ID A0A0F8DGI3_CERFI Unreviewed; 1868 AA.
AC A0A0F8DGI3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=ubr1 {ECO:0000313|EMBL:KKF95049.1};
GN ORFNames=CFO_g2630 {ECO:0000313|EMBL:KKF95049.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF95049.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF95049.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF95049.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-2015) 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|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family.
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:KKF95049.1}.
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DR EMBL; LBBL01000124; KKF95049.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000034841; 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 Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW Transferase {ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 167..221
FT /note="Adaptor protein ClpS core"
FT /evidence="ECO:0000259|Pfam:PF02617"
FT DOMAIN 1446..1868
FT /note="E3 ubiquitin-protein ligase UBR-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18995"
SQ SEQUENCE 1868 AA; 210163 MW; F2B96B4D147546C1 CRC64;
MASSDPPSFA ALSTQERQLC EYFRDLPKKS KYKYTQESAL ELCKMLFWSL AGKDEHLPLL
FPKGMPADMK LRGAQGAEEG AEYSEAARGK RCGHILKSDK GKGVDAFPND LKTSMRMTIG
RVLDYICDVI SCSPEQLRMA KTKESILTDE TQATLFSNYY GDERPEDERQ YCLVIWNDEK
HTLRDVQEQI ARACKKRQIE AHAHARETDS IGRSILATSS DIDALLRMAK KLEEIRVTVT
IRAARDTFRE QMCATMVEWL LDISGCSVGK DHHILLNTVC EEFLKPWREG SSASYKLAGL
SGIDDEADIE DQIERSQHLS HSLLHAFQQR FAGATAPTLD DEDLDSDGLE IIELAVDDHD
NALTDDEDDE DDIMQEIDED EDDDAVDWVS NVQTVADTED VVAAGFPPPP PVPPIDPHNN
IAAGSSTEAT EAGASNAPLP ATVAQIPTIV ASSVSLTSDS VPPARVRPRD LTPSEADIVE
PLIAPNAYPK AEIIPKTPNR KKSEKPKPGR YWTEYPEMYR NRSTEESRAD DVFQRVRLDH
LILFDLRMWK KVRNDLRALY ISTMVTIPNG SVTNRRMYHF YMDLKHLFSS LHVQHCLRTE
PRYLMQFLDL VKLHQGIGPN TRAVGEHVEY ETDSWITASL VTREINRMAR QFSEAFRNLA
PEDMGSLKNA IRTTAKTLIL HCVGAERFRF KNAEIKREVR FKGVGKYEFD IAMEETSVVD
FVVEQEPISF HHALHYTLSW LIECGRSMSN EELRNLLSFT TEDLMLQPRS MGHKTMTHSN
LTPEDYLINT FDFPLRVCAW LSQIKTNMWV RNGISLRHQA ATYRGVSMRD VCYQRDLFML
QTAAVTCNPS RVLASIVDRF GQEKWLAGLF HQNCESQDDN QHLDVVEDMI HLLISILSDR
SALIPIEEEP DPILVSMRQH PNFHSVLEEL STFEFREGIS DVGTFKLRPE LAEEIDIFNS
HFTRNQREES EAVYRKAMAQ RTGKKLEEIV YEPKLRPIHS GAFKDLAALT STGMFAQIVF
FCLLYPLNIA TAKSTVQPSR VEVYLNSVLH LMLIAIAEDK IDETNCDNEE CTSFIEIALT
QESITIATDE KNTIRAATIV GLLRLLLLKS EYSGCHGKIE LILSKIALQR PSLNKEAHDK
LGIAIDSTPE AAEDTALSAE EERERKKKAA ISRQARVMAQ FQKQQQEFMG KQGEIDWGSD
IGDSMDEDEA DAKADGTHQV TWKFPSGTCL QCQEKTDERK TFGTFAMFNE SRIVRLTDIQ
IPAVVREVRN TPESLDQQMP RDRPFESLKR FEFVCPLCKA LANTFVPIVW KPKEEVYPGV
LQPETKMSAF LNKQMLNPLY TNSQPELKVS TIFSNYASTS LIGPLAGSAA EARSGSSQWQ
PVSITAVSGI PGVIGLDLAA QIPQPSSIRE SSFPSTNNPM TDLVRIYSRM SNSLRTQDFL
PCDMGSDSRQ LCFNDTLVRS VAFSIASVEI QQRGVGVVAE PNTAASFVSP GIFVDRIPEI
SMTYLKILSD TARTYILVGE LRSGTDNFIE AQFQRDACTQ LKQLFICDYS DLEDVNNIPP
VLAIDGFVLL TDFAYCMSEV HQFEIAHLVR LCYLAEVVRV VHRISNNIPA PSWSQRLFAL
PENTPSNIRT FAQFCQRLME MTFDAKAPIE TTSEPESSLE NLGFEQAGLS DLAGIYEFVK
KYALVFLRKT AILMHARFGV SFSAYTPSNP TDDELTRLTE ALCLPSFDDI IASILPNATS
LGWPDGLDHL VFGWIRHDLM YPTKSDTKSH KVTTNKLGVV EKSRAFVPMG LAHPAIFELI
GLPKTFDTLI EEATRHKCPT TGKDIQDATI CLLCGEIFCG QSTCCLQEAN FELEGKISVG
GTQQHMWK
//
