ID E9AX18_LEIMU Unreviewed; 1415 AA.
AC E9AX18;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Uncharacterized protein (Calcium/calmodulin-dependent protein kinase,putative) {ECO:0000313|EMBL:CBZ27504.1};
GN ORFNames=LMXM_24_1730 {ECO:0000313|EMBL:CBZ27504.1};
OS Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ27504.1, ECO:0000313|Proteomes:UP000007259};
RN [1] {ECO:0000313|Proteomes:UP000007259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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DR EMBL; FR799577; CBZ27504.1; -; Genomic_DNA.
DR RefSeq; XP_003875990.1; XM_003875941.1.
DR SMR; E9AX18; -.
DR GeneID; 13448949; -.
DR KEGG; lmi:LMXM_24_1730; -.
DR VEuPathDB; TriTrypDB:LmxM.24.1730; -.
DR OMA; SEFLYHR; -.
DR OrthoDB; 169197at2759; -.
DR PhylomeDB; E9AX18; -.
DR Proteomes; UP000007259; Chromosome 24.
DR GO; GO:0005929; C:cilium; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14008; STKc_LKB1_CaMKK; 1.
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; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR000433; Znf_ZZ.
DR PANTHER; PTHR24346:SF77; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE KINASE 1; 1.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 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:CBZ27504.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:CBZ27504.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 568..834
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1415 AA; 153563 MW; DF5E66F63C677905 CRC64;
MGCSTSTHAS PEADEDAPSK RSVYSASRTS GQVVSDHQNS NKDQANDACT AVSGNPSRTR
SSSGMEGRAH GRGIGAIHYP NQFGKDEFDG DEVVVAPLST DKSARTRFTF PPRTHLNAGS
HTEASDSGER KLNSTTASPS SLTALQRRLS DGGRNHSSFT AMPPIPPDAK ETLLQLTQTQ
ALQTAATTPT ARLSIPANGF AGSSASAPGA VALPSQEQHQ IEALHVNDGG FSIEWEEEDN
TPGGRGIPAS TTMESELYSV TRGTMAPSAS FGIGVGGVWR SKSPKWIDLS RKRSQSTVSL
LSLTDTPNNP HVLSSGSDFG RDILGGSHVF GGLATGGGSS RPQSGYAMSR AARVERFDQQ
RHGNGLAVFC NQPRECALCR SATVTFACEV CDDFFLCEDC RFDLEAVRAV HDPTHAMLSI
QDNHYNFSRT FGGDSIFSLS GDGGVSSLFY NPCFQCKRVI DDVEPVYRCD QCDYIVCQEC
FIQHEEPENA MERASSLSAA MAAMREERVS CKPLPIEFAA LALASGPTPP HEHELKRFQR
KSRSNSVHEG AVVTKTRNSG GNKVINDYVV VRQIGHGSYA KVKLVQHVHT QELFALKILR
RQKKAALSGI ILGRSRVKSA MAGISEDDLL REIAVMKFIG HPNVMRLKEV IEDVDSQKVY
IIMEYCEKGP VHVPGDPALP LEQVRRYGAD ILRGLLHLHS EFLYHRDIKP ANCLVNRDGV
VKIADFGTCN SQIRTRLAEG TPAFSCPEQV RGEEVSGEVV DSWAFALTVY EMACGTLPVS
TTSFVQHRLL LMSKDPIPIP KVGDEHLCNL LAQMLEKDLS TRLLLPAATR HPFFAECRVD
VHGAVPGTAP RSIFAVLATS GGSAAAQQQQ QQPSSLAELY DKALESVHRG KNLKDCFHGV
RALRRVRRKE VETARHSGTD DQAGGGGTGA EKGNAYVMNS RDVYSGSDGS GSDGEGEEGA
GRLRVCGRAG HEEEAAAAAV EEAVEHHLFS QEPNFELTHT TLTAPATLEK LNRLHQVTAE
MRLSHNALVR LAPLRLSAFS MLMDIAVTFN RLEAVPQEIL TAPRLVRLDL SHNRIDSIPG
SLVTKALFLE RLSLHHNLIT TVGTTTITVV EPSPVTFRAP TPATQTSLRG RGGSSRSEVV
SVLAAPCLRH VRLSGNPLER LPDALETTHK LQLVLDAIPA LMEEWDTHMQ TDCKTTTSTA
VAAAGGQSRL PAVIVWDDSF PVRIPSVEPA VWLAVNNMAI YRAQTLRLCK TRRVVLCQCA
DPRFPNGLFL SEELDVYFAA LSKALQECRE QRRQHLAAEA PFSFGATAEA IPREALPPIV
AKAARKYVES YFFVTDDENE EEGGYHSLVS YLYDSLSANI PVLVVVVSNG TSCAVRTNIV
AAISTCLTRL RGGDPEQLDA EQAELIVSTM RSLYA
//
