ID A0A2U9CAQ5_SCOMX Unreviewed; 1845 AA.
AC A0A2U9CAQ5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=F2P81_021178 {ECO:0000313|EMBL:KAF0026441.1}, SMAX5B_018164
GN {ECO:0000313|EMBL:AWP13110.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP13110.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP13110.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF0026441.1, ECO:0000313|Proteomes:UP000438429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ysfricsl-2016a {ECO:0000313|EMBL:KAF0026441.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAF0026441.1};
RA Xu H., Xu X.-W., Shao C., Chen S.;
RT "Draft genomes of female and male turbot (Scophthalmus maximus).";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; CP026256; AWP13110.1; -; Genomic_DNA.
DR EMBL; VEVO01000019; KAF0026441.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000022862; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000246464; Chromosome 14.
DR Proteomes; UP000438429; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd16483; RING-H2_UBR3; 1.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF39; E3 UBIQUITIN-PROTEIN LIGASE UBR3; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 82..153
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT DOMAIN 1266..1321
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT ZN_FING 82..153
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 294..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1845 AA; 208396 MW; 278E0C9803E04CF1 CRC64;
MMAASQPLRR DKSATAAHLK ADLARTDTSS GLRQLQELLD VVLNPENPAA DTEALDWCKC
LIAGGEGFEE FCKTVRSYDN ATLCGLVWTA NFVAYRCRTC GISPCMSLCA ECFNNGDHTG
HDFNMFRSQA GGACDCGDGN VMRESGFCRR HRLRTGENVP SIPRDLLLMS EMVLPRFILC
IIQYLRDGYV EQDTAAERDL QKVLQQLEPQ ISFLEELTKM GGAMRTVLTK ILTNQQTFKE
LSMGQEENLY AKKNYDKYLS ALKNSGLVSV EEKAQGATAD VSVGAEGGAG ALALLGTTAP
GSPDESSKEE DPDSGQSVGQ RKRVKLSSST KDPRIIESLK HKCFLEELLF WTIKYEFPQK
MVTFLLNMLP DQDYKITFTK TFVQHYAFIM KTLMKSHESD TMSNRIVHIS VQLFSNEELA
RHVTEECQLL DIMVTVLLYM MESCLIKSEL QDEEHSRHVV VNCSEALLKN NTYWPLVSDF
INILSHQSVA KKFLEDHSLL MLWMSFVSFF QGMNLNKREL NEHVEFESQT YYAAFAAELE
ACAQPMWGLL THCKVKETQE YTKTVVRYCL ETLQIWFDAI GFIDEPSPNQ VTFHLPLHRY
YAMFLSKAIK CQGLDLDSLL PDQEMLMKIM VHPLQIQASL SEIHSNMWVR NGLQIKGQAM
TYVQSHFCNS MIDPDIYLLQ VCASRLDPDY FISSVFERFK VVDLLTMASQ HQNAVLDSEQ
ERPMLEGALT FLVILTSLRI HLGMTDDEIL RSEMVSQLCM NDRTHSALLD LIPENPNPKS
GIVPGSCSFE EMLSAVADFK APVFEPGGSM QQGMYTPKAE VWEKEFDPIM VVLRTVYRRD
VQSAMDRYSA FLKQSGVHTG NPWPPYKERT PLHPCYKGLI KLLHCKTLHI VIFTLLYKIW
MDHQNMSEHV LCMVLYLIEL GLDNQVQDNK EDEEPCIEEH CHDSWFPGTN LLSNLHHVIN
FVRVRVPETA PEVKREAPPS TSSEASSYGQ NLREAQVFSL VAERRRKFQE IINRSNTEAA
QVVRPKSSST RWVPPGTPPQ LVTEILEIRE SMLSLLIKLH QKMSSRQNSL SASWLEDMDT
SRHAHGDGIT AIERILTKAA TRSCQIKRSI QDICGKVCPP VPPKKNSPTD KKAMDKEERR
QRARERQQKL LAEFASRQKS FMETAMDVEP PDTEAAMDLG ASEVMESEVL YDCVICGQSG
PSTEDRPTGL VVLLQASSVL GHRCKNKEAK KLPTSDEEHI YPADTCGVAH DVRLTLMQRF
FKDSSCLQSV SIGWDGGVYV QTCGHTLHID CHKSYMESLR NDQVLQGFSV DKGEFTCPLC
RQFANSVLPC RPGRSTEAGA WHAPTNKKMC VLVKEVEDLQ DKLGLFPTET NLSKEMELVI
KDIKNTTQKK YMDYGKNPAS PDNDFLFMYS VARTNLELEL VHRGGNLCSG GASAAAKRSC
LNQLFHVLAM HMRLYSIDSA YNPWTRLTQI TQNKEADSFD DERPEVPMLF RDVPSLLIIF
VLTMPQPLRK EHFTCVVKML YNLQFIQAVA ALSTRLSPEE RQAWSTSGAL KKNAANADTS
FEVLLSHAIG ELSTDKGVYD VNAEETSMLS SSVWSPQSIE FSLQQFCLPF LRLSCLLQHH
LYGDNLTGCS EEEEFSSLAV CLGLLPSAPQ PSNTVHSASC LEWAVSAFDS VTQWCAEVRG
LTHMQAEQSL TLLDQDPQWA ASRLLQLPDN YNIIFQYYHR KACTSCKKVP KDPALCLVCG
AFVCLKGVCC KQQGVCECVS HSQHCGAATG IFLLINASVI IIIRGHRFCL WGSVYLDAHG
EEDRDLRRGK PLFLCEERYR VLEQQWVSHT FDHINKRWGP HYNGL
//
