NMR1_NEUCR
ID NMR1_NEUCR Reviewed; 488 AA.
AC P23762; Q1K7K4; Q9C226;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Nitrogen metabolite repression protein nmr;
DE AltName: Full=Negative-acting nitrogen regulatory protein nmr;
DE AltName: Full=Nitrogen metabolite regulation protein;
DE Short=NMR;
GN Name=nmr; ORFNames=B7A16.230, NCU04158;
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].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=2146484; DOI=10.1007/bf00283032;
RA Young J.L., Jarai G., Fu Y.-H., Marzluf G.A.;
RT "Nucleotide sequence and analysis of NMR, a negative-acting regulatory gene
RT in the nitrogen circuit of Neurospora crassa.";
RL Mol. Gen. Genet. 222:120-128(1990).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-310.
RX PubMed=1834354; DOI=10.1007/bf00318516;
RA Jarai G., Marzluf G.A.;
RT "Generation of new mutants of nmr, the negative-acting nitrogen regulatory
RT gene of Neurospora crassa, by repeat induced mutation.";
RL Curr. Genet. 20:283-288(1991).
RN [5]
RP MUTAGENESIS.
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=2148799; DOI=10.1007/bf00633823;
RA Jarai G., Marzluf G.A.;
RT "Analysis of conventional and in vitro generated mutants of nmr, the
RT negatively acting nitrogen regulatory gene of Neurospora crassa.";
RL Mol. Gen. Genet. 222:233-240(1990).
RN [6]
RP INTERACTION WITH NIT-2.
RX PubMed=7612627; DOI=10.1021/bi00027a038;
RA Xiao X., Fu Y.H., Marzluf G.A.;
RT "The negative-acting NMR regulatory protein of Neurospora crassa binds to
RT and inhibits the DNA-binding activity of the positive-acting nitrogen
RT regulatory protein NIT2.";
RL Biochemistry 34:8861-8868(1995).
CC -!- FUNCTION: May be a redox sensor protein. Negative transcriptional
CC regulator involved in the post-transcriptional modulation of the GATA-
CC type transcription factor nit-2, forming part of a system controlling
CC nitrogen metabolite repression (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with nit-2. {ECO:0000269|PubMed:7612627}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Tyr residue in position 211 in the active
CC site triad of Ser-Tyr-Lys necessary for dehydrogenase activity,
CC suggesting that it has no oxidoreductase activity. {ECO:0000305}.
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DR EMBL; AL513445; CAC28734.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA32078.3; -; Genomic_DNA.
DR EMBL; S64286; AAB20268.2; -; Genomic_DNA.
DR PIR; S11910; S11910.
DR PIR; T46600; T46600.
DR RefSeq; XP_961314.3; XM_956221.3.
DR AlphaFoldDB; P23762; -.
DR SMR; P23762; -.
DR STRING; 5141.EFNCRP00000003932; -.
DR EnsemblFungi; EAA32078; EAA32078; NCU04158.
DR GeneID; 3877421; -.
DR KEGG; ncr:NCU04158; -.
DR VEuPathDB; FungiDB:NCU04158; -.
DR HOGENOM; CLU_027360_0_0_1; -.
DR InParanoid; P23762; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..488
FT /note="Nitrogen metabolite repression protein nmr"
FT /id="PRO_0000096881"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..488
FT /note="Dispensable for NMR function"
FT REGION 422..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71..76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5AU62"
FT BINDING 75..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q5AU62"
FT BINDING 165..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q5AU62"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5AU62"
FT BINDING 215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q5AU62"
FT BINDING 215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5AU62"
FT BINDING 237..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q5AU62"
FT BINDING 237..240
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q5AU62"
FT MUTAGEN 2
FT /note="P->K: Loss of function."
FT /evidence="ECO:0000269|PubMed:2148799"
FT MUTAGEN 386
FT /note="G->C,S: Few, very slowly growing transformants."
FT /evidence="ECO:0000269|PubMed:2148799"
FT MUTAGEN 386
FT /note="G->D,R: Loss of function."
FT /evidence="ECO:0000269|PubMed:2148799"
FT CONFLICT 322
FT /note="G -> R (in Ref. 1; CAC28734)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="C -> S (in Ref. 1; CAC28734)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="A -> R (in Ref. 1; CAC28734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 54689 MW; CEB2B16AC9D9B383 CRC64;
MPAEILSELP LRPAPRDIKI PNAMHNEERR HKHSRSSYSE MSPLMSRNNS LTWRPAKRPM
PTPDKTIAVI NAAGRQAASF IRVATAVGFH VRAQMRNLEG VVATEVSTNP NVTVLQGELY
TKETPAESDK GQCVDVTKNG PISGIGVNDA LISELFRGAQ LAFINTTFYG DEERIGMALA
DAAKKAGVQH YVYSSMPDHH AYNKDWPSLP LWASKHRVED YVKEIGIPAT FVYTGIYNNN
FTSLPYPLFC TDLQPDGSWI WQAPFHPNAK LPWLDAEHDV GPAILQIFKD GVKKWGGGKR
IALAYEMLTP LEACEVFSRG VGRPVRYVRG PIEVKVKIPE GYRIQLEALE ELFNLHNEDP
EKQPPYFGDI ELERSCPRAA LELWEGPRGL EEYAREVFPL EEQANGLTWM IEEYDGGGGN
NIGNNHNNHH QQEEHYQHQN GHQNGHNGIN GHIVNGGVDS ESEEEDSDSD DEGLVMRGNK
RADEEWLA
