ID A0A1B8GIQ4_9PEZI Unreviewed; 2229 AA.
AC A0A1B8GIQ4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 2.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=VE01_06453 {ECO:0000313|EMBL:OBT95733.2};
OS Pseudogymnoascus verrucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT95733.2, ECO:0000313|Proteomes:UP000091956};
RN [1] {ECO:0000313|EMBL:OBT95733.2, ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT95733.2,
RC ECO:0000313|Proteomes:UP000091956};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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}.
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DR EMBL; KV460233; OBT95733.2; -; Genomic_DNA.
DR STRING; 342668.A0A1B8GIQ4; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000091956; 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:UP000091956};
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 119..191
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 119..191
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 441..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..526
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2229 AA; 252078 MW; 625C7B947D3DD943 CRC64;
MLVATTRKQN ITTPQRNEAA AAHKAHGIAS MAAIGMSTQE RQLCEFFRDL PRVKKNRYDE
SASNDLLYNL FWSLAGGQDK YMRLFFPEGR QPAPNEKWEL RGAQGAVDGA EYTEAARGKA
CGHIFKSGEA TYRCKTCSAD DTCVLCSRCY DSSDHTGHMV YISISPGNSG CCDCGDPEAW
KRNVHCTIHS ESEHEAKRSG KSKEASGLPD ELIESIRMTI GRAFDYVCDV ISCSPEHLRL
PKTVDSIKLD ERMSRLTSPY YRGDIVEEPI EYALILWNDE KHTVEEVSLQ VSRACKVRVA
EGLQRAYETD DMGRAIVKYS FDINELLAVA EVIEHIKVTV SIRSARDTFR EQMCGTIIQW
LGDISGCSVG GDHNILRHVV CEEMLKSWRT GSEAVNAEIG KSGIDDLEIE DQAKEKETRM
MLLGPRNIQI IRLEAAMAEA ERAGVESSED EDEDGDGGEL SEGEDVDEEE LQTIMDVMLV
EAQAGGDQDG DVEMTDDASA QEADEATMAG YPPPPPPPPP PPPGLDTQRV LMDRETTPSD
SDMAEPLITS SIYAKANMDI PKTPGTKHAR PEKVGRPPRY WLETPEAFND RESIPLHEDL
WQRVRLDWMI LFDLRMWKKV RVDLRDLYIS TVVTIPEFKR VLGLRFAGLY TLLAQLYLIA
DREPDYSIIN ISLQMLTTPS ITSEIVERGN FLTHLMSILF TFLTARQVAP PIEINPNAVL
KFETGSVTNR RMYHFFMDLR YLFNAPHVHE RLRTDERYMM QFLDLVKLHQ GICPNVRAVG
DHLEYETDAW ISASLVTREI NRLCRQFSES FKWKLGEDMS AISRAIRFSA NTVIINSLGL
ERRRFEGSEI KEEVKFKTVA DYEFDTSETG EHSVIKFVVE DQPISFHHAL HYTLSWLIEC
GKSMSRDELS NLLTFTQDGL MQKPKLMGQR LMPSNEYNSE DLLMAAFDYP LRVCAWLAQM
KASMWVRNGM SLRHQAGTYR GVTQRDVTHH RDLFLLQTAM VICSPSRVLA SMIDRYGLEM
WMKGIYEQNS DVLDHQQQLD VAEDMIHLLI VLLCDRTSLV PIETEPNPHT VALRRDIVHV
LCFKPLSFSE ICSKLPDKFQ EQEECQDLLD EMTIFKAPEG LSDVGTFELQ EQFLKEIDPY
IAHYNKNQRE ESETAYRNWV SKKTGRPAAD VVFESKLRPI ESGIFTDLAA FTKTGIFAQI
IYYSLLYPLK SQELTPTVPA TRVEAFLHVV LHLVLVSIAE DNTEEDDMSE EALQSFVYIA
LTRNARSNFM NDAPHAKTIV SILEIMSTRE AFKSCHPKIS LVLKRMRQKR PRGFESAFAK
LGASVDRVST ASPAIANPDE ERDKKKKAAL ERQAKVMAQF QQQQKNFLSN QGDADWAQED
LSDEDMDVQA EERKNNWQYP SGNCILCQED TNDNKPYGTF AMMEESGILR QTDFSDQDFV
KEVASVPANL DRSAEAIRPF GVSGQNRHVV HKIATNGQEV LSERQTIGKG FPSKSMKLGP
VSVGCGHIMH YKCFELYYEA SSRRQSHQIA RHHPERLDLN EFVCPLCKAQ GNAFLPIIWR
GKEESYPGLV NTSAPYDEWL DSLLPSAVKR QEKSAAPLGD GEFPGSRYRD MFLNYIQENV
VQSLSSKMPN LDEAWEAVPS SPISLPDNAL NILQANRAPM RRLPGAFPPD AALELPNVTP
PQTSTADHGL IELVSIFRRL SDTIVRNKLI SREIPEPRPE GADAFYAGDT VAQALGFSIS
AVEILQRGVD SESGSTFIEK VPQQSLTHLR ILSETAASYV AIGGLKNDGN NPTAAAFTNA
YDRQLEQLFC GYPQALRSHS EERDHYPLFN CDIFNFLTET SLCLAPVLDL DIMHILRLCY
VAEIVKVVLA MARNTPAAKW LSWAGLLNDQ EAQEDNSFQR ACSYITKLDM RHRVMLGLGN
AQPFEESDDK LEGFDQECFS GIDDCKEFVK KYALVFLRKA SLLLYIRYGT DFNSFFPHNS
DDELGRLSEA LRLPSFDEIC DLIGQKSTAK IDDIIDNDDN LSYDDISTTQ HIIWGWIHAH
FAWQTKNTPE EGKSDQKAKD ISVSHPTIFE LIGLPKNYDT LMEETMKGRC PTTGKDLTDP
MLCLFCGTIF CGQAMCCLKE EPKTRGKPSA KIGGAQQHMR KCQIHIGLFI NIRKCTVFYL
HHNSGSWMVA PYIDKFGEVD PGLRHGRQLH LHQKRYDALL RNTWLQHGIP SVISRKLEQD
INNGGWETI
//
