ID H6BL27_EXODN Unreviewed; 1033 AA.
AC H6BL27;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=HMPREF1120_00983 {ECO:0000313|EMBL:EHY52775.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY52775.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY52775.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY52775.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) 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}.
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DR EMBL; JH226130; EHY52775.1; -; Genomic_DNA.
DR RefSeq; XP_009153236.1; XM_009154988.1.
DR AlphaFoldDB; H6BL27; -.
DR STRING; 858893.H6BL27; -.
DR GeneID; 20305622; -.
DR VEuPathDB; FungiDB:HMPREF1120_00983; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; H6BL27; -.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007304; 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:UP000007304};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 899..1027
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 605
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1033 AA; 114724 MW; 41CB188A9D26FED6 CRC64;
MTDAVMEVDN PGAAIKELQN GEIDESLYSR QLYVLGHEAM KRMGSSNVLI VGLKGLGVEI
AKNIALAGVK SLTLFDPEPV AIADLSSQFF LRPEDVGKPR AEVTTPRVAE LNSYVPVSVH
KSQSLTDDLS QLKQFQAVVL TNTSLKDQLT IAEFCHQNGI YLTITDTFGL FGYLFNDFGD
NFTVGDVTGE NPISGIVADI DETGLVSALD ETRHGLEDGD YVEFAEVRGM EGLNGAPPRK
ITVKGPYSFS IGDVSGLGKY EGGGLFSQVK MPKVLQFQPL SEQIKKPEFL ISDFAKFDRP
AQLHIGIQAL HTFAAEHNGT LPRAHNEEDA KEVLEITKKL AKDNGDDVEI NDKLITELSY
QAQGDISPMA AFFGGLAAQE VLKAVSGKFT PVAQWLYFDS LESLPTSVPR TEELCKPTGS
RYDGQIAVFG KEFQEKIANI KNFLVGSGAI GCEMLKNYAM IGLGTGPNGH ITVTDNDSIE
KSNLNRQFLF RAKDVGKQKS EVAAAAVQAM NPDLKGKITT MTDRIGPDSE DIFNEEFWNS
LDVVTNALDN VEARTYVDRR CVFFMKPLLE SGTLGTKGNT QVILPCLTES YSSSQDPPEQ
SFPMCTLRSF PNKIEHTIAW ARDLFQSYFV GPPETVNLYL TQPDYINTTL RQQGNEKMIL
ETLKDYLVTD KPNDFNDCIA WARLQFEKQY HNAIEQLLYN FPKDSKTSSG ADFWSGPKRA
PTPLNFDPKD PTHMGFIVAA AHLHAYNYGI QAPKLRHEDY VKVIDSMIIP EFRPDANVKI
QADENEPDQN GPAKSGADDE QELNKIISEL PSPKSLPTFR LNVVEFEKDD DTNHHIDFIT
AASNLRAMNY NIPVADRHKT KFIAGKIIPA IATTTALVTG LVILELYKVI DGKTDLEQYK
NGFVNLALPF FGFSEPIASP KGTYKGKNGE VTIDKLWDRF EIDDVTLTEF LKHFEDLGLT
VTMVSSGVSL LYASFYPPSK LKDRMPLKMS KLLETISRKP IPEHQKNIIF EITAEDTTEE
DVEIPYVMVK YKK
//
