ID S8BQI9_DACHA Unreviewed; 2155 AA.
AC S8BQI9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=H072_8783 {ECO:0000313|EMBL:EPS37512.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS37512.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS37512.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS37512.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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|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:EPS37512.1}.
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DR EMBL; AQGS01000635; EPS37512.1; -; Genomic_DNA.
DR RefSeq; XP_011114468.1; XM_011116166.1.
DR STRING; 1284197.S8BQI9; -.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_000684_1_0_1; -.
DR OMA; CCAREER; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000015100; 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 InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
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 PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
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 98..170
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 98..170
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 413..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2036..2075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 786..813
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1290..1320
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 425..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2046..2069
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2155 AA; 242336 MW; 1DD2DF40C1BEC983 CRC64;
MLTDVSSNAP TFASSDPVIS LTRVLRDLPL VHEYRYTDEA RLRLLEELFA SLAGNNREYI
KLFFPNGVPP KTGKDAWNLS KAQGAVEGAE YGPAARGKPC GHIFKNGEAT YRCKTCSLDE
TSVLCAKCFE SSDHRDHSVF VSISPGNSGC CDCGDREAWR RDVKCAIHTA YEHQQSAKTA
SQQTQPLPES LRKSIRDTIA RALDYLCDII ACSPEQLREA KSEDKVREDE AKSRLQATYY
EVAETEMAAP EFSLILWNDE KHTVREVQDQ LGRACRKPKD WCLKRAEETD LIGRSVVDFS
TDIQNLLDKS KIIERIKLTM TLRSSRDTFR EQMCGTIIEW LVDIAGCAVG DDPDVLRRTV
CEELLGVWRQ GSKAWNIEIG MKGIDDHEYA ESQQTLEYAQ SVMQSPEIRL LRAQQEQEER
AQREANGEEE EEEEEAEETE ETQEEDRGSD SMEVDGGEGS AAAAATPAAS ADADGDVNMS
TGETPSAADP TAQAEPTVPF PPPFAPSIPH TPGKHHKRRE AHGKPGVHWL ETTHIPHKTT
PYYEDLRQRV RLDWLIMFDL RMWKKARIDL RELYISTVVA IPQFKRILGL RFAGLYTILS
QLYLIADREP DHSIINLSLQ MLTTPSITAE VVSRGNFLTS LMAILYTFLT TRQVGHPADV
NPNATLAFDT GSLTNRRMYH FFQDMKYLFG SESVKELLRT RVAPTLQFLD LVKLHQGICY
NNRAIGSHIE YESDAWICAS LITREINKLC RQYADAFRRT RAGEDIHLAN AIRLVAKITT
RHAAGMERQR FKNAEIREEV EFVQQEVREG EEDKLIGLPG FDMEGDANGV VPSYRIVKYK
VETEAISFHH AMHYLLSWLI EAGNGMDNAQ LRSLLRFKTE ELGVPESWKR ELDAEDYLSI
LFDYPLRVCV WLSQMKAGMW VRNGFSLRHQ MNTYKGVSQR DLTYNRDIFM LQVASVVIEP
SKWLLTMINR FTLDLWFRGD FRPPTNIEAT QHLDLVEDLY LLLISLLSDR LLLISHDEER
DIPTLQLRRE ITHVLCSKAS SFSDISQRIP DRLMDLENFQ DVLAEMATYK APDGLSDSGI
YELKGEWKEY IDPYILQNSK NQREEAEAIF KKHMATKLNI PEKNVVYEPK LKPIRAGAFM
GLANITRTKV FNQMIYFGLL YGAMHKSINP SIPDTRIDSY MHALLYLMQV AVAEDTSPID
ATEDSYVYYA LTLNAKVSDG LPSEMSEVDT VVMKKETVEK APTVALLLYK IKLEALHESC
TPIIDNLLQH MQEKKPAAFA PLLEIGKGMR EKESEEAAKV QKEEEEFARK KELAKQRQAN
IMAQFQAQQQ SFMQNNFGGF DMDDDDLDDE FMDEDAPGVA IRPTWEFPTG DCIMCSEQLD
DSKAFGTFAM IQETNVLRQT DLKDSDYVYE VLVTPENLDR SAEGLRPFGV AGMNRDSVKK
LAEDGSEITV TRQGLGKGYP RAPEFTRSGP VAVGCGHLMH YDCFESHIAA VQRRHQHQIS
RAHPERLEMK EFLCPLCKAL GNTFLPIVWK PKFEETVAEA VHTKSDFSTW LSQDIGPAVL
RLEKEKAADN NDEGPLGKYK EQFLGYGTSN FIEGIATKLV PVEEEPPAPE VTTPTPEPAT
TATDGTAPAP TPVVVIPVGG AITIEQQLAM LPQQGAPVPP PVATIPPPAP ASRNSDRPSV
DVESIFSIYK RMRDTLQLNK IKTNRPPSTE LANPTNDLHS VDALMRILGF TISTTETWLR
GAEPRQGSNL IERTPEHNLR YLRVLAESVY SYIVFGGLKE ESSTASHYKE IHQDQMVKLF
VGHPKIYGDN NIYQKHSPLF ADDIFVFLAE CSLCLCPALN VDFKHIMTLC YLAEIVKAIV
VISKNSEALD LNAARDDGER FSAIVSQLSY SEQDINNFKG FVEFVAQASA DPDMQGGHSS
PSPILFRHLI SKYINPFLRK CVYLLHARYM VTFSNDNSTN FEPEHVRLTK LLGLPSLETV
FTAHAAKNDD GAEIIRAMVT GWCKHLRFAV EESKREEAEA ATPKPTPTEP IIDAATASTT
TESSSDAQPP PPPPPAADPV APPPPVQPVT EASNKDKLDL ETLVRLSHPS ILELVGLPLH
YDTLVEEAMK RRCPRSGREL SDPVVCLLCG DIFCSQSLCC MDANRHGGAN QHLKM
//
