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Database: UniProt
Entry: W7I256_9PEZI
LinkDB: W7I256_9PEZI
Original site: W7I256_9PEZI 
ID   W7I256_9PEZI            Unreviewed;      1290 AA.
AC   W7I256;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN   ORFNames=DRE_04326 {ECO:0000313|EMBL:EWC46383.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46383.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC46383.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC46383.1,
RC   ECO:0000313|Proteomes:UP000024837};
RA   Liu X., Zhang W., Liu K.;
RT   "Drechslerella stenobrocha genome reveals carnivorous origination and
RT   mechanical trapping mechanism of predatory fungi.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI966418; EWC46383.1; -; Genomic_DNA.
DR   HOGENOM; CLU_001858_0_0_1; -.
DR   Proteomes; UP000024837; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 2.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 2.
DR   Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR   InterPro; IPR032353; AZUL.
DR   InterPro; IPR042556; AZUL_sf.
DR   InterPro; IPR044611; E3A/B/C-like.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR45700:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   Pfam; PF16558; AZUL; 1.
DR   Pfam; PF00632; HECT; 2.
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:UP000024837};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          804..1290
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          227..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1029..1065
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1258
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1290 AA;  143391 MW;  78EE886ED56010C5 CRC64;
     MFTTSAATGS SSLLTHRPQA YQYSTLPPHA PPLIAQNTTT IHDPSAIASF SHAQRHREFN
     ALVKKYVHQL LHGCRRPICT TPTCATCRQQ LNSPAASKGP APSPLGSRRE FTPLSARIIA
     CQLATADQPY RALCPGLETD VKGRTELGCE NRGKVDVGMR DSKSFMQGLF NTTAIRSLEM
     NVLPPPMDVV KVLGGTAADV REDLSDEADL AFNPKNRVVS AALSRLESEA RKDYSSSTPT
     KNAGGGGGDV NVPVTPNAAS VTNSMEKDRN PPVTPYHTRP SFQVSQQSTK SRRKLSHDLS
     SYLTSPKNTF FTPDVNELTP PHVHRQHPRD ITQRRSPDTT PSRTSKLSAL DGKSINSTAT
     STPLSTKSTV PLPQAVTHFT LDIISVLVAM MDDTAVSARA RLDAVRFLRQ SCYYVFGSPD
     TLAACFPEDF QADKSVLVLR SVKMLFDRGM GGEIVDALWK ALGELFPTVE EVLVGNEKKK
     AVRPSKYTAG TATKVFVITL HVIAAACPVA TPEVWERCRK DRSAGTVCLD IPFEDEGLLR
     LVARFSRCWS AYGMFEHRAR NAVREYLLNY AKLEKKARVD KLERELGREL AGDVANSGVG
     KGGWGLVVCA LEWMRAMMLK EWDGSERPRT GGVVDASILF LRFLYEDHEA LGLEESYFHN
     QVLADRLEYK DMPVKWYLRK QKSAAKSANL AETPSETAAA AESQQRRPEP PHLLNHAFLL
     PPIALVKFFR SINFYRMSAA YDNALAMYRF VNQMADVTRL DLFKPWLRNF IMKSYDISMT
     VYLLFEVHRT TIIKDTLDQL LGREPRECLR PLKVRFLDVG EEGVDHGGVQ QEYFRLLWEE
     ATKGEYGCFT TDERTRTSWF SILTLEPMHK FELLGLLVGL AVYNGVTLPV SFPLVVYRKL
     LGWKVELDDL SDGWPELVKG MRQLLQWNDG DVGDVFVRSY EFGYEAYGEV HSVDLMKVGR
     EDRWAPVTIE RAIVFSSSST WQRGPHGASQ APPQLTIAAL AGTSATSSEG DEPFSSAIPL
     ENQLRVPDVA GSPGSSSDSS SGRILTPGIL TPESASPSLS PSRRNSAVVI DENDEAAATW
     KAYDQQQQSL SSAHSTCSST MPAKITSERF IKPEGEESEL VTNANREQYV KDYVFWLTDK
     SIRPQFEAFE KGFHAVLDRS SLSLFNPMTL RHLVEGSKDI DIAALEAAAK YDDGYHPNHR
     CVKDFWAIVR TYDNDQRRAL LEFVTASDRV PVSGISSVMF VIQRNGGDSE RVPTSLTCFG
     RLLLPEYSGR KKMREKLRVA LENGRGFGVP
//
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