ID A0A2H5MVQ1_CITUN Unreviewed; 1093 AA.
AC A0A2H5MVQ1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=CUMW_000530 {ECO:0000313|EMBL:GAY32089.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY32089.1};
RN [1] {ECO:0000313|EMBL:GAY32089.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
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:GAY32089.1}.
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DR EMBL; BDQV01000001; GAY32089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5MVQ1; -.
DR UniPathway; UPA00143; -.
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: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; 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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 966..1088
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 50..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 669
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1093 AA; 121529 MW; DD619BE7E213F668 CRC64;
MLPCKRAGGG EAVVLEVAGP IRSPEASIKK HKITDLPPIA SATTATTAAN TGNVRSAEKS
AASNSNNSNG ADSSIMGLGN GNPSDIDEDL HSRQLAVYGR ETMRRLFASN ILISGMQGLG
AEIAKNLILA GVKSVTLHDE GVVELWDLSS NFIFSEDDVG KNRALASIQK LQELNNAVAI
SALTTELTKE TLSDFQAVVF TDISLEKAVE FDDYCHNHQP PIAFIKSEVR GLFGNIFCDF
GPEFTVFDVD GEEPHTGIIA SISNDNPPLI SCVDDERIEF QDGDLVVFSE VHGMTELNDG
KPRKVKNARP YSFSIDEDTT NYSAYEKGGI VTQVKQPKII NFKPLREALK DPGDFLLSDF
SKFDRPPVLH LAFQALDKSI QELGRFPVAG SEEDAQKIIS LFTNINDNLA DGRVEEIDHK
LLRHFAFGAR AVLNPMAAMF GGIVGQEVVK ACSGKFHPLL QFFYFDSVES LPSEPLDPRD
LQPLNSRYDA QISVFGSKLQ KKLEEAKVFV VGSGALGCEF LKNLALMGVS CGNQGKLTIT
DDDVIEKSNL SRQFLFRDWN IGQAKSSVAA SAAALINPHL NTEALQIRAN PETENVFNDT
FWENLNVVVN ALDNVNARLY IDQRCLYFQK PLLESGTLGA KCNTQMVIPH LTENYGASRD
PPEKQAPMCT VHSFPHNIDH CLTWARSEFE GLLEKTPAEV NAYLTSPTEY ASAMKNAGDA
QARDNLDRVL ECLDKERCET FQDCITWARL RFEDYFADRV KQLTFTFPEN ATTSNGTPFW
SAPKRFPRPL QFSVDDLSHL QFLMAASILR AETYGIPIPD WVKSPVKLAD AVNKVIVPDF
QPKENVKIET DEKATSMSTG SIDDAVVINE LLQKLEKCQK QLPTGYKMNP IQFEKDDDTN
FHMDLIAGLA NMRARNYGIP EVDKLKAKFI AGRIIPAIAT STAMATGLVC LELYKVLDGG
HKLEDYRNTF ANLALPLFSM AEPVPPKVFK HQDMSWTVWD RWILRDNPTL RQLLQWLQDK
GLNAYSISYG SCLLFNSMFP RHKERMDKKV VDLVRDVAKA ELPPYRQHFD VVVACEDEDD
NDIDIPQISI YFS
//
