ID A0A3P8RDE4_ASTCA Unreviewed; 697 AA.
AC A0A3P8RDE4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369081};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369081};
DE AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|RuleBase:RU369081};
GN Name=RNF157 {ECO:0000313|Ensembl:ENSACLP00000040055.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000040055.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000040055.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000040055.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin ligase. {ECO:0000256|RuleBase:RU369081}.
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 ECO:0000256|RuleBase:RU369081};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369081}.
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DR AlphaFoldDB; A0A3P8RDE4; -.
DR STRING; 8154.ENSACLP00000040055; -.
DR Ensembl; ENSACLT00000040998.1; ENSACLP00000040055.1; ENSACLG00000026987.1.
DR GeneTree; ENSGT00390000009925; -.
DR OMA; EDSCPVH; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000265100; Chromosome 8.
DR Bgee; ENSACLG00000026987; Expressed in brain and 8 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996:SF1; E3 UBIQUITIN LIGASE RNF157; 1.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU369081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369081};
KW Transferase {ECO:0000256|RuleBase:RU369081};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369081};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369081};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 278..317
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 340..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 75824 MW; B88F66B6D0C9E365 CRC64;
MGALTSRQNI GVEEVDIPSN SVYRYPPKSG SYFASHFIMG GEKFDSTHPE GYLFGENTDL
NFLGTRPVAF PYAAPPPQEP VKTLRSLINI RKDTLRLVRC SEDLKLPGDE AAGKTRACYN
VEFTFDADTQ VAITIYYQAI EEFHNGVPVY LPQDSSLQSE TVHFKRGVCQ QFCLPSHTVN
LSEWADDELQ FDMDKEIFPM VVQAVVDEGE DHLGHSHILL ATFEKHMDGS YCVKPLKQKQ
VVDGVSYLLQ EIYGIENKYN SQESKVADDE ISDNSAECVV CLSDVRDTLI LPCRHLCLCN
ACADTLRYQA NCCPICRLPF RALLQIRAIR KKLSPLSPSS FNPVITSQTS DSEEHSASEH
IPPGYEAVSL LEALNGPLNT TSVAPPPLHS GPSHVSGALP PYSSEPHPAP ARSLSPLDHS
NSGQALKLKK SGSKSLSQNS SVLPEEDEKS CSESEACRHK LAADQQECGV TPDSENLTFS
SSGAIDQSSC TGTPLSSTIT SPEDPVSSSL AQSVMSMASS HSQHSHISTD TMSSMSGSYL
AGAEGEPGGD EGGDVDCEEN QEASMENRRP SQQDREFSKE PKEQNYSVAV EDQDSEGNDV
TEEDCSSPSN GKGGRSRCPE LANNNQGVAL CDTPSLGLDN EQAPNSRFAD LLYLGGYRPV
LEPLPHHNST SNMNLEEQGA ESRVQSPKHP CRGPLIV
//
