ID E9E2T2_METAQ Unreviewed; 2252 AA.
AC E9E2T2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=MAC_04180 {ECO:0000313|EMBL:EFY89748.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY89748.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY89748.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UQCR10/QCR9 family.
CC {ECO:0000256|ARBA:ARBA00007856}.
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DR EMBL; GL698496; EFY89748.1; -; Genomic_DNA.
DR RefSeq; XP_007810520.1; XM_007812329.1.
DR STRING; 655827.E9E2T2; -.
DR GeneID; 19248491; -.
DR KEGG; maw:MAC_04180; -.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_000684_1_0_1; -.
DR InParanoid; E9E2T2; -.
DR OMA; KYWLEKP; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002499; Unassembled WGS sequence.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:InterPro.
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:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
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; 1.20.5.260; Cytochrome b-c1 complex subunit 9; 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; IPR008027; QCR9.
DR InterPro; IPR036656; QCR9_sf.
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; PF05365; UCR_UQCRX_QCR9; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF81514; Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
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}.
FT DOMAIN 269..341
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 269..341
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 585..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1514..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..609
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2252 AA; 253285 MW; 6A1594FE7E6FA5E7 CRC64;
MASPSIETER PPPRPRQANT TCCSALFRKN YAMLAAVFTA GFAFEVYGPH PGKWPTGIRQ
LLTSRCSGFN NGINKWWDNH NRGRQWKDIR SKVDISRIII CSRDTFCHVR IGGYQALQSQ
LAVSILPGTV IDGASVPVIF DNCQQAPWRA ANIRLSHLGA GPSLPQRLWA YSLDRIGGNH
ELMSMEPEMS TQEQQLCQLL ADLPARFHNR YGEDAARELL TSLFWSLAGG NQDYMRLLFP
EGKPSDSLKL GDAQGAVEGA EYTEAARGKR CGHIFKPGEA TYMCRTCGTD ETCCLCVRCY
DSTDHTGHMV RISMSVGNSG CCDCGDDEAW KTPLFCTIHS DMKSGQAKGK GKEAVGLPDD
LLNSLRMTIG RVFDYICDVI SCSPEQLRQA KTKESILKDE EESRLTSVYY GPEATFCNDF
ALILWNDEKH TVQEVQDQIA RACRKTRREA AQNAWETDAV GRSILTYLSD IDRLLQMAKI
MEAIRVTVTI RSARDTFREQ MCGTLVEWLS DISGCSIGHD SNILRRTVCD EMMKTWRQGS
HASHTSGVID DEDEDEQNIM SQTRIHGINV RFIRALQAAV APGGNLEINV DGGDEDVDQD
DDADMGDNDD DGQSPTSSVA GGDEDEDDDV MMVDARGDVG DLGMNWSQSD QALEEDEATM
AGYPPPPPPP PVQARAARRE RDGTPSDSDT ADPLIAPAVC AKANVDIPKT PGKTEKPTPR
PGRYWIETPQ IYTQRDNVPP AEDVFQRVRL DWLLLFDLRM WKKVRIDLRS LYISTVVSVP
EFKRVLALRF SSLYTILAQL YLVGDREPDH SIINLSLQML TTPSITAEVV ERGNFMSSLL
AILYTFLTTR QVGHPWDVSP DAVLAFESGS VTNRRMYHFY QDLKYLFGSP HVQERVRSEP
RYLMQFLDLV KLHQCIGPNV RAVVEHVEYE ADSWITASLV TRQINLQARI LAEAFRDCPP
DEIHCLQRAI RFTAKTVILN SIGAERHRFK QGEIKDEVKF KTLTDFEFDT ENTSYEVVKF
VVEKDSISFH HALHYTLSWL IECGRSLPAS SIRALMSFTG QELRSKPRLM GRPQIPRKDY
DPEDYLMAAF DFPLRVCAWL AQIKANMWVR NGISLRHQAS TYRGVGQRDV THHRDIFLLQ
TAMVVCNPSR VLASIIDRFG MDSWVKGLFE LKSEAQDDAQ HLDIVEDMIH LLIVLLSDRT
SLVAPDDEPN SRILAMRRDI THVLCFKPLS FNEICSKLPE KYQEQEDFHR VLDEMATFKP
PEGISDVGTF ELRQEFIEDI DPYIAHYNKN QREESEMAYR KKMAKKTGKT IEEIVYEPKH
RPVPSGLFEN LGQFTSTGMF AQIIYYSLLY PLVAQKFTPS VPFTRLETFL QVVLHLILIA
ILEDKSNESE SVGQPPNSFV QIALTTMARS NFMPEANNSR TIVSLLTLMS NKDEFKAVHP
KIALVLRRLR QKRPQAFEIS FVNLGISVDR VDTASPANNS VEEERERRKK AALSRQAKVM
AQFQQQQKSF LENQGGIDWG SDLDEDEDEM GQSEDRKHNW KYPTGTCILC QEDADDRRLY
GTFALLNESR VLRQTDFQDP ELVREASQTP CNLDRSAEDI RPFGIAHENR KMVEKLDING
ETFLAERQTI GKGFKANLSR PGPVASGCGH MMHYRCFEMY YEATNRRHTH QIARHHPEDT
RRNEFVCPLC KALGNAFLPI IWKGLEESYP SYLQPSKSFG EFLDLKMGSA YWLQGGKAPE
VDSASPPNMY TPSVPGSLVE TLTNQHPDAE ISWGRDDPDS QSSVLGTPAS SSFSTAGIPE
PGNSLAAAGS NSQILGDLKA AYRRLRDTLR VNGLHTRHPI DAKATGGDEL YSSDTLVQVV
GFTISSVEIQ QRGVEVQPGL TLLDKIPEQV LVHLRVLSET ASSYIAVGAG HTDGVPNRIE
DEFTNDSERQ HCQLFMCRYV GTQDLPAASS VLRPLDAYPP LLSLDPFTFL VECAYGLVPA
YNAEISHILR LCYLAELVKV VFHMGRNIPF SMWIEGLAGK QSQDPAMVNF ASFALAITKC
GMELEVANFG KTSDNEEERE NKGFQQPGVD TLESWYTFAK KYALTFLRKS VVFLCVKYGV
DFNSHVSSSQ DADSDELDRL TVALRLPSFD EMCASMTENA FACGWPMTTY DLVSGWIKHQ
VVWPNGYGDM SESALVSHPG IFELIGLPKT YDTLIEESIR RRCPSTGKDL TDPVICLFCG
EIFCSQSNCC QKPETVGREF TRIGGAQQHM RK
//
