UniProt: A0A4Q4TIB2

Database: UniProt
Entry: A0A4Q4TIB2_9PEZI

LinkDB:  A0A4Q4TIB2_9PEZI 
Original site:  A0A4Q4TIB2_9PEZI

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (30)   
   InterPro (20)   
   Pfam (7)   
   PROSITE (2)   
   SMART (1)   
All databases (36)   

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ID   A0A4Q4TIB2_9PEZI        Unreviewed;      1404 AA.
AC   A0A4Q4TIB2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN   ORFNames=DL765_009650 {ECO:0000313|EMBL:RYP06002.1};
OS   Monosporascus sp. GIB2.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX   NCBI_TaxID=2211647 {ECO:0000313|EMBL:RYP06002.1, ECO:0000313|Proteomes:UP000291414};
RN   [1] {ECO:0000313|EMBL:RYP06002.1, ECO:0000313|Proteomes:UP000291414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIB2 {ECO:0000313|EMBL:RYP06002.1,
RC   ECO:0000313|Proteomes:UP000291414};
RA   Robinson A.J., Natvig D.O.;
RT   "Complete Genomes of Monosporascus.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC         = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC         L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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:RYP06002.1}.
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DR   EMBL; QJNV01000430; RYP06002.1; -; Genomic_DNA.
DR   STRING; 2211647.A0A4Q4TIB2; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000291414; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd03190; GST_C_Omega_like; 1.
DR   CDD; cd01491; Ube1_repeat1; 1.
DR   CDD; cd01490; Ube1_repeat2; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR   Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR   Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR   Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR   Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR   InterPro; IPR032420; E1_4HB.
DR   InterPro; IPR032418; E1_FCCH.
DR   InterPro; IPR042302; E1_FCCH_sf.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR047047; GST_Omega-like_C.
DR   InterPro; IPR016639; GST_Omega/GSH.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR018965; Ub-activating_enz_E1_C.
DR   InterPro; IPR042449; Ub-E1_IAD_1.
DR   InterPro; IPR038252; UBA_E1_C_sf.
DR   InterPro; IPR019572; UBA_E1_SCCH.
DR   InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR018075; UBQ-activ_enz_E1.
DR   InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   NCBIfam; TIGR01408; Ube1; 1.
DR   PANTHER; PTHR10953:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF16191; E1_4HB; 1.
DR   Pfam; PF16190; E1_FCCH; 1.
DR   Pfam; PF09358; E1_UFD; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   Pfam; PF00899; ThiF; 2.
DR   Pfam; PF10585; UBA_E1_SCCH; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SFLD; SFLDG01206; Xi.1; 1.
DR   SFLD; SFLDG01148; Xi_(cytGST); 1.
DR   SMART; SM00985; UBA_e1_C; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000519};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291414};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          1230..1372
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   ACT_SITE        607
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1404 AA;  157440 MW;  EE028C47D7730EF9 CRC64;
     MASGIPEVDL VTRVQVDESV VGTSEIDESL YSRQLYVLGH EAMKRMSASN VLIVGLKGLG
     VEIAKNIALA GVKSLTLYDP TPVAIADLSA QFFLHPQDVG KPRDAATAPR VAELNAYTPV
     HIHESSSLGN NFSQLDKYQV VVLTNTPLSL QQAIGDYCHS KGIYVVVADT FGLFGSVFCD
     FGKQFTCLDP TGENPVNGIV AGIDEEGLVS ALDETRHGLE DGDYVTFSEI EGMEGLNGAE
     PRKVTVKGPY TFSIGDVSGL GQYKRGGLYQ QVKMPKFIDF KGISDALRDP EFVMSDFAKF
     DRPQQLHVGF QTLHAYVQTH GRLPRPMNEE DAIVLVESAK TFVEKEKLDV ELDEKLIKEL
     SYQARGDLSP MAALFGGLAA QEVLKAVSGK FHPIKQWFYF DSLESLPTST ARTEELCKPL
     GSRYDGQIAV FGKEFQDKIS NMKQFLVGAG AIGCEMLKNW AMIGLGTGPK GKITITDMDS
     IEKSNLNRQF LFRAKDVGQM KSDCAAKAVV AMNPDLEGKI TCLKDRVSPE TEHIFNEEFW
     EDLDGVTNAL DNVEARTYVD RRCVFFHKPL LESGTLGTKG NTQVVLPNLT ESYSSSQDPP
     EQSFPMCTLR SFPNRIEHTI AWARELFETS FVKSPETVNL YLTQPNYLET TLKQGGNEKA
     TLETIRDYLV TDKPLSFEDC IIWARMLFEK QYNNAIQQLL YNFPKDSVSS SGTPFWSGPK
     RAPDPLKFDP KNPTHFGFIV AAANLHAFNY NINTKGVNKD LYLKVLDNMI VPDFSPDPGV
     KIQANDTDPD PNANNAAFDD NAELQKITES LPPANKLAGF KLTPVEFEKD DDTNHHIDFI
     TAASNLRAEN YKIEQADRHK TKFIAGKIIP AIATTTALVT GLVVLELYKI IDGKTDIEQY
     KNGFVNLALP FFGFSEPIAS PKVEYQGPNG KVTLDKIWDR FEVEDITLRE LIDDFKKRGL
     NISMLSSGVS LLYASFFPQA KLKERLPLKL SQLVESVSKK PIPEHQKEVI FEIVAEDEND
     EDVEVPYIKV RTQEPTIGRP LLIRYFRDQE TLRSNVPFGK TLFKEQAKMA SKITDWVKPG
     DKTGEFKRPD SAFRDWISPE PGARFPPEKG RYHLYVSYAC PWANRTLIAR KLKGLEDIIS
     FSVVHWHMGE KGWRFPTPED QDAPGENVVP DPLPGHEGYT HLRDVYFAVD PNYGGRFTVP
     VLFDRKLGTI VNNESSEILR MLGSAFDGLV PEEYARVKLY PEALRADIDE AAGWTYDRIN
     NGVYKSGFAT TQEAYERNVT ALFEALDRAE KHLAGSKGPY WFGDAITETD IRMYVTLVRF
     DPVYVQHFKC NIRDIRSGYP HLHKWLRNLY WNHPAFKETT NFVHIKRHYT KSHTQINPHS
     ITPLGPVPDI LPPDEEVPAV KAAM
//

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