ID A0A0V1HFV0_9BILA Unreviewed; 1655 AA.
AC A0A0V1HFV0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Dual specificity protein kinase CLK2 {ECO:0000313|EMBL:KRZ09401.1};
GN Name=CLK2 {ECO:0000313|EMBL:KRZ09401.1};
GN ORFNames=T11_6121 {ECO:0000313|EMBL:KRZ09401.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ09401.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ09401.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ09401.1};
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000256|ARBA:ARBA00010271}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. Lammer subfamily.
CC {ECO:0000256|ARBA:ARBA00037966}.
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:KRZ09401.1}.
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DR EMBL; JYDP01000073; KRZ09401.1; -; Genomic_DNA.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14134; PKc_CLK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45646; SERINE/THREONINE-PROTEIN KINASE DOA-RELATED; 1.
DR PANTHER; PTHR45646:SF11; SERINE_THREONINE-PROTEIN KINASE DOA; 1.
DR Pfam; PF03016; Exostosin; 1.
DR Pfam; PF09258; Glyco_transf_64; 1.
DR Pfam; PF00069; Pkinase; 1.
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}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRZ09401.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1294..1610
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 783..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..921
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1016
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1655 AA; 191591 MW; 58689C8875FD03D2 CRC64;
MKTKRRYVAL FGIFVISYSS RLLLNIFRHL QTSPLCNQNF SENAQSYGEN VSLNSEIWRS
IYENYSSYIG DDHLEGGGIP RPCSMSSCFN YSRCIDRPFK VYVYPDFPDL DEESKTSASY
RKILQILRQS KYFTDDPDQA CLFVLSYDTL SRDSLSAEYV ENMNAKIKNL PANLWNNGMN
HLIFNLYSGT WPDYDLTELG FEPGQAILAK ASFSTRHYRS HFDISLALFH DILPLRGLNA
TDVEDVNLNW PRSNWSYTLV FKGKRYVFGI GSETRNALYH LHNAKDIIML TTCKHGKDWM
KNQDERCSID NDLYDNWNYE ELMANSKFCL VPRGRRLGSF RFLEALEKGC IPVILSNDWV
LPFSEVIDWD QAVVRGDERT LFQLPSLLRA YPESVIIRMR QQARHLYRLY FASVEKIVYT
TLQIVEERVQ PWAACDHSIW NWAPMGARYY STNFSLLPMD FLNKNHSIFN DTFTAIIHCG
EHFKSEHILQ LVQNISSSSR MEKVVVFCSS GNLHFEHAEV RPLLNVSEMF KFIYQQSSRA
IFCFSDQVYV NTDEVDYAMT LWDQFPHRLV GFSALNAQYD QLENQWRLVE PNVKGYHSLM
TSDAVLFHKY YSLVILEPPL REAAVQLNEH PICWDILLNF FVSDMIDLPP LLVDSQSSSL
WFNSVKTMLS SLKQRQQCLN RLIISAGYSP FIESSLRFHQ FRKEIIFGKL ILAWLLLKKR
STLLHSTVGD RSCCFENGFA DGKGINLNQE GHFMDVSCIE YCRSGEKWIQ LKSGTSFMSQ
NSLFDNNNSQ RRSSSCISQR EVSNSTRRKS VGSELSISGT PCRSNLDKKR HYHDHDDDDD
DSSADRRRFR RRRQDSYSSR SRSSDRRTRR RSECRRKLSH RNGYHHHRSR KHRRSRSRSR
RRHRKSYSNR KRGRYSRRAR RRSYSSYTSS SSYELTVGRK LSFCLDSGAV RTSGRRISLV
DSPVENRLPQ AAVVDGYLHH FQQQQQQQQQ QQQQQQQQHH HHPHQKYQQH HHLQPPLRRR
RRLGWEVYGH PLLKELQSFA DTLRDLDGST VSVQRRAGPS PPMPLNAVAN ATVQHAPIPP
PRRRRRTIAV MPVSLSRSDP SLYVVDFQAQ ASSGEAIDNA GKGVVVEPAE VALSAMLDRF
AIFESASGAQ QLPPTTSLPK KDSKSNAKNV YYQYPCPFSR PNMLAEAVGV VPTPPPPPPS
TDGVATLVAA ATAEEEVKTP LLPVASALSN QQQQQQQQQQ QQQQQSSPPV VEQDINDQPL
LRSESRRSSG DGLIRDDKHG HLIYNIGDII QSRYEVIKTL GEGTFGRVVQ VRDHENEQSE
PLALKIIKNV DKYREAAKLE VNVLKKLMEK DPAGNFLCIH LVHHFNYFGH MCLVFPMMGL
SVFDFLKTNN YYPYPMHQVR HIAYQLCYAV NFMHQNHLTH TDLKPENLLF VHPEYDIKID
MKRNKEYRII RDTSVRVIDF GSATFDHEHH STIVSTRHYR APEVILELGW SHPCDVWSIG
CIIFELLLGT TLFQTHENLE HLAMMERILG PLPYRMCRKT KTRYFYHGRL DWDIRHPSGR
YVRDNCKPLS RYLLAGDVEH EEIFDIVSCM LEYEPSQRIK LADSLDHRFF HRLPENQKLH
KDNSRNQTVS NFSASVKGCC STSTVLSEEF SSATD
//
