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
//