ID A0A093UTG2_TALMA Unreviewed; 1244 AA.
AC A0A093UTG2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative E3 ubiquitin-protein ligase mug30 {ECO:0000313|EMBL:KFX43582.1};
GN ORFNames=GQ26_0340460 {ECO:0000313|EMBL:KFX43582.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX43582.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX43582.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX43582.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX43582.1}.
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DR EMBL; JPOX01000034; KFX43582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093UTG2; -.
DR eggNOG; KOG0941; Eukaryota.
DR HOGENOM; CLU_002173_5_1_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR CDD; cd00078; HECTc; 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; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 883..1244
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1212
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1244 AA; 139579 MW; 01376DF0ED0E82B0 CRC64;
MPTWPSRILP STSSPSSNSN PVHAPPPPSS THRNPIDINR SAIIAIDYNV PILLPTGAPA
ATANTSTSAS RNRRRTHARS ISQPFPSLMN PNAPRKLDKK PTKRDFGLDL DFDFEDDGAA
AVGLDQTRNA SDDMVTGKCI ACNSTCRWPR NVQVFRCTIC LTVNDLEPHP AANIRDRYDD
VKDDAQPPPP PPPPPPKDGA PEVPPAPISI EETRRITETC LLRFLHSRLP GNQDPKSVQP
EQRHREISNG RQEPKTDERQ PVPSNAPSVI ADTRFLSPPT RGSGDMERND GRTRVRSSSD
TPPISQRRGH SAQGRERSPL HVNTEPADYR SRSETRRSIF RPLEEYIIKS FAGCDCLNNS
FMTASALRSM SNAGLEPPKQ PIHHENVPAQ QQENVLSPKS PTSETVMFPE IDPKMLLLGD
LAENSSWWMG GRPRRQDVKN VCPEKREKSP LRPKSVVTTK SPRIDWEEVA EWYQLIVHVG
ENWREVWNKI RLAEQKPGLE GQTKLDAAID LGLIDKEITE ARVHAQKTLL KATENLLKRP
RRPLRRPESV RFLLILLANP QLVYTSNIAP TVSNLLSPDA IADGQKSFPN FSRRYGSGDR
KTSTSSSSRL QSGSLGHHSG IIKRILGLLG NLPNDCHHYL VGWFSRFSKG QFETLVDLVG
RFVTYRLSRQ HGRHRSDSGQ AINGLVPNIP GGIESSPAHL HAVLHESRSS NQPNEDNNRR
RVIYNTEDWQ IRAAARVMAL LFAANNHVSS SIHKRDVLLP QDYNNSTTPL ISQNKRSGST
LIPLNTFYNT LLDFSDLVSD FEAWESRTAR FSFCQYPFFL SIAAKSRILE HDARRQMNIK
ARQAFLDSIL NHKDVSQYLN LRVRRDCLVE DSLRGVSEVV GAGSEDIKKS LRIEFIGEEG
VDAGGLRKEW FLLLVREVFD PNHGLFTYDD DSQFCYFNPY CFESSEQFFL VGVLLGLAIY
NSTILDIALP PFAFKKLLAA APSTSIPAAA QRQPHTSSLD DLAEYRPALA KGLRALLEFD
GDVQETFCYD FVAQVDRYGQ VVNVPLCPNG ENKPVTNTNR HEFVSLYVQY ILDISVQRQF
EPFKRGFYTV CGGNALALFR PEEIELMVRG SDEPLDVPTL RAVATYENWP TSQPKPNDKN
NKDANTEAEP TSEPTICWFW DFLARSTPTN QRKLLSFVTG SDRIPATGAA SLSIRISCLG
EDSSRYPIAH TCFNKLGLFR YASRQKLERM LWDAICNSEG FGLK
//
