ID   UFL1_DROER              Reviewed;         782 AA.
AC   B3P2S2;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-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=GG10135;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
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; CH954181; EDV48094.1; -; Genomic_DNA.
DR   RefSeq; XP_001979136.1; XM_001979100.2.
DR   AlphaFoldDB; B3P2S2; -.
DR   STRING; 7220.FBpp0128681; -.
DR   EnsemblMetazoa; FBtr0130189; FBpp0128681; FBgn0102446.
DR   GeneID; 6553192; -.
DR   KEGG; der:6553192; -.
DR   eggNOG; KOG2235; Eukaryota.
DR   HOGENOM; CLU_012417_1_1_1; -.
DR   OMA; NECSATK; -.
DR   OrthoDB; 289380at2759; -.
DR   PhylomeDB; B3P2S2; -.
DR   Proteomes; UP000008711; 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   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..782
FT                   /note="E3 UFM1-protein ligase 1 homolog"
FT                   /id="PRO_0000391880"
FT   REGION          404..477
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;  87190 MW;  B8523C3940E4BC86 CRC64;
     MGSDWDEIKR LAADFQKAQL TSTLQKLSER NCVEIVTLLL EKQMLEVVFT NDGKEYITPD
     HLEREIQDEL YVNGGRANLV EVSKTLNVDL SRIEVLAERI AAENPSVHLV LGQLIDEDYI
     SHIAQEINEK LVLRGEISIS ELASQFDLPS DFLQHDVVEK HLGKIIKGRQ DAANPRVFFT
     QAYIQRCKAK IRGALAAITR PINVAVILQQ IGVQEKIFHS LLDEIAPAGQ VTSKLANSQY
     VPHIYAKTQA DWVNSFYKQN SFLEYDAIQK LGISDAKSYI RKQFPNEEFL FLKRVALGAR
     LVELTVVTAL NECSATKQYL DLTTILPSNL SEEDIEEVFS TIMAQKHSNP SNFVYLDSIV
     FSQPYLAQLV QPCQALAESQ AKAAIDGGVY QQYIVEKTLA QKGNASTQEL EDDGKVDKRD
     ERRKKASSGK AGGGAQGRET KTKSTKKHQR GKAAAHNDSD DEDDVQQGSR GGGGVNKKAV
     KPLELVKTAD IVKLITASLE EEGLEHLSKP IAALYTNQFN QTALARAQEL FEATPQTNRR
     QTHAAIQDRI NTLLIDIRLY EKGLKLFPQD TQTQLVKYLL KSLGNDICNE LSLYVAGECN
     LTVKNTNLNV DQRNKLAQEC EAQYRAALLE QNKALNKSID EFELATETVL KACSMIIKKV
     DKKKDRLLIA DHKKKLQKQL LECQDPALLL HLAALILFTA ISGSILHASG KFVSAILQHI
     RGSLNEEQNA LLLRYHDLVL QVLQATPDSS ESKMANEHLQ AMQAQVVELA QNFSRASVSK
     AD