ID A0A3Q0FLJ8_ALLSI Unreviewed; 405 AA.
AC A0A3Q0FLJ8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
GN Name=KCMF1 {ECO:0000313|RefSeq:XP_025048516.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025048516.1};
RN [1] {ECO:0000313|RefSeq:XP_025048516.1}
RP IDENTIFICATION.
RG RefSeq;
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_025048516.1; XM_025192731.1.
DR AlphaFoldDB; A0A3Q0FLJ8; -.
DR STRING; 38654.A0A3Q0FLJ8; -.
DR KEGG; asn:102385806; -.
DR InParanoid; A0A3Q0FLJ8; -.
DR OrthoDB; 26661at2759; -.
DR Proteomes; UP000189705; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000189705};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 28..84
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 102..130
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 178..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 405 AA; 44718 MW; 38551312CBFCEF14 CRC64;
MLMVMGRPEG RRQRGGCLPQ KGWVWSQWAG 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 ITQSTATTNT
SNTENSQQTI QNSQFLLTRL NDPKMSEAER QSMESERADR SLFVQELLLS TLMREESSSS
DEDERGEIAD FGAMGCVDIM PLDVALENLN LKESNKGNEP PPPPL
//
