URM11_ARATH
ID URM11_ARATH Reviewed; 101 AA.
AC A0MDQ1; Q570Q1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ubiquitin-related modifier 1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN Name=URM1-1 {ECO:0000255|HAMAP-Rule:MF_03048}; OrderedLocusNames=At2g45695;
GN ORFNames=17K2;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a sulfur carrier required for 2-thiolation of
CC mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu)
CC and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by
CC being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur
CC is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also
CC acts as a ubiquitin-like protein (UBL) that is covalently conjugated
CC via an isopeptide bond to lysine residues of target proteins. The
CC thiocarboxylated form serves as substrate for conjugation and oxidative
CC stress specifically induces the formation of UBL-protein conjugates.
CC {ECO:0000255|HAMAP-Rule:MF_03048}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03048}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03048}.
CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC adenylated (-COAMP) via the hesA/moeB/thiF part of the MOCS3 homolog,
CC then thiocarboxylated (-COSH) via the rhodanese domain of the MOCS3
CC homolog. {ECO:0000255|HAMAP-Rule:MF_03048}.
CC -!- SIMILARITY: Belongs to the URM1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03048}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28333.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC003680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC10588.1; -; Genomic_DNA.
DR EMBL; DQ487520; ABF59216.1; -; mRNA.
DR EMBL; DQ652667; ABK28333.1; ALT_SEQ; mRNA.
DR EMBL; AK220657; BAD95172.1; -; mRNA.
DR RefSeq; NP_001078064.1; NM_001084595.3.
DR AlphaFoldDB; A0MDQ1; -.
DR SMR; A0MDQ1; -.
DR STRING; 3702.AT2G45695.1; -.
DR PaxDb; A0MDQ1; -.
DR PRIDE; A0MDQ1; -.
DR ProteomicsDB; 228573; -.
DR EnsemblPlants; AT2G45695.1; AT2G45695.1; AT2G45695.
DR GeneID; 5007965; -.
DR Gramene; AT2G45695.1; AT2G45695.1; AT2G45695.
DR KEGG; ath:AT2G45695; -.
DR Araport; AT2G45695; -.
DR TAIR; locus:4010713712; AT2G45695.
DR eggNOG; KOG4146; Eukaryota.
DR HOGENOM; CLU_148208_0_1_1; -.
DR InParanoid; A0MDQ1; -.
DR OMA; SLIHFMA; -.
DR OrthoDB; 1541629at2759; -.
DR PhylomeDB; A0MDQ1; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:A0MDQ1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; A0MDQ1; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0032447; P:protein urmylation; IBA:GO_Central.
DR GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:UniProtKB-UniRule.
DR CDD; cd01764; Ubl_Urm1; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_03048; Urm1; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR015221; Urm1.
DR PANTHER; PTHR14986; PTHR14986; 1.
DR Pfam; PF09138; Urm1; 1.
DR PIRSF; PIRSF037379; Ubiquitin-related_modifier_1; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isopeptide bond; Reference proteome; tRNA processing;
KW Ubl conjugation pathway.
FT CHAIN 1..101
FT /note="Ubiquitin-related modifier 1 homolog 1"
FT /id="PRO_0000367867"
FT MOD_RES 101
FT /note="1-thioglycine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ SEQUENCE 101 AA; 11287 MW; 63D66BBF691387DC CRC64;
MQLTLEFGGG LELLCDSEKI HKVNVDLPNG ADSDDFTMKH LLSWVRTNLI KERPEMFMKG
DTVRPGVLVL VNDCDWELSG QLDTVIEDKD VVVFISTLHG G
