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Database: UniProt
Entry: A6RAN9_AJECN
LinkDB: A6RAN9_AJECN
Original site: A6RAN9_AJECN 
ID   A6RAN9_AJECN            Unreviewed;      1162 AA.
AC   A6RAN9;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=HCAG_06027 {ECO:0000313|EMBL:EDN10224.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN10224.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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DR   EMBL; CH476661; EDN10224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6RAN9; -.
DR   STRING; 339724.A6RAN9; -.
DR   VEuPathDB; FungiDB:HCAG_06027; -.
DR   HOGENOM; CLU_002173_2_4_1; -.
DR   OMA; HWLMTNR; -.
DR   OrthoDB; 1386at2759; -.
DR   Proteomes; UP000009297; 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:UP000009297};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          778..1162
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..711
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1130
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1162 AA;  131024 MW;  3C4BFCE34ED6B401 CRC64;
     MFQSFTGKAR RPRQVNLSNR PTNPVSAYSS GRHGQAGQGT QATIALAQQE RRQRQLDRER
     LQATYILQRT WRGYKARKAA KDSWRTEWDN VERNRGPDAR PGSDGDALVW MGLPKPYTDP
     TDCLSQLRKL LCFIWIKDRD DWARLSYFAK SFQMTLEEAP VLQPDGEWPP TLRRLGVVTL
     QFLATTPSSV PSVSLVNDFL QLITFLSTLL PTQMTRLAER YYSALAAITL NLQTSLNTSQ
     TRGMVVRTVL ALLQPITSET LDAYGWFGRV FLAIPSLDSH LGWLDDLAAG VNYKLLASAI
     DSHILPHANS FSEPIDVDRR LWLLSYFIYF HRHAQGDGVV KQAPETLFVK AVSGLLSPIA
     GEVSRRLGGE EKTQTELFPP FVRSQLYTLL DQHSITHLLS HAAPNRLPIV NSNSSQLHLQ
     ASKDVKALAA YALTLLRVFP KRGDEIRMWL YLGSAMETGT GGDSTSGRLP AIKYFWNASK
     STRVFLNIAQ NSLDVLAMLQ TGSALSSQGG SIAEQSSDRE QEWTVILLFL ELYTFLLKVL
     DDEEFFSATP SLGKPSKSNA SWTQESALPL DDVRNLTLFL KNLAFTLYWN SADLTSTNID
     PSDTDGIRNY FSIRSPPLEP VHSNLKSKRS TLVSVTGIPL DYFKGLVTGL LRMVHERDSR
     RKFLPDGHWL MVDRFDMEGF IPAVVAEEEN RHQLQDYDED DDDNDDETLN ETMEDDYDHF
     PVLIFREFIF RDQVQRRRGF IDPDSWRLSI AHSLMGLSND ESLFQDAFDK FYELGDGLKE
     PIQISFIDKF GTPEAGIDGG GVTKEFLTSV ISDAFNPSGP SSLFIENDQH LLYPNPTLIE
     QRKAQLRRQG VPERSPTMNA EVKEILKRYE FLGRIIGKCL YEGILVDVSF AGFFLLKWAL
     TGGTSSARKE SSYRANLNEV RDLDEGLYQG LLQLKNYPGD VEDFALNFTV TDTIAVPIEK
     PDGTLETITE NITKDLKPHG SEIPVTNQNR LVYISYIARH RLQAQPYLQT NAFLQGLGTI
     IQPSWLSMFN QSELQTLVGG DTGEIDVADL RRNTVYSGSY VIGDDNQEHP TIKLFWEVLQ
     TMTNADRQKL LKFVTSTPRA PLLGFSHLNP RFSIRDSSAD EERLPSTSTC ANLLKLPRYT
     RLDTLREKLM YAINAGAGFD LS
//
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