UFL1_TRIAD
ID UFL1_TRIAD Reviewed; 780 AA.
AC B3RYG4;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-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=TRIADDRAFT_25797;
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Trichoplacidae; Trichoplax.
OX NCBI_TaxID=10228;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999;
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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; DS985245; EDV25034.1; -; Genomic_DNA.
DR RefSeq; XP_002112924.1; XM_002112888.1.
DR AlphaFoldDB; B3RYG4; -.
DR STRING; 10228.TriadP25797; -.
DR EnsemblMetazoa; TriadT25797; TriadP25797; TriadG25797.
DR GeneID; 6754137; -.
DR KEGG; tad:TRIADDRAFT_25797; -.
DR CTD; 6754137; -.
DR eggNOG; KOG2235; Eukaryota.
DR HOGENOM; CLU_012417_1_1_1; -.
DR InParanoid; B3RYG4; -.
DR OMA; NECSATK; -.
DR OrthoDB; 289380at2759; -.
DR PhylomeDB; B3RYG4; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0061666; F:UFM1 ligase activity; IEA:InterPro.
DR GO; GO:0071568; F:UFM1 transferase activity; IBA:GO_Central.
DR GO; GO:1990592; P:protein K69-linked ufmylation; IBA:GO_Central.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
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..780
FT /note="E3 UFM1-protein ligase 1 homolog"
FT /id="PRO_0000391897"
FT REGION 403..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 88685 MW; F1F9C86E7076081C CRC64;
MSDWNEIQRL AADFQRIQLT ASAHQLSERN CIEIITKLIA MNKVQVMYTI DGKEYLTPQQ
LEREIRDELF VHSGRINLVE LQQVINVDLT HIDSKVKEML RGDRSLYLIQ GDLIDRDYID
RLAEEINDIL QESGQISVSE LGKTFNLPTD FLQTNIEKRM GIYIHGQVNP LERGTIYTEA
YVARHAAKIR GVFSAITRPT SVSSIIYQYS FPEALLHDIL RKLLDEKRLA GSVQGHQSKA
IYTPNIYSRT QSNWVLSFFR QNDYIEYDSL TRLDITDPKN YLKKCLNKNV IFLESCVSGQ
NILGQVQAAI EDVVATPSWV DIMTLLPSPF TTGDASVLLQ KHCLKSNKNN TSVQCLCDKF
VVSNKFIQNC LQLFDDHMKT KAEKVYFHLL FIDAGKVAAK FASTSSTNPN HSTLTKHDDS
NVTGGKKKKG DDSTSSKRKG KGKDRSTPDD LESTRSHIKQ NKQDLEFMAI PEIIEVLQRE
HSNCEDQFLE EIASQLFSPL KRKYQEVAKS VFLASTSSVT SEKRKLHSDA QDKINGLLTN
AKLFGKGLQH FSGDAHTTLG KHLLHTLCTE ITNIVFSLLI SEHIMVDSDP NSLNPETRSS
ALEKFPNNVK KAASALEKSL SGKDVEQFFD ALDVVLGPSI CQIMIKKLDK KKERQIIFNH
RQSLIEQLNK ESKPAMCLHL CTLLLFQRHT QCMIHAPGRC IPQIISFLKQ HLTDEQYKTI
YEYQQLIIQS IQQSSDKQKP EMSEEPKDSD NSNDNQNIDL QLQEKMTTIK AIALENKKQS