ID   UFL1_DROAN              Reviewed;         784 AA.
AC   B3LYC0;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
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=GF17327;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
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; CH902617; EDV41783.1; -; Genomic_DNA.
DR   RefSeq; XP_001953200.1; XM_001953165.2.
DR   AlphaFoldDB; B3LYC0; -.
DR   STRING; 7217.FBpp0120519; -.
DR   EnsemblMetazoa; FBtr0122027; FBpp0120519; FBgn0094345.
DR   eggNOG; KOG2235; Eukaryota.
DR   HOGENOM; CLU_012417_1_1_1; -.
DR   InParanoid; B3LYC0; -.
DR   OMA; NECSATK; -.
DR   OrthoDB; 289380at2759; -.
DR   PhylomeDB; B3LYC0; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
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   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..784
FT                   /note="E3 UFM1-protein ligase 1 homolog"
FT                   /id="PRO_0000391879"
FT   REGION          401..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  87122 MW;  0E79428B12B9C0A0 CRC64;
     MGSDWDEIKR LAADFQKAQL TSTLQKLSER NCVEIVTLLL EKQLLDVVFT VDGKEYITPD
     HLEREIQDEL YVNGGRANLV EVSKALNVDL SRVVSLAERI AAENPSIHLE LGQLIDEEYI
     THIAQEINEK LALRGEISIS ELASQFDLPS EFLQHKVVEK HLGKIIKGRQ DTTNPRVFFT
     QAYIQRCKAK IRGALAAITR PTNVAVILQQ IGVQEKIFHS LLDEIAPAGQ VTSKMANAQY
     VPHVYAKTQS DWVSSFYKQN SFLEYDAIQK LGISDPKTYI RKQFPSEEFL FLKRVALGAR
     LVELTVVTAL NECSATKQYL DLSSILPSNL SEEDIEEVFA AIMAQKQSNP SNFVYLDSIV
     FSQPYLQQLV QPCQALAETQ AKAAIDSGIY QQHIVEKTLA QKGNSSAQDL EDDGKVDKRD
     ERRKKAASGK AGGGAQGRET KTKSTKKHAR GRAAAAQNDS DDDEDVHQNT KGGGGGGNKK
     TVKPLELVKT ADIVKLITAT LEEEGLEHLA KSIASLYTSQ FNQTALARAQ ELFEATPQTN
     RRQTHAAIQD RINTLLVDIR LYEKGLKLLP QDTQTQLVKY LLKSLGNDIC NELSLYVAAE
     CNLTVKNSNL NVDQRNKLAQ ECDAQYRSAL LEQNKALNKS IDEFELATEA VLKACSMIIK
     KVDKKKDRLL IADHKKKLQE QLLECNDPAL LLHLAALILF TTISGCILHA SGKFVSAILQ
     HIRGSLSDPQ NALLLRYHDL VLQVLQSAAD SSESKIAHEQ LQAMQTEVID LAQNYSRASV
     SKAD