ID A0A0W4ZUE0_PNEJ7 Unreviewed; 790 AA.
AC A0A0W4ZUE0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN ORFNames=T551_00677 {ECO:0000313|EMBL:KTW31995.1};
OS Pneumocystis jirovecii (strain RU7) (Human pneumocystis pneumonia agent).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1408657 {ECO:0000313|EMBL:KTW31995.1, ECO:0000313|Proteomes:UP000053447};
RN [1] {ECO:0000313|Proteomes:UP000053447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU7 {ECO:0000313|Proteomes:UP000053447};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTW31995.1}.
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DR EMBL; LFWA01000003; KTW31995.1; -; Genomic_DNA.
DR RefSeq; XP_018230687.1; XM_018372941.1.
DR AlphaFoldDB; A0A0W4ZUE0; -.
DR STRING; 1408657.A0A0W4ZUE0; -.
DR GeneID; 28939196; -.
DR VEuPathDB; FungiDB:T551_00677; -.
DR eggNOG; KOG0940; Eukaryota.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053447; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000053447};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..111
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 212..245
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 310..343
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 368..401
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 457..790
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 758
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 790 AA; 90967 MW; 0B18F07D03A69C4E CRC64;
MGSNSPFQKI KLTVIAVDGL YKRDLIRTPD PFAVITVDGE QTQTTSVIRK TLNPYWNESF
EITVKESSIL AVQIFDQKKF KKKDQGFLGV VNLRISDVID LSLGGDEMLV RDLKKSNDNM
TVHGKLIISL STFVQVPSHN MSSNSTVQTN GSVSNSTAFS TFIVPTPSRI AMASEHNSAE
NTEAGHSGSH NTHHSVSYQG SNTFSSFEDQ YGRLPSGWER RVDNLGRTYY VDHNTRTTTW
TRPSTNQTES ERASQYQAQS ESERQSRVRP GSREGQQSTT GSTSSQHGAS VNGQNRVPIV
SNITTSPGTG DLPSGWEQRY TPEGRCYFVD HNTRTTTWVD PRRQQYIRMY SGTHMGNTIQ
QQPISQLGPL PSGWEMRLTN TARVYFVDHN TKITTWDDPR LPSSLDQNVP QYKRDFRRKL
IYFRSQPALR PLPGQCHIKV RRNRIFEDSY AEIMRHAPND LKKRFMVKFD GEDGLDYGGL
SREFFFLLSH EMFNPFYCLF EYSSVDNYTL QINPHSGINP EHLNYFKFIG RILGLAIFHR
RFLDAFFIVS FYKMILRKKV TLADMESVDA EFFRSLTWIL ENDITDILEL TFSTEDDRFG
EVTTIDLKPN GRNIQVTNDN KKEYVELVAY WRVFKRVEEQ FNAFQDGFNE LIPQELISVF
DERELELLIG GITEMDMDDW KKYTDYRGYT ESDEVIQWFW KCVRSWDSEK KSRLLQFITG
TSRVPVNGFK DLQGSDGPRR FTIEKAGEIT QLPKSHTCFN RVDLPEYPTY EMLVQKLTLA
VEETIGFGQE
//
