NRDC_ARATH
ID NRDC_ARATH Reviewed; 1024 AA.
AC F4HNU6; Q0WNY2; Q9M9Z4;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Nardilysin-like {ECO:0000305};
DE EC=3.4.24.61 {ECO:0000305};
DE AltName: Full=N-arginine dibasic convertase-like {ECO:0000305};
DE Short=NRD convertase-like {ECO:0000305};
DE Short=NRD-C {ECO:0000305};
GN OrderedLocusNames=At1g06900 {ECO:0000312|Araport:AT1G06900};
GN ORFNames=F4H5.4 {ECO:0000312|EMBL:AAF63132.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves peptide substrates on the N-terminus of arginine
CC residues in dibasic pairs. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and
CC less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys.;
CC EC=3.4.24.61; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63132.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF01167.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC011001; AAF63132.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28051.1; -; Genomic_DNA.
DR EMBL; AK229304; BAF01167.1; ALT_INIT; mRNA.
DR PIR; G86203; G86203.
DR RefSeq; NP_172173.2; NM_100565.5.
DR AlphaFoldDB; F4HNU6; -.
DR SMR; F4HNU6; -.
DR STRING; 3702.AT1G06900.1; -.
DR iPTMnet; F4HNU6; -.
DR PaxDb; F4HNU6; -.
DR PRIDE; F4HNU6; -.
DR ProteomicsDB; 250928; -.
DR EnsemblPlants; AT1G06900.1; AT1G06900.1; AT1G06900.
DR GeneID; 837200; -.
DR Gramene; AT1G06900.1; AT1G06900.1; AT1G06900.
DR KEGG; ath:AT1G06900; -.
DR Araport; AT1G06900; -.
DR TAIR; locus:2033082; AT1G06900.
DR eggNOG; KOG0959; Eukaryota.
DR HOGENOM; CLU_004639_1_1_1; -.
DR InParanoid; F4HNU6; -.
DR OMA; WIFDEMK; -.
DR OrthoDB; 1008844at2759; -.
DR PRO; PR:F4HNU6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HNU6; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..1024
FT /note="Nardilysin-like"
FT /id="PRO_0000435730"
FT REGION 41..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..95
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT ACT_SITE 203
FT /evidence="ECO:0000305"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="R -> G (in Ref. 3; BAF01167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1024 AA; 117172 MW; 7A123B15D8E05B8F CRC64;
MSSMKSVSAL DNVVVKSPND RRLYRVIELE NGLCALLIHD PDIYPEGSVP DQIDEDDEDG
EEEDSDGSSE DDDDDEDDEE DGEGDEEDED EDEDEVKGKG DHQTKKAAAA MCVSMGSFLD
PPEAQGLAHF LEHMLFMGST EFPDENEYDS YLSKHGGSSN AYTEMEHTCY HFEVKREFLQ
GALKRFSQFF VAPLMKTEAM EREVLAVDSE FNQALQNDAC RLQQLQCYTS AKGHPFNRFA
WGNKKSLSGA MENGVDLREC IVKLYKEYYH GGLMKLVVIG GESLDMLESW VVELFGDVKN
GSKIRPTLEA EGPIWKGGKL YRLEAVKDVH ILDLTWTLPP LRSAYVKKPE DYLAHLLGHE
GRGSLHSFLK AKGWATSLSA GVGDDGINRS SLAYVFGMSI HLTDSGLEKI YDIIGYIYQY
LKLLRDVSPQ EWIFKELQDI GNMDFRFAEE QPADDYAAEL SENMLAYPVE HVIYGDYVYQ
TWDPKLIEDL MGFFTPQNMR IDVVSKSIKS EEFQQEPWFG SSYIEEDVPL SLMESWSNPS
EVDNSLHLPS KNQFIPCDFS IRAINSDVDP KSQSPPRCII DEPFMKFWYK LDETFKVPRA
NTYFRINLKG AYASVKNCLL TELYINLLKD ELNEIIYQAS IAKLETSLSM YGDKLELKVY
GFNEKIPALL SKILAIAKSF MPNLERFKVI KENMERGFRN TNMKPLNHST YLRLQLLCKR
IYDSDEKLSV LNDLSLDDLN SFIPELRSQI FIEALCHGNL SEDEAVNISN IFKDSLTVEP
LPSKCRHGEQ ITCFPMGAKL VRDVNVKNKS ETNSVVELYY QIEPEEAQST RTKAVLDLFH
EIIEEPLFNQ LRTKEQLGYV VECGPRLTYR VHGFCFCVQS SKYGPVHLLG RVDNFIKDIE
GLLEQLDDES YEDYRSGMIA RLLEKDPSLL SETNDLWSQI VDKRYMFDFS HKEAEELRSI
QKKDVISWYK TYFRESSPKC RRLAVRVWGC DTNMKETQTD QKAVQVIADA VAFKSTSKFY
PSLC
