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Database: UniProt
Entry: A0A1U8CJX4_MESAU
LinkDB: A0A1U8CJX4_MESAU
Original site: A0A1U8CJX4_MESAU 
ID   A0A1U8CJX4_MESAU        Unreviewed;       752 AA.
AC   A0A1U8CJX4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 2.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE            EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN   Name=Smurf1 {ECO:0000313|RefSeq:XP_012975973.2};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012975973.2};
RN   [1] {ECO:0000313|RefSeq:XP_012975973.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26319212;
RA   Ying B., Toth K., Spencer J.F., Aurora R., Wold W.S.;
RT   "Transcriptome sequencing and development of an expression microarray
RT   platform for liver infection in adenovirus type 5-infected Syrian golden
RT   hamsters.";
RL   Virology 485:305-312(2015).
RN   [2] {ECO:0000313|RefSeq:XP_012975973.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885,
CC         ECO:0000256|PIRNR:PIRNR001569};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR   RefSeq; XP_012975973.2; XM_013120519.2.
DR   AlphaFoldDB; A0A1U8CJX4; -.
DR   STRING; 10036.ENSMAUP00000000645; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd08382; C2_Smurf-like; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254:SF293; E3 UBIQUITIN-PROTEIN LIGASE SMURF1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 2.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 4.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR001569}.
FT   DOMAIN          1..120
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          232..265
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          304..337
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          418..752
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          183..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        720
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   752 AA;  85637 MW;  2D95BA638A6C9D5B CRC64;
     MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKI VVDGSGQCHS TDTVKNTLDP
     KWNQHYDLYV GKTDSITISV WNHKKIHKKQ GAGFLGCVRL LSNAISRLKD TGYQRLDLCK
     LNPSDTDAVR GQIVVSLQTR DRIGSGGSVV DCRGLLENEG TVYEDSGPGR PLSCLMEEPA
     PYTDGTGAAA GGGDCRFVGS PSQDQRLQRL RNPEIRGSLQ TPQNRPHGHQ SPELPEGYEQ
     RTTVQGQVYF LHTQTGVSTW HDPRIPSPLG TIPGGDEAFL YEFLLQGHTS EPRDLNSVNC
     DELGPLPPGW EVRSTVSGRI YFVDHNNRTT QFTDPRLHHI MNHQCQLKEP SQPLQLPSEG
     SMEDEELPAQ RYERDLVQKL KVLRHELSLQ QPQAGHCRIE VSREEIFEES YRQIMKMRPK
     DLKKRLMVKF RGEEGLDYGG VAREWLYLLC HEMLNPYYGL FQYSTDNIYT LQINPDSSVN
     PDHLSYFHFV GRIMGLAVFH GHYINGGFTV PFYKQLLGKP IQLSDLESVD PELHKSLVWI
     LENDITPVLD HTFCVEHNAF GRILQHELKP NGRNVPVTEE NKKEYVRLYV NWRFMRGIEA
     QFLALQKGFN ELIPQHLLKP FDQKELELII GGLDKIDLND WKSNTRLKHC VADSNIVRWF
     WQAVETFDEE RRARLLQFVT GSTRVPLQGF KALQGAAGPR LFTIHLIDAN TDNLPKAHTC
     FNRIDIPPYE SYEKLYEKLL TAVEETCGFA VE
//
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