ID A0A2Y9QYT2_TRIMA Unreviewed; 2563 AA.
AC A0A2Y9QYT2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN Name=LOC101361264 {ECO:0000313|RefSeq:XP_023587257.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023587257.1};
RN [1] {ECO:0000313|RefSeq:XP_023587257.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates.
CC {ECO:0000256|RuleBase:RU369009}.
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|RuleBase:RU369009};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369009}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331, ECO:0000256|RuleBase:RU369009}.
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DR RefSeq; XP_023587257.1; XM_023731489.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd21062; BTHB_HectD1; 1.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.10.720.80; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR041200; FKBP3_BTHB.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR45670:SF19; E3 UBIQUITIN-PROTEIN LIGASE HECTD1; 1.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF18410; BTHB; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51416; MIB_HERC2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 395..427
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 426..458
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1266..1340
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 2104..2563
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 244..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2250..2271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1653
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1696..1710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2532
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2563 AA; 284547 MW; 04DEEBD9BC164845 CRC64;
MADVDPDTLL EWLQMGQGDE RDMQLIALEQ LCMLLLMSDN VDRCFETCPP RTFLPALCKI
FLDESAPDNV LEVTARAITY YLDVSAECTR RIVGVDGAIK ALCNRLVVVE LNNRTSRDLA
EQCVKVLELI CTRESGAVFE AGGLNCVLTF IRDSGHLVHK DTLHSAMAVV SRLCGKMEPQ
DSSLEICVES LSSLLKHEDH QVSDGALRCF ASLADRFTRR GVDPAPLAKH GLTEELLSRM
AAAGGTASGP SSACKPGRST TGAPSTAADS KLSNQVSTIV SLLSTLCRGS PVVTHDLLRS
ELPDSIESAL QGDERCVLDT MRLVDLLLVL LFEGRKALPK SSAGSTGRIP GLRRLDSSGE
RSHRQLIDCI RSKDTDALID AIDTGAFEVN FMDDVGQTLL NWASAFGTQE MVEFLCERGA
DVNRGQRSSS LHYAACFGRP QVAKTLLRHG ANPDLRDEDG KTPLDKARER GHSEVVAILQ
SPGDWMCPVN KGDDKKKKDT NKDEEECNEP KGDPEMAPIY LKRLLPVFAQ TFQQTMLPSI
RKASLALIRK MIHFCSEALL KEVCDSDVGH NLPTILVEIT ATVLDQEDDD DGHLLALQII
RDLVDKGGDI FLDQLARLGV ISKVSTLAGP SSDDENEEES KPEKEDEPQE DAKELQQGKP
YHWRDWSIIR GRDCLYIWSD AAALELSNGS NGWFRFILDG KLATMYSSGS PEGGSDSSES
RSEFLEKLQR ARGQVKPSTS SQPILSALGP TKLTVGNWSL TCLKEGEIAI HNSDGQQATI
LKEDLPGFVF ESNRGTKHSF TAETSLGSEF VTGWTGKRGR KLKSKLEKTK QKVRTMARDL
YDDHFKAVES MPRGVVVTLR NIATQLESSW ELHTNRQCIE GENTWRDLMK TALENLIVLL
KDENTISPYE MCSSGLVQAL LTVLNNSMDL DVKQDCSQLV ERINVFKTAF SENEDDESRP
AVALIRKLIA VLESIERLPL HLYDTPGSTY NLQILTRRLR FRLERAPGET ALIDRTGRML
KMEPLATVES LEQYLLKMVA KQWYDFDRSS FVFVRKLREG QNFVFRHQHD FDENGIIYWI
GTNAKTAYEW VNPAAYGLVV VTSSEGRNLP YGRLEDILSR DNSALNCHSN DDKNAWFAID
LGLWVIPSAY TLRHARGYGR SALRNWVFQV SKDGQNWTSL YTHVDDCSLN EPGSTATWPL
DPPKDEKQGW RHVRIKQMGK NASGQTHYLS LSGFELYGTV NGVCEDQLGK AAKEAEANLR
RQRRLVRSQV LKYMVPGARV IRGLDWKWRD QDGNPQGEGT VTGELHNGTT QSWSSLVKNN
CPDKTSAAAG SSSRKGSSSS VCSVASSSDI SLGSTKTERR SEIVMEHSIV SGADVHEPIV
VLSSAENVPQ AEVGSSSSAS TSTLTAETGS ENAERKLGPD SSVRTPGESS AISMGIVSVS
SPDVSSVSDL TNKEAASQRP LSSSASNRLS VSSLLAAGAP MSSSASVPNL SSRETSSLES
FVRRVANIAR TNATNNMNLS RSSSDNNTNT LGRNVMSTAT SPLMGAQSFP NLTTPGTTST
VTMSTSSVTS SSNVATATTV LSVGQTLSNT LTTSLTSTSS ESDTGQEAEY SLYDFLDSCR
ASTLLAELDD DEDLPEPDEE DDENEDDNQE DQEYEEVMIL RRPSLQRRAG SRSDVTHHAV
TSQLPQVPAG AGSRPIGEQE EEEYETKGGR RRTWDDDYVL KRQFSALVPA FDPRPGRTNV
QQTTDLEIPP PGTPHSELLE EVECTPSPRL ALTLKVTGLG TTREVELPLT NFRSTIFYYV
QKLLQLSCNG NVKSDKLRRI WEPTYTIMYR EMKDSDKEKE NRKMGCWSVE HVEQYLGTDE
LPKNDLITYL QKNADAAFLR HWKLTGTNKS IRKNRNCSQL IAAYKDFCEH GTKSGLNQGA
ISTLQNSDIL NLTKEQPQAK AGNGQNSCGV EDVLQLLRIL YIVASDPYSR ISQEEGDEQL
QFTFPPDEFT SKKITTKILQ QIEEPLALAS GALPDWCEQL TSKCPFLIPF ETRQLYFTCT
AFGASRAIVW LQNRREATVE RTRTTSSVRR DDPGEFRVGR LKHERVKVPR GESLMEWAEN
VMQIHADRKS VLEVEFLGEE GTGLGPTLEF YALVAAEFQR TDLGAWLCDD NFPDDESRHV
DLGGGLKPPG YYVQRSCGLF TAPFPQDSDE LERITKLFHF LGIFLAKCIQ DNRLVDLPIS
KPFFKLMCMG DIKSNMSKLI YESRGDRDLH CTESQSEAST EEGHDSLSVG SFEEDSKSEF
ILDPPKPKPP AWFNGILNWE DFELVNPHRA RFLKEIKDLA IKRRQILSNK DLSEDEKNTK
LQELVLKNPS GSGPPLSIED LGLNFQFCPS SRIYGFTAVD LKPSGEDEMI TMDNAEEYVD
LMFDFCMHTG IQKQMEAFRD GFNKVFPMEK LSSFSHEEVQ MILCGNQSPS WAAEDIINYT
EPKLGYTRDS PGFLRFVRVL CGMSSDERKA FLQFTTGCST LPPGGLANLH PRLTVVRKVD
ATDASYPSVN TCVHYLKLPE YSSEEIMRER LLAATMEKGF HLN
//
