ID A0A1V8SB30_9PEZI Unreviewed; 2474 AA.
AC A0A1V8SB30;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=B0A48_17861 {ECO:0000313|EMBL:OQN96061.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN96061.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQN96061.1}.
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DR EMBL; NAJO01000073; OQN96061.1; -; Genomic_DNA.
DR STRING; 1507870.A0A1V8SB30; -.
DR InParanoid; A0A1V8SB30; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000192596; Unassembled WGS sequence.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
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; cd19672; UBR-box_UBR1_like; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
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; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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:UP000192596};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2474
FT /note="E3 ubiquitin-protein ligase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013206835"
FT DOMAIN 393..465
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 393..465
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 465..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..742
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..809
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2474 AA; 275747 MW; 3344D83615A23EFA CRC64;
MFPIRFLFFA LAAALVSASP ESAKCARVYP TAIPSPYPTS PHANEFSYRG YNESTNGDIN
ERQAIHDAFA DLPPMLAAAI ASLRDLNDDT YNRYFPMFLG EANSSLYDTP LYGRSYVEGV
FGMLIDADSE PLALKPLTAK FKNEQDVGCC CGNGAAACFL LGANSFNVCP ALFEETARAS
AVNCTELGDQ TSWHMDSITS TLLHEFMLSD EVGGKAPSSA GRIIDVAYHP DNCARLAAGP
EGQKAFINAD SYSDFASSVV AHLIFQRVRM RTLPFADGVG VDKRRDDLNF ILPLASHGNN
HNFDMVSAPH SSEARLASVL LSLPAGYLNR YTPTTDAVLR QHLFHSLAAY NSAYLPLFFP
SGPPPPSSSE PWSLRDAQGA QDGAEYMPSA RGAACGHIFK SGESTYSCKT CAADETCVLC
SRCFEGSEHE GHMVYVSVSP GNSGCCDCGD AEAWKREVRC SIHSAASEQG HGKEREHVGQ
GTGNEVPEEV RRAVRMTIAR CLDFMCDVFS CAPEQLRLQK TEESVREDER RARLSPAMYG
GSDVTLGEPE FSVLLWNDEK HTVRDVQYQV AKACRTTKTI GMQRAYEVND TGRAVVHSST
DVADLVHMAK VLEQIKITVT VRSARDTFRE QMCETIVDWL GDIAGCSVGS DGQLLRNIIC
EEFLQPWRMG SEASNMDIGQ QGIDDHEIDE TRKLKSQYRN FLHGMPAGTG VTRFQVEQDE
DEDGEDYEDD DEEDEDEDDD MDIDTMEAEI DDIRRAADAA IEADEAALQA GTAGMDIDLS
GDDEVTGARE ATMAGYPPPP PPPPGPDTAT PRGQRRGAFR LIMTPTESEE GDLEATSVEV
EPAESVKAPY GKMPKTPAQT RKSKPKRPQP TSRHWLVTPD AFQGPRPAEP SEDLWQRVRL
DWLILYDLRL WKTLRVKLRH MYITNVATIP HFKRILGLRF AGLYTPLAEL YLVADREPDH
SVINLSVQML TTPSITEEVV ERGNFLTNLM AILYTFLTTR QVGYPMDVGP RAVLAFDAGS
VTNRRMFHFF VDMRWLFQSE FIQSKMRAEP QYLLQILDLV KLHQGLCPNV RAMGEHVEYE
SDAWISASLI IKEVDRLCKA VASSFKASTF EAASQLQRAI RTVGQMTMIN SFGYERKRFT
AHEMRDDMAW HDTGPYDESG QVYSVPKFVV QAEYMSFHHP LHYLLSWLLE HAKSMDRDEV
RNLLHFTSSD LKDPWTHART APAPTTLTSD ELLCSIFDHP LRVCAWLAQM KAGMWVRNGI
TLRHQAHTYR SVSHRDIGYQ RDLFMIQAGL ALCGSEHEKP GERFLAQIID RYQMGKWIKG
DYSAIEGIEE TQQIDVLEDM YHLLIIALSE RGNLLGNATD EVSDEIIQHD VAHALCFKPL
SYSDLNTRVT EKIADSEPFQ RVLECMTTYR APEGLSDTGT FELRAEYAEL VDPYFAHYSR
NHREEAEMLA RKVVAKKSGK SVEDVVFEPR LLDLSGTLFE ALPAVTRTPL FATTIAAALQ
YALTPRPEAT KVPATRVETF LHMVLHLVVI AVLEDERIEE EGFVELAVSK EHKVAPGQWR
TIVSLLVGLS EMAEYGSCMP SIKHILRKMQ VRRPEKLMAA IGPAAASFAL LDRNDTGSPA
SFSAEDKEKR KQEAAARQAR VMAKMKEQQN SFLQNQGLSG FDSDEFEDIE DDMSLTSETP
NLEEKRKTRS FPTGTCILCQ EETDDQRLYG TFAFMGESNI LRSTPTNDPD FVQEVLDLPS
SLDRSAEHLR PYGVAGKNKQ LVQKTSSSGE TQTFERQGLS KGFPHAQHST KGPVSTTCGH
MMHFSCFENF IAATQKRQAQ QIARSHPETI ALKEFICPLC KALGNTFLPI VWTERECAAE
HELHAAPAFG DWLATDVSKH GPDLVLLEDI AHDTPEYHQY AAGSMQRAAA YIRASFSPSL
ATCLSVTGPA QTGQASVRPD TRSSFRRSLS LGSLFRTNSR NSAPPMDQDA PIAAGDGARQ
VELSKAYLRL LETISANGLG GIEELPAGSA SPVLALSRAL GYSISAVEIQ HRGTNSDALA
TSLLKDLSEQ TVMHLRILSE TTESYAAFHT VWRSTKGTEA MAHRQTIMEA QLFGDEPQPG
MSWARATAKI PALFEEDNFL FLADWLAIVD PSVAEATSML QLLYWAEVVK VVTMYQQVVL
QPDFPNSQNG VQPSDAFARA VYAISVTGAS ASPLRLPYHT VQLQQLRILV EKYTLAFLRK
SIILMHVRYG LDFDCPYNID PMTSELDRLT RLLHIPTLED AFTLYTSDTT SSTVLQRLTH
RWISEADRIR PTTSHPFPIK LLHPSIFELV GLPKNYDVLT ELAIRRKCPT TGKEISDPAV
CLFCAEIFCS QATCCESPLP PSSTAQTTDF LPSQSRGGCW QHMQKCGGRL GIFINIRKCM
VLFLHEPMHG SFAHAPYLDR HGEPDPTLRR HHQLFLNQRR YERLMRDVWL GHGVQSFISR
RLEADINPGG WETL
//
