NRC2_NEUCR
ID NRC2_NEUCR Reviewed; 623 AA.
AC O42626; Q7RXF2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Serine/threonine-protein kinase nrc-2;
DE EC=2.7.11.1;
DE AltName: Full=Non-repressible conidiation protein 2;
GN Name=nrc-2; ORFNames=B1K11.130, NCU01797;
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 [GENOMIC DNA].
RX PubMed=9584090; DOI=10.1093/genetics/149.1.117;
RA Kothe G.O., Free S.J.;
RT "The isolation and characterization of nrc-1 and nrc-2, two genes encoding
RT protein kinases that control growth and development in Neurospora crassa.";
RL Genetics 149:117-130(1998).
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=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
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: Controls entry of the cell into the asexual developmental
CC program. Required to repress entry into the conidiation program.
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. Ser/Thr protein
CC kinase family. KIN82 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF034260; AAC21677.1; -; Genomic_DNA.
DR EMBL; AL669998; CAD21180.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA27239.1; -; Genomic_DNA.
DR RefSeq; XP_956475.1; XM_951382.2.
DR AlphaFoldDB; O42626; -.
DR SMR; O42626; -.
DR STRING; 5141.EFNCRP00000001908; -.
DR EnsemblFungi; EAA27239; EAA27239; NCU01797.
DR GeneID; 3872624; -.
DR KEGG; ncr:NCU01797; -.
DR VEuPathDB; FungiDB:NCU01797; -.
DR HOGENOM; CLU_000288_84_4_1; -.
DR InParanoid; O42626; -.
DR BRENDA; 2.7.11.1; 3627.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; 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:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 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 3: Inferred from homology;
KW ATP-binding; Conidiation; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Sporulation; Transferase.
FT CHAIN 1..623
FT /note="Serine/threonine-protein kinase nrc-2"
FT /id="PRO_0000086446"
FT DOMAIN 242..532
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 248..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 623 AA; 68628 MW; 17B3D2FB73E1ACE7 CRC64;
MPSTKNANGE GHFPSRIKQF FRINSGSKDH KDRDAHTTSS SHGGAPRADA KTPSGFRQSR
FFSVGRLRST TVVSEGNPLD ESMSPTAHAN PYFAHQGQPG LRHHNDGSVP PSPPDTPSLK
VDGPEGSQQP TAATKEELAR KLRRVASAPN AQGLFSKGQG NGDRPATAEL SKEPLEESKD
SNTVGFAEQK PNNDSSTSLA APDADGLGAL PPPIRQSPLA FRRTYSSNSI KVRNVEVGPQ
SFDKIKLIGK GDVGKVYLVK EKKSGRLYAM KVLSKKEMIK RNKIKRALAE QEILATSNHP
FIVTLYHSFQ SEDYLYLCME YCSGGEFFRA LQTRPGKCIP EDDARFYAAE VTAALEYLHL
MGFIYRDLKP ENILLHQSGH IMLSDFDLSK QSDPGGKPTM IIGKNGTSTS SLPTIDTKSC
IANFRTNSFV GTEEYIAPEV IKGSGHTSAV DWWTLGILIY EMLYGTTPFK GKNRNATFAN
ILREDIPFPD HAGAPQISNL CKSLIRKLLI KDENRRLGAR AGASDIKTHP FFRTTQWALI
RHMKPPIVPN QGRGIDTLNF RNVKESESVD ISGSRQMGLK GEPLESGMVT PGENAVDPFE
EFNSVTLHHD GDEEYHSDAY EKR
