPELMKWVN
DEKEVRIYLH ALTAKIAEEV ESMKQQQQAA SQSQSLSQSL TPTSGPYFEG ANNSPYSYAT
LTGGEKGWGS RRSHKVAKME ILDLQRNLQS EIRAKQEITE ELTKFRSAYF ACKQQLEEAE
KKVAEMVCEL QRKAKRLDEL EHLSSLRTPP DPGNFDQLIH LNNMFDLLKQ YSDEVASACN
EGGAAAKAKP VDFADVAASS GSPAKVHDYE PLNSSVTNDV EPAPLPGTMV QPLAESSPNY
ENSPYHLSMA QFQSMNQRTL ANSSSAPFGG IFPPGNTNLR NAAVAHKLHR FNVAIFPQPT
KCNHCTSLMI GLTRQGYVCQ DCQYCCHVIC LPKVQAACPA PPETIRPLGI DPSRGLGTAY
EGMVKVPKPG GVRRGWTPQY LVICDLKLFL YDCSTDKNGK PVDVSPQVSL VIDMRDEDFS
VTSVKESDVI HASRKEVLCI FRVTSSQIHQ PVYLGEPCKM VTLLMADSQN EKQKWVISLN
ELVRFLRKRR LTQKKAFIVR ELVDQSALPF VRTALCTAVV DKDRFLLGSE EGLFCVEVNR
QAAIRIGDSR RVEAIEYVSD EQLIIIMSGT LKNHILPALF NQVVYHLGKE HQIRLIPTAV
LDGRDVKWIK VDHTKQCHAF CVGSVLNGTA YYFCVAVKKT ITVFEINRTP TRHRKLRDLA
MPGFPQSLSM VRGKLCVGYP SGFRMWDFVD NSQHALLNLE DHSLQFMNHA AYDACILIEV
SDKEYLLVFE KLGIYVDLNG RRSRPLELMF PSEPIHFSFS APYLCVYSEC HVTVYNVTTA
EWVQTLNLRK AKPLLRSGAL TLCCVADKMC IVLLSDMLAV DDVMNTPFMV STRNMNQDSS
KRRKYSILVL SEEEKLRKSI GRKSLMISGP SNFSHITHMG PGEGIEFQQL IDLNQSHPKV
VDPRCSAEEA ATSTVKEQSS TSVHSAASSF NTSKRPSSVN SKSSDGSSLS REESLSRTGN
TEILLRTESP PFSLSSGEPS VVTGAAKATQ SGDSLPSHAF QVSSSPKRGT QASGT
//
