ID CPD1_DROME STANDARD; PRT; 355 AA. AC P22058; DT 01-AUG-1991 (REL. 19, CREATED) DT 01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE) DT 01-APR-1993 (REL. 25, LAST ANNOTATION UPDATE) DE CHROMOSOMAL PROTEIN D1. GN D1. OS DROSOPHILA MELANOGASTER (FRUIT FLY). OC EUKARYOTA; METAZOA; ARTHROPODA; TRACHEATA; HEXAPODA; INSECTA; OC PTERYGOTA; DIPTERA; BRACHYCERA; MUSCOMORPHA; EPHYDROIDEA; OC DROSOPHILIDAE; DROSOPHILA. RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-33. RX MEDLINE; 89255282. RA ASHLEY C.T., PENDLETON C.G., JENNINGS W.W., SAXENA A., GLOVER C.V.C.; RT "Isolation and sequencing of cDNA clones encoding Drosophila RT chromosomal protein D1. A repeating motif in proteins which recognize RT at DNA."; RL J. BIOL. CHEM. 264:8394-8401(1989). CC -!- FUNCTION: THIS SATELLITE DNA-ASSOCIATED PROTEIN IS A DOUBLE- CC STRANDED DNA BINDING PROTEIN SPECIFIC FOR TRACTS OF PURE AT DNA. CC IT MAY PLAY A ROLE IN ORGANIZING THE HIGHER ORDER STRUCTURE OF CC EUCHROMATIN AS WELL AS HETEROCHROMATIN. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- D1 MAY BE THE MOST ABUNDANT MEMBER OF A SMALL FAMILY OF D1-LIKE CC PROTEINS. CC -!- SIMILARITY: CONTAINS HMG BOXES. 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; J04725; G157170; -. DR PIR; A33821; A33821. DR FLYBASE; FBgn0000412; D1. KW NUCLEAR PROTEIN; DNA-BINDING; CHROMOSOMAL PROTEIN; PHOSPHORYLATION; KW REPEAT; ACETYLATION. FT MOD_RES 1 1 ACETYLATION (PROBABLE). FT DNA_BIND 7 14 A.T HOOK. FT DNA_BIND 34 41 A.T HOOK. FT DNA_BIND 60 67 A.T HOOK. FT DNA_BIND 94 101 A.T HOOK. FT DNA_BIND 122 129 A.T HOOK. FT DNA_BIND 155 162 A.T HOOK. FT DNA_BIND 174 181 A.T HOOK. FT DNA_BIND 196 203 A.T HOOK. FT DNA_BIND 219 226 A.T HOOK. FT DNA_BIND 262 269 A.T HOOK. FT DNA_BIND 281 288 A.T HOOK. FT MOD_RES 133 133 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 135 135 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 186 186 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 246 246 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 311 311 PHOSPHORYLATION (BY CK2) (POTENTIAL). FT MOD_RES 332 332 PHOSPHORYLATION (BY CK2) (POTENTIAL). SQ SEQUENCE 355 AA; 37000 MW; B7F9CDD7 CRC32; MEEVAVKKRG RPSKASVGGK SSTAAVAAIS PGIKKRGRPA KNKGSSGGGG QRGRPPKASK IQNDEDPEDE GEEDGDGDGS GAELANNSSP SPTKGRGRPK SSGGAGSGSG DSVKTPGSAK KRKAGRPKKH QPSDSENEDD QDEDDDGNSS IEERRPVGRP SAGSVNLNIS RTGRGLGRPK KRAVESNGDG EPQVPKKRGR PPQNKSGSGG STGYVPTGRP RGRPKANAAP VEKHEDNDDD QDDENSGEEE HSSPEKTVVA PKKRGRPSLA AGKVSKEETT KPRSRPAKNI DDDADDADSA DQGQHNSKKE SNDEDRAVDG TPTKGDGLKW NSDGENDAND GYVSDNYNDS ESVAA //