ID   UFL1_DROMO              Reviewed;         783 AA.
AC   B4KDK5;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 52.
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=GI23931;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22;
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; CH933806; EDW13839.1; -; Genomic_DNA.
DR   RefSeq; XP_001998378.1; XM_001998342.2.
DR   AlphaFoldDB; B4KDK5; -.
DR   STRING; 7230.FBpp0173148; -.
DR   PRIDE; B4KDK5; -.
DR   EnsemblMetazoa; FBtr0174656; FBpp0173148; FBgn0146656.
DR   GeneID; 6572236; -.
DR   KEGG; dmo:Dmoj_GI23931; -.
DR   eggNOG; KOG2235; Eukaryota.
DR   HOGENOM; CLU_012417_1_1_1; -.
DR   InParanoid; B4KDK5; -.
DR   OMA; NECSATK; -.
DR   OrthoDB; 289380at2759; -.
DR   PhylomeDB; B4KDK5; -.
DR   Proteomes; UP000009192; 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..783
FT                   /note="E3 UFM1-protein ligase 1 homolog"
FT                   /id="PRO_0000391883"
FT   REGION          404..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..471
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  87757 MW;  1A66EA7DF9CCD49C CRC64;
     MSSDWDEIKR LAADFQKAQL TSTLQKLSER NCIEIVTLLL EKQLLDVVFT NDGKEYITPE
     HLEREIQDEL YANGGRANLV EVSKTLNVDL SRIEALAERI AADNPQIHLM LGQLIDEDYI
     THIAQEINEK LSQRGEISIS DLTSQFDLPS EFLQHNVMEK HLGKTIKGRQ DATNPRVFFT
     QAYIQRCKAK IRGALAAITK PTNVSVILQQ INVQEKIFHS LLDEIMPAGQ VTSKQANAQY
     VPHIYAKTQA EWVNSFYKQN SFLEYEAINK LGISDAKAYI RKQFPNEQFL FLKRVALGAH
     LIELTVVSAL NECSATKQYL DLATILPSNL SEEDIEEAFD AVMAQKHCNP SQFVYLQSIV
     FSQAYLTQLI QPCHDMAHAL AKAAIDSGAY QQYIVEKTLA QKGSNSSANF DADDDGKVDK
     RDERRKKAAS GKAGGGAQGR ETKTKSTKKH QRGRAAAHNH DSDDDEETTQ QSAGSSRKSV
     KPLELVKSSD VINRIKSTLE EEGLEHLAKP IAGLFVNQLN QAALAKAQEL YEATPQTNRR
     QTHAAIQERV NTLLVDLRLY EKGIKLFNTD TQAQLIKYLL KSLGNDICNE LTLYVAAECS
     LSVKMTNLNV DQRIKLIQEC DAQYRNALLE QNKALNKSIE DFELATEAVL KTCSMIIKKA
     DKKKDRALIV SHKEKLMQQL SECREPALLL HLAALILFTT ITGCILHASG KFVSTILQHI
     RPTLNESQNA LLLRYHDLVL QMLQQGTTDS PESKSLNEQL QTLQAEVVDL AQNFSRVSVS
     KAD