ID U9UPH3_RHIID Unreviewed; 2170 AA.
AC U9UPH3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=GLOIN_2v1563266 {ECO:0000313|EMBL:POG75564.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:POG75564.1, ECO:0000313|Proteomes:UP000018888};
RN [1] {ECO:0000313|EMBL:POG75564.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=24277808; DOI=10.1073/pnas.1313452110;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei Dit Frey N., Gianinazzi-Pearson V.,
RA Gilbert L.B., Handa Y., Herr J.R., Hijri M., Koul R., Kawaguchi M.,
RA Krajinski F., Lammers P.J., Masclaux F.G., Murat C., Morin E.,
RA Ndikumana S., Pagni M., Petitpierre D., Requena N., Rosikiewicz P.,
RA Riley R., Saito K., San Clemente H., Shapiro H., van Tuinen D., Becard G.,
RA Bonfante P., Paszkowski U., Shachar-Hill Y.Y., Tuskan G.A., Young P.W.,
RA Sanders I.R., Henrissat B., Rensing S.A., Grigoriev I.V., Corradi N.,
RA Roux C., Martin F.;
RT "Genome of an arbuscular mycorrhizal fungus provides insight into the
RT oldest plant symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20117-20122(2013).
RN [2] {ECO:0000313|EMBL:POG75564.1, ECO:0000313|Proteomes:UP000018888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 181602 / DAOM 197198 / MUCL 43194
RC {ECO:0000313|Proteomes:UP000018888};
RX PubMed=29355972;
RA Chen E.C.H., Morin E., Beaudet D., Noel J., Yildirir G., Ndikumana S.,
RA Charron P., St-Onge C., Giorgi J., Kruger M., Marton T., Ropars J.,
RA Grigoriev I.V., Hainaut M., Henrissat B., Roux C., Martin F., Corradi N.;
RT "High intraspecific genome diversity in the model arbuscular mycorrhizal
RT symbiont Rhizophagus irregularis.";
RL New Phytol. 0:0-0(2018).
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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:POG75564.1}.
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DR EMBL; AUPC02000059; POG75564.1; -; Genomic_DNA.
DR STRING; 747089.U9UPH3; -.
DR VEuPathDB; FungiDB:GLOIN_2v1563266; -.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_000684_1_0_1; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000018888; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd16482; RING-H2_UBR1-like; 1.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF24; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000018888};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
SQ SEQUENCE 2170 AA; 247296 MW; E9B4BCF5B6F817C8 CRC64;
