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Database: UniProt
Entry: F2U0G4_SALR5
LinkDB: F2U0G4_SALR5
Original site: F2U0G4_SALR5 
ID   F2U0G4_SALR5            Unreviewed;      2017 AA.
AC   F2U0G4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIP12 {ECO:0000256|ARBA:ARBA00018006};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE   AltName: Full=HECT-type E3 ubiquitin transferase TRIP12 {ECO:0000256|ARBA:ARBA00030738};
DE   AltName: Full=Thyroid receptor-interacting protein 12 {ECO:0000256|ARBA:ARBA00032457};
GN   ORFNames=PTSG_11742 {ECO:0000313|EMBL:EGD80892.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000256|ARBA:ARBA00004642}.
CC   -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC       {ECO:0000256|ARBA:ARBA00006331}.
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DR   EMBL; GL832958; EGD80892.1; -; Genomic_DNA.
DR   RefSeq; XP_004997453.1; XM_004997396.1.
DR   STRING; 946362.F2U0G4; -.
DR   EnsemblProtists; EGD80892; EGD80892; PTSG_11742.
DR   GeneID; 16078050; -.
DR   KEGG; sre:PTSG_11742; -.
DR   eggNOG; KOG0168; Eukaryota.
DR   eggNOG; KOG0170; Eukaryota.
DR   InParanoid; F2U0G4; -.
DR   OMA; AEPLSQF; -.
DR   OrthoDB; 1093891at2759; -.
DR   Proteomes; UP000007799; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.720.50; -; 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; 2.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR045322; HECTD1/TRIP12-like.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR018123; WWE-dom_subgr.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR   PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF02825; WWE; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00678; WWE; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF117839; WWE domain; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50918; WWE; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          566..642
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          1708..2017
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1061..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1358..1421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1623..1708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..504
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..814
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1184..1201
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1216..1237
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1272..1288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1358..1383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1623..1649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1654..1683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1684..1699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1984
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   2017 AA;  215886 MW;  0471EE2D5EAAD353 CRC64;
     MWRKPRAADV TISGSSSSSS SSNSGANSGN NSGSESVSSR TRSRTSTPLP PSGDAASDTL
     PPPPPRRSSR RKAKKATQPS EAATSATTSK KSTSSKASSS SSRRNKGQAK RKAVATSEWI
     EEDIDTADTA DTGTTTATTA DTATSSSSTR RSRQSGVSQR KRAKTQSFMA GLPFHQIFGA
     PLMQQRGGSS GIVAGLKSGD FLQKEHALDT LNTKFLMEPA EQWRSLPFEE IIDALDAIIK
     SMSPEDAHLA SRAARAASSL LEARPQTASI VAKLGPAIMF RFQQMDMDFT EAGLACLKRL
     AREAPTEVLQ LNAVPTVTMM IDFFMGASQK DAIELISSAA DVCDASTFPQ HMREAVSGLT
     QFLRMFAVRD PAVVEATCVL FFKLTRNLAA SPEHVEALAS DGLPAVFVQI LQTKPLPIAR
     EGLTAVLASL ALMARSSTAT AVALVQDDAL LPMLKMALTD AKHRSRRAGS TRGADGTGAG
     TAGADEDVGV DDEGDDDDDV AVVEGGAEDT ATGASAQQGQ GQEDEKQENQ GGAGIGMQLR
     ANQLLHVVAL IRHLLPPLPT THPFHTFTRD VLPTDDEAVW EWRSGASTWR PYTTAATASI
     ERAYATGAPS VTITVGSQTF VVDVQRMRQI NLSSHGVREV RRTERPAPPP PSGDALHKHY
     AQHPAALSSM IVELIRPLFE LYLASARTDI HAEFAHTLVR MVHAATPPTL VESLRSVSMS
     NYLAQMLHSR EPVVVMGALA TASCLLQRLP DIFAVHFRRK GVLHRVEQLC KMRVEVVAPT
     PATPGASTAA AEGGSTPSTP AAATAATPAT PSDALSAPSP HAAMLSLQRR NTAAAREESR
     NMRRRARKQR MMQAKKVAYD FAREAFGDVL ASTEADADID AIISAVKAAT SELRAATSPF
     DQDKASAALT KLSDLCSGNA DGMTAFEFTH YGTAHALATF LTVEDDTTPH RLALFAHLFL
     VHDAAKLHAL QRLLDLVHGA LNLNENFESS GPTKQQFERR NFTVRVSRAA DEKNLGSVDL
     NLSVPSTVTV QALYDYVDKH LKQARTGPDR LREAHRLLRR HTEAQRRRRQ QQQQQEGGGG
     DDGGEGTRRR SSRRRGQQQP ALGGADADAG GDGDEDTTGS DTTRTHARRL RRSARRHGAR
     RGGSNGNDGG DEDAGLGSGD AASDLLSAIA ATLRSRGRAP GNDEDNEDED DDGDGDVNED
     GLEAEEVLRY LLGGGGEDEE EEEADLEAQE EEGDEETPAD APQKVVVDDA GDDAEGGADA
     DDDDGHGNAG DGGASTGSNA STRARLSRTS RSRASRLRHQ RLARSDSGQS VLRISAGDDW
     WKVIAKGFRN KNALDLTLNG QVLPWNYSMI QAVRELTSAS RPASRSGSRT PGVDASSTGG
     SDDMPTRVHV KYRKASARSR QVSVQSLRPD SRTGGAGIGG VGGGDADGAA TTLDLPAAAT
     SITQAEEVAD LLRILRVLHI LATDGVRWIG AYAAAAIAIS PAAFINRRLA AKIMREVANT
     QALTSGTFPD WVTDAMSCCP FVLSYDQRVR FFRYTAFGCA LGLRYLTGDA GEGDNQPLAQ
     SKVQVSRKHL LASTAHIMHL YATHPTELSV SFVGEVGTGI GPTLEYYART CEQFQRRDLN
     LWRDSSSSSS SSSNSSSSTT TTTTGSSGDG GDAVAKAEEA DEEKKEKTKE EEKQTKQEEQ
     QQVREGGDTS ATAGDSSEHE FVFSPQGLYP KPVHALGERE GYIFELFGAF VAKAMQDNRP
     LDLNLSPAFY GWMVGAPPCT LADVRDVDEG LYKSLVKLQA AADAKKAVDN DTSLDAAARA
     EKLAAITVDG CPVEDLCLDF TLPGHPDVSL GQAGADTPVT LENLGEYVAA VVDFTLLRGV
     RDAMTSFTAG FAAVFDMRTL TLFTVEEVRT VVCGSRVESW DYDELRACIK AEHGYDSSSP
     QVQQLLEVLV ELDVDNKRKF VQFLTGSPNL PVGGFKALKP PFTVVMKDAQ GLSPDQVLPS
     VMTCQNYFKM PTYSSKDVLR EKLLMAITEG QGSFDLS
//
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