ID A0A074XAK2_9PEZI Unreviewed; 2103 AA.
AC A0A074XAK2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 28-JAN-2026, entry version 37.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=M436DRAFT_50119 {ECO:0000313|EMBL:KEQ71621.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ71621.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ71621.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ71621.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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 E3 ubiquitin-protein ligase UBR1-like
CC family. {ECO:0000256|ARBA:ARBA00046341, ECO:0000256|RuleBase:RU366018}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL584713; KEQ71621.1; -; Genomic_DNA.
DR RefSeq; XP_013425790.1; XM_013570336.1.
DR STRING; 1043004.A0A074XAK2; -.
DR GeneID; 25411194; -.
DR HOGENOM; CLU_000684_1_0_1; -.
DR OrthoDB; 26387at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000027730; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
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 FunFam; 2.10.110.30:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform 1; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR055194; UBR1-like_WH.
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; PF22960; WHD_UBR1; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, 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 403..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..423
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2103 AA; 238361 MW; FB5D07E9E8EE278C CRC64;
MAISDLERSL GVFLRDLPRE FNNRYTAEAD SVLRARLFRA LVADDESRLT LLFPDGVPEE
DQWVLRDAQG AVDGAEYTPA AKGHPCGHIF KAGESTYHCK TCAADDTCVL CARCFAESDH
EGHMVYISVS PGNSGCCDCA DDEAWVRPVH CTIHSADDAP GQKAAGKTSQ TPTLPDELLI
PVRTTIAKAF DYMCDVFSCS PEQLRLTKTE GTVRRDELLS RLTSHLYGGA EVDESDEEYA
LVLWNDEKHT VTDVQNQVAK ACRKPKSFGL QKAMEVNDIG RSIIHYSHDL AELLRMAAII
EQLKVTVTVR SARDTFREQM CSSMVDWISD ISGCSIASDP HVLRNTICEE LLRPWRMGSE
ATNATIGEGG IDDHEHEENV KNRREEARWF RPLAGINVVR INVENDDDDN EEIDDDEDED
DENDMTIEEF LMAESEELGV EDTMDLDPET VDPLALALAE NDMDLDLVDI DTEGPAENFE
ATLAGYPAPP PPPPTTRRRT RSATVNESDD GEQHPSSRPD PPSQPSAPFS NLPKTPKVRV
RSNRPVRPAR YWLETPEEYR SQSTSTPAED LWQRVRLDYL ILYDLRMWKT LRIDLRHLYI
STVVTVPQFK RILGLRFAGL YTMLAQLYLI ADREPDHSII NLSVQMLTTP SITAEVVERG
NFLTNLLAIL YTFLTTRQVG FPKDVNPNAT LAFDAGAVTN RRMFHFFLDT RYMFQSAFVQ
EKVRNEPRYL MQFLDLVKLH QGICPNVRAV GEHVEYEADA WISATLIIKE INRLCRQVAE
AFKRSDDGDT APVQRAIRYA AQATFINAFG LERNRYPSAE TKEAQTFLRL LNKKRPKYIE
AIGREATCRD GSYSLPQFDV ATGSMSFHHP MHYLLSWLLE AGVNVTREEM LKVLHFTHAD
FKDPWQTSWK TAPQATNYDS PEIIAMLFEH PLRVCAWLAQ MRAGMWVRNG VTLRHQMHQY
RGTSQRDVSY QRDIFMLQAG LVLCGNPEES LGERFLAQIA DRFDLSGFVN GVFDLYPGYD
EQQRLDVTEE FFHLLIILLS ERQNLLPGQD KPSQHVKLLQ RDIAHVLCFK PLSFSDISNR
LTDRVADSEE FDAILESMTT FRAPEGLNDS GTFELHPRFI ELIDPYYAYY NRNQREEAET
VYREYTAKKT KQSAADIVFE PQLQAINSGL FKNLGAFTQT TFFSEIVYWA LEFCLRHDEA
VDNAQITRIE TMLHVILHLT LLAVMEDAAP TVSHSEESSD KTIVESLFRL SKVKSFASCT
PKVLHILKRM SEKWPEEFAN AKARLLPDDK EQSSETTSTP SEDKEAKKKA ALERQARVMA
QFKAQQTSFM ENQGLDWEAE DYSDLEQDGE LIEKVVETKV CPFPKEPCIL CQEDTDDNRI
YGTFAFIAPS RILRKTPLDD KDFVKEVLDT PENLDQSADA IRPFGVAKFA TETVEKVNTD
GTKGKQEKRG LGKGFPHDSA FQGPVLNSCG HIMHFGCFEQ YLVATRRRHT QHISRNHPER
PDTVEFICPL CKAIGNTFLP IIWKDKHYHS SSTLDQQYKN FDQWLLDQEA YRNADEMSQL
SSNVSVREAH IEYMQKALVP TLATAFPPSL FAQAVEAPSR FDTRNRPATP SSELKRAYNR
IEESLSPIGA LKSNTIGLEP GTQSSTIRLA ETLCNVLAFT VSSTEISYRG VANPLDGETG
TFLDAISEQS MKTLRILSET VRTATATAAV KGGMSEYLGR TRVHSSWTAQ LKKVLGDDPG
EDPALPYASL LGHDLFTFFA NCAVHEVPMG QNMHHILRLC YSAEMVKVIV TFMCRDSLQE
IQQDSRSSSW DLSGIKLFQN WCKEHGAIEF SPHISSVRLC QHGFCDLEWN APALSKLIDT
YALTFLRKAL LLTHVHFGVD FTGSDENLEL SELQRLAKIL RLPAPQEIVV RLGHDEQFQM
TAAKWVNSVI VSTATKERLR TDAQFLSHPT IFELIGLPKH YDTLTEEAIK RRCPTTGKEV
TDPAICLFCG EIFCSQASCC MTDRNKGGCF QHREKCSGSI GIFINIRKCM VLFLHHSHGS
WYHAPYLDRH GEVDPTLRRH HQLFLNQKRY DKLLREAWLN HGIPSVISRR LEGDMNTGGW
ETL
//
