ID A0A5A7PQG9_STRAF Unreviewed; 1148 AA.
AC A0A5A7PQG9;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=STAS_10965 {ECO:0000313|EMBL:GER34712.1};
OS Striga asiatica (Asiatic witchweed) (Buchnera asiatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga.
OX NCBI_TaxID=4170 {ECO:0000313|EMBL:GER34712.1, ECO:0000313|Proteomes:UP000325081};
RN [1] {ECO:0000313|Proteomes:UP000325081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UVA1 {ECO:0000313|Proteomes:UP000325081};
RX PubMed=31522940; DOI=10.1016/j.cub.2019.07.086;
RA Yoshida S., Kim S., Wafula E.K., Tanskanen J., Kim Y.M., Honaas L.,
RA Yang Z., Spallek T., Conn C.E., Ichihashi Y., Cheong K., Cui S., Der J.P.,
RA Gundlach H., Jiao Y., Hori C., Ishida J.K., Kasahara H., Kiba T., Kim M.S.,
RA Koo N., Laohavisit A., Lee Y.H., Lumba S., McCourt P., Mortimer J.C.,
RA Mutuku J.M., Nomura T., Sasaki-Sekimoto Y., Seto Y., Wang Y., Wakatake T.,
RA Sakakibara H., Demura T., Yamaguchi S., Yoneyama K., Manabe R.I.,
RA Nelson D.C., Schulman A.H., Timko M.P., dePamphilis C.W., Choi D.,
RA Shirasu K.;
RT "Genome Sequence of Striga asiatica Provides Insight into the Evolution of
RT Plant Parasitism.";
RL Curr. Biol. 29:3041-3052.e4(2019).
CC -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC glycine residue with ATP, and thereafter linking this residue to the
CC side chain of a cysteine residue in E1, yielding a ubiquitin-E1
CC thioester and free AMP. {ECO:0000256|ARBA:ARBA00002457}.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GER34712.1}.
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DR EMBL; BKCP01004949; GER34712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A7PQG9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000325081; 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; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR NCBIfam; TIGR01408; Ube1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF215; UBIQUITIN-ACTIVATING ENZYME E1 1; 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; 3.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
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:UP000325081};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 1021..1143
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 30..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 724
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1148 AA; 128641 MW; 8BEFD92A453EC675 CRC64;
MLPIKRQGEG EAVNDPDSEI LLKKQRDCFS STNSTDELNS NSKGTGSLEE PTITEMAFDD
GKPNDIDEDL HSRQLAVYGR ETMRRLFASN VLVSGMQGLG AEIGGIVERA DYIPFGLVLL
AFVLLPVEPL IQFLLDFGLQ LLLAKNLILA GVKSVTLHDE GTVELWDLSS NFVFSEKDLG
KNRALASIQK LQELNNAVAI STLTTKLSVE QLSDFQAVVF TDIDLKRAIE FNEFCHNHQP
PIAFIKTEVR GLFGSVFCDF GPEFTVFDVD GEEPHTGIIA SISNDNPSLV GCVDDERLEF
QDGDLVVFSE IRGMTELNDG KTRKIKNARP YSFTLEEDTT NFGRYERGGI VTQVKQPKVL
NFKPLKEAIK DPGDFLLSDF SKFDRPPLLH LAFQALDNFV SEMGRFPVAG SEEDAQRLIS
VTSDMNESLG DGKLDINPKL LRHFAFGARA VLNPMAAMFG GIVGQEVVKA CSGKFHPLFQ
LGTIFAGKRD QIARIVSFLD AHGTYLICMW PHLWLKFFYF DSIESLPTEI SDPSDFRPLN
SRYDAQISVF GSKLQKKLED AKVFVVGSGA LGCEFLKNLA LMGVSCGKQG KLTITDDDVI
EKSNLSRQFL FRDWNIGQPK STVAASAALS INPHFHIEAL QNRVGPETET VFDDAFWENL
SVVINALDNV NARLYVDQRC LYFQKPLLES GTLGAKCNTQ MVIPHLTENY GASRDPPEKQ
APMCTVHSFP HNIDHCLTWA RSEFEGLLEK TPAEVNAYLS NPVEYASAMR NAGDAQARDN
LERVIECLDR ERCESFQDCI TWARLKFEDY FANRVKQLTF TFPEDAATST GAPFWSAPKR
FPRPLQFSNT DPSHLHFVMA GSILRAETFG IPVPDWAKSP MKLAEAVDNV IVPDFQPKKD
VKIVTDEKAT SLATSSMDDA AVIDELIAKL EKCRETLAAK FMMKPIQFEK DDDTNYHMDL
ISALANMRAR NYSIPEVDKL KAKFIAGRII PAIATSTAMA TGLVCLELYK AIDNNHKVED
YRNTFANLAL PLFSMAEPVP PKLFKHRDMS WTVWDRWIVR ENPTLRELLR WLADKGLNAY
SISFGSCLLY NSMFPRHRER MDRKVAELAR DVAKVELPRG RGHLDVVVAC EDEDDNDIDI
PQVSVYFR
//
