ID K9FUK7_PEND2 Unreviewed; 2140 AA.
AC K9FUK7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=PDIG_39170 {ECO:0000313|EMBL:EKV13305.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV13305.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV13305.1}.
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DR EMBL; AKCT01000164; EKV13305.1; -; Genomic_DNA.
DR STRING; 1170229.K9FUK7; -.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_000684_1_0_1; -.
DR InParanoid; K9FUK7; -.
DR OMA; GEASYMC; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR013083; Znf_RING/FYVE/PHD.
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; 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 Ligase {ECO:0000313|EMBL:EKV13305.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882};
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 84..156
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 84..156
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 407..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2140 AA; 241273 MW; A520D18F5F3041FB CRC64;
MFTLGDCEKL LGDGLLRLPK KHNFRYGPAA EKELLELLFR SLVGHNTDLV QQLFPEGTPA
GPWKLAEAQG AREGAEYSEA ARGKRCGHIF RAGEATYRCV TCAADDTCVL CSRCFDSSDH
TGHQYQISLS SGNCGCCDCG DDEAWRLPLF CAIHTDSGNT KGKERAQRVL PSELVASIRL
TISRVLDYFC DVISCSPEQL RLPKTVESIR QDEEASRLRP DWYGAGDEEE EEPEFVVMLW
NDEKHTIRDV SHQVTRACRE RDSFGIARAQ ETNDMGRSAI KYSKDLNRLL GVSKIIEEIK
VTVTVRSSRD TFREQMCTTI VEWLADIAGC EILEDNEIFR QIICEEMLTS WKKGSAGYNE
DIGMKGIDDH QQTEILPGRT LLINLPNHGQ VILTTDDDED DMLEDDVIDE DEDEDYVEAH
DADDEDDDEM DIELSRDQED DEDMILAGAD EELALAERIF AGLTGTQPPP PRPAPAQTAA
RSSVERGPSE PQSPGPESGP AGYIPIPKTP GSYRQRPSNT DSHWQVRPPI PGPGEKVPLY
EDLWQRTRLD WLVLYDLRLW KKTRTDLRDL YISTVVNVPQ FKRIMALRLS ALYTALAQLY
LIADREPDHS IVNLSLQLLT TPSITEEIVV RGNFLTKVMS ILYTFLTTRQ VGDPQSVDPN
ATLAFDAGSV TNRRLYHFFL DLRYLLQSEY VQHRVRTEEQ YLPQFLDLVK LSQGICPNVR
AVGEHVEYET DAWISASILM REINRLCRQF CESFRDPETD NGDNLLRAIE TTTTTAILNS
AGIERKRFDQ AEIKDEVRFK LLPPFDFEVG ASGQVPCHRV VEFVVERGSI SFHHALHYTL
SWLVECGRDI DSATMRDVLF DAANAARRKI HAAKTTNPSS VDDVLLTLGP EDLVLAMFDY
PLRVCAWLAQ MKAGMWVRNG LSLRHQMSQY RGVSSRDFAY YRDIFLLQTA LVTCDPSRVL
ASIAHRFGMV EWMARNYMPR SGYEDAQIVD VAEEFVHLLV ILLTDRTSLT AIDDSTHLTH
ENIKRDIAHV LCFKPLSFSD LSTRLSDKLL DSDMFQDVLE DVANFRPPEG LSDSGTFELK
PEHLDLIDPY SAHYTKNQRD EAENICKEWM AKNTGKNASD IVFEPKLRPI SSGVFSDLPR
FAGTMLFAQI VHQCLEYVIS SKECTPTIPP TRVETFLQVI LHLILAAVLE DDSEETDMAE
DHSNSFNWNA LSKTREIKAG QLTIVGLLER ISVTTEFTAS GPKIRHILKR LWQKRPRTYS
SATASLKFPF DRIDTNSPAI DADNDKEAKK KQALERQAKV MAQFQQQQQQ FLNTQGNIDW
GEEDFSDLES DTDTTPEKKL WKYPSGTCIL CQEETSDSRL YGTFALVQDS IIMRQTDIRD
SDRIREVLRT PTSLDRSAEE VRPFGVSGDN RTTIKRLDSS GGEVISEKIG LSKGFNAKST
LRGPVTTGCG HIMHYSCFEQ YFTATQRRHT QQIARHHPEN TNLKEFVCPL CKALGNSFLP
ITWKGKEESP LFPLSPSESF DQWIQVGLKH ALHQQQNFPV LMEKEKAYPQ PYTDIFVDYL
SKSLVSPLSN NIDQLRVSSF PATSPAHYIT PARMPMPGVF PPTEDLSPSS PIQHVSSHSE
SPISELLQSY RRLTKTFKAN HVYSMFNNIS EANGNEDLVQ TDSLIRSFGF SITAVEIAQR
GVESEPGSTL LDTIPSLTLT HLRVLSETAL TYAAVGCLHS TGPSKGRSTS EFQEMHRQKV
CQLLVGHPCL SGTALLNDVR NIEPLLAVDT FVFLAESSLS LLPVLNIDIR HLVRMCFVAE
IVKVAVTFIL WPLGLKEELA THPEDHNMAA DLSEEQFGVT KQFFDSIVAE LKANSVGRAE
GSSFPAESGY VKDGEETATP SIITAVRRLF TSYGLAFLRK AVILLHVQHG VEFPNTGFAD
VESSELERLT KALQLPSIDE ILMSVKPARN TNSPFDAVIS GWIFHWNASR SGIRFEDHRL
WPSLSHPTIF ELVGLPKYFD SLIEEANRRR CPNSKKELTD PSICLFCGEI FCSQAVCCMS
NKLGGCNQHL KKCGKNVGLF INIRKCTVLY LHNTNGSWHY APYLDRHGEV DPGLRRNRQL
ILNQKRYDRL LRDVWLSHSI PATISRKLEA EINSGGWETI
//
