ID   UFL1_DROWI              Reviewed;         785 AA.
AC   B4NAB3;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=GK12257;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
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; CH964232; EDW81800.1; -; Genomic_DNA.
DR   RefSeq; XP_002070814.1; XM_002070778.2.
DR   AlphaFoldDB; B4NAB3; -.
DR   SMR; B4NAB3; -.
DR   STRING; 7260.FBpp0241400; -.
DR   EnsemblMetazoa; FBtr0242908; FBpp0241400; FBgn0214267.
DR   GeneID; 6647229; -.
DR   KEGG; dwi:6647229; -.
DR   eggNOG; KOG2235; Eukaryota.
DR   HOGENOM; CLU_012417_1_1_1; -.
DR   InParanoid; B4NAB3; -.
DR   OMA; NECSATK; -.
DR   OrthoDB; 289380at2759; -.
DR   PhylomeDB; B4NAB3; -.
DR   Proteomes; UP000007798; 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..785
FT                   /note="E3 UFM1-protein ligase 1 homolog"
FT                   /id="PRO_0000391889"
FT   REGION          404..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..431
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   785 AA;  87848 MW;  228BC0620EF9FCA9 CRC64;
     MGSDWDEIKR LAADFQKAQL TSTLQQLSER NCVEIVALLL EKQLLDVVFT NDGKEYITPD
     HLEREIQDEL YTNGGRANLV EVSKTLNVDL SRIETLAERI AEENPQIHLI LGQLIDEDYI
     SHIAQEINEK LALRGEISIS DLASQFDLPS DFLQHQVVEK HLGKTIKGRQ DSTNPRVFFT
     QAYIQRCKAK IRGALNAITR PTNVATILQQ INVQEKIFHS LLDEISPAGQ VTSKLSNAQY
     VPHIYAKTQS EWVQSFFKQN GFIEYEAINK LGISDPKSYI LKQLPQEELY FLKRIALQQR
     LVDLTVVTAL NECNATKQYL DLSTILPSNL SVEDIEEVFH TLTSGPKQSH LSTLVYLDGI
     VFSQPYLNEL IQPCQELALS QGKSAIDSGI YQQYIVDKTL AQKGGNASNQ LDDDEDGKPD
     KRDERRKKAA SGKAGGGAQG RETKTKSTKK HQRGRAAAAQ HSDDDDDDFQ RGGGGGGSNK
     KSVKPLDLVK CEDVVKLIFP VLEEEGIEHL AKPIAKLYLQ QLNQSALAKA QELYEATPQT
     NRRQTHASIQ ERINTLLVDI RLYEKGLKLL PQDTQAQLVK YLLKSLGNEI CNELALYVAS
     ECNLTVKNNN LNVDQRNKLA QECDAQYRAV LVEQNKALNK SIDDFELATE SVLKVCSMII
     KKVDKKKDRL LIADHKQKLQ QQLLENQEPA LILHLAALIL FTSISGCILH ASGKFVSSIL
     QYIRGSLDDQ QNALLISYHD LVLKVLQASP ESAESKLAHE QLQGLQSKVV ELAQNFSRAS
     VSKAD