ID A0A2B7XS06_9EURO Unreviewed; 1029 AA.
AC A0A2B7XS06;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=AJ80_06996 {ECO:0000313|EMBL:PGH11735.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH11735.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH11735.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH11735.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH11735.1}.
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DR EMBL; PDNA01000128; PGH11735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XS06; -.
DR STRING; 1447883.A0A2B7XS06; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000224634; 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:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000224634};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 895..1023
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 772..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 600
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1029 AA; 113808 MW; A735ECA16466BA91 CRC64;
MQDTTPQETV ERPKHGEIDE SLYSRQLYVL GHEAMKRMSS SNVLIAGLKG LGVEIAKNIA
LAGVKSLALY DPSPVAISDL SSQFFLHPED VGEPRADVTA PRVAELNQYT PVTVHAASNL
TDDLSQLKQY QIIVLTATPL KDQLAVAEYC HDNGIYVVIA DTFGLFGYIF TDFGKNFTVV
DTTGENPVSG IVAGINDEGL VSALDDTRHG LEDGDYVTFS EIKGMEGLND ADPRKVTVKG
PYTFSIGDVS GLGTYQSGGL FTQVKMPKFV DFQPFSQQLE NPEFVISDFA KFDRPAQLHI
GIQALHKFAE ARDGKFPRPH NDADAQEVFK LAEALAGEGE EKVELDDKLL KELSYQAQGD
LSPMAAFFGG LAAQEVLKAV SGKFHPIVQW LFFDSLESLP TSISRSEDLC QPLNSRYDGQ
IAVFGKEFQD KVSNMKQFLV GAGAIGCEML KNWAMIGLGT GPRGEIRVTD MDQIEKSNLN
RQFLFRPTDV GKLKSDCAAA AAQAMNPDLQ GKIVTLRDRV GQDTEHIFNE TFWEELDGVT
NALDNVDART YVDRRCVFFR KPLLESGTLG TKGNTQVILP GLTESYSSSQ DPPEQSFPMC
TLRSFPNRIE HTIAWAREMF QNYFVGPPES VNMYLSSPDY IGKTLKQAGN EQQTLEGLRD
FLVTDKPLSF DDCIVWARHQ FEKQYNNAIQ QLLFNFPKDS VTSSGTPFWS GPKRAPNPLK
FDASNPTHLS YIIAGANLHA INYGIKNPGV GKEYYQKIVG DMIIPEFTPS SGVKIQADDN
EPDPNAQPAG SGFHDTQEIQ QLISSLPTPS SLAGFRLVPV EFEKDDDTNH HIDFITAASN
LRADNYGIAQ ADRHKTKFIA GKIIPAIATT TALVTGLVVL DLYKIIDGKD DIEQYKNGFI
NLALPFFGFS EPIASPKGKY QGKDGEVVID NLWDRFEVAD IPLTQFLQHF KDKGLDISMV
SSGVSLLYAS FYPPAKVKDR LPMKMSKLVE HISKKPIPEH QRNLIFEITA DDQSGEDVEV
PYVMVKLDK
//