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Database: UniProt
Entry: A0A2A2LF99_9BILA
LinkDB: A0A2A2LF99_9BILA
Original site: A0A2A2LF99_9BILA 
ID   A0A2A2LF99_9BILA        Unreviewed;       531 AA.
AC   A0A2A2LF99;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=E3 UFM1-protein ligase 1 homolog {ECO:0000256|ARBA:ARBA00014160};
DE   AltName: Full=E3 UFM1-protein transferase 1 homolog {ECO:0000256|ARBA:ARBA00030452};
GN   ORFNames=WR25_14627 {ECO:0000313|EMBL:PAV84768.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV84768.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV84768.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV84768.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
CC   -!- FUNCTION: E3 UFM1-protein ligase that mediates ufmylation of target
CC       proteins. {ECO:0000256|ARBA:ARBA00003950}.
CC   -!- SIMILARITY: Belongs to the UFL1 family.
CC       {ECO:0000256|ARBA:ARBA00010789}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAV84768.1}.
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DR   EMBL; LIAE01006820; PAV84768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2LF99; -.
DR   Proteomes; UP000218231; 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; E3 UFM1-PROTEIN LIGASE 1; 1.
DR   PANTHER; PTHR31057:SF0; E3 UFM1-PROTEIN LIGASE 1; 1.
DR   Pfam; PF09743; E3_UFM1_ligase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          388..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  60296 MW;  C759C5D8A83BE279 CRC64;
     MTTWKDIQKL ASDLQRIQLA QSVNKLSEQN CVEVISKLFN RKAINVVFTR DGHSYVTTKH
     LMTEVQNECL GNGGRCSLTE AATALNVDFD HVDAAAKRLV AEDDSYKLFN GELFSQEFAQ
     RLHQELLVLL NEHGFQTVQQ LAKHWNISQE LLNSMLLDKV DSNLIVLDES TFYNKDYLES
     RKNVLRGILA AISKPMSIAS IQKRVGLTTK RFWIAYDELQ NEGEVSGRLS ASRTSTACSY
     IPHYYDALIH QCLKNIYRQS NYIQVSLLRK LGIAEDKKEV EKMLEQKNIQ QLPTLFIADS
     FYKEIVNGIN EDLKNNGGLC DVRQYVQANE LPIEDADIDE IGEKIAQEHK NIHSANGYLF
     NTDYLQKIVK LLEEKIELKA KLELDRIQSE KKQPQKSAKP EKDDDWNEGG GKKKKGGAKG
     KGSGAKQQQQ PGRDRDEREE SPIQTEEWLR EVKEVPEDIL DTVAEEIKPA VSERFQSVLT
     HLIATQSTVS VQGQKNSIQA LQRSIKHLYD SICVFDAGCS TFSGQVFFIC F
//
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