NIM1_NEUCR
ID NIM1_NEUCR Reviewed; 858 AA.
AC P48479; Q7RVM3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=G2-specific protein kinase nim-1;
DE EC=2.7.11.1;
GN Name=nim-1; ORFNames=NCU03187;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Protein kinase that plays an important role in mitotic
CC regulation.
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;
CC degraded as cells traverse mitosis.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80145.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L42573; AAA80145.1; ALT_FRAME; mRNA.
DR EMBL; CM002236; EAA36051.2; -; Genomic_DNA.
DR RefSeq; XP_965287.2; XM_960194.3.
DR AlphaFoldDB; P48479; -.
DR SMR; P48479; -.
DR STRING; 5141.EFNCRP00000003020; -.
DR EnsemblFungi; EAA36051; EAA36051; NCU03187.
DR GeneID; 3881436; -.
DR KEGG; ncr:NCU03187; -.
DR VEuPathDB; FungiDB:NCU03187; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; P48479; -.
DR OMA; MQSHDFA; -.
DR BRENDA; 2.7.11.22; 3627.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Kinase; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..858
FT /note="G2-specific protein kinase nim-1"
FT /id="PRO_0000086442"
FT DOMAIN 7..290
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 495..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 291..383
FT /evidence="ECO:0000255"
FT COMPBIAS 544..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 13..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 194
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 858 AA; 94347 MW; 8DA1B619E778E284 CRC64;
MSESDKYELL EKIGHGSFGI IRKVRRKADG MILCRKEISY LKMSQKEREQ LHAEFSILST
LRHPNIVGYY HREHLKATQD LHLYMEYCGN GDLGRVIRNL IKNNQYAEES FVWSIFSQLV
TALYRCHYGV DPPEVGKTVL GLGSTARPKP PSGGMTILHR DLKPENVFLG EDNSVKLGDF
GLSKVMQSHD FASTYVGTPF YMSPEICAAE KYTLKSDIWS LGCIIYELCA REPPFNAKTH
YQLVQKIKEG KIAPLPSVYS GELFATIKDC LRVNPDRRPD TATLLNLPIV RLMRKEKEVV
EFSRTLRTKE ETLNKRIREL DSKLSALETE KSSIRAEIDA SLRREWEVKA RLEIDRLVAQ
EIESLQQKFE QEVQARVEAE LQRHGRGPMF NSHGQQGSFS STAATLVSDY NLSSVGSGDG
DFPSTTDITD ISIAESTDGS DITKKIPRTP FHRAQTYSSA PAESVLGTPM DIEMASPSPI
TIASLSLSPR RMALTKAPTT NPRMIFGEEP TSTDKSNWEV PRETEMIDSG DESEAEALVP
SPKRITKSSK NPFSTVTTRS RPSLNSQQNS NVLPIHGLRS KQTLATRSKT VSGVSSIGQH
PLRSAPSAPS LRDRKPSPTR RLSRIPSVTG VGRRLSANNI NNSSNGGSDA PSSTVTSNIT
VRTRGLKRMS STCDESSFSQ QQNNQPQQSL PQAPPLKKIG LMAAKNIRGS SLVELHQARA
GGRPISAIIS NEAKLRAFKE HATIAASAVD SSSSSSSSSG QSQLPTRPRS QPQPITANFE
QQQQQQQSNT NSISSSNSAG SGSATGTGTG AGTKSMPWPV APVWNREVET EEMPSPFIVK
TSKRPASFVR PASNLSQS
