ID S8EEW9_9LAMI Unreviewed; 600 AA.
AC S8EEW9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=SUMO-activating enzyme subunit {ECO:0000256|PIRNR:PIRNR039133};
GN ORFNames=M569_00206 {ECO:0000313|EMBL:EPS74543.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS74543.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS74543.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718, ECO:0000256|PIRNR:PIRNR039133}.
CC -!- SUBUNIT: Heterodimer. {ECO:0000256|PIRNR:PIRNR039133}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|PIRNR:PIRNR039133}.
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:EPS74543.1}.
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DR EMBL; AUSU01000052; EPS74543.1; -; Genomic_DNA.
DR AlphaFoldDB; S8EEW9; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000015453; Unassembled WGS sequence.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniRule.
DR CDD; cd01489; Uba2_SUMO; 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR028077; UAE_UbL_dom.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030661; Uba2.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF14732; UAE_UbL; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR039133};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR039133,
KW ECO:0000256|PIRSR:PIRSR039133-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR039133};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR039133};
KW Zinc {ECO:0000256|PIRNR:PIRNR039133, ECO:0000256|PIRSR:PIRSR039133-3}.
FT DOMAIN 1..413
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 309..350
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT DOMAIN 423..515
FT /note="Ubiquitin/SUMO-activating enzyme ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF14732"
FT REGION 536..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-1"
FT BINDING 3..8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 35..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 96..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
SQ SEQUENCE 600 AA; 66914 MW; 32857EC1E4BBF22B CRC64;
MVGAGGIGCE LLKTLVLSGF KDIHIIDMDT IEVSNLNRQF LFRQSHVGKS KAKVACDAVL
RFRPHVSIVP YHANVKDSQF NVDFFRQFHV VLNGLDNLDA RRHVNRLCLA SGVPLIESGT
TGFLGQVTVH VKGKTECYEC QPKPAPKTYP VCTITSTPSK FVHCIVWAKD LLFTKLFGDK
NQENDLNVRS SDASSSSQQT ENVFDFRNKE DNTCYGRRIF DHVFGYNIDR ALSNEDTWKN
RNKPRPIYFK DVFPDEIIHQ NGNQSIGKNS GSVSGMASLG LKNPQDVWSL RENATVFFEA
LELLFSTREK EIGSLTFDKD DQLAVEFVTA AANIRASSFG IPLHSLFEAK GIAGNIVHAV
ATTNAIIAGL IVIEAIKVLQ NDIKSYRMTY CLEHPSRNIL VMPVEPFEPN KSCYVCSEMP
LTLEINPYRS KLKDIVDKVV KAKLGMNLPM IMHGSSLLYE AGDDLAEDEV AHYETNLEKI
LSELPCPVIG GTILTVEDLQ QELKCSVNIK HREEFDEEKE PDGLILLGWT QPVAAPVDEQ
PSHENNGVKM TSADDDVIVA SPQPGGKKKK RKLSDESGDP NETKLKRRTE GDDEEEVIML
//
