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Table 2 Local multiple alignment of the two families.

From: Local comparison of protein structures highlights cases of convergent evolution in analogous functional sites

Type

PDB code

SWISSPROT code

Residues in inverted regions

Residues in ploop

Negative charges

Ligand

Organism

Decription

Type 1

1b0uA

Q5PN38_SALPA

H211

T210

V209

V208

V207

39–46

D178

E179

ATP

Salmonella typhimurium

ATP-Binding Subunit Of The Histidine Permease

 

1l2tA

Y796_METJA

H204

T203

V202

V201

V200

38–45

D170

E171Q

ATP

Methanococcus jannaschii

Hypothetical ABC Transporter ATP-Binding Protein Mj0796

 

1q12A

MALK_ECO57

H192

T191

V190

Y189

I188

36–43

D158

E159

ATP

Escherichia coli K12

ATP-Bound E. Coli Malk, Maltose/Maltodextrin Transport

 

1g291

Q9HH32_PYRFU

H198

T197

V196

Y195

I194

36–43

D164

E165

POP

Thermococcus litoralis

Maltose Transport Protein Malk

 

1e3mA

Q8VVV1_ECOLI

H728

T727

A726

F725

L724

614–621

D693

E694

ADP

Escherichia coli

DNA Mismatch Repair Protein Muts

 

1ewqA

MUTS_THEAQ

H696

T695

A694

F693

L692

583–590

D662

E663

-

Thermus aquaticus

DNA Mismatch Repair Protein Muts

 

1fnnA

Q8ZYK1_PYRAE

H166

G165

V164

I163

V162

50–57

D131

D132

ADP

Pyrobaculum aerophilum

Cdc6P, Cell Division Control Protein 6

  

ABCD1_HUMAN

H659

T658

I657

S656

L655

507–514

D629

E630

 

Homo sapiens

adrenoleukodystrophy protein

  

CFTR_HUMAN

H1402

E1401

C1400

L1399

I1398

1244–1251

D1370

E1371

 

Homo sapiens

CFTR NBD2

ABC Type 2

1w1wA

 

L1190

S1189

I1188

V1187

I1186

33–40

D1157

E1158

ATG

Saccharomyces cerevisiae

Structural Maintenance Of Chromosome 1, Head Domain Residues 1–214, 1024–1225

 

1jj7A

Q96CP4_HUMAN

Q701

T700

I699

L698

L697

538–545

D667

D668

ADP

Homo sapiens

Peptide Transporter Tap1, C-Terminal ABC ATPase Domain

 

1ji0A

Q9X0M3_THEMA

Q196

E195

V194

L193

L192

38–45

D163

E164

ATP

Thermotoga maritima

ABC Transporter

 

1xmiA

Q99989_HUMAN

S605

T604

V603

L602

I601

458–465

D572

S573

ATP

Homo sapiens

Cystic Fibrosis Transmembrane Conductance Regulator, Nucleotide Binding Domain One

 

1r0wA

CFTR_HUMAN

S605

T604

V603

L602

I601

458–465

D572

S573

-

Mus musculus

Cystic Fibrosis Transmembrane Conductance Regulator, NDB1 Domain (Residues 389–673)

HPrK/P

1jb1A

HPRK_LACCA

H140

G141

V142

L143

V144

155–162

D178

D179

PO4

Lactobacillus casei

Hprk/P Bound To Phosphate, Hprk Protein

 

1knxA

HPRK_MYCPN

H139

G140

V141

L142

L143

154–161

D177

D178

-

Mycoplasma pneumoniae

Hpr Kinase/Phosphatase

 

1ko7A

HPRK_STAXY

H136

G137

V138

L139

V140

151–158

D174

D175

PO4

Staphylococcus xylosus

Hpr Kinase/Phosphatase

 

1kklA

HPRK_LACCA

H140

G141

V142

L143

V144

155–162

D178

D179

 

Lactobacillus casei

Hprk/P In Complex With B. Subtilis Hpr, Phosphocarrier Protein Hpr

 

1kkm

HPRK_LACCA

H140

G141

V142

L143

V144

155–162

D178

D179

PO4

Lactobacillus casei

Hprk/P In Complex With B. Subtilis P-Ser-Hpr

  1. A sequence alignment of different members of the ABC transporters and HPr K/P families is reported. Column 1 identifies the protein family. ABC transporters are grouped in two different types: a) type 1 members comprise the histidine permease of S. typhimurium and other Nucleotide Binding Domains (NBD) of the same family. They all display the same conserved residues, including the catalytic histidine; b) type 2 members display a non-histidine aligned to the histidine of the first group. In many cases, two different nucleotide binding domains (a non-histidine and a histidine) known as NBD1 and NBD2 belong to the same protein sequence, with different functions: NBD1 (without catalytic H) usually displays a regulative function, while NBD2 (with H) encodes a catalytic function. The remaining columns for each protein report: the PDB code, the Swiss-Prot code, the structurally aligned residues in the inverted region, the sequence range of the ploop, the two negatively charged structurally aligned residues, the bound ligand, the organism and a short description.