ID SRPK_PHYPO Reviewed; 426 AA.
AC Q45FA5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Serine/threonine-protein kinase SRPK {ECO:0000303|PubMed:19657567};
DE Short=PSRPK {ECO:0000303|PubMed:19657567};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q96SB4};
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAZ29249.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=19657567; DOI=10.1093/abbs/gmp054;
RA Liu S., Kang K., Zhang J., Ouyang Q., Zhou Z., Tian S., Xing M.;
RT "A novel Physarum polycephalum SR protein kinase specifically
RT phosphorylates the RS domain of the human SR protein, ASF/SF2.";
RL Acta Biochim. Biophys. Sin. 41:657-667(2009).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, MUTAGENESIS OF 318-PRO--LYS-323 AND LYS-320, AND
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=19703313; DOI=10.1186/1471-2091-10-22;
RA Liu S., Zhou Z., Lin Z., Ouyang Q., Zhang J., Tian S., Xing M.;
RT "Identification of a nuclear localization motif in the serine/arginine
RT protein kinase PSRPK of physarum polycephalum.";
RL BMC Biochem. 10:22-22(2009).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF LYS-86 AND ASP-188.
RX PubMed=21149255; DOI=10.1093/jb/mvq141;
RA Zhang Y.X., Xing M., Fei X., Zhang J.H., Tian S.L., Li M.H., Liu S.D.;
RT "Identification of a novel PSR as the substrate of an SR protein kinase in
RT the true slime mold.";
RL J. Biochem. 149:275-283(2011).
CC -!- FUNCTION: Phosphorylates serine/arginine-rich protein PSR.
CC {ECO:0000269|PubMed:19657567, ECO:0000269|PubMed:21149255}.
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:0000250|UniProtKB:Q96SB4};
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:0000250|UniProtKB:Q96SB4};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19703313}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000255}.
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DR EMBL; DQ140379; AAZ29249.1; -; mRNA.
DR AlphaFoldDB; Q45FA5; -.
DR SMR; Q45FA5; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14136; STKc_SRPK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR47634; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47634:SF9; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..426
FT /note="Serine/threonine-protein kinase SRPK"
FT /id="PRO_0000409664"
FT DOMAIN 56..419
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 318..328
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:19703313"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 62..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96SB4,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 86
FT /note="K->M: Essential for activity."
FT /evidence="ECO:0000269|PubMed:21149255"
FT MUTAGEN 188
FT /note="D->A: Essential for activity."
FT /evidence="ECO:0000269|PubMed:21149255"
FT MUTAGEN 318..323
FT /note="Missing: Eliminates nuclear localization."
FT /evidence="ECO:0000269|PubMed:19703313"
FT MUTAGEN 320
FT /note="K->T: Eliminates nuclear localization."
FT /evidence="ECO:0000269|PubMed:19703313"
SQ SEQUENCE 426 AA; 48772 MW; C517C73592EDF018 CRC64;
MENIFKEKEK GKEKAKEEEK ENDSGDLFDS EDEGTEDYKK GGYHPVKVGE VYKSNYRIVK
KLGWGHFSTV WLAIDEKNGG REVALKIVKS ASHYREAAED EIHLLQTISE GDPESKYCVV
KLLDSFLHTG PHGKHICMVF EKLGSNLLDL IKLHNYKGIP LPLVKCMTKQ ILIGLDYLHT
KCKIIHTDLK PENVLLDHLL RPDTLNWDDQ FLDGASSSSP ISNDAENARQ TRSGKIKWEP
SARIADSLSR KIVKVPIVKI ADLGTACWTH KHFTDDVQTR QYRCPEVILG QKWDTTIDMW
SLACMVFELA TGDLLFCPKK GDKYDKTDDH LALMIELLGR MPRSFITKGS KSEKYFNSKG
ELKYIRKLGP QWGMSDVLYE KYRFPKEEAD KLSAFLLPML QYEPEKRATA RDSLEHPYMA
DVPPFL
//
