ID A0A6A5BKW7_NAEFO Unreviewed; 97 AA.
AC A0A6A5BKW7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 02-APR-2025, entry version 10.
DE RecName: Full=Ubiquitin-related modifier 1 homolog {ECO:0000256|HAMAP-Rule:MF_03048};
GN ORFNames=FDP41_006292 {ECO:0000313|EMBL:KAF0974818.1};
OS Naegleria fowleri (Brain eating amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5763 {ECO:0000313|EMBL:KAF0974818.1, ECO:0000313|Proteomes:UP000444721};
RN [1] {ECO:0000313|EMBL:KAF0974818.1, ECO:0000313|Proteomes:UP000444721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30894 {ECO:0000313|EMBL:KAF0974818.1,
RC ECO:0000313|Proteomes:UP000444721};
RX PubMed=31690847;
RA Liechti N., Schurch N., Bruggmann R., Wittwer M.;
RT "Nanopore sequencing improves the draft genome of the human pathogenic
RT amoeba Naegleria fowleri.";
RL Sci. Rep. 9:0-16040(2019).
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/UBA4
CC homolog. The sulfur is then transferred to tRNA to form 2-thiolation of
CC mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is
CC covalently conjugated via an isopeptide bond to lysine residues of
CC target proteins. The thiocarboxylated form serves as substrate for
CC conjugation and oxidative stress specifically induces the formation of
CC UBL-protein conjugates. {ECO:0000256|HAMAP-Rule:MF_03048}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_03048,
CC ECO:0000256|RuleBase:RU361182}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03048,
CC ECO:0000256|RuleBase:RU361182}.
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/UBA4
CC homolog, then thiocarboxylated (-COSH) via the rhodanese domain of the
CC MOCS3/UBA4 homolog. {ECO:0000256|HAMAP-Rule:MF_03048}.
CC -!- SIMILARITY: Belongs to the URM1 family. {ECO:0000256|HAMAP-
CC Rule:MF_03048, ECO:0000256|RuleBase:RU361182}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF0974818.1}.
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DR EMBL; VFQX01000051; KAF0974818.1; -; Genomic_DNA.
DR RefSeq; XP_044559531.1; XM_044709911.1.
DR AlphaFoldDB; A0A6A5BKW7; -.
DR GeneID; 68113510; -.
DR VEuPathDB; AmoebaDB:FDP41_006292; -.
DR VEuPathDB; AmoebaDB:NF0089840; -.
DR VEuPathDB; AmoebaDB:NfTy_076850; -.
DR OMA; DYELQPN; -.
DR OrthoDB; 10248987at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000444721; 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; RURM1 PROTEIN; 1.
DR Pfam; PF09138; Urm1; 1.
DR PIRSF; PIRSF037379; Ubiquitin-related_modifier_1; 1.
DR SUPFAM; SSF54285; MoaD/ThiS; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03048};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499, ECO:0000256|HAMAP-
KW Rule:MF_03048}; Reference proteome {ECO:0000313|Proteomes:UP000444721};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03048};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, ECO:0000256|HAMAP-
KW Rule:MF_03048}.
FT MOD_RES 97
FT /note="1-thioglycine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03048"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03048"
SQ SEQUENCE 97 AA; 11188 MW; A2B1524F06960D0C CRC64;
MQVKIEFSGG CELLFENKTS LTIVNLEEGT TMQQLILLLR DKYLKEKPEL FMNNENTSIR
PGILVIINDT DWELVDELQY KIQDKDNIVF ISTLHGG
//
