ID A0A1B7N4J2_9AGAM Unreviewed; 1012 AA.
AC A0A1B7N4J2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=K503DRAFT_738832 {ECO:0000313|EMBL:OAX39752.1};
OS Rhizopogon vinicolor AM-OR11-026.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX39752.1, ECO:0000313|Proteomes:UP000092154};
RN [1] {ECO:0000313|EMBL:OAX39752.1, ECO:0000313|Proteomes:UP000092154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX39752.1,
RC ECO:0000313|Proteomes:UP000092154};
RG DOE Joint Genome Institute;
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (JUN-2016) 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}.
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DR EMBL; KV448237; OAX39752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7N4J2; -.
DR STRING; 1314800.A0A1B7N4J2; -.
DR InParanoid; A0A1B7N4J2; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000092154; 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:UP000092154}.
FT DOMAIN 883..1008
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
SQ SEQUENCE 1012 AA; 112281 MW; B16D907B8C1E897D CRC64;
MADASNLAAK MDVDEAAIDE GLYSRQLYVL GHEAMKKMAA SNVLIAGLQG LGAEIAKNVC
LAGVKSVTLY DPEAVTVQDL SSQYFLREED IGKPRAAATL PRLAELNAYV PVRDLGGHAG
QEISIDLIRP FQAVVLCGAS YEKQLEINDW THQNGVHFIS AETRGLFGSI FNDFGPKFTC
VDPTGEQPLT GMIVSVDQSD EGLVTCLDES RHGLEDGDFV TFTEVQGMTE LNNCNPRKVT
VKGPYTFTIG NTSDLGQYIR GGIFTQVKMP KILEFKSLRE SLAAPELFVT DFAKFDRPST
LHAGFQALSQ FKSQQQRLPR PRNVEDAASL IALAKKIDAD ADEKIITELA YQATGDLPPI
SAVIGGFVAQ EVLKACSAKF HPMLQHLYFD SLESLPSLLP SEQDCQPLGS RYDGQIAVFG
KSFQDKIANH RQFLVGAGAI GCEMLKNWSM MGLATGPDAR IHVTDLDTIE KSNLNRQFLF
RAKDLGKFKS EVAAAAVAEM NPALKGHILC RQDPVGQATE NVFDDDFFAA VDGVTNALDN
VVARVYMDQR CILYEKPLLE SGTMGTKGNT QVVIPHLTES YSSSQDPPEK QTLSCTVKNF
PNAITHTIEW SRQEFDAMFV KPVESVNQYL SEPNYLENSL KYSGQSYDHI SQIVSYLVTN
KPLTFEECIV WARLQFEEKY NNSIRQLLHS LPKDHVTSTG QPFWSGPKRA PDPLVFDSSD
PTHLSFIIAA ANLHAYNYGL RGETDPAVFK KVADSVIVPE FSPRSGVKIQ ISETDPVNQS
SSDHDDVSDL VKKLPPPSSL AGYRLTPVEF EKDDDTNHHI DFITAASNLR AMNYTITVAD
RHTTKQIAGK IIPAIATTTA LVVGLVCLEL YKVIDGKNKL DDYKNGFVNL ALPFFGFSEP
IAVKKNKFND TEWTLWDRLE FKNDPTLKEF ISWFKTHHNL DVSMVSQGVS MLWSSFTDKK
KSAERLPMKF SKLVEHVSKK PIPPHTKQLL VEVMLMDEEM EDVEVPFILI KI
//
