GenomeNet

Database: UniProt
Entry: A0A0D2SZI6_GOSRA
LinkDB: A0A0D2SZI6_GOSRA
Original site: A0A0D2SZI6_GOSRA 
ID   A0A0D2SZI6_GOSRA        Unreviewed;       410 AA.
AC   A0A0D2SZI6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=THIF-type NAD/FAD binding fold domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B456_008G030900 {ECO:0000313|EMBL:KJB47536.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB47536.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB47536.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000256|ARBA:ARBA00004718}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673}.
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; CM001747; KJB47536.1; -; Genomic_DNA.
DR   EMBL; CM001747; KJB47540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2SZI6; -.
DR   EnsemblPlants; KJB47536; KJB47536; B456_008G030900.
DR   EnsemblPlants; KJB47540; KJB47540; B456_008G030900.
DR   Gramene; KJB47536; KJB47536; B456_008G030900.
DR   Gramene; KJB47540; KJB47540; B456_008G030900.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000032304; Chromosome 8.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
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   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR042449; Ub-E1_IAD_1.
DR   InterPro; IPR023318; Ub_act_enz_dom_a_sf.
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; PF10585; UBA_E1_SCCH; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT   DOMAIN          4..400
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   DOMAIN          314..366
FT                   /note="Ubiquitin-activating enzyme SCCH"
FT                   /evidence="ECO:0000259|Pfam:PF10585"
SQ   SEQUENCE   410 AA;  45607 MW;  211C9B58D6FDDC3B CRC64;
     MASEEQISAI KGAKVLMVGA GGIGCELLKT LALSGFQDIH IIDMDTIEVS NLNRQFLFRQ
     SHVGQSKAKV ARDAVLRFRP NISITPYHAN VKESRFNVDF YKEFDVVLNG LDNLDARRHV
     NRLCLAADVP LVESGTTGFL GQVTVHLKGK TECYECQAKP APKTYPVCTI TSTPSKFVHC
     IVWAKDLLFA KLFGDKNLEN DLNVRSSDAT NLSEHSEDVF ECRKGEDIEQ YGRRIYDHVF
     GHNIEVALSN EETWKNRNKP CAIYSKDVFP DKLTKENGKT EKGSTTEDVS AMASLGLKNP
     QDVWSLAENS RVFYESLRLF FSKRQKEIGN LTFDKDDQLA VEFVTAAANI RASSFGIPLH
     SLFEAKGIAG NIVHAVATTN AIIAGLIVIE AIKVLKKDSN NYRFSSVILH
//
DBGET integrated database retrieval system