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Database: UniProt
Entry: A0A2D0RJF5_ICTPU
LinkDB: A0A2D0RJF5_ICTPU
Original site: A0A2D0RJF5_ICTPU 
ID   A0A2D0RJF5_ICTPU        Unreviewed;       191 AA.
AC   A0A2D0RJF5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=rnf4 {ECO:0000313|RefSeq:XP_017330657.1,
GN   ECO:0000313|RefSeq:XP_053538281.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017330657.1};
RN   [1] {ECO:0000313|RefSeq:XP_017330657.1, ECO:0000313|RefSeq:XP_053538281.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017330657.1,
RC   ECO:0000313|RefSeq:XP_053538281.1};
RG   RefSeq;
RL   Submitted (SEP-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 {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_017330657.1; XM_017475168.3.
DR   RefSeq; XP_053538281.1; XM_053682306.1.
DR   GeneID; 108269346; -.
DR   KEGG; ipu:108269346; -.
DR   CTD; 6047; -.
DR   OrthoDB; 2919802at2759; -.
DR   Proteomes; UP000221080; Chromosome 8.
DR   GO; GO:0005634; C:nucleus; 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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047134; RNF4-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23041:SF78; E3 UBIQUITIN-PROTEIN LIGASE RNF4; 1.
DR   PANTHER; PTHR23041; RING FINGER DOMAIN-CONTAINING; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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          133..178
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   191 AA;  20948 MW;  92D18F14507324B5 CRC64;
     MSSATQRKRR TTSTSCSRRN SKRSRTQMSQ ASMETIDVLE SDRLSSEFTE VSPGEEVVDL
     TCEGSEPAVV DLTNNDSVVL VDDGAQSRRT QGPESYVLSS DDEEEPSQSL SPALLSSLHA
     SARARSTPGA VSCPVCMDAY AEIIESGRLM VSTKCGHLFC SQCIRDSLAR AHNCPTCRKK
     LTYKQYHPIY I
//
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