CCR1_MAIZE
ID CCR1_MAIZE Reviewed; 626 AA.
AC P0C8M8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Probable serine/threonine-protein kinase CCRP1;
DE EC=2.7.11.21;
DE AltName: Full=Cell-cycle related Protein 1;
GN Name=CCRP1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Helentjaris T.G., Habben J.E., Sun Y.;
RT "Cell cycle genes and methods of use.";
RL Patent number WO0065040, 02-NOV-2000.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=18726113; DOI=10.1007/s00425-008-0805-2;
RA Lu T.-C., Meng L.B., Yang C.-P., Liu G.-F., Liu G.-J., Ma W., Wang B.-C.;
RT "A shotgun phosphoproteomics analysis of embryos in germinated maize
RT seeds.";
RL Planta 228:1029-1041(2008).
CC -!- FUNCTION: May play a role in the division of some cell types.
CC {ECO:0000250}.
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=2.7.11.21;
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;
CC -!- TISSUE SPECIFICITY: Embryo. {ECO:0000269|PubMed:18726113}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AX040998; CAC17052.1; -; mRNA.
DR AlphaFoldDB; P0C8M8; -.
DR SMR; P0C8M8; -.
DR iPTMnet; P0C8M8; -.
DR PRIDE; P0C8M8; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P0C8M8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; 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:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR Gene3D; 3.30.1120.30; -; 2.
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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..626
FT /note="Probable serine/threonine-protein kinase CCRP1"
FT /id="PRO_0000361269"
FT DOMAIN 36..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 478..546
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 579..626
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 399..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18726113"
SQ SEQUENCE 626 AA; 70234 MW; 6A317230B17F5EDD CRC64;
MDPKATSTSK TDNIDQITII EEKVNKIGTE PTIRKYSKGR MLGKGGFAKC YEVTNLENKK
VLAGKIICKA SLTKSRAKQK LISEIKIHKS LRHSNIVEFE HVFEDQENVY ILLELCPNQS
LHDLIKRRKR LTEIEVQCYT LQLICGLKYL HSRRVIHRDL KLGNLLLNDK MELKICDFGL
AAKLEFDGEK RKTVCGTPNY IAPEVIEGKG GHSYEVDTWS LGVIIYTLLV GRPPFETSDV
KQTYKRIKAC EYSFPDHVSV SDTAKNLVQK MLTLDPSKRP SLDEILQHPF LKNANNIPKF
LPASTLACPP STSYLNQFAS PENSVKVPSQ PAPKSAEATP LAAQKNGRFI NTQGSNMFGS
EKTLVTSPHS ATTQAHTNEN VVLTSQLDRH QTQGEKGWNF TKTGSWQSNL NGTQSVKGSS
RPQTVQQKGD LKSAQSLKAP ALLNNLGSRL RVSGSAVGSN RGQVLSGNEV WVKKWVDYSS
KYGMGYNLSN GTTGVFFNDN TKIVFNQKTD QVTYIQRGKN DRQDTVTHYS LTEYPKDLQK
KMTLLQHFKK YLEGSEYGGS ESINDGTETQ IGVYVKKWVK TKNATLFRLS NKTVQVHFTD
RTEIILNSEN KQVTYVARKE TEPISP
