ID SELD_HUMAN STANDARD; PRT; 383 AA. AC P49903; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE SELENIDE,WATER DIKINASE 1 (EC 2.7.9.3) (SELENOPHOSPHATE SYNTHETASE 1) DE (SELENIUM DONOR PROTEIN 1). GN SELD. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 95394923. 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). 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 -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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 MIM; 600902; -. DR PFAM; PF00586; AIRS; 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. SQ SEQUENCE 383 AA; 42268 MW; 3AF1A4A8 CRC32; 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 AAGLMHTFNT HAATDITGFG ILGHAQNLAK QQRNEVSFVI HNLPVLAKMA AVSKACGNMF GLMHGTCPET SGGLLICLPR EQAARFCAEI KSPKYGEGHQ AWIIGIVEKG NRTARIIDKP RIIEVAHKWP LKT //