UniProt: L2FIH5

Database: UniProt
Entry: L2FIH5_COLFN

LinkDB:  L2FIH5_COLFN 
Original site:  L2FIH5_COLFN

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (31)   
   InterPro (21)   
   Pfam (7)   
   PROSITE (2)   
   SMART (1)   
All databases (38)   

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ID   L2FIH5_COLFN            Unreviewed;      1367 AA.
AC   L2FIH5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN   ORFNames=CGGC5_12947 {ECO:0000313|EMBL:ELA25965.1};
OS   Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS   (Colletotrichum gloeosporioides (strain Nara gc5)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA25965.1};
RN   [1] {ECO:0000313|EMBL:ELA25965.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA25965.1};
RA   Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT   fructicola.";
RL   Submitted (AUG-2012) 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 GST superfamily.
CC       {ECO:0000256|ARBA:ARBA00007409}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR   EMBL; KB021087; ELA25965.1; -; Genomic_DNA.
DR   RefSeq; XP_007284947.1; XM_007284885.1.
DR   STRING; 1213859.L2FIH5; -.
DR   EnsemblFungi; ELA25965; ELA25965; CGGC5_12947.
DR   HOGENOM; CLU_002556_1_0_1; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00143; -.
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; IPR040079; Glutathione_S-Trfase.
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; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01206; Xi.1; 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   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          1202..1335
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          782..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        608
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1367 AA;  153448 MW;  171A25BE12D1A02E CRC64;
     MADKKLTEVD LVTRMQVDDS VVGLTEIDES LYSRQLYVLG HEAMKRMGAS NVLIAGLKGL
     GVEIAKNIAL AGVKSLTLYD PGLVSLADLS SQFFLHPEDV GKPRDEVTAP RVAELNAYTP
     IKVHQSSNLG ENLSQFDKYQ VVVLTSLPLK LQTLIGDYCH SKGIYVVAAD TFGLFGSIFC
     DFGENFTVID QTGESPLSGI VAGIDEEGLV SALDETRHGL EDGDYVTFSE IEGMEGLNGC
     EPRKITVKGP YTFSIGDVSG LGQYKRGGLY QQVKMPKSIN FKSITAAIKE PEFVMSDFAK
     FDRPQQLHLG FQALHAFVES QGRFPNPLDD GDATVILRSA EEFAKAEGLE VEFDEKLIKE
     LSYQALGDLN PMAALFGGIT AQEILKAVSG KFQPIKQWMY FDSLESLPTS TARTAELCKP
     LGTRYDGQIV VFGREYQEKI ANLRQFLVGA GAIGCEMLKN WAMIGLGTGP KGKITVTDMD
     SIEKSNLNRQ FLFRAKDVGN MKSDCAAAAV QAMNPDLNGH IVCLKDRVSP ETEETFNEQF
     WNDLDGVTNA LDNVEARTYV DRRCVFFRKP LLESGTLGTK GNTQVVLPHL TESYSSSQDP
     PEKEFPMCTV KSFPNKIEHT IAWAKDHMFE NLFITSPSTV NLYLTQPNYI EATLKQGGSA
     KLTLETLRDY LTTDRPRTFE DCIAWARILF EKEFNNKIQQ LLHNFPKDST TSSGTPFWSG
     PKRAPDPLKF DAKNPTHFAF VVAAANLHAF NYNIKSPGTD KDIYLRELEN VIVPDFSPAE
     GVKIQANDSD PDPNAEGGEG SSFDDNNELQ KIIASLPSPN DLAGFQLQPV DFEKDDDSNH
     HIDFITACSN LRAANYKIEQ ADRHKTKFIA GKIIPAIATT TALVTGLVIL ELYKVIGGKQ
     DLEQYKNGFI NLALPFFGFS EPIASPKVEF KGPNGIVKLD KIWDRFEVAD ITLKELLEHF
     EKQGLSISML SSGVSLLYAS FFPPAKLKDR QNLKLSQLVE TVSKKPIPSH QKEVIFEMVA
     EDVDGEDVEA SKITEWVKSG DKSGEFKRQQ SSFRDSISRE KGVKFQAEKG RYHLYVSYAC
     PWACRTLITR QLKGLEDIIS YSVVHWHLGE KGWRFVTKGE QESVPGDNVV PDPIQGHENF
     THLRDVYFES EPNYEGRFTV PVLYDKKLKT IVSNESSEII RMLYTEFDDL VDEKYRRVDL
     YPETLRTQID ETNEWTYDKI NNGVYKSGFA TTQEAYERNV VALFKALDKA EAHLKSTYSE
     GPFYFGKVTT EADIRLFVTI IRFDPVYVQH FKTNIRDIRS GYPFLHRWMR NLYWNVQAFR
     DTTQFEHIKW HYTKSHTHIN PFSITPVGPL PDVLPLDEEV PAVSTKL
//

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