PRP4B_DICDI
ID PRP4B_DICDI Reviewed; 811 AA.
AC Q54WE5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Serine/threonine-protein kinase prpf4B;
DE EC=2.7.11.1;
DE AltName: Full=PRP4 kinase;
DE AltName: Full=PRP4 pre-mRNA-processing factor 4 homolog B;
GN Name=prpf4B; ORFNames=DDB_G0279703;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000032; EAL67626.1; -; Genomic_DNA.
DR RefSeq; XP_641608.1; XM_636516.1.
DR AlphaFoldDB; Q54WE5; -.
DR SMR; Q54WE5; -.
DR STRING; 44689.DDB0216281; -.
DR PaxDb; Q54WE5; -.
DR EnsemblProtists; EAL67626; EAL67626; DDB_G0279703.
DR GeneID; 8622186; -.
DR KEGG; ddi:DDB_G0279703; -.
DR dictyBase; DDB_G0279703; prpf4B.
DR eggNOG; KOG0670; Eukaryota.
DR HOGENOM; CLU_000288_5_5_1; -.
DR InParanoid; Q54WE5; -.
DR OMA; GQFKEQH; -.
DR PRO; PR:Q54WE5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd14135; STKc_PRP4; 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 InterPro; IPR044092; STKc_PRP4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..811
FT /note="Serine/threonine-protein kinase prpf4B"
FT /id="PRO_0000355207"
FT DOMAIN 490..808
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 619
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 496..504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 811 AA; 93837 MW; AEAE8DE1C52B84EE CRC64;
MVIESEINDK KRGLESSSPT INDPKKVKVE SPSSGKEDGE VDEVTSSPAS RETSSSKLMS
PSKNQSSSSS RSYHDSNNGY RRKDERYSSS RSYDRNYRDR DISRDGDRER DRDRERDRDR
DRDRDRDRDR DRDRERDRDR DRDRDRDRDR DRDRDRERER ERDRDRNSQE RGSRNSHERD
YRDNRDYSRD SRDNMDSRDN KNGSRQSINN NTLSYEKQAD RKDEVRVKDN ISVNDDKTNH
GENLTNESIT ATSTNEPTKP AVIIEEDEET KTKRILEENR LQRQLIMEKY NKEQPQPITS
SLSTTEKEQS NTNTNSNSTP VATTTTSILA KSPSNLENQI EEEDESIIIE WRKDQNSENS
SAFNDNNNDE SCSSEEDLKK RGKIKEEDIK AKDKPITTTT TTTTINNVSI KLPPKPEPIK
AKTSAPVFDM FSDSPSDETD ESNRDLNETN GGGVMVDANI VVNPSINLSD NWDDADGYYK
FRVGEIMDKY QIFSPIGSGV FSTVVSAKET KTNEDVVIKI IRNRPSMHRS GLKEIEILQK
ISNTPTSSNQ KSHCIQMKDH FNYRNHLCIV FEPMSMSLHQ LIKKYGKDIG LSLNAVRVYA
KQLFLALKHI KNSKILHADI KPDNIVVNEA KNTIKIVDFG SAGEIHESEI TPYLVSRFYR
APEIILGHKY DYSIDVWSVG CCLAEFFTGK FLFPGKTNND MIRLFMEYRG AFSKKMLKKS
EFVSNHFNEN LVFMKQEIDN IEKTVRKVPH DITKPTKDIL QFLLPKNVSI PDQDMKKLIQ
LKDLIEKCTI LDPEKRITPF EALNHEFLKP F
