ID A0A0A2JKP7_PENEN Unreviewed; 1028 AA.
AC A0A0A2JKP7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=PEX2_006040 {ECO:0000313|EMBL:KGO55959.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO55959.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO55959.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO55959.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO55959.1}.
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DR EMBL; JQFZ01000176; KGO55959.1; -; Genomic_DNA.
DR RefSeq; XP_016597855.1; XM_016737881.1.
DR AlphaFoldDB; A0A0A2JKP7; -.
DR STRING; 27334.A0A0A2JKP7; -.
DR GeneID; 27673300; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030143; 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:UP000030143};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 894..1022
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 773..797
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 1028 AA; 114324 MW; 58C0472DA64E7440 CRC64;
MQVENPQETI EAIKHGEIDE SLYSRQLYVL GHEAMKRMGS SNVLIVGLKG LGVEIAKNIA
LAGVKSLTLY DPAPVAISDL SSQFFLQPED VGKPRAEVTA PRVAELNSYV PVTVHEGESL
VGDLEQLKRY QAVVLTQTPL KEQLVIADFC HQNKIYLTIT DTFGLFGYIF NDFGKNFTVG
DPNGEEPAGG IVADIDDEGL VSALDETRHG LEDGDFVTFT EVKGMDGLNN SDPRKVTVKG
PYTFTIGDVS GLGSYQGGGL FTQVKMPKFI DFQPLEDQLK KPELLMSDFA KFDRPQQLHI
GIQALHKFAE THNGQLPRPH NDSDAQEVLK VANDLAAAGE EKVELDEKII KELSYQARGD
LNPLAAFFGG IAAQEVLKAV SGKFSPVHQW LYFDSLESLP TSVTRSEESC KPLGTRYDGQ
IAVFGKEYQD KLANVTQFLV GSGAIGCETL KNWAMMGLGT GPRGKLYVTD MDQIEKSNLN
RQFLFRPKDV GRLKSECASA AAQAMNPELK DKIVTLRDRV GADTEHVFNE DFWNGLDGVT
NALDNVDART YVDRRCVFFR KPLLESGTLG TKCNTQVVLP FITESYSSSQ DPPEKSFPMC
TLKSFPNRIE HTIAWARDVF QTYFVGPPES VNMYLSQSDY IQQTLKQAGN EKQTLEHLRD
FLVTEKPLTF DDCIVWARQQ FEAQYNNAIQ QLLYNFPRDS KTSSGQLFWS GPKRAPTPLK
FDSTNLTHLG FVVAGANLHA FNYGIKNPGA DKDYYRRVVD DMIVPEFTPS SNVKIQANEN
DPDPNAQPAG SSTDEEEIQK LVASLPSPKS LAGFRLQPVE FEKDDDTNHH IDFITAASNL
RADNYEIPQA DRHKTKFIAG KIIPAIATTT ALATGLVALE LYKIVDGKDD IEQYKNGFVN
LALPLFSFSE PIGSEKGKYQ GKQGEVTIDK LWDRFEVEDI PLQEFLDFFA EKGLDITMVS
SGVSLLYASF YPPSKVKDRL PLPMSKLVEH VSKKPVPEHQ KNIIFEVTAE DQTEEDVEVP
YVMVKLAN
//
