NUG2_ARATH
ID NUG2_ARATH Reviewed; 576 AA.
AC Q9C923; C0Z385;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Nuclear/nucleolar GTPase 2 {ECO:0000303|PubMed:21205822};
DE Short=AtNug2 {ECO:0000303|PubMed:21205822};
DE AltName: Full=DAR GTPase 5 {ECO:0000303|PubMed:16849600};
GN Name=NUG2 {ECO:0000303|PubMed:21205822};
GN Synonyms=DGP5 {ECO:0000303|PubMed:16849600};
GN OrderedLocusNames=At1g52980 {ECO:0000312|Araport:AT1G52980};
GN ORFNames=F14G24.25 {ECO:0000312|EMBL:AAG52287.1};
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 {ECO:0000312|Proteomes:UP000006548};
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP DOMAIN, AND GENE FAMILY.
RX PubMed=9573393; DOI=10.1016/s0378-1119(98)00088-2;
RA Fu G., Melville S., Brewster S., Warner J., Barker D.C.;
RT "Analysis of the genomic organisation of a small chromosome of Leishmania
RT braziliensis M2903 reveals two genes encoding GTP-binding proteins, one of
RT which belongs to a new G-protein family and is an antigen.";
RL Gene 210:325-333(1998).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16849600; DOI=10.1534/genetics.106.060657;
RA Hill T.A., Broadhvest J., Kuzoff R.K., Gasser C.S.;
RT "Arabidopsis SHORT INTEGUMENTS 2 is a mitochondrial DAR GTPase.";
RL Genetics 174:707-718(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND INTERACTION WITH RPL10AA; RPL10AB AND
RP RPL10AC.
RX PubMed=21205822; DOI=10.1074/jbc.m110.200816;
RA Im C.H., Hwang S.M., Son Y.S., Heo J.B., Bang W.Y., Suwastika I.N.,
RA Shiina T., Bahk J.D.;
RT "Nuclear/nucleolar GTPase 2 proteins as a subfamily of YlqF/YawG GTPases
RT function in pre-60S ribosomal subunit maturation of mono- and
RT dicotyledonous plants.";
RL J. Biol. Chem. 286:8620-8632(2011).
CC -!- FUNCTION: GTPase involved in pre-60S ribosomal subunit maturation.
CC {ECO:0000269|PubMed:21205822}.
CC -!- ACTIVITY REGULATION: The GTPase activity is stimulated in the presence
CC of the 60S ribosomal subunit. {ECO:0000269|PubMed:21205822}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.087 min(-1) for GTP. {ECO:0000269|PubMed:21205822};
CC -!- SUBUNIT: Interacts with the 60S ribosomal proteins RPL10AA, RPL10AB and
CC RPL10AC. {ECO:0000269|PubMed:21205822}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21205822}.
CC Nucleus {ECO:0000269|PubMed:21205822}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C923-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C923-2; Sequence=VSP_057528;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in meristematic
CC regions. {ECO:0000269|PubMed:21205822}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern. {ECO:0000305}.
CC -!- DOMAIN: The DARXP motif is also sometime designated as G6 region.
CC {ECO:0000305|PubMed:9573393}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AC019018; AAG52287.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32873.1; -; Genomic_DNA.
DR EMBL; AK319049; BAH57164.1; -; mRNA.
DR RefSeq; NP_175706.1; NM_104176.4. [Q9C923-1]
DR AlphaFoldDB; Q9C923; -.
DR SMR; Q9C923; -.
DR STRING; 3702.AT1G52980.1; -.
DR iPTMnet; Q9C923; -.
DR PaxDb; Q9C923; -.
DR PRIDE; Q9C923; -.
DR ProteomicsDB; 248622; -. [Q9C923-1]
DR EnsemblPlants; AT1G52980.1; AT1G52980.1; AT1G52980. [Q9C923-1]
DR GeneID; 841731; -.
DR Gramene; AT1G52980.1; AT1G52980.1; AT1G52980. [Q9C923-1]
DR KEGG; ath:AT1G52980; -.
DR Araport; AT1G52980; -.
DR TAIR; locus:2011561; AT1G52980.
DR eggNOG; KOG2423; Eukaryota.
DR HOGENOM; CLU_011106_4_2_1; -.
DR InParanoid; Q9C923; -.
DR OMA; PAPFQGR; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q9C923; -.
DR PRO; PR:Q9C923; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C923; baseline and differential.
DR Genevisible; Q9C923; AT.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0042254; P:ribosome biogenesis; IDA:TAIR.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR024929; NOG2.
DR InterPro; IPR012971; NOG2_N_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11089:SF9; PTHR11089:SF9; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF08153; NGP1NT; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTP-binding; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..576
FT /note="Nuclear/nucleolar GTPase 2"
FT /id="PRO_0000432556"
FT DOMAIN 206..367
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..257
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 283..285
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 316..323
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 342..346
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 360..363
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 502..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 224..228
FT /note="DARXP motif"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..576
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 254..257
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 319..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 363
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT VAR_SEQ 1..158
FT /note="MVKKEKKANVSGKPKHSLDANRADGKKKTTETRSKSTVNRLKMYKTRPKRNA
FT GGKILSNEYQSKELPNSRIAPDRRWFGNTRVVNQKELEYFREELQTKMSSNYNVILKER
FT KLPMSLLTDNKKQSRVHLLDMEPFQDAFGRKTKRKRPKLVASDYEAL -> M (in
FT isoform 2)"
FT /id="VSP_057528"
FT CONFLICT 171
FT /note="E -> G (in Ref. 3; BAH57164)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="T -> N (in Ref. 3; BAH57164)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="I -> N (in Ref. 3; BAH57164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 65038 MW; E0CCAEAFA979CBB0 CRC64;
MVKKEKKANV SGKPKHSLDA NRADGKKKTT ETRSKSTVNR LKMYKTRPKR NAGGKILSNE
YQSKELPNSR IAPDRRWFGN TRVVNQKELE YFREELQTKM SSNYNVILKE RKLPMSLLTD
NKKQSRVHLL DMEPFQDAFG RKTKRKRPKL VASDYEALVK KAAESQDAFE EKNGAGPSGE
GGEEEDGFRD LVRHTMFEKG QSKRIWGELY KVIDSSDVIV QVIDARDPQG TRCHHLEKTL
KEHHKHKHMI LLLNKCDLVP AWATKGWLRV LSKEYPTLAF HASVNKSFGK GSLLSVLRQF
ARLKSDKQAI SVGFVGYPNV GKSSVINTLR TKNVCKVAPI PGETKVWQYI TLTKRIFLID
CPGVVYQSRD TETDIVLKGV VRVTNLEDAS EHIGEVLRRV KKEHLQRAYK IKDWEDDHDF
LLQLCKSSGK LLKGGEPDLM TGAKMILHDW QRGRIPFFVP PPKLDNVASE SEVIVPGIDK
EAIADNSQAA AALKAIAGIM STQQQKDVPV QRDFYDEKDL KDDKKAKEST ETDAENGTDA
EEDEDAVSED GVESDSDADE DAVSENDEED ESDSAE
