URM1_BOTFB
ID URM1_BOTFB Reviewed; 106 AA.
AC A6S5X1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Ubiquitin-related modifier 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN Name=urm1; ORFNames=BC1G_08187;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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 the MOCS3 homolog
CC UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of
CC mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is
CC required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL)
CC that is covalently conjugated via an isopeptide bond to lysine residues
CC of target proteins such as AHP1. The thiocarboxylated form serves as
CC substrate for conjugation and oxidative stress specifically induces the
CC formation of UBL-protein conjugates. {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 UBA4, then
CC thiocarboxylated (-COSH) via the rhodanese domain of UBA4.
CC {ECO:0000255|HAMAP-Rule:MF_03048}.
CC -!- SIMILARITY: Belongs to the URM1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03048}.
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DR EMBL; CH476888; EDN28264.1; -; Genomic_DNA.
DR RefSeq; XP_001553357.1; XM_001553307.1.
DR AlphaFoldDB; A6S5X1; -.
DR SMR; A6S5X1; -.
DR GeneID; 5433888; -.
DR KEGG; bfu:BCIN_16g02100; -.
DR VEuPathDB; FungiDB:Bcin16g02100; -.
DR OMA; DYELQPN; -.
DR OrthoDB; 1541629at2759; -.
DR UniPathway; UPA00988; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0032447; P:protein urmylation; IEA:UniProtKB-UniRule.
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; tRNA processing; Ubl conjugation pathway.
FT CHAIN 1..106
FT /note="Ubiquitin-related modifier 1"
FT /id="PRO_0000367875"
FT MOD_RES 106
FT /note="1-thioglycine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ SEQUENCE 106 AA; 11787 MW; 766DAD8B51E077E3 CRC64;
MATDTLSIVV EFTGGLEMLF SDQRSHKLSV PKTDSKGAPV TVGWLVNYLC DEIMQDSRKD
MFVLDDHVRP GILVLINDAD WELEGEASYE LQSNDNILFV STLHGG