ID   KCMF1_XENLA             Reviewed;         381 AA.
AC   Q6GPB6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=E3 ubiquitin-protein ligase KCMF1;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase KCMF1 {ECO:0000305};
GN   Name=kcmf1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes
CC       ubiquitination. {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   -!- SIMILARITY: Belongs to the KCMF1 family. {ECO:0000305}.
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DR   EMBL; BC073225; AAH73225.1; -; mRNA.
DR   RefSeq; NP_001085703.1; NM_001092234.1.
DR   AlphaFoldDB; Q6GPB6; -.
DR   SMR; Q6GPB6; -.
DR   BioGRID; 102292; 1.
DR   IntAct; Q6GPB6; 1.
DR   DNASU; 444129; -.
DR   GeneID; 444129; -.
DR   KEGG; xla:444129; -.
DR   CTD; 444129; -.
DR   Xenbase; XB-GENE-1021681; kcmf1.L.
DR   OrthoDB; 1107794at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 444129; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.60.90; -; 1.
DR   InterPro; IPR008598; Di19_Zn-bd.
DR   InterPro; IPR039858; KCMF1.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR12268:SF13; PTHR12268:SF13; 1.
DR   Pfam; PF05605; zf-Di19; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Metal-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..381
FT                   /note="E3 ubiquitin-protein ligase KCMF1"
FT                   /id="PRO_0000349222"
FT   ZN_FING         4..60
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   ZN_FING         78..101
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          154..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          223..261
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        169..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ   SEQUENCE   381 AA;  41943 MW;  2AF9B21642C63FAC CRC64;
     MSRHEGVSCD ACLKGNFRGR RYKCLICYDY DLCASCYESG ATTTRHTTDH PMQCILTRVD
     FDLYYGGEAF SVEQPQSFTC PYCGKMGYTE TSLQEHVTSE HAETSTEVIC PICAALPGGD
     PNHVTDDFAA HLTLEHRAPR DLDESSGVRH VRRMFHPGRG LGGPRARRTN MHFTSSSTGG
     LSSSQSSYSP SNREAMDPIA ELLSQLSGVR RSTGGQLNSS GPSASQLQQL QMQLQLERQQ
     AQAARQQLET ARNATRRNNA SNVTTTITQS TAATNTSSTE NNQQSIQNSQ FLLTRLNDPK
     MTEAERQSIE SERADRSLFV QELLLSTLMQ EESSSSDEDE RGEIADFGAM GCVDIMPLDV
     ALENLNLKES NKGNEPPPPP L