ID   A0A1V6UKZ8_9EURO        Unreviewed;      1225 AA.
AC   A0A1V6UKZ8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=PENCOP_c007G01596 {ECO:0000313|EMBL:OQE39108.1};
OS   Penicillium coprophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE39108.1, ECO:0000313|Proteomes:UP000191500};
RN   [1] {ECO:0000313|Proteomes:UP000191500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE39108.1}.
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DR   EMBL; MDDG01000007; OQE39108.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6UKZ8; -.
DR   STRING; 36646.A0A1V6UKZ8; -.
DR   OrthoDB; 1386at2759; -.
DR   Proteomes; UP000191500; 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:UP000191500};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          849..1225
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..717
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1193
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1225 AA;  138532 MW;  BCFBACD631DDD6A6 CRC64;
     MFQSFTGNSR RPRQVNLSGR ATNPFAAFPG NSPNRQTPHA ANPESAVAIA QRERALRQHE
     RDRQTASRTV QRVWRGHQSR NATYKSWKSE WDNFEWERVM SALGLEDDQR PTTEVERLEC
     LARLSAPPYH TAEQCLDQLR LLVQFVGMVK RKDDVLRLVY FCNVFEQTFN ALPTIATENE
     WTELLKRLAI AILHALSLAK ESPTHEAAVL PLLRTIVFLV DLIPKRMATI AKQYYQTMAF
     LTKNIELWRD TLSPELITNA VLALLRPITS ETMTAYEALA MSYLTIPNLP TYLSDLDGLA
     HQINYKLLAP AIELCIPATK ERLSTDDVEG IEGRLWLLAY LIFFHRYALP GQANLQAPDL
     EFLNVVSGLL NSTSIYLTRS LDADESGADP IRGPYLDQFV TDQVSSLVNQ SSITGLLSRI
     KSAHLSHTGL SSNESHASKE AKIVATYALN LLRVFPRRGD DIRMWLYLGS APSAGSASGE
     PGAKIPAIKY FWQASKSSRI FDIISKDSTQ VLPLLQPPQD GNQEDQDQEW TIILLFFELY
     TFLLKVMDDE EFFSSASPFT SSSNALSSWT KESALPLGDI KDITVFLKNL AFTLYWNVAD
     LTKKGPVPSS AVDLRSYFNN TAQVSEPTER FEVEVKKEIN DLPGVTGIPL DYFKGLVTGL
     LRMLHERDSR RKFLPPNHWL MTDRFDMEGF IPAVVAEEEK RHEFQDDDED SEPDLLDEEY
     SEPSHLVGNS HARRLIHIQA MRNSQRRQAH NNALAAIAPR LEILRNMPFF IPFATRVQIF
     RQFIFRDQQR RRKGFVDPES WRLSVAQNAM INGPPEGAAN ILARHHADIR RESVFEDAFS
     QYYSLGDGLK EPIQISFIDQ FGAMEAGIDG GGVTKEFLTS ITSQAFKTDD YESMFAENDH
     HLLYPSPTAV DQLKKVLSEA GLTSSSVEWQ DDVRGLLRRY EFLGRIIGKC LYEGILVDVN
     FAPFFLLKWA LTGGSRSAVK ESSYRANLND LKDLDEGLYQ GLLQLKNYTG NVEDFGLDFT
     INNVIRMPSG KNRTVTVDLK PSGSQTAVTN KNRLVYISYI ARYRLQLQPA LQTNAFLQGL
     GQIIQPAWLS MFNQSELQTL VSGDKADIDV EDLRRNTLYG GVYVIGDDNL EHPTIALFWQ
     VMHEMTNEER QKVIRFVTST PRAPLLGFSH LRPHFSIRDS SEDQERLPST STCVNLLKLP
     RYSDAETLRS KLLYAVSSGA GFDLS
//