ID A0A010QV74_9PEZI Unreviewed; 1895 AA.
AC A0A010QV74;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=CFIO01_08230 {ECO:0000313|EMBL:EXF80510.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF80510.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF80510.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF80510.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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:EXF80510.1}.
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DR EMBL; JARH01000435; EXF80510.1; -; Genomic_DNA.
DR RefSeq; XP_007595847.1; XM_007595785.1.
DR STRING; 1445577.A0A010QV74; -.
DR KEGG; cfj:CFIO01_08230; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR HOGENOM; CLU_000366_1_1_1; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000020467; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; 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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1537..1895
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..799
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1862
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1895 AA; 205707 MW; 741FCCB9A9ED350C CRC64;
MPPKNQSLMS PRITRSSARQ AASLAASSTQ SAASADPAAA APAPPSSSPP NPPTSASRKR
KASTQATSPT PGPQQSASAS SRRSKRQKVA EAVPPPQLPT QPPAPPRSKR KGKSTVAMSS
PDISADPANA SENTAPSASS SRKSSSSRSK RTATGTLDPS ANTSSSSRKT KRNAANNADP
DTAMTGTDDT EKESLPLPPP PPPPEHHDDD DDDSDDNDDD DEGQRYDDDV DDDPFGGFGG
PGGPGGLSST LRALTGMMTG ISSRLRDLLN SLRQKDDPSV QLIALQELSE ILLVSNEDNL
SGHFSPDAFV KELVTLMQPN EMTGEENPEL MLLACRCLAN LMEALPASVA NVVYGGAVPV
LCQKLLEISF IDLAEQALST LEKISAEYPS SIVREGGLTA CLSYLDFFAT STQRTAVTTA
ANCCRNIPED SFPVIRDVMP TLLNVLGSSD QRVVEKASIC VSGIVESFKY QSAKLEELVS
VDLLKAVLRL LVPGTTNLIG ADIHTQFLRV LAFTARASPQ LSADLFKLNI VETLYQILTG
VSPPSGTEDV ASKLDSVVIM QALIHRPKEQ IIETLNVICE LLPSLPRNAD PSYGDFVEMN
TTEPITPSST AAGKTRKSPN DKRIELLDSC KSEVRRFALI LFPTLTDAFS STVNLNVRQK
VLTAQLKMLS NLDEEILSEA LKTVSYASFL ASILSQQDHP SLVMLALQAT ELLLSRLEDV
YRYQLYREGV ISEITKLAIE EHTPPPAPEP AGSQESHNTE PQAAADSGDQ SSDNEESEDD
EEHEESDDEE NEEDNENEPH LDDISGSPVS SRGSTMSLDG PPQHFLSDVP SMRSRIREVA
KKFLESHETE KHGKAMKKKA TKILTNLSDL AEEIEAFYLN RSAGNLSPEN GVELFKKLAS
SFDADVLESV TSAELLASGL VRVLLEVFSN PDEDLARTAQ ADFLQVFMGY SVKSKPKTAT
ADSPATPFSV MVHKLQDLLS RSEHFEVITV HQNTFDGNRS SAASMLAKQI RLRLVADDES
IPKSYRNIMV SIHAIATFKS LDDYLRPRIS LSERPRGSSR RADNLSRALA SLAGSAGLPL
SHAAARLAER ASAASGSSPI PPPPSVPTPS GSRSLRKTKS KTTPQSESAA TPDTSSSTRD
KGVLRRSTRR SAASAADSPV PSRPPPEDDD LENALECADE KHLSDDEEIG GSSALDAIVG
DLDEDMSESP GPEPGAVNME IAAGGRVTAR KDDGTRVPTP SQSSLPTRSS ALPPPPAAQS
TPTPATSSRP MSYAAAIQAV PQDWHIQFTL DNKVITSETT IYRAVHTSAA NSDEHFSRSV
WSAVHPIKFR RAPGPPPAET LSFSSNAQAS TEENGEGNVP ASLAKHPSTA SILRLLNILH
DLNANIEDVM VENSEKDAVR LNVEPLSQFV NTKLTAKLNR QLEEPLIVAS NCLPSWVEDL
ARLYPFLFPF ETRHLFLQST SFGYARSMTR WQNAHSADDS RRDRRDDRPF LGRLQRQKVR
ISRSKILESA LKVMELYGAS QSILEVEYFE EVGTGLGPTL EFYSTVSREF SKKKLKLWRE
MDSNDSEEYI SGASGLFPRP LSDDEAVAPN GERILQLFKT LGKFVARSMI DSRIIDLNFN
PTFFRIGDGS SAPGVKPSLG AVKVVDPGLA RSLKTIKKFA VAKKEIDEDP SRTPAQKVAD
TEDIVIDGVK LDDLCLDFTL PGFPEIELMP NGGQIRVTID NVDAYLERVI DMTLGTGVRR
QVDAFRTGFS QVFPYSALSA FTPDELVTLF GRVDEDWSLE TLMDSIKADH GYNMDSKTVK
NLLQTMSELS APERRDFLQF TTGSPKLPIG GFKSLTPMFT VVCKPSEHPY TSDDYLPSVM
TCVNYLKLPD YTNIEAMRKQ LSTAIKEGQG AFHLS
//
