ID C1GRI7_PARBA Unreviewed; 2162 AA.
AC C1GRI7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=PAAG_01132 {ECO:0000313|EMBL:EEH38211.1};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH38211.1, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH38211.1, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(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|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; KN293993; EEH38211.1; -; Genomic_DNA.
DR RefSeq; XP_002797273.1; XM_002797227.1.
DR AlphaFoldDB; C1GRI7; -.
DR STRING; 502779.C1GRI7; -.
DR GeneID; 9100158; -.
DR KEGG; pbl:PAAG_01132; -.
DR VEuPathDB; FungiDB:PAAG_01132; -.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_000684_1_0_1; -.
DR OMA; GEASYMC; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002059; Partially assembled 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; 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; 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; 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:UP000002059};
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}.
FT DOMAIN 82..154
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 82..154
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 405..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2162 AA; 244827 MW; 2E763B38EB56F7AD CRC64;
MLSDLERKLG RALLEHPSKH GYRYTREASH DLLELLFRSL TGYNEEYLRL LFPDGLPKGK
WKLSEAQGAV EGAEYTEAAR GKRCGHIFKN GEASYHCMTC STDDTCALCS RCFDSSDHTG
HKYSISLSSG YNGCCDCGDE EAFKIPVLCA IHTATADIEQ KGKSSAQTPA DLVESITTTI
GRVYDYFCDV ISCSPEQLRL AKSETSIRQD EVTSRLSSEW YGGSDPAEEE PEFALVLWND
EKHTVTEVAN QVVRACREVS RFGKEKANET HEIGRSVVKY SRDLGNLLAV SNIIEQIRVT
VTVRSARDTY REQMCGTIIE WLSDIASCYV GNDSDLLRQT VCDQMIQPWR LGSSASNASI
GKKGIYDNEQ EDRMRGYAIS FTINPNGPFI ELAATDDVMD DNDEGAIEED RDEEEEGEDD
EVDDEEDDDM DVVNPVRLNL EQIAEAFEAR ANAMNADVEM ATEDHLEVEE ATLAGYPPPP
PPPPPRTLQQ GGQDVTPLIA PTGPESERFA NSIASARITI PKTPGVRSKP YSRAPTYWGI
KPDRYFDNQD LAPYEDFRKR TRLDWIILFD LRLWKKTRTD VRELCLGTVV NVPRFKRILG
LRFSALYTTL AQLYLIADRE PDHSIINLSL QLLTTPSITE EVVDRGNFLT NIMAILYTFL
TTRQVGEPRD VDPTATLSID TGSATNRRLY HFFLDLRYLL LSEHVKSKIR CERQYLMQFL
DLVKLPQGIC PNVRAVEAHV EYETETWIAA SILMREINRL CRMFCDAFRI NDTEENEAFI
VDAIATTAYS TMVNSLGLER HRFSQAEIKE LVRFKSVPFV EFENYSFKQV THHRLVDFAV
DRGSISFHHA LHYTLSWLVE CGRDMPENKM REVFYRTANM VKSQRLINTQ IQGLDADDII
FTMFDFPLRV CAWLAQMKAG MWVRNGLSLR HQMSQYRAVT TRELAYYRDI FLLQTAFVVC
DPIRFLASVV DRFGVGDWMR GGYVTRPGYE DLKHVDILEE FIHLMIVLIT DRTSLSSPED
QDNVRTSTMA RDIAHALCFK PLSFSDLSQR MNEKFGESTN FQEVLSEVAT FRPPEGMNDT
GTFELKPDYL DLVDPYCAHY TKNQRDEAEN LYKQWMAKKT GKDASQIVFE PKLRVIQSGA
FVRLTAFTQT TLFAQIIHHC LDYCLTFKSV TANVTTTRVE TFLHLVLHLI LLATMEDNVS
EDDLDESGEH PDSTQSFIYH ALCRTKLTRM AEISIIGLLQ NISNVPEFSS CGPKIRHILK
KLWQMRPKAY VAATSTLEFP YDNIEAPSPA AKTESELEIK KKQALDRQAK VMAQFQQQQQ
NFLNAQGNID WGEEDDDMSE VGEPNHLSLT EKKLWKYPSD RCILCQEDTN DSRIYGTFAL
ITESKILRQT DTEDASYVGE VLKTPSSLDR SADAIRPFGV AGDNRKMVRS LDSTGGEVIM
EKQGLGKGYN PKRAVVGPVM TGCGHIMHYH CFEDYYNAAQ RRHHHQVARN HPERLSLNEF
VCPLCKALGN SFLPIIWKGK EESYPGALGT TESFDEFFNE TLVYAVSRFR NHALIMESDK
LYTSGFQDLF VDYVSKNFIS PLSNKVDQLT TPPLPELLSF SQPARMQMPG LFPQPDEIAA
MGPPTTQQPT SNTNYSLMPE LVTIYKRLRE SIRSNGIYSQ FGYQGNISDD LIFSDVLLRS
LGFSIAAVEI AQRGVGSQGG STLLAQVPQM TLTHLRVISE TAFSYCSIGG LNPTATNKTG
YEFRDMNRRK LCQLFVGHPG LSGLSNLAYD NKSIEPLLGQ DSFVFLAECS LSIVPALNFD
IIHVVRLCYI AEIVKTALVY MLHPTGFLEL ESKHDSDSST DDGVINPRES LMRNVFNWLI
NTYKTSSTNN QLPEEGVSSL FIDSETFSNS MIKTLRRMVD KYALPFLRKT VILLHVRFGV
EFPNTGSDYS DLAEIDRLST LLHLPSIDSI FESLINNVAA ESSNSMALLV TGWISHFISW
LQERTNVDDH QQQYQQQLEP LSLPHPAIFE LVGLPKYFDS LLDEATRRRC KTTGKELADP
SICLFCGDIF CSQAVCCRSG GDRKLGGCNR HVAECGGNVG LFINIRKCMV LFLHNKNGSW
HHAPYLDIHG EVDPGFRHHR RLILNQKRYD RLLRDAWLSH GIPAVISRRL EAEINNGGWE
SI
//
