ID A0A0D2LBC8_HYPSF Unreviewed; 1013 AA.
AC A0A0D2LBC8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=HYPSUDRAFT_65431 {ECO:0000313|EMBL:KJA24552.1};
OS Hypholoma sublateritium (strain FD-334 SS-4).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Hypholoma.
OX NCBI_TaxID=945553 {ECO:0000313|EMBL:KJA24552.1, ECO:0000313|Proteomes:UP000054270};
RN [1] {ECO:0000313|Proteomes:UP000054270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-334 SS-4 {ECO:0000313|Proteomes:UP000054270};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-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}.
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DR EMBL; KN817536; KJA24552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2LBC8; -.
DR STRING; 945553.A0A0D2LBC8; -.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054270; 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:UP000054270}.
FT DOMAIN 884..1009
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 768..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 111880 MW; 70C9E0BF7BEF901E CRC64;
MAESSNAANQ MDIDETAIDE GLYSRQLYVL GHEAMKKMAA SNVLIVGMSG LGVEIAKNIV
LAGVKTVTIF DPAPVTVQDL SSQFFLRAGD IGKARAAATL PRLAELNAYV PVRDLGGKAG
DEVTVALIKG FHVVVLCGVS YKKQLEINNW THENGVHFIA AETRGLFGSA FNDFGPKFTC
VDPTGEQPLS GMIVSVDKDK EGVVTCLDET RHGLEDGDYV TFSEVQGMTE LNGCEPRKIT
VKGPYTFSIG DTSGLSDYKT GGIFSQVKMP KLLDFKPLTE SLKSPEFFIT DFAKFDRPAI
LHAGFQAISE FESLHNRSPR PRNDEDADEI VALAKQLDSD ADEKVLKEMA YQATGDLSPM
NAVLGGFVAQ EVLKACSAKF HPTFQHMYFD SLESLPNNLP TEADVQPIGS RYDGQIAVFG
KSFQDKIASH RQFLVGSGAI GCEMLKNWSL MGVGSGPDGI IHVTDLDTIE KSNLNRQFLF
RAKDLGHFKA EVAAAAVAEM NPDLKGKILA KQEPVGPATE NIYDEAFFAG IDGVTNALDN
VKARLYMDQR CVFYRKPLLE SGTLGTKGNT QVIIPNLTES YASSQDPPEK ETPSCTIKNF
PNAINHTIEW SRTQFDHLFV KPAQASNAYL SEPNYLESTL KYSGQQKEQV EQIVSFLVTN
KPLTFEECII WARLQFERDY NNDIRQLLFS LPKDAVTSTG QPFWSGPKRA PEPLVFNSSE
PTHLEYVIAA ANLHAFNYGL RGDNNPALFR KVVDSVIVPE FTPRSGVKVQ INDSDPVPAA
EGSTDDDPED LTSKLPSPSS LAGYRLNPCE FEKDDDTNHH IDFITAASNL RAMNYNITPA
DKHTTKQIAG KIIPAIATTT SLVTGMVCLE LYKIIDGKNK LEDYKNGFVN LALPFFGFSE
PIAAAKSKYG ETEWTLWDRF EFSNDPTLAE IQQFFEENHK LTITMVSQGV SMLWNPWIGK
KKSDERLHMK FSALVEHVSK KPIPPHVNYL IVEVMVSDED DEDVEVPFIV VRI
//
