ID M7WWD3_RHOT1 Unreviewed; 1023 AA.
AC M7WWD3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN ORFNames=RHTO_05087 {ECO:0000313|EMBL:EMS24907.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS24907.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS24907.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS24907.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(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 sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
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DR EMBL; KB722644; EMS24907.1; -; Genomic_DNA.
DR RefSeq; XP_016276026.1; XM_016418750.1.
DR AlphaFoldDB; M7WWD3; -.
DR GeneID; 27369100; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
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; IPR018074; UBQ-activ_enz_E1_CS.
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; PS00536; UBIQUITIN_ACTIVAT_1; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 892..1018
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 771..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 113872 MW; A685563E4E18E047 CRC64;
MAAPAQQPVS NDAGLDESLY SRQLYVLGHE AMKRMAASDV LVIGLSGLGV EIAKNICLAG
VKSVTLSDPT PVSLPDLGTQ FFLRDSDVGQ RRDEATRPRL AELNAYTPVS VLPDLNLDAV
KRFTVVVLVQ GSTEDQLKLN DFTHANGIKF IAAETAGLFA SAFCDFGEQF PVVDQTGENP
LSGMVVEIEE AEDALVTCLD ESRHGLEDGD YVRFSEVEGM NINSDGVEGA RKITVTGPYT
FKIGDTRGLG QYKRGGWFHQ VKMPKMYDFK PLRESMTAPE FLITDFAKFD RPPTLHIGFQ
ALSAYRTQHN RLPKPRNPAD AATFVQLAKD IAAQVKFEGD LDEKVLEELA FQAVGDLAPV
NAVIGGFVAQ EVLKACSGKF SPLYQHLYFD ALEALPVDLP SEEECAPSNP ASRWDNQIAV
FGRSFQQKIE NNRQFLVGSG AIGCEMLKNW AMMGVASGQN GHVYITDLDT IEKSNLNRQF
LFRPKDVGSF KSEAARRAAT EMNAGLDGKV EVFKLAVGPD TENVFGDSFF DSIDCVTNAL
DNVSARQYMD QRCVYYAKPL LESGTLGTKG NVQVVLPHVT ESYSSSQDPP EKSHPSCTIK
NFPNQIEHTI AWAKERFEEC FEKPAEVVNS YLSQPNFVEA AKQSGETAQL LKVKSYLVDH
KPLGFEECIT WARQQFETEY VNEIKQLLFS LPKDLLTKEG TPFWSGPKRA PEPLQFDYNN
PTHMEFIVAA ANLHAYNYGL MGETNLETFK RVLDQVHLPE FVPKSGVQVQ IKDDEPVNND
KDAPPSTDAD DLASLAASLP PPSTLAGYRM VPAQFEKDDD TNHHIDFITA ASNLRAQNYG
IQPADRHRTK GIAGKIIPAL ATTTAVVAGL VCIELYKLLD EKKRGAEMLE RYKNSFCNLA
LPFFAFSEPI AAPKMKYRDT EYTLWDRFEI EGDITLEQLV EHFKEKYKLE ISMLSSGVSM
LYSGFMPKKK LEERLKMPLS QLVETVSKKP IPEHVRDIVF EIMCNDMDTD DDVEVPYLKV
RVR
//
