ID   UFL1_DROVI              Reviewed;         778 AA.
AC   B4LZW7;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=GJ24026;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
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; CH940650; EDW67195.1; -; Genomic_DNA.
DR   RefSeq; XP_002053675.2; XM_002053639.2.
DR   AlphaFoldDB; B4LZW7; -.
DR   STRING; 7244.FBpp0238443; -.
DR   PRIDE; B4LZW7; -.
DR   GeneID; 6629718; -.
DR   KEGG; dvi:6629718; -.
DR   eggNOG; KOG2235; Eukaryota.
DR   HOGENOM; CLU_012417_1_1_1; -.
DR   InParanoid; B4LZW7; -.
DR   OMA; NECSATK; -.
DR   PhylomeDB; B4LZW7; -.
DR   Proteomes; UP000008792; 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..778
FT                   /note="E3 UFM1-protein ligase 1 homolog"
FT                   /id="PRO_0000391888"
FT   REGION          404..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..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   778 AA;  87097 MW;  1A5DE494CC832091 CRC64;
     MSSDWDEIKR LAADFQKAQL TSTLQKLSER NCIEIVTLLL EKQLLDVVFT NDGKEYITPD
     HLEREIQDEL YANGGRANLV EVSKTLNVDL SRIVTLAERI AAENPHIHLL LGQLIDEDYI
     THIAQEINEK LAQHGEISIS DLTSQFDLPS DFLQQNVVEK HLGKIIKGRQ DASNPRVFFT
     QAYIQRCKAK IRGALAAITK PTNVAVILQQ INVQEKIFHS LLDEISPAGQ VTSKQANAQY
     VPHIYAKTQA DWVNSFYKQN SFLEYEAINK LGISDAKTYI RNQFPNEQFL FLKRVALGAR
     LIELTVVSAL NECSATKHYL DLSTILPSNL SEEDIAEAFD AVIAQKHCNP SHFVYLESIV
     FSQAYLTELV QPCHDMALAL AKSAIDNGVY QQYIVEKTLA QKGNNLSTSH DADDDSKTDK
     RDERRRKAAS GKAGGGAQGR ETKTKSTKKH QRGRAAAHNH DSEDEEDTVQ QSAGNTRKSV
     KALELVKSSD IINLIKITLE EEGLEHLAKP IAALYLNQLN QVALSKAQEL YEATPQTNRR
     QTHAAIQERV NMLLVDIRLY EKGLKLFHAD TQTQLVKYLL KSLGNEICNE LTLYVAAECS
     LSVKSTNLNV DQRIKLIQEL DAQYRNALLE QNKALNRSIE DFELATESVL KACSMIIKKA
     DKKKDRALII GHKEKLLQQL LECHEPALLL HLAALILFTT ITGCILHASG KFVSAILQHI
     RASLNEPQNA LYLVLQMLQQ ATPDSAESKS INEQLQSLQA EVVDLAQNYS RASVSKAD