ID   UFL1_DROYA              Reviewed;         784 AA.
AC   B4PS24;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=E3 UFM1-protein ligase 1 homolog;
DE            EC=2.3.2.-;
DE   AltName: Full=E3 UFM1-protein transferase 1 homolog {ECO:0000305};
GN   ORFNames=GE25823;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: E3 UFM1-protein ligase that mediates ufmylation of target
CC       proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UFL1 family. {ECO:0000305}.
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DR   EMBL; CM000160; EDW96424.1; -; Genomic_DNA.
DR   RefSeq; XP_002096712.1; XM_002096676.2.
DR   AlphaFoldDB; B4PS24; -.
DR   STRING; 7245.FBpp0270833; -.
DR   EnsemblMetazoa; FBtr0272341; FBpp0270833; FBgn0242873.
DR   GeneID; 6536104; -.
DR   KEGG; dya:Dyak_GE25823; -.
DR   eggNOG; KOG2235; Eukaryota.
DR   HOGENOM; CLU_012417_1_1_1; -.
DR   OMA; NECSATK; -.
DR   OrthoDB; 289380at2759; -.
DR   PhylomeDB; B4PS24; -.
DR   Proteomes; UP000002282; Chromosome 3R.
DR   GO; GO:0061666; F:UFM1 ligase activity; IEA:InterPro.
DR   GO; GO:0071569; P:protein ufmylation; IEA:InterPro.
DR   InterPro; IPR018611; Ufl1.
DR   PANTHER; PTHR31057; PTHR31057; 1.
DR   Pfam; PF09743; E3_UFM1_ligase; 1.
PE   3: Inferred from homology;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..784
FT                   /note="E3 UFM1-protein ligase 1 homolog"
FT                   /id="PRO_0000391890"
FT   REGION          405..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  87581 MW;  EAD140BE719E87BD CRC64;
     MGSGDWDEIK RLAADFQKAQ LTSTLQKLSE RNCVEIVTLL LEKQMLEVVF TNDGKEYITP
     DHLEREIQDE LYVNGGRANL VEVSKTLNVD LSRIEVLAER IAAENPSVHL VLGQLIDEDY
     ISHIAQEINE KLVLRGEISI SELASQFDLP SDFLQHDVVE KHLGKIIKGR QDASNPRVFF
     TQAYIQRCKA KIRGALAAIT RPINVAVILQ QIGVQEKIFH SLLDEIAPAG QVTSKLANSQ
     YVPLIYAKTQ ADWVNSFYKQ NSFLEYDAIQ KLGISDAKSY IRKQFPNEEF LFLKRVALGA
     RLVELTVVTA LNECSATKQY LDLTTILPSN LSEEDIEEVF STIMGQKHSN PNNFVYLDSI
     VFSQPYLAQL VQPCQALAES QAKAAVDGGV YQQYIVEKTL AQKGSVSTQE LEDDGKVDKR
     DERRKKASSG KAGGGAQGRE TKTKSTKKHQ RGKAAAHNDS DDEDDVQQSS RGGGAGNKKA
     MKPLELVKTA DIVKLITASL EEEGLEHLAK PISALYTNQF NQTALARAQE LFEATPQTNR
     RQTHAAIQDR INTFLIDIRL YEKGLKLFPL ETQTQLVKYL LKSLGNDICN ELSLYVAGEC
     NLTVKNTNLN VDQRIKLAQE CEVQYRASLL EQNKALNKTI DEFELATETV LKACSMIIKK
     VDKKKDRLLI ADHKKKLQNQ LLECQEPALL LHLAVLILFT TITGSILHAS GKFVSAILQH
     IRGSLNDEQN ALLLRYHDLV LQVLQATPDS SESKVANEHL QAMQVQVVEL AQNFSRASVF
     KADC