ID A0A2C5Y543_9HYPO Unreviewed; 2142 AA.
AC A0A2C5Y543;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=CDD81_5474 {ECO:0000313|EMBL:PHH63817.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH63817.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH63817.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH63817.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PHH63817.1}.
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DR EMBL; NJET01000042; PHH63817.1; -; Genomic_DNA.
DR STRING; 1399860.A0A2C5Y543; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000226192; 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; 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:UP000226192};
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 85..157
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 85..157
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 408..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2142 AA; 241609 MW; B6DAF890C0718613 CRC64;
MDAPLSTQEQ QLCQFLAELP ARFDFRYTED ASKELLRNLF WSMAGGNHGY MGLLFPTGRL
ADSLKLREAQ GAVEGAEYTE AARGKRCGHI FKPGEASYVC RTCGTDETCC LCSRCFDSTD
HSGHMVRMQL SVGNSGCCDC GDDEAWTHRL LCIVHSDIDT GPDKGKAKQA AALPDEFLAS
LRMTVARAFD YICDVVSCSP EQLRQAKSQE SILKDEESSR LSSKYYGAQG PPCTEFALVL
WNDEKHTVQD VQDQVARACS KTMREASRNA LETDLVGRSI LTYSTDIAQL LKMAKIMEAI
RVTVTIRAAR DTFREQMCGT LVEWLSDISG CTAGHDSHIL RQTVCEQAMR PWRQGSRATH
TLGLIDDEEE DEQSMSSSTL HGVNAHFILA LQRAAGTTNV EIAIETGAVM TGDDEDGDEE
EEEEIDEVEQ DDDEVEVDDD ADMDDGEDGN HSVSSSAAVL DEDQDVMMVD ARGDVTDLGM
NWSQSDQALE EDEATMAGYP RPPPPPPPPA QTRGAGRERD GTPSDSDTAD GLIAPAMSAK
ANAKIPKTPG KTRLLTPRPA KYWVETPQVY TQRGNVPPAE DVFQRVRLDW LLYFDLRLWK
KVRNDLRSLY ISTVVQMPEF KRVLALRFAS LYTVLAQLYL VGDREPDHSV INLSLQMLTT
PSITAEVVER GNFMSSLFAI LYTFLTTRQV GHPWDVSPEA VLAFESGSVT NRRTYHFYQD
LKFLLGSQHV QERIRCEPRY LMQFLDLGKL HQGMGPNVRA VAEHVEYEPE SWITTSMVTR
QMSLQARNVA EAFRNCPADE IHYLQRAIRF TTKTVIINSV GAERHRFKQA EINDEVRFKT
LGDFEFDSEA TSYQVVKFVV DRESISFHHA LHHTLSWLIE CARGLPASNL RTLMSFSLQE
LKSPPRLMGR PQLPKKEYEP EDYLMAAFDY PLRVCAWLAQ IKASMWVRNG ISLRHQAGTY
RGVGQRDVTH HRDIFLLQTA MVVCNPSRVL CSIMDRFGMD GWVKGIFELK SEAQDDVQHL
DVVEDMVHLL IVLVSDRTSL MAPEDEANSR LLAMRRDIIH VLCFKPLSFN EICNKLPDKY
QEQQEFYMAL DELATFKPPE GTSDVGTFEL RHEFIEDIDP YISHYNKNQR EEAELAYRRK
MANKTGKTLD EIVYEPKQRP IPSGLFQGLG AFTGTGVFAQ IIYYSLLYPL VAHKLTATVP
VTRLEAFVQV VLHLMLIAIV EDKTVEDKTD EATQEQGSFV YTALTKMARS NFMPEASNSR
TIVSLLHLLS TRQEFKSAQA KIALVLKRLK QKRPQAFESA FASLGIAADR ISTASPASTG
GEEERERKKK AALSRQAKVM AQFQQQQKSF LEKQGGMDWG SDVDEDDEAK QQQTEERKHD
WKFPRGTCIL CQEEVDDQLL YGTFALLAES RMLRQTDFQD ASLVREASQT PCSLDRSADE
VRPFGMAQEN RKMVEKLNWR GEKFLAERQT IGRGYAGDLS RPGPLASGCG HMMHYHCFEV
YYEATNSRHT HQIARHHPEM MALNEFVCPL CKARGNVFLP IIWKGMQESY PGRLQARMSF
ADLLEHQVAL DKWPGQGAEP GAMDAMTPPR AAPPPPWERL MSVAPLMMPA TALCLPIGRD
GSRGVDGANL NMNIMNELEN AYARLKESVR LNKLDKRYDE AQVDDGAQLD LTEMLVYTVA
FTLSSVELQQ RGVEAQPGMT LLERIPEQTI TQLRVLAETA SALITVRGRF GSFDNLMGER
RFRQSCQLFI SRHLAMEPPK LRRLMNLYPP LLSLDPFIFL VECTYGLGSV QSVDVKHLLS
LCYLAELVKV VYHMSRNMNM SKWLEALQQR QTHDEAINNF ADFALAVTEY GMCDDEPTLH
AQRANEAFDQ PGVDSLQAWY SFVKKYALVF LRKSLLLLYI KYGIDFNSFV SSNAEADELH
RLTEAMMLPS FDQMCASLTS KSLACGWPET IRDVVLGWVK HQVLGSNKPS QVRQTAIVSH
PGIFELIGLP KTYDTLIEEA SRRKCPTTGK DVMDPAICLF CGEMVCSQST CCQKLCTVGN
ESVKLGGGQQ HMRRCQRNIG VFLNIRKCTI IFFFNQSGSF AAAPYMDRYG ETDYQLRHGR
QLFLSQKRYD SMIRNAVVNN DVPAFVSRRL ELDVNNGGWD TL
//