ID A2WZR6_ORYSI Unreviewed; 1682 AA.
AC A2WZR6;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=OsI_05457 {ECO:0000313|EMBL:EAY84076.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EAY84076.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EAY84076.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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}.
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DR EMBL; CM000127; EAY84076.1; -; Genomic_DNA.
DR STRING; 39946.A2WZR6; -.
DR EnsemblPlants; BGIOSGA007312-TA; BGIOSGA007312-PA; BGIOSGA007312.
DR Gramene; BGIOSGA007312-TA; BGIOSGA007312-PA; BGIOSGA007312.
DR HOGENOM; CLU_000366_1_0_1; -.
DR OMA; THFDISH; -.
DR Proteomes; UP000007015; Chromosome 2.
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; IPR000225; Armadillo.
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:SF4; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00185; ARM; 3.
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:UP000007015};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1288..1682
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 313..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1643
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1682 AA; 182988 MW; 3B52F7D6ABFEC5EE CRC64;
MQLCEMLSIG TEESLAAFPV DAFVPILVGL LGPGEDGAGG ASPDVMLLAA RALANLVDVL
PSSCSAVVHY GAIPCFCARL LTIEYMDLAE QSLQALKKIS QEHPTACLRA GALMAVLSYL
DFFSTGVQRV ALSTAANICR KLPSDASEFV MEAVPLLTNL LNHHDSKVLE HASVCLTRVA
EAFASYPEKL DDLCNHGLVA QSASLVSISN SAGQASLSTS TYTGLIRLLS TCASGSLLAA
KTLLLLGISG TLKDILSGSG LVAGASVSPA LSRPAEQMFE IVSLADDLLP HLPSGIISLP
AYFHVLVKGS SSKKSASTKQ DGTSSTENER SGHERLLREH PELLKQFGMD LLPIMTQVYG
SSVNAPIRHK CLSIIGKLMY YSSAEMIQSL LGTTNISSFL AGILAWKDPQ VLIPALQIAE
IMMEKLPETF SKLFVREGVV HAVESLICPE SSDMVPSQVL PHDKDNESVM PSRSRRQRRR
GAAAPTENSS LDESNTSNPG IASSTPCSTE VQNTSLRFAV SDRAKSFKDK YFPSDHESRD
LGVTDDLLKL RTLCAKLNSA SENVVTKAKG KSKALSATHF DISHDVEAQF ELIITQILTE
LSKTNGVSTF EFIRSGVVAA LLDYLSCGTF GKERVSEANL PKLRQQALRR YKSFISVALS
IDHERNETPM AFLVQKLQSA LCSLERFPVV LSQSSRIGIG GSRLTSGLSA LAQPFKLRLC
RGQGEKSLRD YSSNIVLIDP FASLAAVEEF LWPRVQRSEA ASKPTVPSGN NSESGIPGTA
AGASSTAAPA PSGRRPTTRS KSSAASSGAS KKDSQEESTN TAKGKGKAVA KPNSEEPKGP
NTRNATRRKA ASEKDLEMKR AHGDSSSEDE ELDTSPIEID DALMIDDDDM SEDEEDDHEV
LQDGSLPICV QDGVHDVKLG DTDDSNIGSA SDSQVQPSSG SSTRNIMSRG VDPNTFGSRG
AMSFVAATMA GLASVGGRGV RGSRDRRGLS LGGSINEHNK LIFMAGGKQL SKHLTVYQAL
QRQLMFEEDD DEKFNGSDLS NDGNRFWGDV FTITYQKADS QAEKVSQGGS TSLNSKSDPS
RSISELKGVS LLDSILQAEL PCDLERTNST YNILALLRVL EGLNQLSPRL RVHAASDDFA
EGKITTLDEL YRTGAKVPSE EFVNSKLTPK LARQMQDVLA LCSGSLPSWC YQMTKACPFL
FPFETRRQYF YSTAFGLSRA LNRLQQQQGD NQNAGGEREI RFGRLQRQKV RVSRNRILDS
AAKVMEMFSS QRAVLEVEYF GEVGTGLGPT LEFYTLLSHE LQSVRLGLWR SSSPSDTGMQ
IDRSASPDDD LAAKELSSDL PDNGSHLIQA PFGLFPRPWP LTVDASEGSR FSKVIEHFRL
VGRVMAKVLQ DGRLLDLPLS TALYKLILGQ ELDLFDIISF DAEFGKTLQE LQILVERKRF
LESTYGMNQL EVTDLRFRGT PIEDLCLDFT LPGYPDYILK EGEENTIVNI YNLEEYVTLV
VDATVKSGIM RQVEAFRSGF NQVFDISSLK IFSPEELDYL ICGRREIWEP DSLVDNIKFD
HGYTAKSPAI VNLLEIMAEF TPEQQHAFCQ FVTGAPRLPP GGLAALNPKL TIVRKHPSSA
VNTSNIAGVT ESADDDLPSV MTCANYLKLP PYSTKVRFLS LEVMRKKLLY AILEGRGSFD
LS
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