ID C5LV85_PERM5 Unreviewed; 681 AA.
AC C5LV85;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=Pmar_PMAR027985 {ECO:0000313|EMBL:EEQ99323.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EEQ99323.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; GG685819; EEQ99323.1; -; Genomic_DNA.
DR RefSeq; XP_002766606.1; XM_002766560.1.
DR AlphaFoldDB; C5LV85; -.
DR EnsemblProtists; EEQ99323; EEQ99323; Pmar_PMAR027985.
DR GeneID; 9045503; -.
DR InParanoid; C5LV85; -.
DR OrthoDB; 179296at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR010644; ChdC/CLD.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF184; SERINE_THREONINE-PROTEIN KINASE TRICORNERED; 1.
DR Pfam; PF06778; Chlor_dismutase; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Kinase {ECO:0000313|EMBL:EEQ99323.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW Transferase {ECO:0000313|EMBL:EEQ99323.1}.
FT DOMAIN 290..549
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 681 AA; 77526 MW; 1D49531D1462D4E0 CRC64;
MSSSPTDTTK AISDLPMAPL AIAGSVAAAL SAGVLIYRHR HQELPLPRSL RRIAPALLTR
AGGQAESAHF KMPVFDGPVL YEKGANGQKM DKRLYCQLYV LDCINAAKLP EAREKLQLEL
VRRNIPSVIY DDVNSPKTIG LLTWSEDPKH FPTVVNPVLQ LEGIGDVLEP RQGWTMLGKT
YSSGHEADLG DYLLQKVIRN VTMKDTEYAI WYPMRREGKF SMEKPGDQCQ MLLQHAAIGK
AYSKVGAWDV RLNCYGLDAA DNEFVIGLVH KELNPLSKLV EDMRKTEHTA LFMKSLGPFF
VGHRVFVREK STGNIYAMKQ MRKKDMDRKK QVHHVLAERD VLALAHTDWV IDLKYTFMDK
HFLYMVMEYL PGGDLMTHMI RKDKFTEEET RFYVAELVQA VDYIHTSLSY IHRDVKPDNI
LFDARGHIKL LDFGLSKYHP DLVTNLAGTP DYMAPEVFSG TGYDESIDWW SVGVIMYEML
FGGPPFSNET HDPLVTSRRV QNWRRYFHIP TSNGGCSPEA EDLLRRLICD AKDRLSFFSA
DAIRAHPLFA GLDWDHLREL EAPINETDTQ NFDDFPEEMH AGTHAFPSQG GAESRDRVDY
ITHYLFAHAE LISGHLPMAP VAKNDRYSES DVLEIFKLPS RPRGGGEVVV NLERIANTLM
SHLLTRDLLL RERRIHSERR I
//