ID   C0NSS6_AJECG            Unreviewed;      1286 AA.
AC   C0NSS6;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=HCBG_06206 {ECO:0000313|EMBL:EEH05942.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH05942.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG663370; EEH05942.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NSS6; -.
DR   STRING; 447093.C0NSS6; -.
DR   VEuPathDB; FungiDB:I7I50_06580; -.
DR   HOGENOM; CLU_002173_2_4_1; -.
DR   InParanoid; C0NSS6; -.
DR   OrthoDB; 1386at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
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   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   PANTHER; PTHR45700:SF2; 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.
DR   PROSITE; PS50096; IQ; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          902..1286
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          66..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1254
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1286 AA;  145209 MW;  A562B0D9E7A87CD4 CRC64;
     MRVKVFGVSD YISVVPADDD VAMFPRNTRK HLHPTSKLLE SAAPSSRDNT TLDIATFFDS
     ISMSRPRQVN LSNRPTNPVS AYSSGRHGQA GQGTQATIAL AQQERRQRQL DRERLQATYI
     LQRTWRGYKA RKAAKDSWRT EWDNVERNRG PDARPGSDGD ALVWMGMPQP YADPTDCLSQ
     LRKLLCFIWI KDRDDWARLS YFAKSFQMTL EEAPVLQPDG EWPPTLRRLG VVTLQFLATT
     PSSVPSVSLV NDFLQLITFL STLLPTQMTR LAERYYSALT AITLNLQTSL NTSQTRDMVV
     RSVLALLQPI TSETLDAYGW FGRVFLAIPS LDRHLGGLDD LAAGVNYKLL ASAIDSHIPP
     CANSFSEPID VDRRLWLLSY FIYFHRHAQG DGVVKQAPET LFVKAVSGLL SPIAGEVSRR
     LGGEEKTQAE LLPPFVRSQL YTLLDQHSIT HLLSHAAPNR LPTVNSNSSQ LHLQASKDVK
     ALAAYALTLL RVFPKRGDEI RMWLYLGSAM ETGTGGDSTS GRLPAIKYFW NASKSTRVFL
     NITQNSRDVL AMLQTGSALS SQGGPIAEQS SDREQEWTVI LLFLELYTFL LKVLDDEEFF
     SATPSLGKPS KSNASWTQES ALPLDDVRNL TLFLKNLAFT LYWNSADLTS TNIDPSDTDG
     IRNYFSIRSP PLEPVHSNLK SKRSTLVSVT GIPLDYFKGL VTGLLRMVHE RDSRRKFLPD
     SHWLMVDRFD MEGFIPTVVA EEENRHQLQD YDEDDDDNDD EALNETMEDD YDHFPVLVGT
     GRAHHLRRIE ELRKRQQQVA RRKELEAVAP RLEILRNIPF FIPFATRVQI FREFIFRDQV
     QRRRGFIDPD SWRLSVAHSL MGLSNDGMSR GHDILSKHHA NIRRESLFQD AFDKFYELGD
     GLKEPIQISF IDKFGTPEAG IDGGGVTKEF LTSVISDAFN PSEPSSLFIE NDQHLLYPNP
     TLIEQRKAQL RRQGVPERSP TMNAEVKEIL KRYEFLGRII GKCLYEGILA DVSFAGFFLL
     KWALTGGTSS ARKESSYRAN LNEVRDLDEG LYQGLLQLKN YPGDVEDFAL NFTVTDTIAV
     PIEKPDGTIE TITENITKDL KPHGSEIPVT NQNRLVYISY IARHRLQAQP YLQTNAFLQG
     LGTIIQPSWL SMFNQSELQT LVGGDTGEID VADLRRNTVY SGSYVIGDDN QEHPTIKLFW
     EVLQTMTNAD RQKLLKFVTS TPRAPLLGFS HLNPRFSIRD SSADEERLPS TSTCANLLKL
     PRYTRLDTLR EKLMYAINAG AGFDLS
//