URM1_CHICK
ID URM1_CHICK Reviewed; 101 AA.
AC Q5ZJU4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ubiquitin-related modifier 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN Name=URM1 {ECO:0000255|HAMAP-Rule:MF_03048}; ORFNames=RCJMB04_15k18;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ720340; CAG31999.1; -; mRNA.
DR RefSeq; NP_001007844.1; NM_001007843.1.
DR AlphaFoldDB; Q5ZJU4; -.
DR SMR; Q5ZJU4; -.
DR STRING; 9031.ENSGALP00000007958; -.
DR PaxDb; Q5ZJU4; -.
DR Ensembl; ENSGALT00000007972; ENSGALP00000007958; ENSGALG00000004971.
DR GeneID; 417221; -.
DR KEGG; gga:417221; -.
DR CTD; 81605; -.
DR VEuPathDB; HostDB:geneid_417221; -.
DR eggNOG; KOG4146; Eukaryota.
DR GeneTree; ENSGT00390000005101; -.
DR HOGENOM; CLU_148208_0_1_1; -.
DR InParanoid; Q5ZJU4; -.
DR OMA; DYELQPN; -.
DR OrthoDB; 1541629at2759; -.
DR PhylomeDB; Q5ZJU4; -.
DR TreeFam; TF336363; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q5ZJU4; -.
DR Proteomes; UP000000539; Chromosome 17.
DR Bgee; ENSGALG00000004971; Expressed in granulocyte and 13 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
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"
FT /id="PRO_0000367849"
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; 11427 MW; B29166555EE2AD02 CRC64;
MAAPVSLQVE FGGGAELLFD GVKKHQVTLP SQPEPWDIRN LLKWIKQNLL KERPELFMQG
ESVRPGILVL INDADWELMG ELDYKLQDQD NVLFISTLHG G
