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Database: UniProt
Entry: A0A0V0Z7D7_9BILA
LinkDB: A0A0V0Z7D7_9BILA
Original site: A0A0V0Z7D7_9BILA 
ID   A0A0V0Z7D7_9BILA        Unreviewed;       714 AA.
AC   A0A0V0Z7D7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=TP53RK {ECO:0000313|EMBL:KRY08333.1};
GN   ORFNames=T12_5255 {ECO:0000313|EMBL:KRY08333.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY08333.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY08333.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY08333.1};
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.
CC       {ECO:0000256|ARBA:ARBA00010630}.
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:KRY08333.1}.
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DR   EMBL; JYDQ01000343; KRY08333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0Z7D7; -.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR022495; Bud32.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   NCBIfam; TIGR03724; arch_bud32; 1.
DR   PANTHER; PTHR12209:SF0; EKC_KEOPS COMPLEX SUBUNIT TP53RK; 1.
DR   PANTHER; PTHR12209; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF06293; Kdo; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50181; FBOX; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 4.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRY08333.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   DOMAIN          106..151
FT                   /note="F-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50181"
FT   REPEAT          214..233
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          236..275
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          282..321
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          322..355
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          363..402
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          408..447
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          491..714
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   714 AA;  80501 MW;  B24BE4914B561D04 CRC64;
     MERLLEETVS DMEGLGNGSE NDSELKSSNA AAHNGSQNSN AQASSTCFLS FSDKLEKLCE
     WMAHFTDDEK NIVVSNILLY CGPEQLKPVA DFMESSSHNY FSENAVDPFE LFPSNILMHI
     FSFLEPIDVA SCALVSKLWN RFVEYQGWKS MCLFNSNYRL ASTELEQKLT SRYCIGEGRV
     EWKGIFLERY RLRRNWMKAR CVVRTFYGHS AGNGSSDKSI KLWDIRTNNP LAVMTLLGHS
     GTVRCLQLNG SRLASGSNDH TLKVWDLSSN EHWSSIACRS TMIGHTDAVR CLQMDDEKII
     SGSYDKTLRT WDLKTGQQSA TFSGHEGEVL CLQFDRRKLI SGSSDRSIRI WDLRTQIAGM
     ILHNVHAKAV TCLQFNETQI VSASFDCTIK VWDVRTGRCF RTINWKENEG HTGVVRCLQA
     DRWRFVSGAD DKTLKVWNLN TGERICTLHS HTDGVTCLSF NDFRIVSGSY DTCVKLTMGS
     CSSEKKIAFS DSTVTLIAQG AEARIFKANF YGRPAVIKER FRKKYRHVAL DELLTKERMR
     AEIRGLMHCR KLGIPVPPIY FVDSKQNLIV FGAIEDATTL KNLLDGMHEV GAVGLVDNLA
     STIGQVLAKM HMNGVIHGDL TTSNLLVKQP LSPDNCRHVV LIDFGLSFVS SMVEDKAVDL
     FVLEKAFMST HPNAESFYRT ILDSYVKFYG KLGSEVLAQL EQVRLRGRKR LIVD
//
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