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UFL1_DROGR
ID   UFL1_DROGR              Reviewed;         783 AA.
AC   B4JV25;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=GH17388;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
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; CH916374; EDV91345.1; -; Genomic_DNA.
DR   RefSeq; XP_001994716.1; XM_001994680.1.
DR   AlphaFoldDB; B4JV25; -.
DR   STRING; 7222.FBpp0151294; -.
DR   PRIDE; B4JV25; -.
DR   EnsemblMetazoa; FBtr0152802; FBpp0151294; FBgn0124858.
DR   GeneID; 6568384; -.
DR   KEGG; dgr:6568384; -.
DR   eggNOG; KOG2235; Eukaryota.
DR   HOGENOM; CLU_012417_1_1_1; -.
DR   InParanoid; B4JV25; -.
DR   OMA; NECSATK; -.
DR   OrthoDB; 289380at2759; -.
DR   PhylomeDB; B4JV25; -.
DR   Proteomes; UP000001070; 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..783
FT                   /note="E3 UFM1-protein ligase 1 homolog"
FT                   /id="PRO_0000391881"
FT   REGION          406..476
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   783 AA;  87899 MW;  AEF958628C45B4CF CRC64;
     MSSDWDEIKR LAADFQKAQL TSTLQKLSER NCIEIVTLLL EKQLLDVVFT NDGKEYITPE
     HLEREIQDEL YANGGRANLV EVSKTLNVDL SRIEKLAERI AADDPQIHLM LGQLIDEEYI
     THIAQEINEK LSQRGEISIS DLTSQFDLPS DFLQHQVVEK HLGKLIKGRQ DASNPRVFFT
     QAYIQRCKAK IRGALAAITK PTNVSVILQQ ISVQEKIFHS LLDEINPAGH VTSKQANAQY
     VPHIYAKTQA DWVNSFYKQN SFLEYDAINK LGISDAKSYI RKQFPNEEFL FLKRVALGAR
     LIELTVVASL NECSATKQYL DLSTILPSNL SEEDIEEAFN AVMAQKHCNP SQFVYLESIV
     FSQAYLTQLV QPCQEMAQSL AKTAIDNGVY QQYIVEKTLA QKAGNTLGTT HDADEDSKLD
     KRDERRKKAT SGKAGGGSQG RETKTKSTKK HQRGRAAHNH DSDDEEDAVQ QSANSSRKSV
     KSLELVKISD ITNLIKGTLE EEGLEHLAKP VASLYLNQLN QMALAKAQEL YEAAPQTNRR
     QTHAAIQERV NTLLVDIRLY EKGLKLFNGD TQTQLVKYLL KSLGNDICNE LTLYVAAECS
     LMVKSTNLNV DQRVKLVQEC DAQYRNALLE QNKALNKSIE EFEVATEAVL KACSMIIKKV
     DKKKDRQLIV GHKEKLLQQL LECQEPALLL HLAALILFTT ITGCILHASG KFVSSILQHI
     RSTLNEPQNA LLLRYHDLVL QVLQQTSPDS AESKSVNEQL QALQGEVMDL AQNYSRASVS
     KAD
 
 
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