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Database: UniProt
Entry: A0A2C5Y543_9HYPO
LinkDB: A0A2C5Y543_9HYPO
Original site: A0A2C5Y543_9HYPO 
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
//
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