ID A0A2P5W6V2_GOSBA Unreviewed; 848 AA.
AC A0A2P5W6V2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=GOBAR_AA33847 {ECO:0000313|EMBL:PPR86840.1};
OS Gossypium barbadense (Sea-island cotton) (Egyptian cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3634 {ECO:0000313|EMBL:PPR86840.1, ECO:0000313|Proteomes:UP000239757};
RN [1] {ECO:0000313|EMBL:PPR86840.1, ECO:0000313|Proteomes:UP000239757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Xinhai21 {ECO:0000313|Proteomes:UP000239757};
RC TISSUE=Leaf {ECO:0000313|EMBL:PPR86840.1};
RA Chen X., Liu X., Zhao B., Zheng H., Hu Y., Lu G., Yang C., Chen J.,
RA Shan C., Zhang L., Zhou Y., Wang L., Guo W., Bai Y., Ruan J., Shangguan X.,
RA Mao Y., Jiang J., Zhu Y., Lei J., Kang H., Chen S., He X., Wang R.,
RA Wang Y., Chen J., Wang L., Yu S., Wang B., Wei J., Song S., Lu X., Gao Z.,
RA Gu W., Deng X., Ma D., Wang S., Liang W., Fang L., Cai C., Zhu X., Zhou B.,
RA Zhang Y., Chen Z., Xu S., Zhu R., Wang S., Zhang T., Zhao G.;
RT "Genome of allotetraploid Gossypium barbadense reveals genomic plasticity
RT and fiber elongation in cotton evolution.";
RL Submitted (JAN-2015) 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; KZ668832; PPR86840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5W6V2; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000239757; Unassembled WGS sequence.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; 2.
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; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
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; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000239757};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 112..475
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 286..356
FT /note="Ubiquitin-activating enzyme E1 FCCH"
FT /evidence="ECO:0000259|Pfam:PF16190"
FT DOMAIN 357..427
FT /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT /evidence="ECO:0000259|Pfam:PF16191"
FT DOMAIN 548..841
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 637..786
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT ACT_SITE 638
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 848 AA; 93607 MW; C6321876EB09A5D1 CRC64;
MITFAALTIV FLGFYGIFGS LMHYMLPRKR AGEGEVVEEE SENNNSNIKD VTVSPPIKKH
RISTTDAADL TADNKIVTTG DNSSNYSNTC VDEPSVMASR DVNHNDIDED LHSRQLAAYG
RETMRRLFAS NILISGMQGL GAEIAKNLIL AGVKSVTLHD EGVVEMWDLS SSFVFSENDV
GKNRALASLQ KLQELNNAVV ISTITTTLTK QKLSDFQAVV FTDISLEKSL EYNDYCHNHQ
PPISFIKTEV RGLFGTVFCD FGPKFTVFDV DGEEPHTGII ASISNDNPAL VSCVDDERLE
FEDGDLVVFS EIQGMKELND GKPRKIKSVR PYSFTLEEDT TNFGTYVKGG IVTQVKQPRV
LNFKPLRAAL KDPGDFLLSD FSKFDRPPLL HIAFQALDRF ICEIGRFPVA RSEEDAQKFI
SIAGNINECL GEGGVEDINP KLLTHFAFGA RAVLNPMAAM FGGIVGQEVV KALESLPVEP
LDPIDFKPLN NRYDAQISVF GSKLQKNLED AKVFIVGSGA LGCEFLKNVA LMGVSCGSQG
KLTITDDDLK IEALQNRVGP ETEFVFNDDF WENLTVVINA LDNVDARLYV DQRCLYFQKP
LLELGTLGAK CNTQMVIPHL TENYGASRDP PEKQAPMCTV HSFPHNIDHC LTWARSEFEG
LLEKTPAELT FTFPEDATTS TGAPFWSAPK RFPRPLQFST TDPSHLQFIM AASILRAETF
GIPVPDWVKN TKMLAKAVEK VIVPDFQPKE GVKIETIETD ERATSLSTGS VDDAAVINEL
LFKLERSGLA NMRARNYSIP EVDKLKAKFI AGRIIPAIAT STAMATGLVC LELYKVLDGA
HKVEDYVG
//
