ID C4R0F0_KOMPG Unreviewed; 767 AA.
AC C4R0F0;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN OrderedLocusNames=PAS_chr2-1_0354 {ECO:0000313|EMBL:CAY68974.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY68974.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY68974.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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; FN392320; CAY68974.1; -; Genomic_DNA.
DR RefSeq; XP_002491254.1; XM_002491209.1.
DR AlphaFoldDB; C4R0F0; -.
DR SMR; C4R0F0; -.
DR STRING; 644223.C4R0F0; -.
DR EnsemblFungi; CAY68974; CAY68974; PAS_chr2-1_0354.
DR GeneID; 8199042; -.
DR KEGG; ppa:PAS_chr2-1_0354; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_0_0_1; -.
DR InParanoid; C4R0F0; -.
DR OMA; DNYTIQI; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000314; Chromosome 2.
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; 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; 2.
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:CAY68974.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000314};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..110
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 189..222
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 290..323
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 345..378
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 434..767
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 134..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 735
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 767 AA; 87792 MW; 939AE7ADA43DC579 CRC64;
MSALQPMKIT VQVVGADGLY KRDVFRSPDP FAVITVDGAQ TKSTSTAKRT LHPFWNESFE
FNCTQNSILA IQIFDQKKFK KKDQGFLGVI NLRIGDVIDL ENDISQSETL TRPLKKSNDN
LIVSGEVFIT LSHKGRGRQG GAASHMSPPN GPPAELLTPG PSANDAGSNP PGLISASNRQ
YSSFEDQYGR LPPGWERRTD NFGRTYYVDH NSRTTTWTRP ALDQSEADRT NQRVNATEAE
RRQHMDRSLP GENSSSTTVG NLSSSGSVNA SNNQTALSMA SNGYTTFGLG ELPPGWEQRL
TAEGRPYFVD HNTRTTTWVD PRRQQYIRSV GPNTTVQQQP VSQLGPLPSG WEMRLTNTAR
VYFVDHNTKT TTWDDPRLPS SLDQNVPQYK RDFRRKVIYF RSQPALRILP GQCHIKVRRS
HIFEDSYQEI MRQSPEDLKK RLMIKFDGEE GLDYGGVSRE FFFLLSHDMF NPFYCLFEYS
THDNYTLQIN PNSGINPEHL NYFKFIGRVV GLGIFHRRFL DAFFVGALYK MILHKKVILQ
DMEGVDAEFY RSLKWILEND ITDVLDLTFS AEDERFGEIV TVDLKEGGRD IEVTEENKME
YVELITEWKI HRRVEQQFKA FMDGFNELIP QELINVFDER ELELLIGGIA DVDVEDWKKH
TDYRGYQESD EVIQWFWKCV TEWDKEQKAR LLQFTTGTSR IPVNGFKDLQ GSDGPRRFTI
EKAGESNQLP KSHTCFNRVD LPPYKDYGSL KQKLTLAVEE TVGFGQE
//
