ID L7FKH4_ENTIV Unreviewed; 1791 AA.
AC L7FKH4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Protein serine/threonine kinase, putative {ECO:0000313|EMBL:ELP86670.1};
DE EC=2.7.11.25 {ECO:0000313|EMBL:ELP86670.1};
GN ORFNames=EIN_007910 {ECO:0000313|EMBL:ELP86670.1};
OS Entamoeba invadens IP1.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP86670.1, ECO:0000313|Proteomes:UP000014680};
RN [1] {ECO:0000313|EMBL:ELP86670.1, ECO:0000313|Proteomes:UP000014680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP1 {ECO:0000313|EMBL:ELP86670.1,
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; KB206943; ELP86670.1; -; Genomic_DNA.
DR RefSeq; XP_004186016.1; XM_004185968.1.
DR EnsemblProtists; ELP86670; ELP86670; EIN_007910.
DR GeneID; 14885647; -.
DR KEGG; eiv:EIN_007910; -.
DR VEuPathDB; AmoebaDB:EIN_007910; -.
DR OrthoDB; 22132at2759; -.
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 CDD; cd13999; STKc_MAP3K-like; 1.
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; 5.
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; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM01411; Ephrin_rec_like; 11.
DR SMART; SM00261; FU; 14.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 9.
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:ELP86670.1};
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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ELP86670.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1791
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003973726"
FT TRANSMEM 1343..1372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1521..1787
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1791 AA; 192225 MW; DE48718EA16B2EBD CRC64;
MIFYVANTLL LILLTTKTNA AISCSSGQYL SGTSCYYCRA GTYSSGGTTT SCSFCSPGYF
SGSGSSLCKQ CSAGSYSSFG SSSCSKCSSG TYSGSGSSSC INCNAGKYAS SSGSSSCSSC
GAGTYSGSGA SSCTKCSAGY YSNFEASTCS KCEAGTYSGA ESSSCKKCNA GYYSVSGSSS
CTKCDAGTYS SNSGASNCQN CDPGYYSEKG ATTCAPCPVG YYSQFSVSAE CTECAAGTFA
DEQGSSECKV CGDGFFSKSG YSKCIQCVST SCKSCSKTTG ECTSCNVGYS YDSSNKNCSI
CPASYYSSGG TSLCSKCATG YYSLGGSSGC SACSTSCKMC DQTNGNCLSC NDGYFLNGKM
CDTCSAGTYQ SGGSCVTCAD MQYSLAGSTT CKSCSSTCSS CDKTNGYCTS CELGMGITTT
TCSICSAGTY NFLYKCEKCP IGTFSSSPKS LSCDTCRDGT YSSTPGSTNC KICDILCKGL
CERTNGKCNA CVSGAVLSTG VCSLCNSGTM ANQTTNKCDT CKAGTYAGEG SSECKSCGEM
TYSTAGSLLC QQCDSHCDGC DATNGYCVNC VTGYGLAAGK CTICPKGTYY LSSACQSCGE
MAYQDVEGQT TCKLCDSSCA SCNATNGKCL TCAAGYGFDS GVCTLCGDLT YSGGGVLQCQ
PCSTECKNCD RKSGACTSCE VGNKRVDNSC VSCAPSGYCD LCTDETSDGI CVSCGDGFYL
NSSDDCQPCS DIHEDCLTCS KTTKTCLSCA GNMISTGNSC VACEVGLVKV TETTCDYSYN
VIPKCQIADY VNNQHICTTC FAPYVTSSDL KACNLGYTTT TYYNTDDHKL HTNMNGCINQ
IDTTCYSCNT TIMLLNGVCN EKNEKCETYS QHGCDKCVSD VITSNNNCVV NTFCKYEINK
ENNTECLYCE YDVSCGKAKL NCGISNNEYC YSAVNGYHTT NNNIIEQCES EVCVISNGII
TDLKCQDDKL LIDGLCTTNT MCLAISSNDC IKCDAKHHLS QGKCSQNSAN CDNQNGDICI
VCNNTINVDG VCTDTQSIHC TSFDKVCVTC ESGYYKDVDG CKEKTGVLSN CGVVLSLNTK
CVECETNYNF DGISCVPQTL SNETTKQATK NEDTQTDSHC EVSTTKGCLR CLSGYYLADR
MCVKCEYPCV YCSNRTFCTK CDDYSYANSN GVCTEINELV GVCDVLMSTY RGCVVCKEGY
MRSSDGSICI NCDESCKSCT NEGNCVVCNE AFYRTSSNVT KLCSPQSELT SCANKTIVGC
MQCEGGYYLF NNLCVKCQDT CTQCNGIDEC TDCVKDNVLV SGVCINYTVI ENCVGSANNK
CSKCDDNYKL SDDMLSCIHT TNYGVVVGIP IVSVIILILI IICIIVVTII VIQKRKETKK
MEKICVFKMN RSNIAMSVLD NNILTNKKSL TFDDASEVIP VEKESRELLC VGNKGKGILK
VQITTRGGCD KYSIHTEPQL VTLKKGEACE FEIFVTPHCT MKLHDEMMIV TMNIVNSETV
SVPIAIEITT ENSTKLDYDE LKEDKKLGEG SFGIVYKGTY RGNVVAIKKL KEVGDNKGSM
EEFENEVSML DKFRSEYIVH FYGAVFIPSK VCMVTEFAQY GSLQDLIKKT KQEMPRFAVR
VKLMLDASKG ISYLHENNVL HRDIKPDNFL VFCIDNSTNV STKLTDFGSS RNVNMLTTNM
TFTKGIGTPK FMAPEVLERE KYKKPADVYS FAMTMYEAFT WDFAFKNTDV QFKHAWSIAD
FTTSGKRLQI PTSVPDKLGI IIQQSWEHEP KKRLEINNIT QKLEEFYNTI N
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