ID A0A0A1TXQ1_ENTIV Unreviewed; 1998 AA.
AC A0A0A1TXQ1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Protein serine/threonine kinase, putative {ECO:0000313|EMBL:ELP86152.1};
DE EC=2.7.11.25 {ECO:0000313|EMBL:ELP86152.1};
GN ORFNames=EIN_328190 {ECO:0000313|EMBL:ELP86152.1};
OS Entamoeba invadens IP1.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP86152.1, ECO:0000313|Proteomes:UP000014680};
RN [1] {ECO:0000313|EMBL:ELP86152.1, ECO:0000313|Proteomes:UP000014680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP1 {ECO:0000313|EMBL:ELP86152.1,
RC ECO:0000313|Proteomes:UP000014680};
RA Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KB207015; ELP86152.1; -; Genomic_DNA.
DR RefSeq; XP_004185498.1; XM_004185450.1.
DR EnsemblProtists; ELP86152; ELP86152; EIN_328190.
DR GeneID; 14885104; -.
DR KEGG; eiv:EIN_328190; -.
DR VEuPathDB; AmoebaDB:EIN_328190; -.
DR Proteomes; UP000014680; 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:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 9.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR45756; PALMITOYLTRANSFERASE; 1.
DR PANTHER; PTHR45756:SF1; SERINE_THREONINE-PROTEIN KINASE DDB_G0278665-RELATED; 1.
DR Pfam; PF07699; Ephrin_rec_like; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00181; EGF; 11.
DR SMART; SM01411; Ephrin_rec_like; 15.
DR SMART; SM00261; FU; 16.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 8.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Kinase {ECO:0000313|EMBL:ELP86152.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW Transferase {ECO:0000313|EMBL:ELP86152.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1554..1584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1731..1997
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1759
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1998 AA; 215260 MW; 5FB14E03C387F5E5 CRC64;
MYCGGGQYEN GGSCRACPVG TWSHGGYGIT SCTPCSWGES AVVGSYDCVA CKAGYYANSS
VSSCPICPAG TFSPAGASKC TYCGGGQYQP SSGSSKCKVC TAGTYATNGA ATCSNCPAGS
YSLDGASFCP SCSAGYSSYS GSSSCYKCSA GTYATSGSSS CYSCSAGTYG PSSGASSCYS
CSPGTYSSSG STSCSSCPAG KSSNGGASSC TPCSAGTYSS SSGSTSCGTC SPGTYSSSGS
TSCSSCPKGT FSNYGSSSCS NCPAGTYGST TGLSSCPSCS AGYYSSSGST SCSICSAGKY
SSSGSSSCTS CSAGTYSSTS GSPSCTLCTA GKYSSSYGST SCSTCPAGTF SSSGSSSCSV
CSAGTYASSG ASSCTKCSMG YYSSSSGFST CISCPAGKYS SSTGSTSCST CPAGKYSSSG
ASVCISCPSG QYSASSGSSI CTKCPAGTYS SNGSSACSSC KDGEYSLSGS SICKICNSTC
ATCYITNGNC KTCKPGYAYT PSTGCTICQA SYFSIGGTSS CSKCPSNTYS LEKSSECLSC
SDKCATCNQM NGNCITCVNG YGLEAGVCKL CPAGTFANSS SCVTCGDMTY SLGAQTYCDN
CDTICKTCDK TNGHCTSCYS GKGISGNSCV VCQAGYYSLN NQCEKCPLGT FTDSNGKDNC
ETCGDYNFVN VTGSTTCLPC DTLCAVQCEK TSGNCSTCVG GYVATEGVCK MCLGGTKSNS
ITNLCDKCPA GTYSNNKSSS CSNCKNLEFS LKGSSSCQTC NSVCRECNST NGNCTACFDG
YGISNSFSCE MCQEGTFSFD SKCTNCEEMN YQDEKGKTTC KKCNSSCSTC DKTNGKCTNC
KAGDGFNKTE GSCTTCTPKT YSTGNTSECV SCQSECTNCF KETGYCSSCE DGFKTKENKC
VSCSLNGNCT SCNTTGDEQN WVCKKCENGL YLDNNNCILC EEIAHCASCS QTQKECLYCH
EDYVTDGNKC FKCEEGKVKN GDKTCIDICY LIPNCKNGYY DNATLKCTEC FEPFELTSDS
LSCFANKDYQ KFYYDKQTNT FKENDVNCTN QIYSTCYVCQ DSILLNGKCE KFDDNCKNSA
IKGCDLCKDS ILTSSNNCTK DEKCKYQLNK NDTMECLQCV NDTVCGLKEE ECSISQNSYC
YTTKEGSYTN KNDIIPCESG KVCALIDGKE LDFECEKETI LTRNNVCTKD PNCLISKGNY
CVKCVDDYHI YNGWCELNNN DCDTQNRDFC VWCKSHIGDG HECYNQTKIN CPSFNDTCVK
CEENNYKTET KCELIEDVFP NCKNVYKMCV DCQENFILES GDCLHKNETN TSSETNETTK
TTFKNENDSN CIEKTTKGCV RCSDTYYLKD YKCIKCEYPC VKCKNLTYCT GCDAYSYTNN
KGECIEINDL LSKCDLVMAT YTGCVVCKDG YMRSSDGKTC EKCHMSCKTC TNDGTCISCN
NEYYRTATNN TKYCTIQSEL NNCLNKTISG CYECDNGFYI SNNLCKPCNE KCTTCTSLDY
CTNCTENNVL LNDICTSFTE IPNCISASSN KCDKCAEKYQ LNTNKYVCED QTNYGILIGI
PIASFVLILF IIAIIITILI FVILHKKEEH EMVNVCVFKI DRSNIRMTDL DKGIVSNKKQ
LIFGEGVLNP VEEEVRELIC IGNTQHRNLK IQFTTKDLCD KFKVRTSPQI VNLKRGEACE
FEVFLTLFCT TDLEDEILLI SLDLKSGQKV MTPIKIYAKT ELSTKLDYEE VKVDKKLGEG
SFGIVYKGTY RGNVVAIKKM KQSMNEDGKE KEFRNEVSML DKIRSDYIVH FYGAVFIPKK
ICMVTEFAQF GSLQDVLKRM KGVEVRMKLR FKVCLDAAQG IQYLHTNGIL HRDIKPDNFL
VFSLDYGDEI TAKLTDFGSA RNINLLMTNM TFTKGVGTPK YMAPEVLDRK KYKKAADVYS
FAVTMFEVLG WCEAFDKNDE RFKFAWNIAD FTSAGKRLVI PETIPEQARN LIENGWKQDT
KDRIPIETII DDLQQFLK
//