ID   UFM1_DICDI              Reviewed;          85 AA.
AC   B0G186;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Ubiquitin-fold modifier 1;
DE   Flags: Precursor;
GN   Name=ufm1; ORFNames=DDB_G0295709;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Ubiquitin-like modifier which can be covalently attached to
CC       substrate proteins as a monomer or a lysine-linked polymer in a post-
CC       translational process called ufmylation. Ufmylation on lysine residues
CC       of proteins may play a crucial role in a number of cellular processes.
CC       {ECO:0000250|UniProtKB:P61960, ECO:0000250|UniProtKB:P61961}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61960}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P61960}.
CC   -!- SIMILARITY: Belongs to the UFM1 family. {ECO:0000305}.
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DR   EMBL; AAFI02000179; EDR41022.1; -; Genomic_DNA.
DR   RefSeq; XP_001733049.1; XM_001732997.1.
DR   AlphaFoldDB; B0G186; -.
DR   SMR; B0G186; -.
DR   STRING; 44689.DDB0252554; -.
DR   PaxDb; B0G186; -.
DR   EnsemblProtists; EDR41022; EDR41022; DDB_G0295709.
DR   GeneID; 8628285; -.
DR   KEGG; ddi:DDB_G0295709; -.
DR   dictyBase; DDB_G0295709; ufm1.
DR   eggNOG; KOG3483; Eukaryota.
DR   HOGENOM; CLU_175114_0_0_1; -.
DR   InParanoid; B0G186; -.
DR   OMA; INPAQNA; -.
DR   PhylomeDB; B0G186; -.
DR   PRO; PR:B0G186; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR005375; UFM1.
DR   PANTHER; PTHR15825; PTHR15825; 1.
DR   Pfam; PF03671; Ufm1; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..83
FT                   /note="Ubiquitin-fold modifier 1"
FT                   /id="PRO_0000329966"
FT   PROPEP          84..85
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
FT                   /id="PRO_0000329967"
FT   CROSSLNK        69
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in UFM1)"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
FT   CROSSLNK        83
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000250|UniProtKB:P61960"
SQ   SEQUENCE   85 AA;  9365 MW;  2BBDC0C043CCC0A1 CRC64;
     MSKVTFKITL TSDPKLPFRV INVTEDTPFT AVLRFACEQF NVPWQTSAII TNDGIGINPA
     QTSGNIFLKN GSDLRLIPRD RVGGL