ID A0A161XX79_9PEZI Unreviewed; 1929 AA.
AC A0A161XX79;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=CI238_01740 {ECO:0000313|EMBL:KZL81789.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL81789.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL81789.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL81789.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL81789.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFIW01001556; KZL81789.1; -; Genomic_DNA.
DR STRING; 1573173.A0A161XX79; -.
DR Proteomes; UP000076584; 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; 2.
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:UP000076584};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1571..1929
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 15..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..833
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1896
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL81789.1"
SQ SEQUENCE 1929 AA; 209196 MW; CA5ED243BDAC684C CRC64;
LSPFVFCFIG SVGMPRKNQS LMSPRITRSS ARQAASLAAS SAQSTAGADL AATAPASATS
SSPNPPPTAS RKRKAPAQAA SPAPGTQPPT SASTRRSKRQ KVADAVPPPQ PPPTQTPAPS
RPKRKGNSTA TMSSPDNPAD LANASENTAP SASSSRKSSR SKRTAPSASG KSEAAPNKAI
LEDHDTDTAY TDPSANTSSS SRRTKRNAAN NADQDTAMTG TDDAEKESIP SPPPPPPPDH
HDDDDDSDEN DDDDEEGRRY DDEDDDPFGG FGGPGGPGGL SSTLRALTGM MSGISSRLRE
LLNNLRQKDD PSIQLIALQE LSEILLVSNE DNLSGHFSPD SFVKELVILM QPNEITGEEN
PEIMLLACRC LANLMEALPA SVANVVYGGA VPVLCQKLLE ISFIDLAEQA LSTLEKISAE
YPSSIVREGG LTACLSYLDF FATSTQRTAV TTAANCCRNI PEDSFPVIRD VMPTLLNVLG
SSDQRVVEQA SICVSGIVES FKYQSAKLEE LVSVDLLKAV LRLLVPGTTN LIRSDIHTQF
LRVLAFTARA SPQLSAELFK LNVVETLYQI LTGVSPPSGT EDVASKLDSV VIMQALIHRP
KEQIIETLNV ICELLPSLPR NADPSYGDFV EMNSTEPVTP SSTAPGKARK SPNDKRIELL
DGCKAEVRRF ALILFPTLTD AFSSTVNLNV RQKVLTAQLK MLSNLNEEIL GEALKTVSYA
SFLASILSQQ DHPSLVMLAL QATELLLSRL EDVYRYQLYR EGVISEITKL AAEEQTPPPA
LEPTGSQETS NTDPQASVDS GDHSSDNEES EDDEDHEESE DEENEEENEN ENEPHPDDIS
GSPVSSRGST MSLDGPPQHF LSDVPSMRSR IREVAKKFLE SHETEKHGKT MKKKATKILS
NLSDLAGEIE AFYLHRTATN LAPENGVELF KRLASSFDAD VLESVTSAEL LASGLVRVLL
EVFSNPDEEL ARTAQSAFLQ VFMGYTVKSK PKTATADSPA TPFSVMVHKL QDLLSRSEHF
EVITVHQNTF DGNRSSAASM LAKQIRLRLV ADDDSDIPRS YRNIMVSIHA IATFKSLDDY
LRPRISLSER PRGSRRADNL SRALASLAGS AGLPLSHAAA RLAERASAAS ASSPIPPPPS
AATPSGSRSL RKTKSKSTPQ SENAASPDTS STTRDKGVLR RSTRRSAASA AESPAPSRPP
PEEDNLENAL ECADEKHLSD DEEIGGSSAL DAIVGDLDED MSESPGPEPG AVNMEIAAGG
RVTARKDDGT RVPTPSQSAL PTRSSAVPPP PAQGTPTPST SSSRPMSYAA AIQAVPQDWH
IEFTLDGKVI PSETTIYRAV HTSAANSDEH FSRSVWSAVH PIKFRRAPGP PPAETLSFGS
NAELSTEDGD GSVPASLAKH PSTASILRLL NILHELNANI EDVMVENSEK DAVRLNVEPL
SQFVNTKLTA KLNRQLEEPL IVASNCLPSW VEDLARLYPF LFPFETRHLF LQSTSFGYAR
SMTRWQNAHS ADDSRRDRRD DRPFLGRLQR QKVRISRSKI LESALKVMEL YGASQSILEV
EYFEEVGTGL GPTLEFYSTV SKEFSKKKLK LWREMDSNDS EEYISGASGL FPRPLSDDEA
GAPNGERILQ LFKTLGKFVA RSMIDSRIID LNFNPTFFRI GDGSSAPGVK PSLGAVKVVD
PGLARSLKTI KKFAVAKKEI DEDPSRTPAQ KVADTEDIAI DGVKLDDLCL DFTLPGYPEI
ELIPNGGQIR VTIDNVDSYL ERVVDMTLGT GVRRQVDAFR TGFSQVFPYS ALSAFTPDEL
VTLFGRVEED WSLETLMDSI KADHGYNMDS KSVKNLLQTM SELSPSERRD FLQFTTGSPK
LPIGGFKSLT PMFTVVCKPS EHPYTSDDYL PSVMTCVNYL KLPDYTSIGV MRKQLSTAIK
EGQGAFHLS
//
