NIMA_EMENI
ID NIMA_EMENI Reviewed; 699 AA.
AC P11837; Q5AQC6;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=G2-specific protein kinase nimA;
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis;
GN Name=nimA; ORFNames=AN9504;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3359487; DOI=10.1016/0092-8674(88)90385-6;
RA Osmani S.A., Pu R.T., Morris N.R.;
RT "Mitotic induction and maintenance by overexpression of a G2-specific gene
RT that encodes a potential protein kinase.";
RL Cell 53:237-244(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP CHARACTERIZATION.
RX PubMed=7889945; DOI=10.1002/j.1460-2075.1995.tb07080.x;
RA Pu R.T., Osmani S.A.;
RT "Mitotic destruction of the cell cycle regulated NIMA protein kinase of
RT Aspergillus nidulans is required for mitotic exit.";
RL EMBO J. 14:995-1003(1995).
RN [5]
RP PHOSPHORYLATION AT THR-199, AND MUTAGENESIS OF CYS-38; GLU-41; TYR-91;
RP THR-199 AND LEU-304.
RX PubMed=7629122; DOI=10.1074/jbc.270.30.18110;
RA Pu R.T., Xu G., Wu L., Vierula J., O'Donnell K., Ye X.S., Osmani S.A.;
RT "Isolation of a functional homolog of the cell cycle-specific NIMA protein
RT kinase of Aspergillus nidulans and functional analysis of conserved
RT residues.";
RL J. Biol. Chem. 270:18110-18116(1995).
CC -!- FUNCTION: Protein kinase that plays an important role in mitotic
CC regulation. Seems to be phosphorylated and thereby activated by
CC CDC2/cyclin B during mitotic activation. It is also required for
CC spindle formation and for nuclear envelope breakdown.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Accumulates when cells are arrested in G2 and is
CC degraded as cells traverse mitosis.
CC -!- PTM: Recessive mutations of NIMA cause a specific cell cycle block in
CC G2 at restrictive temperature due to lack of phosphorylation that
CC normally activates the G2-kinase. {ECO:0000269|PubMed:7629122}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; M20249; AAA33316.1; -; mRNA.
DR EMBL; AACD01000214; EAA60031.1; -; Genomic_DNA.
DR EMBL; BN001303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A43734; A43734.
DR RefSeq; XP_868886.1; XM_863793.1.
DR AlphaFoldDB; P11837; -.
DR SMR; P11837; -.
DR STRING; 227321.P11837; -.
DR iPTMnet; P11837; -.
DR PRIDE; P11837; -.
DR EnsemblFungi; EAA60031; EAA60031; AN9504.2.
DR GeneID; 3684103; -.
DR KEGG; ani:AN9504.2; -.
DR VEuPathDB; FungiDB:AN9504; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; P11837; -.
DR BRENDA; 2.7.11.22; 517.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:AspGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:AspGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:AspGD.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:AspGD.
DR GO; GO:0043987; P:histone H3-S10 phosphorylation; IDA:AspGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:AspGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:AspGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..699
FT /note="G2-specific protein kinase nimA"
FT /id="PRO_0000086443"
FT DOMAIN 11..295
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 386..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:7629122"
FT MUTAGEN 38
FT /note="C->S,A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:7629122"
FT MUTAGEN 41
FT /note="E->G: In NIMA7; block in G2."
FT /evidence="ECO:0000269|PubMed:7629122"
FT MUTAGEN 91
FT /note="Y->N: In NIMA5; block in G2."
FT /evidence="ECO:0000269|PubMed:7629122"
FT MUTAGEN 199
FT /note="T->A: Great decrease in activity."
FT /evidence="ECO:0000269|PubMed:7629122"
FT MUTAGEN 304
FT /note="L->P: In NIMA1; block in G2."
FT /evidence="ECO:0000269|PubMed:7629122"
SQ SEQUENCE 699 AA; 78913 MW; 50FDC86E249ABC99 CRC64;
MAIALAEADK YEVLEKIGCG SFGIIRKVKR KSDGFILCRK EINYIKMSTK EREQLTAEFN
ILSSLRHPNI VAYYHREHLK ASQDLYLYME YCGGGDLSMV IKNLKRTNKY AEEDFVWRIL
SQLVTALYRC HYGTDPAEVG SNLLGPAPKP SGLKGKQAQM TILHRDLKPE NIFLGSDNTV
KLGDFGLSKL MHSHDFASTY VGTPFYMSPE ICAAEKYTLR SDIWAVGCIM YELCQREPPF
NARTHIQLVQ KIREGKFAPL PDFYSSELKN VIASCLRVNP DHRPDTATLI NTPVIRLMRR
EVELNNLSRA ARKREEATMQ KAKDVEQAFA KLEKEKQQIR SELENSIRRE WEVKARLEID
RQVQNELDKL RKRFECEVQD RVAQEVEKQR RNANYREDAS LRSSGHSSQM SSSNSEDSDF
PSSTDISQLS LESPTNKAAK LPKKESRTPF TRSKTVVDSP MDIQMAEPSP ISIASLSLSP
RRTSATYSGK NIFAEGERKR PKFEPTLAYS DDEDDTPELP SPTRPKVKPD PFKAPSRPLL
RQNTTALMQK LSTQPPIFPA NPSRLPQMSA PDVRESKSRS PHRRLSKIPS SANLAADAGS
PTRKNGVKSS PSKMNGGDEM FKAVMQRNMG GRTLVELAQA RAGGRPIDEV KRCASDSRSG
CSVPMKSADR DPPAVWDPER DEMPSPFLAR GRKVIRNLR
