ID K2GHK9_ENTNP Unreviewed; 1961 AA.
AC K2GHK9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Leucine rich repeat-containing protein {ECO:0000313|EMBL:EKE42166.1};
GN ORFNames=ENU1_030300 {ECO:0000313|EMBL:EKE42166.1};
OS Entamoeba nuttalli (strain P19) (Amoeba).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=1076696 {ECO:0000313|EMBL:EKE42166.1, ECO:0000313|Proteomes:UP000006769};
RN [1] {ECO:0000313|EMBL:EKE42166.1, ECO:0000313|Proteomes:UP000006769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P19 {ECO:0000313|EMBL:EKE42166.1,
RC ECO:0000313|Proteomes:UP000006769};
RA Hannick L., Karamycheva S., Lorenzi H., Caler E.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH925575; EKE42166.1; -; Genomic_DNA.
DR RefSeq; XP_008855502.1; XM_008857280.1.
DR EnsemblProtists; EKE42166; EKE42166; ENU1_030300.
DR GeneID; 20071676; -.
DR VEuPathDB; AmoebaDB:ENU1_030300; -.
DR OMA; REIYICY; -.
DR OrthoDB; 24392at2759; -.
DR Proteomes; UP000006769; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056:SF81; LEUCINE-RICH REPEAT CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 677..828
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1687..1958
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..50
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"
FT COMPBIAS 28..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1961 AA; 226883 MW; 8924F9A5F4EA95AD CRC64;
MEKDSTKHRK KNNNVPSSQE IKSKGKKNET SLSFTQPNTP KGTSTIYSSY SEDKYDSPRI
TESSLNPKTF KGIPNVVDNS IKYLRDTLIL NTLYHRSIEQ WDNEEIYSLN FVQNIPALKQ
LLSTLNNPKT ILQFNYQDFI NNKLNIFESQ RVIHYISQLR MLPNIFKHLT SLTYFDTADI
KYVFNLLHRY KNGSSINLYQ EANPFIVLIL LKYFFLSLPQ SFFCDKLIIE LLSLINSSST
DSEISSTSNR GIQCYSCSSE HTKSSDETTN SNDAVGLHAL SPKKGCKEKE IKMVLKQYLD
IEEQLIFQEI IELIIDIKEV YGNEEGSYCT KFFFDCFSPE YSFEEPIYSV IPSLYTKHKY
ESLFLFDSED SYIGEITKCI FDNVRCPLSV LNEPLTCQEV TIPGKLAITN YRIIFIPSVN
LDVQRKAILG RFSQCPLNNI IEKKLIEIEG HSIEYAMRII TTNYSILTFF SFDNIFKIID
KVIDEIINEG IHCIFVNSNL KYPVNNTTDW KNRIKRYHWE IFKINENNDK LPFNAPLIET
NIKCSETNRE IYICYHIINT GANLYRLTIP FIKNLKNEIT VDIINDEKIK CVEVNISDLE
TFDKTFNDIL NNLSNNKDSL NYRIFIEKVG KVNTFVTHFL LICEEIISLL NRGKSVLLIP
KNLKENEVGL FSGFIEIILD PYFRTFNGFI EMIHCEFSSL HFDFEIQRNS FCFFFVCLFL
LYKTYPTQFE FNESLLHFIF YHYNSRVFKD FNQNDMSSLQ SYIQSHLNDF KNEFYESTLE
VIPLQFIKVH FCNEIFCQVQ TYNPQTVAKL LQNCRTGDLN LQEMNLFFFP IHPSFPVLNG
ITKLDLSNNK INDFPTEIGK LTGLIELNLS QNKLIILNDI VSKLTLLTLL NIANNNLSSI
PKSITTLNII NLDISNNDLQ RLTSVNFPSS IQRLSLRSNF FSSSISNLQL TYLDISETHG
LEQGDFALSL PKSLVELILN KCFIEHVPLS ISKLTNLERL DLSMNEISNL HPSFFTMTQL
KQLNLKKNPI PQISIMFTRL VCLTNLLIDD IVSIPTVMKD MFPERVIKEK VIKKVNDEEF
QVFLTGDISK SEILSLLAKK SGKEIDGRSF LLEKNIIVSD IPCEVIEENP FLILKNSVFV
ICKRVTKAKT NAVPFSRLLS FFSFIRLKQP IICVSVRVNE ETLLKQDDSI QEKLKTTYPE
LKVSFTYFDI NGKDKQIKDF LKVIKNATEQ CKINISPLTI KVIDELKYID TIPGILEMDY
LKMLMESLCI NNSQCKLIID TLQTLNQIFL YPETYSTKLS NYTIHILNKR PHKNHFVLLS
YQLPEIIYQI LSKNETSIGI QLPDFFLNAE IPHLTLEQQE YILILLEYFQ IIFVLRKSFF
ERIGLADEYE QLNRCVNNPN LMTKYTSQSM SKSTNETILS QSTRLPFNNS TNSLTTIPLK
KSSSFKKHGR TPRLQLPIES LSPTSGSPFS RSPRGSRIEV TDKKQTLPKV MILNYYGLSP
NMEDKLWEEC KKDEVEIGRC YRYNCLPIQF CMMLYSLLTV KYAVIRGWRG GILCNITIEE
SHYQLLVEWD LDKLRISFRL KIIVSGVNSF LRTKDIWQEI KILHDITMKY FPQIISTCDV
LCPHCLTKLV SVDNCYCISM DEIDETLQCG LFADTFGEHC IAFALNCWDV LVNILEMKKE
PIKKEDIEIL STITHGSSSQ INLCKVKGFN ENVVVKEMEI DLTGMLMNGD DYVSYYIDRV
EDFLRECEFL TFPESPYIAK IYGYCLNPLS IVMEYFNGGS LFQYISKNHN IPWKERIQIA
ISIAKGMTVF TNQKCPVVHR DLKSPNVILK INKEGKITQV AITDFGQSIP TFAENFKSCH
CVECLYWLAP EVIETSTFEL ESDVYSYGMI LWELSTLSAP FPQFNFMEEV RSFIMSGNLL
EIPPSPYPEF DSIIADCWKV AKARPSFAAL VVKLTKIYKQ M
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