ID K2M0N6_TRYCR Unreviewed; 716 AA.
AC K2M0N6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Serine/threonine-protein kinase PLK {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
DE AltName: Full=Polo-like kinase {ECO:0000256|RuleBase:RU361162};
GN ORFNames=MOQ_007752 {ECO:0000313|EMBL:EKF28498.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF28498.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF28498.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF28498.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF28498.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHKC01015623; EKF28498.1; -; Genomic_DNA.
DR AlphaFoldDB; K2M0N6; -.
DR EnsemblProtists; EKF28498; EKF28498; MOQ_007752.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000007350; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50078; POLO_BOX; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361162};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007350};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 48..302
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 512..590
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 638..704
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 716 AA; 81358 MW; 3BBE54AB0D9881E3 CRC64;
MHQPQAQQPL MPARRFPSAQ QPLSEKPDFH EGSTLKEFDK QGRVVGRFRC GRLLGRGGFA
KCYEVERDGE SYALKVVDRS ILQKTKTLQK LHSEISIHRR MKHKNIVNFI RTFQDDWNVY
MLLEKCSNQT LMEISKRRPR FSVPETQHIM LQALAAIHYM HDQCVIHRDL KLGNMMMDAE
MNVKIGDFGL AAELQYDGER KRTICGTPNY IAPEIIDSAH EGHSYEVDIW SLGVILYTLL
VGEPPFQTSD VKATYRRIKQ CRYEFPPRLD IPESGKELIH RILQSRPDHR PTLVEIRTHS
FFRFPTPPSS APLSLFPSSR RRMEVEGQQQ PQKTWKGSET APAAKTQREI LRPLNTNTVA
PGRQPAQPGG ASQALFFGGT VPSACNQGKV EEAGDPPCVD SARPSPRGLP KGERHVTAPR
SKYHLLDDEE RNHLTVVHDH LQRTLLGEVD PYGGEKPLMS LPPHNTGKVP KPPTMTATTK
AGGGGIEKVE EDRGVKNEFP LPSVWVTDYA DFSAKYGLCY RLSTSHTGVH FNDSTKMVWE
PITGRVEYYA RVKEVVPHNN GGVVHARDQR QAFHMETFPE SLNKKVTLIK YFKSYLSRTR
NGCEGVEVVR CSPYMDPTPV LLSEPHMIED IVYVKRWLLT PHAMIFRLSN KTIQVCFHDK
AEVILSSESR VVTYTDASGH RITVPLYSAT SHSNEIASRL RYTKDILCEL IQNREL
//
