ID Q49BM7_TETTH Unreviewed; 685 AA.
AC Q49BM7;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=SUMO-activating enzyme subunit {ECO:0000256|PIRNR:PIRNR039133};
GN Name=UBA2 {ECO:0000313|EMBL:AAY18579.1};
OS Tetrahymena thermophila.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5911 {ECO:0000313|EMBL:AAY18579.1};
RN [1] {ECO:0000313|EMBL:AAY18579.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16682458; DOI=10.1128/EC.5.5.806-815.2006;
RA Matsuda A., Forney J.D.;
RT "The SUMO pathway is developmentally regulated and required for programmed
RT DNA elimination in Paramecium tetraurelia.";
RL Eukaryot. Cell 5:806-815(2006).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|PIRNR:PIRNR039133}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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 ---------------------------------------------------------------------------
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; AY941813; AAY18579.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49BM7; -.
DR OMA; ICEDNDN; -.
DR UniPathway; UPA00143; -.
DR UniPathway; UPA00886; -.
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 GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR030661; Uba2.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_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; PF10585; UBA_E1_SCCH; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 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 10..419
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 289..352
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 565..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-1"
FT BINDING 28..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 60..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 121..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
SQ SEQUENCE 685 AA; 79431 MW; 6BF510029C4A0534 CRC64;
MSLGRINQLL FGKEFLNYLN EINILLIGVG GIGCEVLKVL QQFKVKSLHI LDLDTIEVSN
LNRQFLFRKH HRGHFKAHVA RDVLKQEYPD MNIISYNSNI KDAQFGLKFF KNFQLVIMAL
DNQETRSFVN KQCMILNIPL IDAGTTGYKG QSFILKRGET RCYDCFPRSE NKKTYPACTI
RTLPEKPVHC IIWAKYLYTV LFNEKLEDDD DSNLLQDIAK YIEGENHTDL EKGQYLFKAI
FETDVNRQKE GEDNQKFQHL KVLVREELEG KLDKSQDYLH RQDLKFLQST HTEEVYMDIF
IKSFEHLIKE KRQKSCVPFE KDDNLCMKFI TAACNLRCIV FSIPLQTQFQ VKEVAGNIVP
AIASTNSIVS AIEITETIKL LQRQFYNNPQ KYKNRELYIQ NDIKTKILDA KPGNFNPNCM
SCNQNLLPHI IYCDFNKVTL GEFINSELRS KAMQDEDDDE GNDDNKLVNF SISSGQFIIY
EEDEYQEEDE QEQNEAKRQK LISEIFKDFS DSRVVVTNED NNSIHQTYLF CHIENHKIPG
LDIVRQEKNP NNTVTWKTVI AQSDTVNKDE EQKKQEEEEQ NKKNYKEVKG DDKNNNTLEI
LDSDSEDDLV ICEDNDNPSQ GAAEKEKSKQ SNGKQPHSET DVSSLNQKRK AVQEISDGGA
MQIIDDSDDE IIFEDQQDNK KLKVD
//
