URM1_SCHPO
ID URM1_SCHPO Reviewed; 97 AA.
AC Q9P3U9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Ubiquitin-related modifier 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN Name=urm1; ORFNames=SPCC548.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329672; CAB94946.2; -; Genomic_DNA.
DR RefSeq; NP_587744.2; NM_001022738.3.
DR AlphaFoldDB; Q9P3U9; -.
DR SMR; Q9P3U9; -.
DR BioGRID; 275348; 6.
DR STRING; 4896.SPCC548.04.1; -.
DR MaxQB; Q9P3U9; -.
DR PaxDb; Q9P3U9; -.
DR EnsemblFungi; SPCC548.04.1; SPCC548.04.1:pep; SPCC548.04.
DR GeneID; 2538765; -.
DR KEGG; spo:SPCC548.04; -.
DR PomBase; SPCC548.04; urm1.
DR VEuPathDB; FungiDB:SPCC548.04; -.
DR eggNOG; KOG4146; Eukaryota.
DR HOGENOM; CLU_148208_0_0_1; -.
DR InParanoid; Q9P3U9; -.
DR OMA; SLIHFMA; -.
DR PhylomeDB; Q9P3U9; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q9P3U9; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0031386; F:protein tag; ISO:PomBase.
DR GO; GO:0032447; P:protein urmylation; ISO:PomBase.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; ISO:PomBase.
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..97
FT /note="Ubiquitin-related modifier 1"
FT /id="PRO_0000330335"
FT MOD_RES 97
FT /note="1-thioglycine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ SEQUENCE 97 AA; 10717 MW; 40942ABA65D7D30A CRC64;
MAIKVELLGG LDLLFNKQKA LSLSLSNLGS TKLGSLIDYM AQIIEKPSQK DLFILNGTVR
PGIIVLVNDQ DWELLEKEEY NLEEGDEVVF VSTLHGG
