URM1_BOMMO
ID URM1_BOMMO Reviewed; 109 AA.
AC Q1HQ10;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Ubiquitin-related modifier 1 homolog {ECO:0000255|HAMAP-Rule:MF_03048};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Niu B.L., Meng Z.Q., Weng H.B., Shen W.F., He L.H., Zheng K.F., Ye S.T.,
RA Lin T.B., Chen J.E.;
RT "Blast silkworm EST database for functional genes.";
RL Submitted (MAR-2006) 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}.
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DR EMBL; DQ443242; ABF51331.1; -; mRNA.
DR RefSeq; NP_001040521.1; NM_001047056.1.
DR AlphaFoldDB; Q1HQ10; -.
DR SMR; Q1HQ10; -.
DR STRING; 7091.BGIBMGA001700-TA; -.
DR EnsemblMetazoa; BGIBMGA001700-RA; BGIBMGA001700-TA; BGIBMGA001700.
DR GeneID; 733109; -.
DR KEGG; bmor:733109; -.
DR eggNOG; KOG4146; Eukaryota.
DR HOGENOM; CLU_148208_0_1_1; -.
DR InParanoid; Q1HQ10; -.
DR OMA; DYELQPN; -.
DR OrthoDB; 1541629at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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; Reference proteome; tRNA processing;
KW Ubl conjugation pathway.
FT CHAIN 1..109
FT /note="Ubiquitin-related modifier 1 homolog"
FT /id="PRO_0000367853"
FT MOD_RES 109
FT /note="1-thioglycine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ SEQUENCE 109 AA; 12623 MW; E1EFBB1E06A16D7A CRC64;
MAETLTVEVM FGGGAELLFN KVKRKEIALP PLKTFLPDSQ NQNWTLKELL IWLKDNLLVE
REELFLKDDS VRPGILVLIN EEDWELHGQL NYELKENDKI MFISTLHGG
