ID G8BU25_TETPH Unreviewed; 2003 AA.
AC G8BU25;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=TPHA0E03130 {ECO:0000313|EMBL:CCE63403.1};
GN OrderedLocusNames=TPHA_0E03130 {ECO:0000313|EMBL:CCE63403.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE63403.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE63403.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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}.
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DR EMBL; HE612860; CCE63403.1; -; Genomic_DNA.
DR RefSeq; XP_003685837.1; XM_003685789.1.
DR STRING; 1071381.G8BU25; -.
DR GeneID; 11531507; -.
DR KEGG; tpf:TPHA_0E03130; -.
DR eggNOG; KOG1140; Eukaryota.
DR HOGENOM; CLU_238060_0_0_1; -.
DR OMA; VQLFTCP; -.
DR OrthoDB; 51389at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005666; Chromosome 5.
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; cd19672; UBR-box_UBR1_like; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF26; 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; SSF57850; RING/U-box; 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:UP000005666};
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 120..194
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 120..194
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 1843..1870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..1905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1971..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1973..2003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2003 AA; 233669 MW; FCB764C46FD23309 CRC64;
MSDWNLNELE SSNMTEYTTE LRTLLNTIHT VNEFVDVRGF RERMELETHL NYYIGRILNY
FLLDEGKNIN YLYNTETEHD QGPFKESIEK IRNEVENVSS YIVSPKTDNN DTSSKCHAGR
SCGRKFRNGE PIYRCQECGF DDTCVLCINC FEPKDHVNHH VYTGISNDNF NTGICDCGDN
EAWNVTLSCK ADNDLLENEK KDDSLNIFET EHNRKIFEAV LFEAIDYVID VFNHQVEVLY
PTHSEFTSFI RKTYHDITDE SLRISTIRRF IDDFSYRNKS FDIEENKGYT LIVYNDEFHN
YSQATTALRQ GKPDNPHIDI LTTRIDTEGR AVIKTSPTLT DDFIRSLFAI ETNGLTAFIF
QWQEYLHQES ANRIMWWISQ CLELENPSFQ KVFRQSLTKV LCTKFDKDST TNLANEFDFR
GIKIGLSKDH FRYSELSILN EENSIPQISH KILDFTSLND INDYHIPPNR CSSTIEVDPV
PYSGLRLQYI LYFDNRFWKA LRKNVQSIII PIVSSDADYK KLFSDEFLQI FSHMLRSVAY
NDREPHLTII KELIVQLLTV PTNVESLMNN KHMFEEIMWS IIDFFCKFAK VDNGQLVWQR
VQISNITKSY NFLFKQSLYF IEIVLGKVMD YRKLLEPNNF ITLLNFLKLF NGAWKINRKE
GEHVLHEDQY FIPYLEYTTY IYNIIENFDV ILRKNIESAR NDPMLHGAIK ILLNYLISAN
STNATFKKLD SFGNRSVIKF DVSKERTTYM NPVSTLFSIL VDKISIDDFV RLVSEVPEKD
KFIFSADVEM RTLVLCSQVE CGFWIRNGMS VLHQLSYYKN NQELDSYGRD LHVVQLGAIN
SCSNKEEGMT EELETFTYNM LDRWGLIECL NKPYNSEKTI YEDKLYPMIQ QFIVFCYHML
TTRIFFEEFQ DAEENRIEQL QTMIIYKLFS KPLSYSKLLK SIPNYLIENN NNQDFDISLE
KLSIFEEPKG LSDNGVYKLK KQNYSLIDPL NMFNMGNDFE SSVNIIKSKL AGKVRKPEEI
IIEPYFNEKV RDERIGRFLR TTIFVNLIEN LLEEVILSNN ATYLYELLHL LHAIFKDYRL
CNNYSNKIPP EYKSESIISS LIAVLKDSSN KQFSGNIIAK ANWVLESIIQ DNQKKFYEKL
SKLYGSEFSE NFRLKRSNED NARAEVESEI DKKRRLAKKR QKKLMARFDN QQAKFMEEHK
NSFEKPLHDS AQSYMNCSGD KGKEVTAIED STCVLCQDDV DNEVFIIPAY HDYSPIFRGS
SKVDLYDVKY EWDGFKNDSD NLTYYDDATI KNIINSSSSG SKKVFTSCNH AIHSNCFRRF
IQKKRLSVHG FICPLCQTYS NCIIPVVPSS NYKLNLSLKS IIDNSLTVNE FSELFSSGKF
DSVVDKSNPL STVLNFSIYH ANSFDIDIHK IIDGKKENVT LILSMHWANT ISMLEIASRT
DENPQISFLI TREQKYKTLK NILCFIMLIY KVYGQPDLNF KPYDFKGKNR IENQLFHYIV
YNFLYSKMPL RKIVTNALST YLRQLVKLSI DNIHELKNEK KLDILLDCKE VSPIHVSLKK
RIEKIVMDHI IIDYDDKVYC LIYKYLVRSI LPTLRRCLII VKVFHDTIKV SENDTFIVDD
KRLEDLLDVD DLCEYVNLMI DLLTDYESLE YLLDAECSTP SDILLKKIPI ESSKIIKMAN
LVNNLNTYIT NSKELRLREE HFISKYKLED RLDFKICLTC GSKVHMRSDH HEMSHHLQRE
CFKSYGAFLV PNNNEVCLFL ANPPSVVYIS APYLNSHGES GKNAMKRGDL TTLSTRRFEY
LNTLWVNNEI PGYISRAMGD DFRLNILSNG FLFAMNRIPP QFRRRDDGDS DSSGEEDLNF
SDEEEGGLRV EDMTRVEFEE AFEFFNPTEN DGLNDDDVET GNRERRRVRT LPFAILQEQI
RRLDGMGGNG TQVFNLADLL DGARNPVTET ATPPTNAQLG TPVENIIDSI NLTDENETRE
ENNTNPNEEN SDREWEDDDM THW
//
