ID SPS1_HUMAN STANDARD; PRT; 392 AA. AC P49903; Q9BVT4; DT 01-OCT-1996 (Rel. 34, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Selenide,water dikinase 1 (EC 2.7.9.3) (Selenophosphate synthetase 1) DE (Selenium donor protein 1). GN Name=SEPHS1; Synonyms=SPS1, SPS, SELD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., FUNCTION, ATP-BINDING, AND MUTAGENESIS OF GLY-268; RP GLY-270; GLY-273 AND HIS-274. RC TISSUE=Liver; RX MEDLINE=95394923; PubMed=7665581; RA Low S.C., Harney J.W., Berry M.J.; RT "Cloning and functional characterization of human selenophosphate RT synthetase, an essential component of selenoprotein synthesis."; RL J. Biol. Chem. 270:21659-21664(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP. CC -!- CATALYTIC ACTIVITY: ATP + selenide + H(2)O = AMP + selenophosphate CC + phosphate. CC -!- SIMILARITY: Belongs to the selenophosphate synthetase 1 family. CC Class II subfamily. CC -!- CAUTION: The conserved active site Cys (or Se_Cys) residue in CC position 29 is replaced by a Thr. However, as function in CC selenoprotein synthesis is proven, it is possible Cys-31 is the CC active site. 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; U34044; AAA87567.1; -. DR EMBL; BC000941; AAH00941.1; -. DR Genew; HGNC:19685; SEPHS1. DR MIM; 600902; -. DR GO; GO:0005524; F:ATP binding; TAS. DR GO; GO:0005525; F:GTP binding; TAS. DR GO; GO:0006464; P:protein modification; TAS. DR InterPro; IPR000728; AIR_synth. DR InterPro; IPR010918; AIR_synth_C. DR InterPro; IPR004536; SelD. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR TIGRFAMs; TIGR00476; selD; 1. KW Transferase; Selenium; ATP-binding. FT ACT_SITE 31 31 Potential. FT SITE 32 32 Important for catalytic activity (By FT similarity). FT NP_BIND 268 274 ATP (Potential). FT MUTAGEN 268 268 G->C: No change in ATP-binding. FT MUTAGEN 270 270 G->R: No change in ATP-binding. FT MUTAGEN 273 273 G->A,D,V: Loss of ATP-binding. FT MUTAGEN 274 274 H->N: Reduced ATP-binding. FT MUTAGEN 274 274 H->Y: Increased ATP-binding. FT CONFLICT 260 260 A -> T (in Ref. 1). FT CONFLICT 377 392 PQVATQNVNPTPGATS -> HKWPLKT (in Ref. 1). SQ SEQUENCE 392 AA; 42910 MW; E9636E38146D926D CRC64; MSTRESFNPE SYELDKSFRL TRFTELKGTG CKVPQDVLQK LLESLQENHF QEDEQFLGAV MPRLGIGMDT CVIPLRHGGL SLVQTTDYIY PIVDDPYMMG RIACANVLSD LYAMGVTECD NMLMLLGVSN KMTDRERDKV MPLIIQGFKD AAEEAGTSVT GGQTVLNPWI VLGGVATTVC QPNEFIMPDN AVPGDVLVLT KPLGTQVAVA VHQWLDIPEK WNKIKLVVTQ EDVELAYQEA MMNMARLNRT AAGLMHTFNA HAATDITGFG ILGHAQNLAK QQRNEVSFVI HNLPVLAKMA AVSKACGNMF GLMHGTCPET SGGLLICLPR EQAARFCAEI KSPKYGEGHQ AWIIGIVEKG NRTARIIDKP RIIEVAPQVA TQNVNPTPGA TS //