ID A0A3B5QR25_XIPMA Unreviewed; 389 AA.
AC A0A3B5QR25;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000033593.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000033593.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000033593.1};
RG Ensembl;
RL Submitted (NOV-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_005798702.1; XM_005798645.1.
DR AlphaFoldDB; A0A3B5QR25; -.
DR Ensembl; ENSXMAT00000027595.1; ENSXMAP00000033593.1; ENSXMAG00000021858.1.
DR GeneID; 102229397; -.
DR KEGG; xma:102229397; -.
DR CTD; 56888; -.
DR GeneTree; ENSGT00510000047171; -.
DR InParanoid; A0A3B5QR25; -.
DR OMA; RDLLWSY; -.
DR OrthoDB; 26661at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000002852};
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 259..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 42575 MW; C3E31661DCCE40EC 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 GNNPNNTGNS IPPPNSSTAN TSAVGDSNPA SSSQSSQFLL
ARLNEPKMSE AERQFLEGER ADRSLFVQEL LLSTLMHEES SSSDEDERRD FADFGAMGCV
DIMPLDVALE NLQLRESSSS GREPPPPPL
//
