ID A0A0V0RKG5_9BILA Unreviewed; 2640 AA.
AC A0A0V0RKG5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=lrk-1 {ECO:0000313|EMBL:KRX14842.1};
GN ORFNames=T07_5212 {ECO:0000313|EMBL:KRX14842.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX14842.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX14842.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX14842.1};
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 -!- 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:KRX14842.1}.
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; JYDL01000149; KRX14842.1; -; Genomic_DNA.
DR STRING; 6336.A0A0V0RKG5; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF165; IPT_TIG DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX14842.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2356..2377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 43..75
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 79..111
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 217..240
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 373..405
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1061..1280
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1862..2166
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 862..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2533..2573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1895
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2640 AA; 293189 MW; 87DC97452F09661C CRC64;
MIDAKVEDDI SVILQTLSYG NGDLLRELLR SDFQHYVHWQ NEFGQTFLHI ASSVPGNSCV
KVLLEEGSEV NATTHVTCGS KTPLHLSAAG NDVNTCILLV QYGADLFARD SEGNTPLQCA
QMQDFKEVSN YLLDEIEKRR IKIMELQDKL HVACMKADLN ETEFLLKEAE SNFIYGIVNE
PLLDGSNLLF KVCEAGLTRV AELLIKFGSV GIVNAASFNS PLHIAITANH VDIVKLLLKH
FPELVQMSTS GKCLPIHTAA KVGNLEMVKI LLENPYPKYV LNSYMVENSE WQYRMPFDVN
AVDDGHRSAL LIAVEADYTG LVEYLLQFHV VARPLSGQQL LLSQNSTAAP LASGDVLQFK
KFRPVQADLR CASGYTALHL AVLKGNVELV KLLAKHGADL QAPISGTALQ LFDNSGEELS
GAAGALLLAC SKENTAMVDL LLKVGATDVD NKVLAYCLAS SNRDTLVTKL LSRLVFPDPE
FRVNKKAVNV DWMFQVGRGK PVAPSALYPS TAVMLNWHGS HLGRIEDHWL ASAALQLNPR
CRPSPTGVLL SACLSAAITR IDVSKNSLST LPRCLFQLPS LRILNASNNK ITSLGLENDT
SNKSFAVSLE DLYLERNLLD SVPSVVFTFP NLVTLNLADN KLKHLPNNMW QCVALKELNL
AGNQLRTLPA KTANTVNSSS SSLLCATSSS SSSSLAACCC CCCSANNSST TSDYCCLSDS
DMSFSSEQKS SDLTTTLSPS SVSVVDAVSV EFADESVSIR QFSRHSLWPK QAELLKLTDD
SSTKGDRNFS LSTLNLARNA FEQVPQALSC LAPALTRLNL SHNFLQQLGP IHCYPSTLKH
LDVSHNRVQH WFTVKRKGCL DTSHESRSPS RGPPPHSSPI INSRRSHSVS RMHHRLSAGT
YERSSDRSPL ATGVCCAHRQ HCRLINLRTL LLADNCLKSV TFFPENDNEK QAENFESNLS
GLNTQEKRLA LMFPNVSTLD LARNMIVNVP VSIALLQSLA VLNLSENRQI ACLPPEMGLL
GKLWNLNLTG CGLDEPFSSM IESKKCKTID IISYLKSVLE DSKTYSRLKL MVVGVQGIGK
TSLLEQLRAE GIGPRRPAQE GWARRMGNKT VGSKTASGIN ISTVGVDVNE WTYQPKRQKG
RQRPPITFRT WDFGGQREYY ATHQYFLSKR SIYLVVWKVS DGEAGIAEFT QWLINIQARA
PNSPVIIVGT HVDAIRSNHK RFPAEYLEKL QTTIRERFIS ISDPDKRGLP RVVDSIAVSC
VTREQIRTLC ELIYHTAYEL RTPGSKERLI EQRIPSSYVA LEEIVTKLAA ERKQAGREPV
INAETFRNSV QELMLKQTGR SFRDTHELNL AVVFLHENGV LLHYDDATLK DLYFLDPQWL
CDVLAHVITV REINPFAKGG LMKVDDLKIL FKATRLSVAN IRSYALNLLQ KFEVALTWDN
KTLLIPSLLP DEYQLRAGYP GCNVKVPVSA RIEDKKDDHW SILSAQATVE SCLTSMQANL
SIVDNVEGGD SSEYKVVAFH ENVQQSIRRL YVMLYFPSGF WSRLITRIIG DDKIAAILND
HYLHVSQAEN FPLVEQLSRT VLADNKLEWR LWQTGLEVNV FGVTLISVKE FLPLAQVRDV
DYRDVSMRYK QDTFWSVVNA DQSSVLELYF PHVSFEIVPT SSGQEANYLQ ARFTLATNRK
AAIRLLALTV EILDTLLEDW YPSLGTRFIH TSEGRYLVTR LVPCPCCLSS CMNLSGQSVE
DDDWTVLPNK KRSSSNVIDV ADFSTNTSEL TTVAAALKEF EQMIEKSKPR QHPDDDDNVS
TDQQQSLLEC VCCFTVEECI HAASEASTVK CFKHGALSLG TVAPDTVFLD LSDGQLIVPT
TVKRGKMLGR GAFGFVFKAT ANLRNNDDCK DVALKILHPV DPGFGAKASA LAAFKVGKIG
AASSKWKRDP VQHACRSYCT ARQELNILLK LKHSCIVPLV GVCPRPLSLA FVLAPLGSLG
ALLMNYRRSG ARINWTSLQE TAFQIAKALE YLHRSHVIYR DLKSENVLVW HFPPPFSLLT
TVEVKLGDYG ISRNALPAGH MKGFGGTEGF MAPEIMRYNG EEEYTDKVDC FSFGMFLYEL
YTLRLPFEGQ EQVKEYILDG GRPNISVKDI AYPCNFLDLM IKCWSQQPSE RPSSSQLVSL
TAAPEFSHLL DVVSLNDPEV YFTVGEAFIN DNFPVADENM ALEGEIWICR TDGQVSILSS
DGGSWFEYKN ITIDKDTFVA ALCLVNDFVW VADLTGMIRI YCTKIYSEVM KFSIANCIQR
PAEWNGVVSQ VQVERVHYVE KLDLVVLSVC TPPTLILCSS DPHSSEALVI KSVHDCCTEG
SSIICSTFFP SATADGYVDC ILLLFIIFGL GVVEVIFPCT DCRTEIYFTW NRFHIVQHLM
IMTLKLASWC PAAIAAVTFG LICFQASSVI YQWETETKKT VAKLDCSKLV PCSESLYTMN
VEERLTPSFC QVSALYLLEK EDCSQLYVGT TWGVIIVAEA DQLKPITAFR PYVEDVRLIA
AFTADKRTAV SSATHQAASS TGSDRSARHQ SASSEYAQGT KCSGGSLPPY QERRSSLETA
GTFSAYSGRG PLLVTVGRGY RSLISRFVDS SSSKQDPKSN SLLERDHFAI LWRTDDWTNF
//
