ID A0A2A2JUP6_9BILA Unreviewed; 162 AA.
AC A0A2A2JUP6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=Ubiquitin-fold modifier-conjugating enzyme 1 {ECO:0000256|ARBA:ARBA00013306, ECO:0000256|PIRNR:PIRNR008716};
GN ORFNames=WR25_19310 {ECO:0000313|EMBL:PAV65388.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV65388.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV65388.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV65388.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- FUNCTION: E1-like enzyme which specifically catalyzes the second step
CC in ufmylation. Ufmylation is involved in reticulophagy (also called ER-
CC phagy) induced in response to endoplasmic reticulum stress.
CC {ECO:0000256|PIRNR:PIRNR008716}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UFC1
CC subfamily. {ECO:0000256|ARBA:ARBA00008451,
CC ECO:0000256|PIRNR:PIRNR008716}.
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:PAV65388.1}.
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DR EMBL; LIAE01010209; PAV65388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JUP6; -.
DR STRING; 2018661.A0A2A2JUP6; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0061657; F:UFM1 conjugating enzyme activity; IEA:InterPro.
DR GO; GO:0071569; P:protein ufmylation; IEA:InterPro.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR014806; Ufc1.
DR PANTHER; PTHR12921; UBIQUITIN-FOLD MODIFIER-CONJUGATING ENZYME 1; 1.
DR PANTHER; PTHR12921:SF0; UBIQUITIN-FOLD MODIFIER-CONJUGATING ENZYME 1; 1.
DR Pfam; PF08694; UFC1; 1.
DR PIRSF; PIRSF008716; DUF1782; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR008716}.
FT ACT_SITE 115
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR008716-1"
SQ SEQUENCE 162 AA; 18558 MW; C7FB8727A5C960BE CRC64;
MDEESKSRLK AIPLCKTKAG PRDGDLWIER LKEEYESLIK FAQNNKESGS DWFRLESNEN
GTKWYGKCWH FHNMVKYEFD VEFDIPVTYP VTAPEIALPE LDGKTAKMYR GGKICLSEHF
KPLWARNAPK FGIAHAFSLG LGPWLAVEIP DLVEKGLIQP KS
//