ID   UBR7_DICDI              Reviewed;         465 AA.
AC   Q54DV0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Putative E3 ubiquitin-protein ligase ubr7;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase ubr7;
GN   Name=ubr7; ORFNames=DDB_G0292022;
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: Putative E3 ubiquitin-protein ligase. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SIMILARITY: Belongs to the UBR7 family. {ECO:0000305}.
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DR   EMBL; AAFI02000187; EAL61367.2; -; Genomic_DNA.
DR   RefSeq; XP_629772.2; XM_629770.2.
DR   AlphaFoldDB; Q54DV0; -.
DR   STRING; 44689.DDB0302514; -.
DR   PaxDb; Q54DV0; -.
DR   EnsemblProtists; EAL61367; EAL61367; DDB_G0292022.
DR   GeneID; 8628448; -.
DR   KEGG; ddi:DDB_G0292022; -.
DR   dictyBase; DDB_G0292022; ubr7.
DR   eggNOG; KOG2752; Eukaryota.
DR   HOGENOM; CLU_025221_0_0_1; -.
DR   InParanoid; Q54DV0; -.
DR   OMA; GQPYFCR; -.
DR   PhylomeDB; Q54DV0; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q54DV0; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR040204; UBR7.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR13513; PTHR13513; 2.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Metal-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..465
FT                   /note="Putative E3 ubiquitin-protein ligase ubr7"
FT                   /id="PRO_0000371349"
FT   ZN_FING         100..174
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT   ZN_FING         237..293
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          65..98
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        12..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  53363 MW;  61081B37B086C1BE CRC64;
     MDNEKVTDTN PKEPSNVESI ITTSEVTPSP PPSTTTSTTT NATTTITTSQ PQANIIGGKR
     SRKDDEIISI QEALNDQLEE EKNLLEEAKE QEQEDWGDES ICTFDKGYIN QSVFACKTCQ
     LSNDKLFGFC YGCSMHCHLY HDVYELFNKR NFRCDCGTKI QEPNNSFKCQ LSGILKEDDN
     NNVNNINNSN NTTTTTTTTT TTTTTTNNNH LNDIDIGSYD KSQILNERNH YNHNFKGKYC
     YCDSPYDYKE DMIQCIFCED WFHENCLKLN SNVTDIPSPG EFSDLICADC LSKNQFLLLY
     PQIRCYIEND HIIIGDNNNN NNNSNNSNSI CKVEGGVITP NKKYDLFCKE LWKDELCSCL
     KCKEIYKDKK VEFLFEKDEN SLKKKNKTVD ENLDNKPVNV FEMGQDVFSK TLPPTQQRAL
     IEGFSDMKEK LKELFSKKLD KNQVITKQDI QSFFVDLNVN KKFKK