ID A0A3Q2WKL9_HAPBU Unreviewed; 632 AA.
AC A0A3Q2WKL9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Checkpoint with forkhead and RING finger domains protein {ECO:0000256|ARBA:ARBA00031332};
DE AltName: Full=RING-type E3 ubiquitin transferase CHFR {ECO:0000256|ARBA:ARBA00029800};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000026301.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000026301.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body
CC {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the CHFR family.
CC {ECO:0000256|ARBA:ARBA00005797}.
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DR RefSeq; XP_005933390.1; XM_005933328.2.
DR RefSeq; XP_005933391.1; XM_005933329.2.
DR RefSeq; XP_005933392.1; XM_005933330.2.
DR AlphaFoldDB; A0A3Q2WKL9; -.
DR STRING; 8153.ENSHBUP00000026301; -.
DR Ensembl; ENSHBUT00000003713.1; ENSHBUP00000026301.1; ENSHBUG00000008924.1.
DR GeneID; 102295794; -.
DR CTD; 55743; -.
DR GeneTree; ENSGT00400000022306; -.
DR OMA; SNYWFPG; -.
DR OrthoDB; 450556at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd22672; FHA_CHFR; 1.
DR CDD; cd16503; RING-HC_CHFR; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.40.140; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR019406; APLF_PBZ.
DR InterPro; IPR040909; CHFR_Znf-CRD.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR Pfam; PF10283; zf-CCHH; 1.
DR Pfam; PF17979; zf-CRD; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 28..79
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 253..292
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 188..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 70782 MW; 2887D27234B4DFD1 CRC64;
MDSRRGRAWG KLVKVDSSET VMLFNSECTV GRKKGCYLSF PANKLVSGEH CKIVKDESSG
LVWLEDMSTN GTVINMSKLV KKQTHMLQNG DVIYFVYRKS EPEQNIAYVY HSIKMDHTAS
QHNYGSEMAL SVEPVMLSKA PRDATQEEPQ PSTSASHFCI ETAYSSGAMA TTGSPVTGGF
STHALLKGQA KDPTTTQEEE TENLEPTSKR RKTDDDKSYE LGVPCSSRPE VVSSSKPPVE
GTKTDKMEES LTCVICQDLL HDCVSLQPCM HVFCAACYSG WMERSSLCPT CRCPVERIHK
NHILNNLVEA YLIQHPEKCR SEDDLKSMDS RNKITQDMLQ PKVERSFSDE EGSSDYLFEL
SDNDSDSSDI SQPLVMCRQC PGYRSDVNQL LFASSSSYWF PGLPSLQPMP PPPNPVSEEA
AAKASAEMPS TSSDNNNESP QEYRCPPQGC HLICTCCLQP MPDRRAELGN QQVIAQQCVL
CQRPFCHMYW GCQRIGCQGC LARFCDLNLT DKCLDGVLNN NNYESEVLRN YLSSRGQSWK
DLLKDSLQGL QQGNYLLTDC RVSANAILCF CCGLRAFKEL AYKYRQNIPS SELPATVTSR
PDCYWGRNCR TQVKAHHAAK FNHICEQTRF KS
//
