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<a name="input.1"></a><h3>Input files for usage example </h3>'tsw:amir_pseae' is a sequence entry in the example protein database 'tsw'<p><p><h3>Database entry: tsw:amir_pseae</h3><table width="90%"><tr><td bgcolor="#FFCCFF"><pre>ID AMIR_PSEAE STANDARD; PRT; 196 AA.AC P10932;DT 01-JUL-1989 (Rel. 11, Created)DT 01-JUL-1989 (Rel. 11, Last sequence update)DT 15-DEC-1998 (Rel. 37, Last annotation update)DE ALIPHATIC AMIDASE REGULATOR.GN AMIR.OS Pseudomonas aeruginosa.OC Bacteria; Proteobacteria; gamma subdivision; Pseudomonas group;OC Pseudomonas.RN [1]RP SEQUENCE FROM N.A.RC STRAIN=PAC;RX MEDLINE; 89211409.RA LOWE N., RICE P.M., DREW R.E.;RT "Nucleotide sequence of the aliphatic amidase regulator gene (amiR)RT of Pseudomonas aeruginosa.";RL FEBS Lett. 246:39-43(1989).RN [2]RP CHARACTERIZATION.RX MEDLINE; 95286483.RA WILSON S.A., DREW R.E.;RT "Transcriptional analysis of the amidase operon from PseudomonasRT aeruginosa.";RL J. Bacteriol. 177:3052-3057(1995).CC -!- FUNCTION: POSITIVE CONTROLLING ELEMENT OF AMIE, THE GENE FORCC ALIPHATIC AMIDASE. ACTS AS A TRANSCRIPTIONAL ANTITERMINATIONCC FACTOR. IT IS THOUGHT TO ALLOW RNA POLYMERASE READ THROUGH A RHO-CC INDEPENDENT TRANSCRIPTION TERMINATOR BETWEEN THE AMIE PROMOTER ANDCC GENE.CC --------------------------------------------------------------------------CC This SWISS-PROT entry is copyright. It is produced through a collaborationCC between the Swiss Institute of Bioinformatics and the EMBL outstation -CC the European Bioinformatics Institute. There are no restrictions on itsCC use by non-profit institutions as long as its content is in no wayCC modified and this statement is not removed. Usage by and for commercialCC entities requires a license agreement (See http://www.isb-sib.ch/announce/CC or send an email to license@isb-sib.ch).CC --------------------------------------------------------------------------DR EMBL; X13776; CAA32023.1; -.DR PIR; S03884; S03884.KW Transcription regulation; Activator.SQ SEQUENCE 196 AA; 21776 MW; 560A8AE3 CRC32; MSANSLLGSL RELQVLVLNP PGEVSDALVL QLIRIGCSVR QCWPPPEAFD VPVDVVFTSI FQNGHHDEIA ALLAAGTPRT TLVALVEYES PAVLSQIIEL ECHGVITQPL DAHRVLPVLV SARRISEEMA KLKQKTEQLQ DRIAGQARIN QAKVLLMQRH GWDEREAHQH LSREAMKRRE PILKIAQELL GNEPSA//</pre></td></tr></table><p><p><h3>Database entry: tsw:flav_nossm</h3><table width="90%"><tr><td bgcolor="#FFCCFF"><pre>ID FLAV_NOSSM STANDARD; PRT; 35 AA.AC P35707;DT 01-JUN-1994 (Rel. 29, Created)DT 01-JUN-1994 (Rel. 29, Last sequence update)DT 15-DEC-1998 (Rel. 37, Last annotation update)DE FLAVODOXIN (FRAGMENT).OS Nostoc sp. (strain MAC).OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.RN [1]RP SEQUENCE.RA Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.;RT "N-terminal amino acid sequences of flavodoxins from Chondrus crispusRT and Nostoc strain MAC.";RL Phytochemistry 25:2113-2115(1986).CC -!- FUNCTION: LOW-POTENTIAL ELECTRON DONOR TO A NUMBER OF REDOXCC ENZYMES.CC -!- COFACTOR: FMN.CC -!- SIMILARITY: BELONGS TO THE FLAVODOXIN FAMILY.DR PIR; PA0004; PA0004.DR HSSP; P11241; 1RCF.DR INTERPRO; IPR001226; -.DR PFAM; PF00258; flavodoxin; 1.DR PROSITE; PS00201; FLAVODOXIN; 1.KW Electron transport; Flavoprotein; FMN.FT NON_TER 35 35SQ SEQUENCE 35 AA; 3820 MW; B6EEB5CA7A45DDA6 CRC64; SKKIGLFYGT ZTGKTESVAE IIDEFGDEVV TLDID//</pre></td></tr></table><p>
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