ID D2V6A2_NAEGR Unreviewed; 856 AA.
AC D2V6A2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Serine/threonine kinase {ECO:0000313|EMBL:EFC47536.1};
GN ORFNames=NAEGRDRAFT_78755 {ECO:0000313|EMBL:EFC47536.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC47536.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC47536.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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DR EMBL; GG738854; EFC47536.1; -; Genomic_DNA.
DR RefSeq; XP_002680280.1; XM_002680234.1.
DR AlphaFoldDB; D2V6A2; -.
DR STRING; 5762.D2V6A2; -.
DR EnsemblProtists; EFC47536; EFC47536; NAEGRDRAFT_78755.
DR GeneID; 8861602; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_78755; -.
DR eggNOG; KOG0198; Eukaryota.
DR InParanoid; D2V6A2; -.
DR OrthoDB; 5351614at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR025197; DUF4116.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR PANTHER; PTHR44167:SF8; OVARIAN-SPECIFIC SERINE_THREONINE-PROTEIN KINASE LOK; 1.
DR Pfam; PF13475; DUF4116; 10.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EFC47536.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transferase {ECO:0000313|EMBL:EFC47536.1}.
FT DOMAIN 114..408
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 856 AA; 97502 MW; 0C3542DFED5FF627 CRC64;
MKRKYEQDDH TTSLNGGGEE CEPTIKQAKA NTSPNINPHD QNKSIISDIK FEHDTKPHLR
YFLKLLEDFD DDHDNAKFSQ GITNSVLGYF NKFLNGLPEI IGSNNEQVDD GVKTWHAEKI
GAGGFGTVLK VIKRNSNGQN VKAIKVIPII STMGPNEAVS GAKLDHPNVV KVYNSILIRQ
TCCIEMEFIE MGSLQDLIKK KIKLPSIAIF KMMFQCCEVL LFMKQRGMVH SDIKPANILV
KKLDLNSNEV EVAIGDFGLT LLNDTVASQM RGGTTSYAPP EVLEVNEKGK RIFKANFKPT
FNTDLFSLGK TFRALFNNHD SDQFTTDILE MIEQLISSDI QQRAIGFYNI GFNGIIYFNN
KSLIWKNEKE LSAFSSLEYL MKDLTTLPHK NRDFILQNNI LQSAHKSLKQ DRNFLVEIVV
KDVRNLLTID ESVRTDKSFA IHVLERNETA FNYFDESLMR DREFINDIVG RNGLLLKYTT
FLNDREIVLT AFKNNREALQ YANESLRKDR EFVMSAIQHD GIVFTYADES FRKDREFVLA
AVQHKGLLLD SIDISFRKDR EIVLKSVKQN GLALEYVDKS LTKDIEIVTE AVKQNRFAIK
YADESLRKDK EIVLNAVAQN EHVLQIVDGS FVKKREIVLK AVKQNGLTLE SADKELRKDR
EIVLESIQQN GLALKYADEM LRRDKEIVMR AIQQNRLAIN FVSESLRKDR EFASETVQRD
GLLLECMHKS IKNEKEIVMK AVQQNGLALK YANEKMKKDR EIVTTAVQQN GLALEYADRS
LRKDSAIAIM AVSQNGLALE YTDKSLTKDR RVVMEAVQQN GLALGFAANS FKQDQEIVTK
AIQQTPNARF FSLIKN
//
