ID A0A3B3TRF1_9TELE Unreviewed; 389 AA.
AC A0A3B3TRF1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000003173.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000003173.1}
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}.
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DR RefSeq; XP_014899526.1; XM_015044040.1.
DR AlphaFoldDB; A0A3B3TRF1; -.
DR STRING; 48699.ENSPLAP00000003173; -.
DR Ensembl; ENSPLAT00000011820.1; ENSPLAP00000003173.1; ENSPLAG00000004595.1.
DR GeneID; 106954506; -.
DR KEGG; plai:106954506; -.
DR CTD; 56888; -.
DR GeneTree; ENSGT00510000047171; -.
DR OrthoDB; 26661at2759; -.
DR Proteomes; UP000261500; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 4..60
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 78..106
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 155..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 42531 MW; F4EEAC8AB4595591 CRC64;
MSRHEGVSCD ACLKGNFRGR RFKCLICYDY DLCASCYESG ATTTRHTTEH PMQCILTRVD
YDLYYGGDTF SVEQPQSFTC PYCGKMGFTE TSLQEHVTSE HSETSTEVIC PICAALPGGD
PNHVTDDFTA HLTLEHRAPR DLDESSSVRH VRRMFHPGRG IGGPRARRTN MHFTSGSTGG
LSSSSSQSST YTPSNRETMD PIAELLSQLS GVRRAAGGQI NSSGPSASQL QQLQMQLQLE
RQQAQAARQQ VEAGRHATRR GNNPGNTGNS IPPPNSSNAN TSAVGDSNPA SSSQSSQFLL
ARLNEPKMSE AERQFLEGER ADRSLFVQEL LLSTLMHEES SSSDEDERRD FADFGAMGCV
DIMPLDVALE NLQLRESSSS GREPPPPPL
//
