ID A0A1S3SWM8_SALSA Unreviewed; 665 AA.
AC A0A1S3SWM8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=LOC106612253 {ECO:0000313|RefSeq:XP_014068740.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014068740.1};
RN [1] {ECO:0000313|RefSeq:XP_014068740.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014068740.1};
RG RefSeq;
RL Submitted (NOV-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_014068740.1; XM_014213265.1.
DR AlphaFoldDB; A0A1S3SWM8; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR Bgee; ENSSSAG00000067265; Expressed in camera-type eye and 3 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 Reference proteome {ECO:0000313|Proteomes:UP000087266};
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 389..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 665 AA; 72693 MW; 02D51404B65088E0 CRC64;
MGALTSRQNA GVEEVDIPST SVYRYPPKSG SYFASHFIMG GEKFDSTHPE GYLFGENTDL
NFLGTRPVVF PYASPPPQEP VKTLRSLINI RKDTLRLVRC SDGQKLPGEE VAGKSKACYN
IEFTFDADTQ VAITIYYQAI EEFHNGVPIY LPQDSSLQSE MVHFKRGVCQ QFCLPSHSVN
LSEWADEELL FDMDKDVFPM VIQATVDEGE DHMGHSHVLL ATFEKHMDGS YCVKPLKQKQ
VVDGVSYLLQ EIYGIENKYN SQESKVADDE ISDNSAECVV CLSDVRDTLI LPCRHLCLCN
ACADTLRYQA NCCPICRLPF RALLQIRAMR KKLSPLSPAR FNPVITSQTS DSEEHSVSDH
IPPGYEIVSL LEALNGPLSV SPSAPPLQDL SVGHISGTLP PYSSETHPAP AHSMSPLDHS
NSSQRLKLKK SGSKSLSQNS SVLPGEEGKK SQHSESEVQA CRRKQQLESG VTSESENLTL
SSSGAIDQSS CTGTPFSSTI TSPEDPVNSS LAQSVMSIAF SHSQHSQIST DTLSSMSGSY
LAGPEGEVEG GDIEGEKIQD APMESRGPSQ QDGECFLIVK ELPIEPKEHN FSLAVSEEQD
SEGNDVTGEH CPSPSHKQGG RSRCPELANN NHALCDTPCM RGLDNEQVPD SRFADADSCP
VHIEE
//