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Database: UniProt
Entry: A0A1F5LFA9_9EURO
LinkDB: A0A1F5LFA9_9EURO
Original site: A0A1F5LFA9_9EURO 
ID   A0A1F5LFA9_9EURO        Unreviewed;      1188 AA.
AC   A0A1F5LFA9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN   ORFNames=PENARI_c012G00549 {ECO:0000313|EMBL:OGE51825.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE51825.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE51825.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE51825.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT   high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
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:OGE51825.1}.
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DR   EMBL; LXJU01000012; OGE51825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5LFA9; -.
DR   STRING; 1835702.A0A1F5LFA9; -.
DR   OrthoDB; 5471864at2759; -.
DR   Proteomes; UP000177622; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; 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; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR45622:SF60; UBIQUITIN-PROTEIN LIGASE E3A; 1.
DR   PANTHER; PTHR45622; UBIQUITIN-PROTEIN LIGASE E3A-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          841..1188
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1156
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1188 AA;  133092 MW;  F451E1959930E8C2 CRC64;
     MPSWSDRPLP PIPPISTSGS AANPPHPSPV TGPESSSRRQ LRPRDAPNIP SVTGNMPKNS
     YHRGHNRSIS NPFAGFGRKR DKTAVKYETW DSDDEDDDVT YPIEPESSSP RKAAARGGHA
     SDLAQGKCQT CDATVRWPQH LKVFRCTDCL MVTDLEPDFH ESKDTGHNGI PSQGSQAQPK
     PPSKVAHLSA HQTRGMIGGC LNTYFEGLLD ESSRSWLSLD DDKYEKPKQD SSQASNTGSN
     YLSVPGAGDS RSRSASQSSN HERVGASKEN LMHLPQQTVR WEGKDTPVRV RANSDLQSSP
     KPDRHPQDGS QSAHPDIQSR ESQVEIFKRL ENTIIAAFKG CDCLNESFTT HPPLRSASSG
     NPPKMKMDPA PMPVPAQDAP VFEPDAKTLL LGDLTENSTW WMNEWAEAEG QTPVSAKEKD
     TPKSRMVSSR SPRINWAEVS QWYHLVLSAG SSWAEQWAAK KPDPQRSEAD MLRAKRWASV
     DPTLIGRQIS ESRSHLQRTL LKATENLLKR PRRVLKKPED TRFLFILLAN PILSSPTSYP
     QHAPTSTSHR EERRPSHPKE YPKSTARNGK QKDSTKPLPR LPSSNHYGII KRVLGLMSNL
     PNDCHHYFVS WSARFSIGHF ERLVELIGGF LTYRLSRQHG RKPPQKPQNG DDLIPSFASA
     SGNTPAELHA AINRRGPNKK PAKKTEDPIV YTEDWQIRAA ARIMSLLFTA NISGSSRKSD
     GSPRHVELPK APGPRQGHVI PISAFYNTLL DYSDLIGDFE IWESRSSKFS FCQYPFFLSI
     WAKIHIMEHD ARRQMEVKAR EAFFNSILNH RAVSQYLVLK VRRECLVEDS LKGVSEVVGS
     GQEEIKKGLR IEFSGEEGID AGGLRKEWFL LLVREVFDPH HGLFIYDDDS QYCYFNPYCF
     ESSEQFFLVG VLLGLAIYNS TILDVDLPPF AFKKLLASAP QTSGPQPANS MRSSFKCTLE
     DLAEYRPVLA KGLRGLLEFE GDVAETFCYD FVAQVDRYGE NISVPLCAGG ENRPVTNSNR
     REFVDLYVHY LLDTAVARQF EPFKRGFFTV CGGNALSLFR PEEIELLVRG SDEPLDVNSL
     RAVATYDNWS YAQPESVPVV QWFWDFFESA PPKQQRKILS FVTGSDRIPA MGATSLSIRL
     ACLGDDSPRY PIARTCFNTL GLYRYSSRDK FLRLLSDAVV NSEGFGLK
//
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