ID A0A168C144_9HYPO Unreviewed; 2173 AA.
AC A0A168C144;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=AAL_04311 {ECO:0000313|EMBL:KZZ96015.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ96015.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ96015.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ96015.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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 E3 ubiquitin-protein ligase UBR1-like
CC family. {ECO:0000256|ARBA:ARBA00046341, 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:KZZ96015.1}.
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DR EMBL; AZGY01000008; KZZ96015.1; -; Genomic_DNA.
DR STRING; 1081109.A0A168C144; -.
DR OrthoDB; 26387at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000078544; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
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 FunFam; 2.10.110.30:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform 1; 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; IPR055194; UBR1-like_WH.
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; PF22960; WHD_UBR1; 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:UP000078544};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 81..153
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 81..153
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 355..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..370
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..430
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2173 AA; 243586 MW; 4FDBE87E7EFE9E6B CRC64;
MSTQEQQLCQ LLADLPARFG YRYTQDAAQE LLRSLFWSLA GGKADYMRLL FPDGSFPDVL
KLSDAQGAVE GAEYTEAARG RRCGHIFKAG EASYMCRTCG TDETCCLCSR CFDSTDHVGH
MVRISISVGN SGCCDCGDDE AWKTPMLCTI HSDMQSGPNK GKGKEAVALP SDLVNSLRMT
IGRVFDYICD VISCSPEQLR QSKTKESIVK DEEASRLSSK YYGAEAEPCN DFALILWNDE
KHTAQEVQDQ VARACSKRRD EAAHDAWETD AVGRSILKYS SDIARLLSMA KIMENIRVTV
TIRSARDTFR EQMCGTLVEW LSDISGCSVG SDSRILRELV CDEVMKPWRQ GSLATHTSGL
IDDEDEDDQN QETRTRIHGA NVRFIMALQA AAGTGAELQM NIDIGGLDEE DEEDEDEDED
EDADMGENDD DNHSPSSSLA GGGEAGNHDD DVMMVDARGD VGDLALNWSQ SSQALEEDEA
TMAGYPPPPP PPASAGQAVN TTVAVSVIAP LAQRIPLSVA SRERDGTPSD SDTAEPAIFA
KANADIPKTP GRTERVTPRP GRYWIETPHI YTQRNDIAPA EDVFQRVRLD WLLLFDLRMW
KQVRNDLRAL YISTVVSLPA FKRVLALRFA SLYTILAQLY LVGDREPDHS IINLSLQMLT
TPSITAEIVE RGNFMSSLLA ILYTFLTTRQ VGHPWDVSPD AILAFESGSV TNRRMYHFYQ
DLKYLFGSPH VQERVRSEPR YLMQFLDLVK LHQCIGPNVR AVVEHVEYEA DAWITASLVT
RQINLQARNL AEAFRDCPQD EIHYLQHAIR FTTKTVILNA IGAERHRFKQ GEIKDEVKFK
SMGDFEFDPQ NASYDVVEFV VEKDPISFHH ALHYTLSWLL ECGRSLPAAN IKTLMSFTAQ
ELRSKPRLMG RPSIPKQDLG PEDYLMALFD FPLRVCAWLA QIKANMWVRN GISLRHQAGT
YRGVGQRDVS HHRDIFLLQT AMVVCNPSRV LASIVDRFGM DHWIKGFFEQ KSEAQDDAQH
LDIAEDMIHL LIILLSDRTS LIADESNTRM LAMRRDITHV LCFKPLSFNE ICNKLPEKYQ
EQEDFHSVLD EMATFKPPEG VSDVGTFELR PEYIEEIDPY IAHYSKNQRE ESEMAYRRKM
AKKSGKRIED IIFEPKPRPV LSGLFEGLGQ FTSTGMFAQI LFYCLLYPLV AHKFTPSVPL
TRLETFLQVV LHLILIAILE DKTDEAEPSV GPPASFVHIA LTSSARSNFL PDAVSARTIV
SLLNIAASRD EFKSAHPKIA LVLRRLKQKR PLAFESSFAR MGITVDRVNT ASPANTSAEE
ERERRKTAAL SRQAKVMAQF QQQQKSFLEN QAAIDWGSDL ESEEEEMKQS EDRRHNWKYP
SGTCILCQEE ADDRRLYGTF ALMTESRIFR LTDFQDPDAV REASQTPCSL DRSAEDIRPF
GIARENRKMV EKLDAHGEVF LAEKQTIGKG HTISATQPGA VASGCGHIMH YRCFEMYYEA
TNRRHGHQIA RHHPEDTRRN EFVCPLCKAL GNTFLPIIWK GLEESFPGYL EPQSSFEDFL
DRQMKFTYLL GGSKAREVDE PALPAILTPS VPGSLVETLT NSHPVNEPFW GRDELDVQSS
VLGTPASSSF SLTGTPEPKT SHALAPAVNG HIVGDLLSAY RRLRDTMRLN EFQSRHGNDE
KAKGGESLCS SDTLVQAVSF SISAVEIQQR GIEVQPGTTL VDKIPEQVVG HLRVLAETAS
SYVSIGARYS DPDSYIETEF RTDIMRQHCQ LFMCRYSGSG TPSSQRPMDV FPPLLSIDCF
HFLVECAYAL MPAHKGDVSN MLRLCYLAEM VKVVHHMSCN MHATAWHAGL ARYRNGDAAM
QNFAAFASSV TQLGIDHDSA SGADPRSHDR KNEGFVQPGV DTLENWYMFV KKYALTFLRK
SVVFLHVKYG VDFNSHVPSV HDPDADELDR LTEALRVPTF DSLCAALTEN AADCGWPSTT
QALVSGWIKH QVIWRKARSG YRADPTAVVS HPGIFELIGL PRTYDTLIEE ATRRKCPTTG
KDLTDPVICL FCGELLCSQS TCCQKAENAG RGATKIGGAQ QHMRTCQSNI GVFLNVRKCS
TVYLFRQSGS YAPAPYIDKY GETDPQLRHG RQLFLNQKRY DTMIRNTVLN HGVPSLISRK
LEAEINNGGW DTL
//
