ID A0A1C7NB94_9FUNG Unreviewed; 2174 AA.
AC A0A1C7NB94;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=ubr11 {ECO:0000313|EMBL:OBZ86019.1};
GN ORFNames=A0J61_05930 {ECO:0000313|EMBL:OBZ86019.1};
OS Choanephora cucurbitarum.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC Choanephora.
OX NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ86019.1, ECO:0000313|Proteomes:UP000093000};
RN [1] {ECO:0000313|EMBL:OBZ86019.1, ECO:0000313|Proteomes:UP000093000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ86019.1,
RC ECO:0000313|Proteomes:UP000093000};
RA Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT "Choanephora cucurbitarum.";
RL Submitted (MAR-2016) 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|ARBA:ARBA00004906, 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:OBZ86019.1}.
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DR EMBL; LUGH01000336; OBZ86019.1; -; Genomic_DNA.
DR STRING; 101091.A0A1C7NB94; -.
DR InParanoid; A0A1C7NB94; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000093000; 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; 3.30.1390.10; -; 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; 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; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; ClpS-like; 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:UP000093000};
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 127..199
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 127..199
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..494
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2174 AA; 248508 MW; 671A83916BEC66D1 CRC64;
MSQPPLHTSQ TESTDGARHM NTTPVTPAQL KTFLTEAPLL YKSKLHKGAA KHILTNCYRS
LWSNDAEVMQ HYFFREGLSD SDNLSKLLEK YNLFGSEEHD HDDYVQNEPN LNKTQEEPEY
WESQRGKQCG HLFKKGESVY RCRNCGHDDT CVMCSKCFHA TNHEGHDVKI WISRGAGGCC
DCGDPEAWKI PLQCAIHSLH PHSDMSMDDS SASTSRPQLE PLSSVPANVI QSVRDTITVV
ADYILETFAT SPEDVISVGT PESIRQDCMD SHKALGLPSD PSKQTYACVL WNDEKHSFDA
VINIVVEALG CSKEEAAYAA ECVDDYGRHI IKESSDVEEL ISIANTISSI NLAVTVCSMP
KTVREDISGL LLDWLKELTG GRYKFFNNVD GGNCIIRDIV CEVLSEDWAL SPDLSRLSTR
CRRERMPEDE DDDFDPEGAD TDMDEDDEMI FGDDEGITDG GLLLNAFLEQ HAHVDDDDDD
EEEEEEEESS VSDFEDASEV LLSVINTEQN SQVDNAHEQG DSDMDMHEVE HTYQVTSPSA
SQMSNESLSR RRQSDTQAHA SDNQAAHSLS QGRESEELKR RRLSSSSHSK SHKAHKTRDI
LDLDWNLDVW LDYVEQLEME ERNIAKDLST SFESSSNSVQ QDLANAHRIN TNLKKEFKRK
LRLDYLLHFD LRLWKTARVS IKDLLIGTFI SNLQYKPIIG TRFARNYPEL VDAFFFKDRE
PENSVSTLSV QLLTVPTVAS MLVKDYRFFG IVCSILENFF LTDHIHMILP NEYSRAQVDC
SSRAIGRHRY AYTIFDLRYV MNAEQVKFEI SKNPLYLRHF IDMLYQFQEM DALKRQENAH
VEFESQSWVT AFNMTLQTSK LCRLFAGCFE TTGLASSDAS RNLCRSIYRV LKAIIEWTPV
LAPRKTSSEH QPDTRLKILG LHEQKFHQIN TPNAGSFEIV DYDVTKSPVS FHHPFHWLLS
ELFENVSLLH DCVLNELGWL GGFTQMVNEA FKDKQHDMFL MILEYPIRTL AILSQINCNI
WVRNGYNIRN QAHSYKDVNV RENTLDCDIY LLQVGLTVCE SDKILLTLMD RFQLIDWFRG
KPRKHATYDA SQTVYMVEDF LNLLIVCASE HGYASGITLE QRIRQSIIQF LGISSMAYSE
LLKLIPESLT EHESFESQLN LLANFKAPDG LSDKGIYELK PEYIDEIEPY YWHYTRNQRE
EAYCVLKKRW NQLHPESKLN DKEEFLLTPK TKYIEVGPFR HLGKFLHSHT LCQIIAYALW
DAKFHKESKN DTILDEAIYL AMLAVTDPNS PASELAAMKV KGKYRADMMV DEVKSFVDFA
EEDEYSIQIN EIERTHASLL TILIRCLDDP ELSHAYKRLG FILDKIEAQG SEKAKEVISE
YKHKKSRDVK AEMERNNGNN ISELERKKAA AKARQEAIMS QFANAQSKFM EQHGDLYRSD
EDEDIQETYE EAAVASNEMN SEDDIQIFRK CHFPKDNCIV CQEELDDSKL YGMLGLIQQS
NIHRLAPMNN KDVLADILES SNSAHPWDTK DEASDKLPPF TSFPTDAHVP GLDISSCGHL
MHSECFDTYQ KSVENQLLRE LGRMLPLALS PKTRFLCPLC KALGNVLVPI VWKGKKESYP
GVMAPTSPYA DLTKTVQDVA IETKRCSESF PGTFDEEVPF VNNDPDLVIS DKEKLKYIYN
QMLKVMQVTL KHRHLDRPLH LPDSILSLHD MYAYTIADFE IAQRGTEGTR ARDLTIEHTG
TFIDDISSTS QTLLKILGMT SNLIQNLLNT PWQAEDRFTK EKLRLRAMNQ FMPNTTMNLV
KDLIDFDPLQ PLLMDDPFRA LVGLSFTLSE QPSIEAHHLL RSMYIADLTK TIIAVVHSIL
NGDKLLKDQK ISQLLDKLNT EQQQIVGVEG LQQFANYVLC LLKVPQSQID RFFQIISPSA
FMALVRTFTL PFLRKSLLFM VVYHGFIPQN PSDDVIEEKG EYDKLVDILN LPSLEAVFDM
QAFEQDLVNS WCQDYMRHPG ALTELHSSGT ISTVSPISLN LPTQYRMTTL PYRLDQLLDE
SSKRVCRKCK TVPEHSAICL ICGTFVCARR FCCTEDSKGE CNVHMKQCGG EIGIYLMIKD
CFLLLLHDNG GSIMNAPYLD IHGEADIFFK RGAPQYLNAK RYEQIRQMWL TQTIPAFVRR
RMESAYSATI WEAF
//