ID D4DB79_TRIVH Unreviewed; 1840 AA.
AC D4DB79;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=TRV_04378 {ECO:0000313|EMBL:EFE40913.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE40913.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE40913.1}.
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DR EMBL; ACYE01000220; EFE40913.1; -; Genomic_DNA.
DR RefSeq; XP_003021531.1; XM_003021485.1.
DR GeneID; 9578492; -.
DR KEGG; tve:TRV_04378; -.
DR HOGENOM; CLU_000366_1_1_1; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000008383; 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; 3.30.2410.10; 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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1470..1840
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..753
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1142
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1807
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1840 AA; 203214 MW; BF2B90F26FB92126 CRC64;
MERRVTRSAA RLAAGSAASV SESTSPPNPA PQTRKRKAPS RREVARADPE VPPSPQPASR
SKRQKLTPAR QPASRYSARQ SAAMSQPRSP GGSEERPKSV AASSSSSKNR TSRNRKTTRD
SSQHVSPPRR QKKRGKRDTD VDMKDGAEER KEKANEKDDE ETSPTSDSHE EANQMDTAED
DEHESFRNGI FGSGGHFGLQ STLRALSGMM SGMSSRLRDI LSNLKTNEDP SVQLIALQEL
SDLLLVSNED NLAGHFSPDP YVHELVNLMQ PNDFGEENPE IMLLACRCLA NMMEAIRGSA
GSVVQGGAVP ILCQKLLDIQ FIDLAEQALS TLAKISVDFP ASIVREGGLT ACLTYLDFFP
TSTQRTAVTT AANCCRNVPQ DSFPVVKDVM PILLNVLSSS DQKVVEQGCL CVCRVVESFR
YKPEHLEELI EPDLLRAVLR LLLPGTTNLI GPHIHTYFLR ILGIICKSSP RLSVELLKMN
IVDTLYQILT GVSPPSDESI GPAKSDTVHI MQALIHRPRE QVYETLNIVY ELLPAASKGS
VVLLDDQLRF TLGGGPLPLS ATPKIKAMGE KRLELLRNCQ PEIKRFATIL LPTLTDVYSS
TVNLRVRQKV LLAQLKMVQA LDVNIIEEAL RSVPYASFLA GILSQKDHIS LVALALQCAE
LLYERLRDIY QYQFHREGVI NEIKVLATAS VLGKDDKSAE EKTGSVLGSK HHLSHDDGVN
RGHDNDSGNE HDIQDDIHDH EDESNDEDDF NGDYPDDPEH HDEHENEHDD ASDSEASSIV
HPPAQSLDHT LQDLITNGAK HFLELYEESK TAGMHEKAEV VLATLRGLTK KIEDCYKASV
VGNRGFKLFS ELAAYFDQDA FDSITSYELL NSGIIRVLVD VIENSKGQAG ADFLKAFKCS
QSPLKHSSER KSAFGAFIHQ LQDLLSRTEN FEVVTFHHNA FDSRSTLSML SKQIRLRLVA
EEGSNIPKPY KNMMVSIHAI ANFKTLDDYL RPRISLSERP RHSRHRDPTF PHLPSGTNPQ
DPESASRGSD TGSPHLSDFP SYRLPTGRDS SNGTSSRGTN KGRSARPSTL QGSGNGEREG
VGRRRSARHQ PPPPPMESDD TDGPLECADE PNGSDDEEDD EEGDTLDTIV DDIDDDLSED
DVPDPSAVNM EVASTGKVTA RKEDGTRVST PSQSTPVAKS STTSLARSSP QSFGRSLSMA
GRSFTSYAAA MLAMPQDWHI EFVVNGKPIT NDTTIYRAVQ CNRSNDNNSP ARNVWSTVHT
IYFRRAQGPP PPEPTTLTPA TSNVSAMVDD VDMPESLNNV PTTASILRLL RALHNLNSQS
DDELANDSGV IGIAPEPPSQ FINTKLTAKL NRQLEEPLIV ASSCLPSWSE DLGRHFAFLF
PFETRHLFLQ STSFGYARSM VRWQGAQSND DGQRERRRDD RAYSGRLQRQ KVRISRTRIL
ESAMKVLELY GSSPSVLEIE YFEEVGTGLG PTLEFYSTVS KEFAKRKLKL WRDSDSSGDG
EYVDNKLGLF PAPMSQEQVT QEAGKKQLQY FKALGKFVAR SMLDSRIIDI GFNPLFFSVG
RGAYTKKPPS IGSVKRVDAE LANSLKFLKK FADKAAAIKT DSSLSAAEAA CAMEQCEVDD
TKLADLGLDF TLPGYPHIKL IPNGQNTPIT MSNVELYIDR VIDMTLGTGI KAQLDAFAAG
FSQVFLYSSL KTFTPDELVM LFGQVDEDWS IEKDLSRPFT DFTLPALMDS IKADHGFNMD
SRSVRNLLAT LSEFNLQQRR DFLQFVTGSP KLPIGGFKGL TPMFTVVCRP SEPPYTPDDY
LPSVMTCVNY LKLPDYSSAE VLLNKLSIAM REGQGAFHLS
//
