KCMF1_BOVIN
ID KCMF1_BOVIN Reviewed; 381 AA.
AC Q1LZE1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) 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; BC116058; AAI16059.1; -; mRNA.
DR RefSeq; NP_001069743.1; NM_001076275.1.
DR AlphaFoldDB; Q1LZE1; -.
DR SMR; Q1LZE1; -.
DR STRING; 9913.ENSBTAP00000051183; -.
DR PaxDb; Q1LZE1; -.
DR GeneID; 613522; -.
DR KEGG; bta:613522; -.
DR CTD; 56888; -.
DR eggNOG; KOG1280; Eukaryota.
DR InParanoid; Q1LZE1; -.
DR OrthoDB; 1107794at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 Acetylation; Coiled coil; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT CHAIN 2..381
FT /note="E3 ubiquitin-protein ligase KCMF1"
FT /id="PRO_0000349218"
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 250..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 224..257
FT /evidence="ECO:0000255"
FT COMPBIAS 169..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..314
FT /note="Basic and acidic 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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0J7"
SQ SEQUENCE 381 AA; 41947 MW; AAEFE00BBEE7CB0F CRC64;
MSRHEGVSCD ACLKGNFRGR RYKCLICYDY DLCASCYESG ATTTRHTTDH PMQCILTRVD
FDLYYGGEAF SVEQPQSFTC PYCGKMGYTE TSLQEHVTSE HAETSTEVIC PICAALPGGD
PNHVTDDFAA HLTLEHRAPR DLDESSGVRH VRRMFHPGRG LGGPRARRSN MHFTSSSTGG
LSSSQSSYSP SNREAMDPIA ELLSQLSGVR RSAGGQLNSS GPSASQLQQL QMQLQLERQH
AQAARQQLET ARNATRRTNT SSVTTTITQS TATTNTANTE SSQQTIQNSQ FLLTRLNDPK
MSETERQSME SERADRSLFV QELLLSTLVR EESSSSDEDE RGEMADFGAM GCVDIMPLDV
ALENLNLKES NKGNEPPPPP L
