ID B0CU64_LACBS Unreviewed; 1666 AA.
AC B0CU64;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=LACBIDRAFT_176411 {ECO:0000313|EMBL:EDR14039.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR14039.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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 ---------------------------------------------------------------------------
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; DS547092; EDR14039.1; -; Genomic_DNA.
DR RefSeq; XP_001874598.1; XM_001874563.1.
DR STRING; 486041.B0CU64; -.
DR GeneID; 6071060; -.
DR KEGG; lbc:LACBIDRAFT_176411; -.
DR HOGENOM; CLU_000366_1_1_1; -.
DR InParanoid; B0CU64; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000001194; 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 Reference proteome {ECO:0000313|Proteomes:UP000001194};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1303..1666
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 613..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1633
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1666 AA; 181073 MW; D7A9EDD552A17F70 CRC64;
MVPSSDGPPI PGGLDETAAM AIFGDYRQFG SYMMSLSSRL KTMLTNIKST ADPTTRLVTL
QELSELLSIS TEDTLAGSFQ VEQFVRELVK ILGGRGADED EDDEGDEENA EQDEDAALAA
ALAMSTGGSF QGDDNLEAQV LACRCLANLM EALPGVAHTV VYHGAIPVLC SKLIEISYID
LAEQTLSTME KISEEFPSSI VREGGLAALL NYLDFFSIAV QRTALQAASN CCRNVSPEHF
PMIHGVWPII RNCLSYSDQR LVEFACLCVI RVVDSYHRAS VENLEALVDT ALIRAVNQLL
LPAGGSPLIA SNTYTLLLRA LATSARASPK ITVALLEADI VDTLYQILTG VLPSASEAAE
GQGGAAGGQG LGGGLADMTI MDNLAHRPKD QVEEALSLIS ELLPPLPKDG VFDHKAYTEK
SLARMVKAKA KAERAAARQV PQPTPSPTIM PSLDTVSAPL AENEASPAPG PASEVAGPES
EDAAVISGIK DVAPDRTEIL RSTHAVSRFM QLLVPILIDV YAASVITPVR IKTLTGLLKA
VSFMDADGLK SVLMFVPVAS FASSILSSKD HPSLVIGALQ LVDLLLAKLP SLYKPTFRRE
GVFHEIETMS ERTVTSTKSK DKDKESNESP EPVVQPISTS SIPGFKKLSS LSLDPEDAIT
LRARVIQFKY LNGDEDKNED SAFESLRRLV DRISDQNATE KELSEGLWEL AELFSSPHTS
VSSFELLQSG VVDGLLQFAV DEHRAVNSKR RKEMFLDAFA GRKVKSMGNS QSPFAILVKK
LQESLTRMES FDVITVTQNS DDSKRSSPSL LARQLRLRLI TGDESDVPRN LHNIVVSIHA
IATFQALHDY LRPRVAGLLG PGSRLSGMFA ALAASNFTGS TSRALNEESS QASKTVSGAL
ETNPPPPVAP AIVTRRRSQR LSAKANPSAA SESVSATDQI VADASASAGP SLQGETTVVE
PAPSETVVDS ELQADFSDDE DIDAEVYDEE VDPDISVADK TISLSTHICA TDGSKIEAQT
PDGTRVATPS ASVQDGPTPP SLRASLSNKA SYAAALKAKP TDWHLEFSMD DQVLPLDLTV
YGAIHQHEMR KKTGALPLNM IWQGVYTIKF KKVAGPLPSS ESRGDDIGTK NRSPSPSLSS
LPDDAPHAKI LRLLRVLNQL NTLEAERSVF VGEKRNLPDS AFINNKLTAK LSRQLEEPMI
VASSCLPDWA LDLPQHFPFL FPFATRYNFI QSTSFGYARL ILKWQNSSRR DDGIGFLGRL
QRQKVRISRK HILESAVKVF ELYGSSSSVL EVEYFEEVGT GLGPTLEFYS LVSKEFARKD
LKIWRDSDAA GSGVYVDHPT GLYPAPISRE DIANDGGQKR SHILRVVGQF VAKAMLDSRI
IDLSFSKVFL KLVLGEEVPL TLASLKLVDM DLANSLAKLQ SIAQDSSNIA TDPVSFRLTS
NNIFTKNSVK LSLKVARIEK VTIEDLELDF TIPGYDVELR ENGRNIPVTS ANVDEYVHEV
LDAILGKGIQ IQAKAFRDGF SKVFPMSDLR AFTADELVML FGNADEDWSI ETLSEALKAD
HGFNVESRAI RDLLEIMAQY DRPTRRAYLQ FITGSPKLPI GGFRGLNPAL TVVRKPHEAP
LTADDYLPSV MTCVNYLKLP EYSTKAVMRE KLRIAIQEGV GSFHLS
//
