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Database: UniProt
Entry: A0A1C7NB94_9FUNG
LinkDB: A0A1C7NB94_9FUNG
Original site: A0A1C7NB94_9FUNG 
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
//
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