ID   URM1_COPC7              Reviewed;         124 AA.
AC   A8P008;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Ubiquitin-related modifier 1 {ECO:0000255|HAMAP-Rule:MF_03048};
GN   Name=URM1 {ECO:0000255|HAMAP-Rule:MF_03048}; ORFNames=CC1G_11440;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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; AACS02000006; EAU84002.1; -; Genomic_DNA.
DR   RefSeq; XP_001837795.1; XM_001837743.1.
DR   AlphaFoldDB; A8P008; -.
DR   SMR; A8P008; -.
DR   STRING; 5346.XP_001837795.1; -.
DR   EnsemblFungi; EAU84002; EAU84002; CC1G_11440.
DR   GeneID; 6014355; -.
DR   KEGG; cci:CC1G_11440; -.
DR   VEuPathDB; FungiDB:CC1G_11440; -.
DR   eggNOG; KOG4146; Eukaryota.
DR   HOGENOM; CLU_148208_0_0_1; -.
DR   InParanoid; A8P008; -.
DR   OMA; DYELQPN; -.
DR   OrthoDB; 1541629at2759; -.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000001861; 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..124
FT                   /note="Ubiquitin-related modifier 1"
FT                   /id="PRO_0000367880"
FT   REGION          34..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         124
FT                   /note="1-thioglycine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
FT   CROSSLNK        124
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03048"
SQ   SEQUENCE   124 AA;  13788 MW;  5C5AE4C59351DB46 CRC64;
     MAEPTPTTTL NIKIEFGGGL ELLFSNQRSH KVSIPSLVPK DNTTSAKNPP PKDDLLKPAD
     ITYLIHHMRD HLLQEREELF VENGTVRPGI LVLVNDTDWE LEGEGDYVLK DGDEVVFIST
     LHGG