GenomeNet

Database: UniProt
Entry: A0A384AEN5_BALAS
LinkDB: A0A384AEN5_BALAS
Original site: A0A384AEN5_BALAS 
ID   A0A384AEN5_BALAS        Unreviewed;       575 AA.
AC   A0A384AEN5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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|RefSeq:XP_007185806.1,
GN   ECO:0000313|RefSeq:XP_007185807.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007185806.1};
RN   [1] {ECO:0000313|RefSeq:XP_007185806.1, ECO:0000313|RefSeq:XP_007185807.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007185806.1,
RC   ECO:0000313|RefSeq:XP_007185807.1};
RG   RefSeq;
RL   Submitted (JAN-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   RefSeq; XP_007185806.1; XM_007185744.2.
DR   RefSeq; XP_007185807.1; XM_007185745.2.
DR   AlphaFoldDB; A0A384AEN5; -.
DR   GeneID; 103002490; -.
DR   CTD; 114804; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000261681; Unplaced.
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   CDD; cd16817; mRING-HC-C3HC5_RNF157; 1.
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   SMART; SM00184; RING; 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   Reference proteome {ECO:0000313|Proteomes:UP000261681};
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          277..316
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          339..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..575
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  63699 MW;  C9BD2334644A5AD7 CRC64;
     MGALTSRQHA GVEEVDIPSN SVYRYPPKSG SYFASHFIMG GEKFDSTHPE GYLFGENSDL
     NFLGNRPVAF PYAAPPPQEP VKTLRSLINI RKDTLRLVKC AEEVKTPGEE AGRAKVHYNV
     EFTFDTDARV AITIYYQATE EFQNGIASYI PKDNSLQSET VHYKRGVCQQ FCLPSHTVDP
     SEWAEEELGF DLDREVYPLV VHAVVDEGDE YFGHCHVLLG TFEKHTDGTF CVKPLKQKQV
     VDGVSYLLQE IYGIENKYNT QESKVAEDEV SDNSAECVVC LSDVRDTLIL PCRHLCLCNT
     CADTLRYQAN NCPICRLPFR ALLQIRAMRK KLGPLSPTSF NPILSSQTSD SEEHSSSENI
     PPGYEVVSLL EALNGPLTPS PAVPPLHVLG DRRRSGMLPS YGSDGHLPPV RTLSPLDRLS
     DCSSPGLKLR NSLSKSISQN SSVLHEEEDE RSCSESETHL SQRPSAQHLR EECGITPESE
     NLTLSSSGAI DQSSCTGTPL SSTISSPEDQ HRHRLLHVRL LHRPWHGRGG GGSPLPPGCQ
     QDPLGRRRGD TGGVSRLQLC GPRRRRRRRA GCRGK
//
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