ID A0A0N4VGZ0_ENTVE Unreviewed; 1642 AA.
AC A0A0N4VGZ0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=EVEC_LOCUS9436 {ECO:0000313|EMBL:VDD94685.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0001007901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0001007901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD94685.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) 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};
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DR EMBL; UXUI01010048; VDD94685.1; -; Genomic_DNA.
DR STRING; 51028.A0A0N4VGZ0; -.
DR WBParaSite; EVEC_0001007901-mRNA-1; EVEC_0001007901-mRNA-1; EVEC_0001007901.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:InterPro.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR016255; Gcn2.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042:SF197; EIF-2-ALPHA KINASE GCN2; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF05773; RWD; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 4.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000274131};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..146
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 510..922
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 581..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 769
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 516..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1642 AA; 184570 MW; 0E8B94495B7CC176 CRC64;
MCIVKAVKLC ILAYLQQQCL GGKNWLSVRD FLLILNIVFF NVVSAVNYTV FKQLWRPLDL
VIHLHPAYSG PANDFTAFVS IDLHITCSDD YPLKSAPKVF LENPKGLSDG DVKKLNCILT
KKSDEMLGSE VVLELCQIVE DFLSKNNKPP EGSFHDGMLR EKAAAEHEIK KQKATTEQRE
REEIAAFQEI RREKLLWKEA ENYERTSNRH LSIFSSELLC CIDGVERRIC PSSSSGPRAL
SNNIYKEYSA HVFDTGSEVL VTEWRFIYSL GRRGALRKAD FRVQPFLEKL SALEDQMLRL
TKWKVASQNL CSYSFFSVLK NSVSPTKVDV RILLAQSVGS GDTVLSRCAT DLLFRPTVLS
KLAAQTLLAL KSLHCQQLLH SNLSPDTIWV TTNESFQTSD YYLIPFIEEV REAFESGAGK
DDLSTKRSFS RKDDILQLRN LLQAYSSKLS DGKFKDSLYS FLLACASAES IEELVDHPFL
LCVESPSFAA SMLNNEGINF DGSNRLKNEF VYLDFLGKGG FGDVVLARNK LDGNDYAIKR
IPLDPRDEKL NRKVMREAKL FSGLCHTNVV RYFSAWIEHV PKPSSPSRST TAEKAEEGER
QSSCENSMLP ANLRNIESRV ADIPVESAAE WSTSFHKLDV HSSSSTSGSD DEELPFFKKN
HSSNVISTTN NSDFEILFEE NEVREAVGEI SERELAESDE KSRGTDSASS LDLGFRVLYI
QMEYCEQSTL RSLIDSGELS AIPRRIWQIL KQILLGLQYI HQEGMIHRDI KPMNILIDGT
GTAKIGDFGL ATRNYLERQS ACTISSEKEE SLTKDIGTAL YIAPELLSTS GLKVDYTAKI
DVYSVGIVLF EMFYRPLLPG MERISILKTL RNCFFFPDDF ATEVPEVHRK TAKDLIKLML
TLSPDERPSV RDVLESERIP LIELEESEFQ KIFSQTYRSR NSKLRQWMLD TMFSEPVPQA
VDFLYDQFIC LPKNSLGIPA VRAMDMIEQQ LSKICLNHAF VKFPAHSIVP SRLSPSAVSR
MKECKFIDDC GTSVSLPFDL RRAFVRYCVR NGINRLKRFH SGKVYGYTDE LAGTHPAERS
EFSVDYLGPH SSSPLLDAEI LIITLEAVSC IELFQSFKWE LKVGHLSLIA AAATYLGYSD
SSAQMKILNA LHKISSSEEL LNKKQRIDRL QTCAEMSQNQ ATSLLSILEG DEFTMNALRE
RFRPLLRSRN DMVREFAKKG LDDLTSCCGI LETFSDMTDR VIFDSSLCCR PSTFSNGLVF
QLTILYPRKR GGMRPVVICY GGHYEGMLEQ ERRGRDPAPP TPTCLVGCGF IMDSLAKLHC
ARFPGFGKSL CSALVCSVSS ELIMEEVCLV RLLWENNISA DILYDPVSSV HELGLLEHCS
EKEIGNILIV TDRNEVFLRS HNTDYGKLSF SDAVAKIDSA GENGTVSSCE IMARSRQATN
SSSVATAANI SIHFATSEKL AYNTRKRIEV QVPLFMQKTL ANFSSSARIE VVVCDLPSDA
VRQLVAAIDR NLSLEELHVV FDNLSLQLNK YKKGLKFIHE TLENAVLFGR QTWLKAIFRF
FGVLSKSIFA PIDFPEGTTK SVIGDGRGRR LAVRGERELQ STRGWELHCG PVQVVSTGDD
NDGASDDDVG HHCSIHFAAY NK
//
