ID   UFL1_DROPE              Reviewed;         785 AA.
AC   B4GEL3;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 51.
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=GL22034;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479182; EDW34048.1; -; Genomic_DNA.
DR   RefSeq; XP_002016948.1; XM_002016912.1.
DR   AlphaFoldDB; B4GEL3; -.
DR   STRING; 7234.FBpp0186141; -.
DR   EnsemblMetazoa; FBtr0187649; FBpp0186141; FBgn0159627.
DR   GeneID; 6591462; -.
DR   KEGG; dpe:6591462; -.
DR   eggNOG; KOG2235; Eukaryota.
DR   HOGENOM; CLU_012417_1_1_1; -.
DR   OMA; NECSATK; -.
DR   PhylomeDB; B4GEL3; -.
DR   Proteomes; UP000008744; 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_0000391884"
FT   REGION          404..482
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        451..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   785 AA;  87540 MW;  41670662CAFD256A CRC64;
     MGSDWDEIKR LAADFQKAQL TSTLQKLSER NCVEIVTLLL EKQLLEVVFT NDGKEYITPD
     HLEREIQDEL YANGGRANLV EVSRTLNVDL SRIVALAERI AAENPLVHLV LGQLIDEDYI
     SHIAQEINEK LALRGEISIS DLASQFDLPS EFLQQDVVEK HLGKIIKGRQ DATNPRVFFT
     QAYIQRCKAK IRGALAAITR PTNVAVILQQ INVQEKIFHS LLDEISPAGQ VTSKLANAQY
     VPHIYAKTQA DWVNSFYKQN SFLEYDAINK LGISDAKSYI RKQFPNEEFL FLKRVALGAR
     LVELTVVTAL NECSATKQYL DLTTILPSNL SEEDIEEVFS AIMAQKHSNP SNFVYLDSIV
     FSQPYLTELV QPCHALAEAQ AKAAIDSGVY QQFIVEKTLA QKGNASFQDQ DDDGKLDKRD
     ERRKKASSGK AGGGAQGRET KTKSTKKHQR RSAAAQNDSD VEDDVQHQGS RGAGGGGGNK
     KTVKPLDLVK TADIEKLINA SLQEEGLEHL APSIAALYLN QLNQAALAKA QELYEATPQT
     NRRQTHAAIQ DRINTLLIDI RLYEKGLKLF SHDTQTQLVK YLLKSLGNDI CNELSLYVAS
     ECNLTVKNTS LNVDQRIKLA QECDAEYRSA LLEQNKALNK SIDDFELATE SVLKACSMII
     KKVDKKKDRL LIADHKNKLQ QQLLDCQEPA LLLHLAALIL FTTISGCILH ASGKFVSAIL
     QHIRGSLSDP QNDMLLRYHD LVLQVLQTAP ESDDSKMAHE QLQIMQSKVV ELAQNYTRAS
     VSKAD