ID M9LPA7_PSEA3 Unreviewed; 850 AA.
AC M9LPA7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN ORFNames=PANT_9d00326 {ECO:0000313|EMBL:GAC73911.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC73911.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
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; DF196775; GAC73911.1; -; Genomic_DNA.
DR AlphaFoldDB; M9LPA7; -.
DR STRING; 1151754.M9LPA7; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:GAC73911.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..115
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 267..300
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 370..403
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 428..461
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 517..850
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 149..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 818
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 850 AA; 93835 MW; D88195E4D7261E15 CRC64;
MVNPRSPGSL SRKIRITVVA ADGLAKRDVF RLPDPFAIVT VDGEQTHSTS VIKKTLNPYW
NDSFDVTVTD SSVIAVQIFD QKKFKKRDQG FLGVINIRVA DVLDLELGGK RLLNKELKKS
NDNLVVHGKL IIDLNTNVST PINNNSTAGP TNLLVPGTSN ASSASLATPS STGAARSDAR
PSTSGSGTTT PVAASAANGD VASRPASTAD GVSPSTSATA AAATTTASST ATPASSGPAS
DARSSAAPAS SAARPAGSQD ARSDEYGPLP TGWERRTDHL GRTYYVDHNT RSTTWTRPST
SSSANTAAAA STTAADRQRH SNRALADDFL GVSDGDTSRS SATGSAIASP GAAAAANSLP
ASSSTTAGNG PLPAGWEQRH TPEGRPYFVD HNTRTTTWVD PRRQQILRIM GPNGSNLTVQ
PQSVSQLGPL PSGWEMRLTS TARVYFVDHN TKTTTWDDPR LPSSLDQNVP QYKRDFRRKL
IYFRSQPALR PIPGQCHIKV RRTHIFEDSY AEIMRQQPND LKKRLMIKFD GEDGLDYGGL
SREFFFLLSH EMFNPFYCLF EYSAHDNYTL QINPHSGINP EHLNYFKFIG RVLGLAIFHR
RFLDAYFIVS FYKMILKKKI TLSDLESVDA DYHRSLQWML DNSIEGIVEE TFTAVEDKFG
EMVTIELKKG GEEVEVTDEN KKEYVELMTE WRISKRVEEQ FKAFISGFTE LIPQDLINVF
DERELELLIG GMSEIDVDDW KKFTDYRGFT EQDQVVQWFW QCVRAWPTEK KSRLLQFATG
TSRIPVNGFK DLQGSDGPRR FTIEKSGDVN QLPKSHTCFN RIDLPPYPSF ETLESKLALA
IEEGMGFGNE
//
