ID S7QKI5_GLOTA Unreviewed; 1011 AA.
AC S7QKI5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=GLOTRDRAFT_125688 {ECO:0000313|EMBL:EPQ59902.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ59902.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ59902.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ59902.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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}.
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DR EMBL; KB469297; EPQ59902.1; -; Genomic_DNA.
DR RefSeq; XP_007862762.1; XM_007864571.1.
DR AlphaFoldDB; S7QKI5; -.
DR STRING; 670483.S7QKI5; -.
DR GeneID; 19301282; -.
DR KEGG; gtr:GLOTRDRAFT_125688; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030669; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd01491; Ube1_repeat1; 1.
DR CDD; cd01490; Ube1_repeat2; 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; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
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; 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; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000030669}.
FT DOMAIN 882..1007
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 765..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 112051 MW; 0D594D64DC160829 CRC64;
MAANLPSAMD IDETAIDEGL YSRQLYVLGH EAMKRMAASN ILIVGVQGLG VEIAKNVCLA
GVKSVTIFDP EPVKIQDLST QFFLREEDIG KSRAAVTVPR LAELNAYVPV RDLGGQPGQE
ITVDMIQGFQ VVVLCGVPIA KQLEINDWTH KNGVHFIAAE TRGLFGSAFN DFGPKFTCVD
PTGEQPLTGM IVSVEKDKEG LVTTLDETRH GLQDGDFVTF SEVQGMEELN GCEPRKVTVK
GPYTFTIGDT SNFGDYKTGG IFTQVKMPKI LEFKSLRESL KSPEYFITDF AKWERPATLH
AGFQALSEFR VQNGRLPRPR NAEDAAQILA LAKKLEQEVD EKVITELAYQ ASGDVSPIIA
VMGGFVAQEV LKACSAKFHP MVQHMYFDSL ESLPATAPTE ADCQPIGSRY DGQVAVFGKV
FQDKIANFRE FLVGSGAIGC EMLKNWSMMG LGAGPRGIIH VTDLDTIEKS NLNRQFLFRA
KDLGKFKAEV AAAAVAAMNP DLKGHILSKQ EPVGPDTENV YGDEFFDGID GVTNALDNVK
ARQYMDQRCV FYLKPLLESG TLGTKGNTQV IVPHLTESYS SSQDPPEKET PSCTVKNFPN
AIQHTIEWSR QEFDNLFVKP AQSVNSYLSE PNYLESTLKY SGQQKEQLEQ LVSFLVTNKP
LTFEECIVWA RLQFEEKFNH NIRQLLYSLP KDAVTSTGQP FWSGPKRAPD PLNFDSNDPQ
HLAFIIAAAN LHAYNYGLRG ETDPAIFKKV ADSVVVPEFT PKSGVKVQIN DNDPAPEGGN
TDSGDASELV KKLPAPSSLA GYRLSPVEFE KDDDTNHHID FITAASNLRA MNYHIQIADR
HTTKQIAGKI IPAIATTTSL VVGLVCLELY KLIDGKDKLE DYKNGFVNLA LPFFGFSEPI
AAKKNKYGST EWTLWDRFEF KGDPTLKEVI DWFKKELNLE VGMVSQGVSM LWSSFIGKKK
SDERLPMRFS KLVEHVSKKP IPPHVKHLIV EVMVSDENDE DVEVPFIVVR I
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