ID A0A0R3VTH8_TAEAS Unreviewed; 1083 AA.
AC A0A0R3VTH8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 38.
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=TASK_LOCUS549 {ECO:0000313|EMBL:VDK21263.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000054801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000054801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK21263.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UYRS01000075; VDK21263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3VTH8; -.
DR STRING; 60517.A0A0R3VTH8; -.
DR WBParaSite; TASK_0000054801-mRNA-1; TASK_0000054801-mRNA-1; TASK_0000054801.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF35; SERINE_THREONINE-PROTEIN KINASE PAK; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000282613}.
FT DOMAIN 111..124
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 785..1062
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 52..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 815
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1083 AA; 115788 MW; 96C91FC13D02F5ED CRC64;
MSANTSNLNG SLVGYIEMQE STAVQRRLST GTNAHLPAAS SATFLYGDIG TSTSAPAPPV
RSSSTLKKER PLISPPSKPL PTPPQKKEKK RKVKLFRLPL FNRSGSTEPS ISGPTDVKHD
LHVVFDQTSG DFLGMPLQWV QLLKSSNIPS SEQAKNPDLM LDVLQCYDES AKPKEKYMTN
FSGVTSTSTP PFCVVYIESR LFCLIGQKIF SSLAPLSTES GNGANTTSSV VVSIMKLMGC
GSRLASETTR ADDPRTRLLA YCDSLLAVFF HCFRSSGSVD SMSQASSSRC STTTHPFSPP
PPAPSSMSEG LHLLSDPPSS STPPPHKLST LSSPLSSFMP SNPTDTSPFR GYSYNETSGA
VTANSTCSTP PPMYAGSQRR TSEVVGVAVA GTGAVGARPP PPTPPHRTCS GGGGGEAKQS
QLQQQQSERE QTASSSSAVS CNASSVPSLP TTSGVSVGGG SSSFTSSGCS FYYYSGSGET
SNSPTSGCGF TAPAPPPPIP PHHVSSTPTA SSTDPAATLR GSHHRSVPPA AAVTHDKGEV
SGDVNGGDQR ALSSTEDYPS SPASHSQPQP ALPPPPPETF TSEEEECDEQ DEEEEEESSE
EESDEMVIIT EVEVEEKEMS PETVHDMTVE LERRVCLRDV SPVDGAVRDA TATLLPPPSS
SAIENGGTLT NGHAKKHPMG EFVPPIGVIG SDNAENTVKS PPPSADLVQK PVSPALAGIS
PAVHHFPNSP KSAHHHHTNN NHNQQQHQHA APRRRTNNNH HRLTDLQVYE KLRTIVSPGC
PTDKYCVVEK IGQGASGVVC SGYEIATKKL VAVKKMNIAQ QPKKELIINE ILVMRANRQP
NIVNFLDAYL VAPSPSAALA APVKTLNPAA NGNGGGSGEE LWVVMEYLDG GSLTDVVTET
CMEEGHIAAV CKEILQALEF LHANNVIHRD IKSDNILLGM DGSVKLTDFG FCAQLSNERM
KRSTMVGTPY WMAPEVVTRR QYGYKVDIWS LGILAIEMVD GEPPYLTENP LRALYLIATI
GKPEIKERDR LSATFLDFLD RCLEESVDKR ATASELLQHP FITTQAKPLS SLIPLIQLAR
EQK
//
