ID B6HJN8_PENRW Unreviewed; 1033 AA.
AC B6HJN8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=Pc21g02440 {ECO:0000313|EMBL:CAP95141.1}, PCH_Pc21g02440
GN {ECO:0000313|EMBL:CAP95141.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP95141.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP95141.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM920436; CAP95141.1; -; Genomic_DNA.
DR RefSeq; XP_002567308.1; XM_002567262.1.
DR AlphaFoldDB; B6HJN8; -.
DR STRING; 500485.B6HJN8; -.
DR GeneID; 8305453; -.
DR KEGG; pcs:Pc21g02440; -.
DR VEuPathDB; FungiDB:PCH_Pc21g02440; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR BioCyc; PCHR:PC21G02440-MONOMER; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000724; Contig Pc00c21.
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:UP000000724};
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 REGION 775..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 605
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1033 AA; 114744 MW; 57A00F5D3D87820B CRC64;
MTDVKMQVEN PQETIEAIKH GDIDESLYSR QLYVLGHEAM KRMGSSNVLI VGLKGLGVEI
AKNIALAGVK SLTLYDPAPV AISDLSSQFF LQPEDVGKPR AEVTAPRVAE LNSYVPVTVH
EGESLVGDLE QLKRYQAVVL TQTPLKEQLA IADFCHKNKI YLTITDTFGL FGYIFNDFGK
NFTVGDPNGE EPASGIVADI DEEGLVSALD ETRHGLEDGD FVTFTEVKGM EGLNNSDPRK
VTVKGPYTFT IGDVSGLGSY QGGGLFTQVK MPKFIDFQPL EDQLKNPEIV MSDPAKFDRP
QQLHIGIQAL HKFAETRDGQ LPRPHNDSDA QEVLKIANNL AAAGEEKVEL DEKIIKELSY
QARGDLNPLA AFFGGIAAQE VLKAVSGKFG PVHQWLYFDS LESLPSSVTR SEESCKPLGT
RYDGQIAVFG KEYQDKLANV TQFLVGSGAI GCETLKNWAM MGLGTGPKGK IYVTDMDQIE
KSNLNRQFLF RSKDVGRLKS ECASAAAQAM NPDLTNKIVT LRDRVGPDTE HIFNEDFWNG
LDGVTNALDN VDARTYVDRR CVFFRKPLLE SGTLGTKCNT QVVLPFVTES YSSSQDPPEK
SFPMCTLKSF PNRIEHTIAW ARDVFQTYFV GPPESVNMYL SQSDYIQQTL KQGGNEKQTL
EHLRDFLVTE KPLTFDDCVV WARQQFEAQY NNAIQQLLYN FPRDSKTSSG QLFWSGPKRA
PTPLKFDSTN PTHLGFVVAG ANLHAFNYGI KNPGADKDYY RRVVDDMIVP EFTPSSNVKI
QANENDPDPN AQPAGSSTDD QEIQKLVASL PSPKSLAGFR LQPVEFEKDD DTNHHIDFIT
AASNLRADNY EIPQADRHKT KFIAGKIIPA IATTTALATG LVALELYKVV DGKDDIEQYK
NGFVNLALPL FSFSEPIGSE KGTYQGKQGE VTIDRLWDRF EVEDIPLQEF IDFFAEKGLD
ITMVSSGVSL LYASFYPPSK VKDRLPLPMS KLVEHVSKKP VPEHQKNIIF EVTAEDQTEE
DVEVPYVMVK LTK
//
