NOB1_ARATH
ID NOB1_ARATH Reviewed; 602 AA.
AC Q9FLL1; Q681U9;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=RNA-binding NOB1-like protein {ECO:0000303|PubMed:23382868};
DE Short=AtNob1 {ECO:0000303|PubMed:23382868};
DE EC=3.1.-.- {ECO:0000269|PubMed:23382868};
GN Name=NOB1 {ECO:0000303|PubMed:23382868};
GN OrderedLocusNames=At5g41190 {ECO:0000312|Araport:AT5G41190};
GN ORFNames=MEE6.26 {ECO:0000312|EMBL:BAB09721.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, MUTAGENESIS OF ASP-50, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=23382868; DOI=10.1371/journal.pone.0054084;
RA Missbach S., Weis B.L., Martin R., Simm S., Bohnsack M.T., Schleiff E.;
RT "40S ribosome biogenesis co-factors are essential for gametophyte and
RT embryo development.";
RL PLoS ONE 8:E54084-E54084(2013).
CC -!- FUNCTION: Essential protein required during embryogenesis and pollen
CC development (PubMed:23382868). Endonuclease cleaving pre-rRNA at the 3'
CC end of the mature 18S rRNA (D-site); cleaves 20S pre-rRNA in the
CC cytoplasm (PubMed:23382868). Required for processing of 20S pre-rRNA
CC precursor and biogenesis of 40S ribosomal subunits (PubMed:23382868).
CC {ECO:0000269|PubMed:23382868}.
CC -!- SUBUNIT: Component of the small ribosomal subunit, ribosomal RNA
CC processing complex (SSU RRP complex). {ECO:0000269|PubMed:23382868}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULX3}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:23382868}. Cytoplasm
CC {ECO:0000269|PubMed:23382868}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers and siliques and at
CC lower levels in roots, hypocotyls, stems, leaves and seeds.
CC {ECO:0000269|PubMed:23382868}.
CC -!- DISRUPTION PHENOTYPE: Delayed pollen development with reduced nuclei
CC content leading to reduced pollen germination capacity, and pale seeds
CC with arrested embryo development at the globular stage in homozygous
CC plants (PubMed:23382868). In heterozygous plants, strong accumulation
CC of the 23S-like precursor P-A3, and moderate increased levels of
CC 35S/33S precursors and 20S pre-rRNAs (PubMed:23382868). Alterated leaf
CC morphology and inhibited inflorescence elongation leading to a loss of
CC reproduction, seeds abortion and slightly reduced siliques size
CC (PubMed:23382868). {ECO:0000269|PubMed:23382868}.
CC -!- SIMILARITY: Belongs to the NOB1 family. {ECO:0000305}.
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DR EMBL; AB010072; BAB09721.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94652.1; -; Genomic_DNA.
DR EMBL; AK175518; BAD43281.1; -; mRNA.
DR RefSeq; NP_198935.1; NM_123484.3.
DR AlphaFoldDB; Q9FLL1; -.
DR IntAct; Q9FLL1; 1.
DR STRING; 3702.AT5G41190.1; -.
DR PaxDb; Q9FLL1; -.
DR PRIDE; Q9FLL1; -.
DR ProteomicsDB; 187155; -.
DR EnsemblPlants; AT5G41190.1; AT5G41190.1; AT5G41190.
DR GeneID; 834121; -.
DR Gramene; AT5G41190.1; AT5G41190.1; AT5G41190.
DR KEGG; ath:AT5G41190; -.
DR Araport; AT5G41190; -.
DR TAIR; locus:2163071; AT5G41190.
DR eggNOG; KOG2463; Eukaryota.
DR HOGENOM; CLU_024666_1_0_1; -.
DR InParanoid; Q9FLL1; -.
DR OMA; GYELECE; -.
DR OrthoDB; 765237at2759; -.
DR PhylomeDB; Q9FLL1; -.
DR PRO; PR:Q9FLL1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLL1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000469; P:cleavage involved in rRNA processing; IDA:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR CDD; cd09876; PIN_Nob1-like; 1.
DR Gene3D; 6.20.210.10; -; 1.
DR InterPro; IPR039907; NOB1.
DR InterPro; IPR017117; Nob1_euk.
DR InterPro; IPR036283; NOB1_Zf-like_sf.
DR InterPro; IPR014881; NOB1_Zn-bd.
DR InterPro; IPR033411; Ribonuclease_PIN.
DR PANTHER; PTHR12814; PTHR12814; 1.
DR Pfam; PF08772; NOB1_Zn_bind; 1.
DR Pfam; PF17146; PIN_6; 1.
DR PIRSF; PIRSF037125; D-site_20S_pre-rRNA_nuclease; 1.
DR SUPFAM; SSF144206; SSF144206; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing; Zinc;
KW Zinc-finger.
FT CHAIN 1..602
FT /note="RNA-binding NOB1-like protein"
FT /id="PRO_0000448721"
FT DOMAIN 48..134
FT /note="PINc"
FT /evidence="ECO:0000255"
FT ZN_FING 452..522
FT /note="NOB1"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..365
FT /evidence="ECO:0000255"
FT BINDING 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT BINDING 480
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT MUTAGEN 50
FT /note="D->N: Impaired endonuclease activity."
FT /evidence="ECO:0000269|PubMed:23382868"
FT CONFLICT 591
FT /note="N -> D (in Ref. 3; BAD43281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 66725 MW; 23A240CCFCF14A5E CRC64;
MDPKPTSMWS SIVKKDPPSK PPVNDGAPAA ILGMVGNCKS TKGISIAVVD ANAIIEGRQS
LTNFADKFVT VPEVLSEIRD PASRRRLAFI PFTIDTMEPS PESLSKVIKF ARATGDLQSL
SDVDLKLIAL SYTLEAQVYG TKNLRDVPPP IQTVRVKRLP EKDLPGWGSN VANLEEWEAL
ENETEEKSNA NSKILPLKDL NMNIIASDNV SEVGSVVSHT ENHEEDVQEG GKKHRRYPPK
KTEIKLEGKM VVEGVDASQG QYDDDDDASD WRPAVSRSTH SKYLRRKARW EHYNALAEQE
IQKDQEADKA RHTKEANETH AKDSGKNGED ISSILKDMRL EEESLRALQE ETEETNAEAT
LINGEDDIDH DIEVEAEGID VANQALENLE IASEAEDTFE ASSIGDDGSS EQSWSLRALS
ESSVACITGD YAMQNVILQM GLRLLAPGGM QIRQLHRWIL KCHACYTVTP EIGRIFCPKC
GNGGTLRKVA VTIGANGAII AACKPRITLR GTQYSIPMPK GGREAITKNL ILREDQLPQK
LLHPRTKKKA SKPGDEYFVS DDVFLNHHSD RKAPLQPPVR KAMSVFSQKR NPNDNHYSRS
MH
