ID A0A1E4TDD7_9ASCO Unreviewed; 807 AA.
AC A0A1E4TDD7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN ORFNames=CANCADRAFT_144090 {ECO:0000313|EMBL:ODV89775.1};
OS Tortispora caseinolytica NRRL Y-17796.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trigonopsidaceae; Tortispora.
OX NCBI_TaxID=767744 {ECO:0000313|EMBL:ODV89775.1, ECO:0000313|Proteomes:UP000095023};
RN [1] {ECO:0000313|Proteomes:UP000095023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17796 {ECO:0000313|Proteomes:UP000095023};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Jeffries T.W., Grigoriev I.V.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (FEB-2016) 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 ECO:0000256|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR EMBL; KV453843; ODV89775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4TDD7; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000095023; Unassembled WGS sequence.
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; 3.
DR Gene3D; 2.20.70.10; -; 2.
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:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
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; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000095023};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..108
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 225..258
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 327..360
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 385..418
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 474..807
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 137..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 775
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 807 AA; 91092 MW; 6DBB278DD29F91DC CRC64;
MSSSRRLVIT VVAADGLYKR DIFRLPDPFA VVTVDGEQTH TTAAIRKTLN PYWNESFTVN
VTESSIIAIQ IFDQKKFKKK DQGFLGVINL RVGDVIDLEN GGEEVLAKDL KKSNDNLVVH
GKLIVNLSTN VSAATSNSAT PAAAASGPSR AHRSGSGSTY GPSHSAQIPT SNPASNALAV
SAAAVSSAAA VSSAAATPSA SNPPTPVSVN HPSSSSFNAF EDQYGRMPPG WERRVDNLGR
IYYVDHNTRT TTWTRPSSNF NQNVQNANLQ SNTELERVRH HARTLPGDRH SPADPTASGM
SNSSHSPAPS ANAVHMMATG TTTVGLGDLP PGWEQRYTPE GRSYFVDHNT RTTTWVDPRR
QQYIRMYGPN AASATIQQQP VSQLGPLPSG WEMRLTNSAR VYFVDHNTKT TTWDDPRLPS
SLDQNVPQYK RDFRRKLIYF RSQPAMRILP GQCNLKVRRD HIFEDSYQEV MRQSPQDLKK
RLMIKFEGEE GLDYGGVSRE FFFLLSHEMF NPFYCLFEYS AHDNYTLQIN PHSGINPEHL
NYFKFIGRIV GLAIFHRRFL DAFFVGAFYK MLLRKKVGLI DMEGIDADVY RNLQWTLEND
ITDILDLTFS AEDDKFGELV TIDLKPNGRN IPVTNENKKE YIDLISEWRI HKRVEEQFEA
FITGFNELIP QELINVFDDK ELELLIGGIA DIDVDDWKKH TDYRGYTETD DVIQWFWKCI
RSWDSEKKSR LLQFTTGTSR IPVNGFKDLQ GSDGPRRFTI EKAGEINQLP KSHTCFNRVD
LPPYKDYETL EQKLSLAVEE TMGFGQE
//
