ID S7Q7S7_MYOBR Unreviewed; 2675 AA.
AC S7Q7S7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN ORFNames=D623_10017376 {ECO:0000313|EMBL:EPQ16917.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ16917.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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 EMBL; KE164318; EPQ16917.1; -; Genomic_DNA.
DR eggNOG; KOG4276; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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; 3.20.19.10; Aconitase, domain 4; 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; 2.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
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; PF00694; Aconitase_C; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF18410; BTHB; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF06701; MIB_HERC2; 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 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 478..510
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 509..541
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1331..1403
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 2216..2675
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 346..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1842..1862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2363..2383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1740..1765
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1808..1822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2644
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2675 AA; 296798 MW; 0EE40DAA836FDDD6 CRC64;
MSLEIVIVLA IAGTLKFNPE TDFLIGKDGK KFKLEAPDVD ELPHAEFDPG QDTYQHHPKD
SSGQWVVWLK FRGHLDISNN LLIGAINIKN GETNTLYNAV TQEFDTARYY KKHGIWWMVI
GDKNYGSLAS IVAYHVSPIG YLVMLRCPPR TFLPALCKIF LDESAPDNVL EVTARAITYY
LDVSAECTRR IVGVDGAIKA LCNRLVVVEL NNRTSRDLAE QCVKVLELIC TRESGAVFEA
GGLNCVLTFI RDSGHLVHKD TLHSAMAVVS RLCGKMEPQD SSLEICVESL SSLLKHEDHQ
VSDGALRCFA SLADRFTRRG VDPAPLAKHG LTEELLSRMA AAGGTISGPS SACKPGRSTT
GAPSTAADSK LSNQVSTIDL LRSELPDSIE SALQGDERCV LDTMRLVDLL LVLLFEGRKA
LPKSSAGSTG RIPGLRRLDS SGERSHRQLI DCIRSKDTDA LIDAIDTGAF EVNFMDDVGQ
TLLNWASAFG TQEMVEFLCE RGADVNRGQR SSSLHYAACF GRPQVAKTLL RHGANPDLRD
EDGKTPLDKA RERGHSEVVV ILQSPGDWMC PVNKGDDKKK KDTNKDEEEC NEPKGDPEMA
PIYLKRKASL ALIRKMIHFC SEALLKEVCD SDVGHNLPTI LVEITATVLD QEDDDDGHLL
ALQIIRDLVD KGGDIFLDQL ARLGVISKVS TLAGPSSDDE NEEESKPEKE DEPQEDAKEL
QQGKPYHWRD WSIIRGRDCL YIWSDAAALE LSNGSNGWFR FILDGKLATM YSSGSPEGGS
DSSESRSEFL EKLQRARGQV KPSTASQPIL STPGPTKLTV GNWSLTCLKE GEIAIHNSDG
QQATILKEDL PGFVFESNRG TKHSFTAETS LGSEFVTGWT GKRGRKLKSK LEKTKQKVRT
MARDLYDDHF KAVESMPRGV VVTLRNIATQ LESSWELHTN RQCIESENTW RDLMKTALEN
LIVLLKDENT ISPYEMCSSG LVQALLTVLN NSMDLDVKQD CSQLVERINV FKTAFSENED
DESRPAVALI RKLIAVLESI ERLPLHLYDT PGSTYNLQIL TRRLRFRLER APGETALIDR
TGRMLKMEPL ATVESLEQYL LKMVAKQWYD FDRSSFIFVR KLREGQNFIF RHQHDFDENG
IIYWIGTNAK TAYEWVNPAA YGLVVVTSSE GRNLPYGRLE DILSRDNSAL NCHSNDDKNA
WFAIDLGLWV IPSAYTLRHA RGYGRSALRN WVFQVSKDGQ NWTSLYTHVD DCSLNEPGST
ATWPLDPPKD EKQGWRHVRI KQMGKNASGQ THYLSLSGFE LYGTVNGVCE DQLGKAAKEA
EANLRRQRRL VRSQVLKYMV PGARVIRGLD WKWRDQDGSP QGEGTVTGEL HNGWIDVTWD
AGGSNSYRMG AEGKFDLKLA PGYDPDTVAS PKPVSSTVSG TTQSWSSLVK NNCPDKTSAA
AGSSSRKGSS SSVCSVASSS DISLGSTKTE RRSEIVMEHS IVSGADVHEP IVVLSSAENI
PQTEVGSSSS ASTSTLTAET GSENAERKLG PDSSVRTPGE SSAISMGIVS VSSPDVSSVS
ELTNKEAASQ RPLSSSASNR LSVSSLLAAG APMSSSASVP NLSSRETSSL ESFVRRVANI
ARTNATNNMN LSRSSSDNNT NTLGRNVMST ATSPLMGAQS FPNLTTPGTT STVTMSTSSV
TSSSNVATAT TVLSVGQSLS NTLTTSLTST SSESDTGQEA EYSLYDFLDS CRASTLLAEL
DDDEDLPEPD EEDDENEDDN QEDQEYEEVM ILRRPSLQRR AGSRSDVTHH AVTSQLPQVP
AGGGSRPIGE QEEEEYETKG GRRRTWDDDY VLKRQFSALV PAFDPRPGRT NVQQTTDLEI
PPPGTPHSEL LEEVECTPSP RLALTLKVTG LGTTREVELP LTNFRSTIFY YVQKLLQLSC
NGNVKSDKLR RIWEPTYTIM YREMKDSDKE KEKEKMGCWS IEHVEQYLGT DELPKNDLIT
YLQKNADAAF LRHWKLTGTN KSIRKNRNCS QLIAAYKDFC EHGTKSGLNQ GAISTLQSSD
ILNLTKEQPQ AKAGNGQNSC GVEDVLQLLR ILYIVASDPY SRISQEEGDE QPQFTFPPDE
FTSKKITTKI LQQIEEPLAL ASGALPDWCE QLTSKCPFLI PFDTRQLYFT CTAFGASRAI
VWLQNRREAT VERTRTTSSV RRDDPGEFRV GRLKHERVKV PRGESLMEWA ENVMQIHADR
KSVLEVEFLG EEGTGLGPTL EFYALVAAEF QRTDLGTWLC DDNFPDDESR QVDLGGGLKP
PGYYVQRSCG LFTAPFPQDS DELERITKLF HFLGIFLAKC IQDNRLVDLP ISKPFFKLMC
MGDIKSNISK LIYESRGDRD LHCTESQSEA STEEGHDSLS VGSFEEDSKS EFILDPPKPK
PPAWFNGILT WEDFELVNPH RARFLKEIKD LAIKRRQILS NKALSEDEKN TKLQELVLKN
PSGSGPPLSI EDLGLNFQFC PSSRIYGFTA VDLKPSGEDE MVTMDNAEEY VDLIFDFCMH
TGIQKQMEAF RDGFNKVFPM EKLSSFSHEE VQMILCGNQS PSWAAEDIIN YTEPKLGYTR
DSPGFLRFVR VLCGMSSDER KAFLQFTTGC STLPPGGLAN LHPRLTVVRK VDATDASYPS
VNTCVHYLKL PEYSSEEIMR ERLLAATMEK GFHLN
//
