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Table 3 Residues showing evidence of functional divergence in SDP and DIVERGE2 analyses

From: Module evolution and substrate specificity of fungal nonribosomal peptide synthetases involved in siderophore biosynthesis

Position 1AMU_A

Feature

Fragments (Fig. 7)

SDP

Type II

Type I

Position 1AMU_A

Feature

Fragments (Fig. 7)

SDP

Type II

Type I

200

   

.95

 

270

    

.96

201

   

.78

 

271

     

202

     

272

     

203

α-Helix 1

   

.95

273

     

204

D203-S217

  

.85

.95

274

  

5.41

 

.75

205

    

.90

275

β-Strand 2

  

.95

 

206

  

6.56

.95

 

276

T275-P280

 

6.26

.88

 

207

    

.80

277

  

6.44

  

208

   

.77

.87

278

 

x fragment 2

9.43

.90

.87

209

     

279

 

T278-P280

  

.97

210

     

280

 

x

   

211

  

5.5

  

281

     

212

    

.94

282

  

7.2

  

213

    

.94

283

  

6.54

 

.93

214

  

10.7

.95

 

284

    

.92

215

     

285

     

216

     

286

     

217

     

287

     

218

     

288

     

219

     

289

  

6.68

  

220

     

290

     

221

     

291

     

222

     

292

     

223

     

293

     

224

β-Strand 1

    

294

     

225

D224-F229

    

295

     

226

  

9.16

  

296

β-Strand 3

   

.81

227

     

297

Q296-A301

   

.80

228

     

298

    

.98

229

 

x fragment 1

   

299

 

x fragment 3

7.88

 

.75

230

 

x F229-M243

 

.90

 

300

 

I299-A304

  

.84

231

  

6.76

.74

 

301

 

x

10.82

.95

.74

232

  

8.92

.75

 

302

   

.75

 

233

   

.95

 

303

     

234

     

304

  

5.94

 

.94

235

α-Helix 2

x

   

305

     

236

D235-L245

x

   

306

  

6.71

.95

 

237

    

.90

307

    

.97

238

     

308

   

.70

.81

239

 

x

8.59

 

.95

309

    

.77

240

 

x

   

310

  

7.02

 

.98

241

  

6.00

.95

 

311

     

242

     

312

    

.97

243

 

x

5.64

 

.88

313

  

8.31

  

244

  

5.58

 

.94

314

     

245

     

315

     

246

    

.95

316

     

247

   

.87

.99

317

β-Strand 4

    

248

    

.85

318

V317-Y323

    

249

    

.98

319

     

250

    

.98

320

 

x fragment 4

  

.78

251

    

.99

321

 

I320-C331

6.46

.76

 

252

  

5.99

.85

.93

322

 

x

8.25

.90

.90

253

     

323

     

254

   

.70

.93

324

     

255

     

325

     

256

   

.73 C

 

326

 

x

5.98

  

257

    

.97

327

   

.80

 

258

     

328

     

259

  

5.47

  

329

   

.95

 

260

     

330

 

x

 

.95

.71

261

     

331

 

x

12.46

.80

.94

262

     

332

β-Strand 5

   

.90

263

     

333

A332-V336

    

264

     

334

     

265

     

335

     

266

     

336

     

267

           

268

     

517

 

x

   

269

           
  1. Left to right columns: 1) positions in 1AMU_A, bold are sites corresponding to the 10 or 13 AA code. 2) Loops and strands in 1AMU_A (Fig. 7A). 3) Fragments defining the substrate binding site; 'x' indicates key sites identified by structural modeling (Fig. 7C, Table 2). 4) Sites identified using the SDP algorithm showing significant Z-scores. 5), 6) Sites identified using tests for Type II and Type I functional divergence, respectively. The highest posterior probability for sites above a .70 cutoff for any of the pair-wise comparisons with a significant ΘI and Θii value are shown. All amino acid changes for Type II divergence are radical, indicating a change in amino acid properties; the single exception is indicated with 'C'.