ID   UFL1_DROSE              Reviewed;         782 AA.
AC   B4I4N0;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
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=GM10514;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480821; EDW55173.1; -; Genomic_DNA.
DR   RefSeq; XP_002038636.1; XM_002038600.1.
DR   AlphaFoldDB; B4I4N0; -.
DR   STRING; 7238.B4I4N0; -.
DR   EnsemblMetazoa; FBtr0193499; FBpp0191991; FBgn0165461.
DR   GeneID; 6614189; -.
DR   KEGG; dse:6614189; -.
DR   HOGENOM; CLU_012417_1_1_1; -.
DR   OMA; NECSATK; -.
DR   PhylomeDB; B4I4N0; -.
DR   ChiTaRS; eIF-3p66; fly.
DR   Proteomes; UP000001292; 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..782
FT                   /note="E3 UFM1-protein ligase 1 homolog"
FT                   /id="PRO_0000391886"
FT   REGION          405..478
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   782 AA;  87412 MW;  844F0D427AFF988A CRC64;
     MGSDWDEIKR LAADFQKAQL TSTLQKLSER NCVEIVTLLL EKQMLEVVFT NDGKEYITPD
     HLEREIQDEL YVNGGRANLV EVSKTLNVDL SRIEVLAERI AAENPSVHLV LGQLIDEDYI
     SHIAQEINEK LVQRGEISIS ELASQFDLPS DFLQHDVVEK HLGKIIKGRQ DASNPRVFFT
     QAYIQRCKAK IRGALAAITR PINVAVILQQ IGVQEKIFHS LLDEIAPAGQ VTSKQANSQY
     VPHIYAKTQA DWVNSFYKQN SFLEYDAIQK LGISDAKSYI RKQFPNEEFL FLKRVALGAR
     LVELTVVTAL NECSATKQYL DLTTILPSNL SEEDIEEVFS TIMAQKHSNP SNFVYLDGIV
     FSQPYLAQLV QPCKALAESQ AKAAIDGGVY QQYIVEKTLA QKGNVSTQEL EDDGKVDKRD
     ERRKKASSGK AGGGAQGRET KTKSTKKHQR GKAAAQFDSD DEDDVQQGTR GGGGASKKAV
     KPLELVKTAD IVKLITASLE EEGLEHLSKP IAALYTNQFN QTALARAQEL FEATPQTNRR
     QTHAAIQDRI NTLLIDIRLY EKGLKLFPQD TQTQLVKYLL KSLGNEICNE LSLYVASECN
     LTVKNTNLNV DQRNKLAQEC EAQYRAALLE QNKALNKSID EFELATETVL KSCSMIIKKV
     DKKKDRLLIA DHKRKLQKQL LECHEPALLL HLAALILFTT ITGSILHASG KFVSAILQHI
     RGSLNEEQNA LLLRYHDLVL QVLQATPDSN ESKLANEHLQ AMQTQVVELA QNFSRASVSK
     AD