MEPEATTSHT FPFNNNESES LSLSTYLNSC PKIFGYRLKE SAQQEILKRL FSELWNSNED
HRSLFFPNGF GEGPDAYKLS LSQGEEYSPT QKGKACGHVF RKGEGVYRCR NCALDETCVF
CSRCFHATNH EGHDVTFSVN SGSGSSGCCD CGDPEAWKIP IHCAYHSPDA SSPDSSEFEQ
IQYEEILPDD LLDSIHVTIS TVLDFILDTL YASPEEMSPL SEEEVREEAK RAANFIRDPI
NNVDEEKLFA VVLWNDEHHS FHEVIEQLMD ATSCSKAEAK AIAERVDSYG RDIVQISEDI
QRLLNIARAI TSIGLAVTVR SARDTFREGM CGLFIDWLKD LAGGKIGSNV TILRNIICEE
LCKECKVWNK SRNAKRAKID EKWRILNDIG IGDTRNGETE GTTSEYMSDD EMVMIDDDNE
NNEDDASNNY KRSSEFSGDY DISMEEDSSD TIEPMDEDES IIYRGTSSLM KTVEDFKKEL
RLDRLLILDL RLWKEARAGL RELYIGTLVI NPEYKKIMGI RFARNYVNLA KAFLTPDREP
EHSIILFSVQ LFTVPTISTI LVTQYKFLTT IFTILHTFFT SNAVGDDLDS IDLNAKIDCD
SEAFKNRRYF HVFQDLRYII SNDSVEKTVP KNPHYLQQYL NLIALFHGMN LNIRATQQHV
EYENDSWVNA FNVTLQIAKS CRQFSECYTG NTRTLCVTIR KVLRKLYELS SRRDNDDDDD
DDDDDDKMDE TCDAQHETPY HSSVWGTSTP GSYGPFAKFS DEESEDKESN LSSLRGTEFH
DVIFHQSPYF LSFRVVKFEV ASQPVSFHNP LHWFLAELLE NVNLLDDELL IQHGFGNFQS
MIGLDTESNE EVVQRVKEKI LGVFDYPLRV LVLLVQIRAG LWVRNGFGIR GQCHHYREIS
LRENTFDEDI FLLQTAFIIL DPNIVLATIL DRFDLVEWFN GGTDHKIYDN SQLTFISEEL
LTLLIICVSE RSNAAGLTIE QEIKREIIHG LCLGPIAYSE LIKRIPERLT QNSMFDEILV
KLANYRAPDS LTDHGIYELH DEYFDEVDPY FVHYSRNNRE EAEEALKSRL KKKDGTHSTP
LLIPKLLPIK SGPYTKLGNI LHTRLLNQLI YYALLHVRND EKIKSDTLVE EALHLIMLAL
LDENNNIVGE SKRKGKQKAT DTSISSDIDE EMTGFIYYAV SDFFQVDMKP QGTCLLDLLL
QLSCEQNFKE FHNKLDFIIS KFEQFGSDSV KIKIDQHREK VRIDLQSKGT EDSELSEYER
KKQAARERQK KIMEQFAKAQ QSFIEKHEDL YEEYEDMEED WEHPASEVQS GTDSSKPMET
IWSYPAGTCI VCQEETNASS LYGMLGLIQP SSLLRRTPFD DKDYVFEVVN LPENLDFTYD
RSVPYGVASS IYNNDATSSS EPSHLSKGFP SKSCRQGLYA STCGHLMHVK CFDTYFASLE
QRHQLQLARN HPEDVKRKEF MCPLCKSLGN VLLPIIWKTK KEVFPGILDT QEDYDTWLRD
KVGPGLEKLK SSFSAGSNLP FSHNDPNNYT TFTTGTPIDA REMSTNTGFS NFTQTQQRRR
NSSIRDALTQ FVHMLRTPVA NQNNDESGSS TAVSDDFSVQ GSSTREASAV SDDEDQESIR
RMYNRLADVV QMAYRNITPE ITFQTVPLKS IEYMWDLFGY TISCIEIGQR GIGKTTSEGL
VGPTLIDGIN SQTLTLLRVL SETIFTYINT MLVGQTGEFG LKQITLHRNQ QIFYGYPLFQ
QEENVQNIGS KPFADDKRKM IGPYGPSFLF TQVKPLLLED PFFVLVEICV CTASVTEYEV
YHMMRLLYTA EIVKVIVSLI ESAINDKTKE WIDDDRVKKK FNGLRDTSIR DFVIWVAKQV
GNNEHDIVKF LDGIDESTFI KLIKTFCLPY LRKCVILLHA MFGVAFPKGV DTDETELTRL
TKLLGFPSVE HICSIPTTSA NDITMLSVIS GWCNHLYTLR QVPPSPITPS GTPHDISMIH
GLLVSSGVTS GNSQAPQEHH QLYQKIDVKV NHPAIFELVG LPKRLDSLFE ESLKKVCKKC
KTVPHDPALC LLCGTFVCSQ SYCCSENDRG DNDRGECNLH TKSCGGDIGI YLLVKKCVIL
LLHVDNGCFM NAPYLDTHGE TDLGLKRGRP QFLNQKRYDE IRKLWLTHGV PIHVARKIEQ
TFDLGGWPTM
//
