ID   A0A914K0R2_9BILA        Unreviewed;       735 AA.
AC   A0A914K0R2;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   18-JUN-2025, entry version 11.
DE   RecName: Full=E3 UFM1-protein ligase 1 homolog {ECO:0000256|ARBA:ARBA00014160};
DE   AltName: Full=E3 UFM1-protein transferase 1 homolog {ECO:0000256|ARBA:ARBA00030452};
OS   Panagrolaimus sp. JU765.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae;
OC   Panagrolaimus.
OX   NCBI_TaxID=591449 {ECO:0000313|WBParaSite:JU765_v2.g5896.t1};
RN   [1] {ECO:0000313|WBParaSite:JU765_v2.g5896.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2022) to UniProtKB.
CC   -!- FUNCTION: E3 UFM1-protein ligase that mediates ufmylation of target
CC       proteins. {ECO:0000256|ARBA:ARBA00003950}.
CC   -!- SIMILARITY: Belongs to the UFL1 family.
CC       {ECO:0000256|ARBA:ARBA00010789}.
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DR   WBParaSite; JU765_v2.g5896.t1; JU765_v2.g5896.t1; JU765_v2.g5896.
DR   Proteomes; UP000887576; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:TreeGrafter.
DR   GO; GO:0061666; F:UFM1 ligase activity; IEA:InterPro.
DR   GO; GO:1990592; P:protein K69-linked ufmylation; IEA:TreeGrafter.
DR   GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:TreeGrafter.
DR   InterPro; IPR018611; Ufl1.
DR   InterPro; IPR056580; Ufl1_dom.
DR   InterPro; IPR056579; Ufl1_N.
DR   PANTHER; PTHR31057; E3 UFM1-PROTEIN LIGASE 1; 1.
DR   PANTHER; PTHR31057:SF0; E3 UFM1-PROTEIN LIGASE 1; 1.
DR   Pfam; PF09743; E3_UFM1_ligase; 1.
DR   Pfam; PF23659; UFL1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000887576};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          6..275
FT                   /note="E3 UFM1-protein ligase 1-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09743"
FT   DOMAIN          509..619
FT                   /note="E3 UFM1-protein ligase 1-like"
FT                   /evidence="ECO:0000259|Pfam:PF23659"
FT   REGION          402..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..434
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   735 AA;  82372 MW;  A64EAA4AF6FC1F7E CRC64;
     MATWADIQRL ASDLQRAQLS ISAEKLSDAN CVEVIGKLIE SGAIDVVFTV DGKEYITKKH
     LLTELKLECG AAGGRIPFVD LATNLRIDLS AVRQGVQNLL KESDEYLVSQ DELIAVEYID
     DLCKKLNEMF ADTGRLSILG LTQLWGVPIE FLNQYIFSEV GKKIHAQRDG DLLYTNEFVD
     AQYRKLQCAL WAVTRSIKLA NLFSYFDITQ SLFFSLINKL SGENKLHGTI LGSKNSLNSV
     YVSEVQERNA QEYIRNALLN QRVISIDTVR KLDLEPKVVK ESIFADKPVN ILKKTILMGD
     FYKELLSTIE EKLQNDSYCS FDAIFRDYPL IDSEDAHHIM EVGTKQASKG KEWVYNEGSP
     YSYFKSIVEK AVDGLDEYIK QKAVEDAPKI VLALKELNTA TGAAKKPAKD DDDDWKVGAK
     GGKKKGPAGK KGGKKTGTNV EEASKDTSGI FVLPQDEVLT KLVELNVFPE ELLSEIIDDA
     MPLVNAMYKK EVEAQFTAGS SKDQKQLIQE KQKKVKELYT SFCCFEQGTE IFTEGLKEDL
     RQALLKATGT DIAITVLSLY VDVPNNQQMT TKVRNECLAS ITDKNARNEL TELFESLTDL
     TKFHDSVAKL DACNIFVKQP DKRSRAEFLA NHIQHYKDLL NECDEPSRML LLIIVLIIAI
     KCKVAVYATG KFVSKIAKEL TDVCSEAKNP IPEDVIEKIT EAMPLVVKMI QGKTDDDQTE
     HLNQLLNDLK AYVLA
//