ID A0A2K6A7W4_MANLE Unreviewed; 375 AA.
AC A0A2K6A7W4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=E3 ubiquitin-protein ligase KCMF1 {ECO:0000256|ARBA:ARBA00014999};
DE AltName: Full=RING-type E3 ubiquitin transferase KCMF1 {ECO:0000256|ARBA:ARBA00030767};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000036156.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000036156.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes
CC ubiquitination. {ECO:0000256|ARBA:ARBA00003752}.
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; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- SIMILARITY: Belongs to the KCMF1 family.
CC {ECO:0000256|ARBA:ARBA00010938}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K6A7W4; -.
DR STRING; 9568.ENSMLEP00000036156; -.
DR Ensembl; ENSMLET00000059756.1; ENSMLEP00000036156.1; ENSMLEG00000042199.1.
DR GeneTree; ENSGT00510000047171; -.
DR OMA; RDLLWSY; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd02338; ZZ_PCMF_like; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR PANTHER; PTHR12268:SF13; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 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 SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 1..54
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 72..100
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 148..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 221..248
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 163..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 41248 MW; 21F56763A85C1AB3 CRC64;
VSCDACLKGN FRGRRYKCLI CYDYDLCASC YESGATTTRH TTDHPMQCIL TRVDFDLYYG
GEAFSVEQPQ SFTCPYCGKM GYTETSLQEH VTSEHAETST EVICPICAAL PGGDPNHVTD
DFAAHLTLEH RAPRDLDESS GVRHVRRMFH PGRGLGGPRA RRSNMHFTSS STGGLSSSQS
SYSPSNREAM DPIAELLSQL SGVRRSAGGQ LNSSGPSASQ LQQLQMQLQL ERQHAQAARQ
QLETARNATR RTNTSSVTTT ITQSTATTNI ANTESSQQTL QNSQFLLTRL NDPKMSETER
QSMESERADR SLFVQELLLS TLVREESSSS DEDDRGEMAD FGAMGCVDIM PLDVALENLN
LKESNKGNEP PPPPL
//
