ID A0A094AIB1_9PEZI Unreviewed; 1122 AA.
AC A0A094AIB1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=V493_06250 {ECO:0000313|EMBL:KFY22895.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY22895.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY22895.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY22895.1}.
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DR EMBL; JPJV01002351; KFY22895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094AIB1; -.
DR STRING; 1420906.A0A094AIB1; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000029327; 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; 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; 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.
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:UP000029327};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 988..1116
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 862..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 692
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1122 AA; 123983 MW; 041033F47584623E CRC64;
MMDPSISNRH IGQRHIFRRD SCLGDYETSL GRSVHCIRIE SISPAVSATG KTFKIPSITD
TEGVTQLGKR KASSEAEPRL AKRSLTSNLK SGTDMATKMQ VDGPSATNND IDESLYSRQL
YVLGHEAMKR MSASNVLIVG LKGLGVEIAK NIALAGVKSL TLYDRTPAAI SDMSSQFFIH
AEDLGKERAL VTAPRVAELN AYTPVSVLEE PSLTANLAAL DQFQVVVLTG TPIKDQIVIG
DYCHQKGIYL VVADTFGLFG SIFCDFGKQF TVLDPDGETP ASGIVASINE EGLVSALDET
RHGLEDGDYV TFTEIQGMDA LNNSDPRKIT VKGPYTFSIG DVSGLGEYKT GGIYTQVKMP
KFIDFKPFSE CLKTPEFLIS DYAKMDRPEQ LHVGFQALHA FAEGHGRFPR PQNDDDAAIV
IGSAKLFVER EKLSVEIDEK LIRELSYQAQ GDLNPMAAFF GGLAAQEVLK AISGKFYPIV
QWLYFDSLES LPTSFKRSEE LCKPINSRYD GQIAVFGKDF QDKLANTNEF LVGAGAIGCE
MLKNWAMIGL ATGPKGKINV TDMDSIEKSN LNRQFLFRPK DVGKMKSDCA AAAVVAMNPE
LEGHIVTMRD RVGQDTEHIF NEEFWESLDG VTNALDNVDA RTYVDRRCVF FRKPLLESGT
LGTKGNTQVI LPHLTESYSS SQDPPEQSFP MCTLKSFPNK IEHTIAWGRE LFESYFVKPA
ETVNLYLSQP NYIDTTLKQG GNEKATLESI RDYLVTDKPL SFEDCVVWAR LQFENQYNNA
IQQLLYNFPK DSNSSSGVPF WSGPKRAPTP LKFDPNNEEH LRFVIAGANL HAFNYGINAK
DADGEVIQKV LDNMIIPDFS PNPAVKIQAD DSEPDPNAPA ANSSSFDDGS ELQEITKSLP
PPSSLAGFKL QPVEFEKDDD TNYHIDFITA ASNLRADNYK IAPADRHKTK FIAGKIIPAI
ATTTALVTGL VIFELYKILD GKDDIEQYKN GFVNLALPFF GFSEPIASAK GSYKGPNGEV
TVDKLWDRFE VDNITLRELI DMFKAKGLDI TMLSSGVSLL YASFFPPAKL KDRYGLKLSE
LVAQISKKPI PEHQKNVIFE ICADDESGED VEVPYIMMKM GN
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