|
Name |
Accession |
Description |
Interval |
E-value |
| Biopterin_H |
pfam00351 |
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ... |
32-362 |
0e+00 |
|
Biopterin-dependent aromatic amino acid hydroxylase; This family includes phenylalanine-4-hydroxylase, the phenylketonuria disease protein.
Pssm-ID: 459776 Cd Length: 331 Bit Score: 710.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 32 PWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALY 111
Cdd:pfam00351 1 PWFPRKISDLDKCAHLVLKYGPELDADHPGFTDPVYRKRRKEIADIAFNYKHGDPIPRVEYTEEEIKTWGTVYKKLTSLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 112 KTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYT 191
Cdd:pfam00351 81 PTHACREYLENFPLLEKNCGYREDNIPQLEDVSNFLKERTGFTLRPVAGLLSARDFLAGLAFRVFHCTQYIRHHSSPMYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 192 PEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL 271
Cdd:pfam00351 161 PEPDCCHELLGHVPLLADPDFAQFSQEIGLASLGASDEDIEKLATCYWFTVEFGLCKQNGELKAYGAGLLSSFGELEYAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 272 SDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSIN 351
Cdd:pfam00351 241 SDKPEYKPFDPEVTAVQKYPITTYQPVYFVAESFEDAKEKLRKFASTIKRPFSVRYNPYTQSVEVLDSKDKLKNLLSQIK 320
|
330
....*....|.
gi 1958787735 352 SEVGILCNALQ 362
Cdd:pfam00351 321 GDLDILTDALE 331
|
|
| Phe4hydrox_tetr |
TIGR01268 |
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form ... |
31-365 |
0e+00 |
|
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form of phenylalanine-4-hydroxylase, as found in metazoans. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. It is closely related to metazoan tyrosine 3-monooxygenase and tryptophan 5-monoxygenase, and more distantly to monomeric phenylalanine-4-hydroxylases of some Gram-negative bacteria. The member of this family from Drosophila has been described as having both phenylalanine-4-hydroxylase and tryptophan 5-monoxygenase activity (. However, a Drosophila member of the tryptophan 5-monoxygenase clade has subsequently been discovered.
Pssm-ID: 130335 [Multi-domain] Cd Length: 436 Bit Score: 700.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 31 VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKAL 110
Cdd:TIGR01268 102 VPWFPRKINDIDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAFNYKHGQPIPRVEYTDEEIATWRTVFNNLTVL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 111 YKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY 190
Cdd:TIGR01268 182 YPTHACQEYNHIFPLLQQNCGFREDNIPQLEDVSQFLQDCTGFTLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHHSKPMY 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 191 TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYC 270
Cdd:TIGR01268 262 TPEPDICHELLGHVPLFADVEFAQFSQEIGLASLGAPDDYIEKLATLYWFTIEFGLCKQDGEKKAYGAGLLSSFGELQYC 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 271 LSDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSI 350
Cdd:TIGR01268 342 LSDKPEVVDFDPEVTCVTKYPITEFQPLYFLAESFEDAKEKLKSFAATIPRPFSVRYNAYTQRVEILDKKAQLQRLADDI 421
|
330
....*....|....*
gi 1958787735 351 NSEVGILCNALQKIK 365
Cdd:TIGR01268 422 RSEISILQEALGKLN 436
|
|
| eu_PheOH |
cd03347 |
Eukaryotic phenylalanine-4-hydroxylase (eu_PheOH); a member of the biopterin-dependent ... |
32-337 |
0e+00 |
|
Eukaryotic phenylalanine-4-hydroxylase (eu_PheOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic phenylalanine-4-hydroxylase (pro_PheOH), eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH catalyzes the first and rate-limiting step in the metabolism of the amino acid L-phenylalanine (L-Phe), the hydroxylation of L-Phe to L-tyrosine (L-Tyr). It uses (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) as the physiological electron donor. The catalytic activity of the tetrameric enzyme is tightly regulated by the binding of L-Phe and BH4 as well as by phosphorylation. Mutations in the human enzyme are linked to a severe variant of phenylketonuria.
Pssm-ID: 239463 Cd Length: 306 Bit Score: 649.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 32 PWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALY 111
Cdd:cd03347 1 PWFPRTIQDLDRFANQILSYGAELDADHPGFKDPVYRARRKEFADIAYNYKHGQPIPRVEYTEEEKKTWGTVFRELKSLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 112 KTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYT 191
Cdd:cd03347 81 PTHACYEYNHVFPLLEKNCGFSEDNIPQLEDVSNFLQTCTGFRLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHPSKPMYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 192 PEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL 271
Cdd:cd03347 161 PEPDICHELLGHVPLFADPSFAQFSQEIGLASLGAPDEYIEKLATVYWFTVEFGLCKQGGSIKAYGAGLLSSFGELQYCL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958787735 272 SDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVL 337
Cdd:cd03347 241 SDKPELLPFEPEKTAVTKYPITEFQPLYYVAESFEDAKEKLRNFAATIPRPFSVRYNPYTQRIEVL 306
|
|
| PhhA |
COG3186 |
Phenylalanine-4-hydroxylase [Amino acid transport and metabolism]; |
73-321 |
8.50e-82 |
|
Phenylalanine-4-hydroxylase [Amino acid transport and metabolism];
Pssm-ID: 442419 Cd Length: 279 Bit Score: 250.88 E-value: 8.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 73 QFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLekycGFREDNIPQLEDVSQFLQTCTG 152
Cdd:COG3186 7 LARDPAYLARYTDPQGYIDYTAEEHAVWRRLYRRQVALLPGRACDEYLDGLEKL----GLPADRIPQLDEVNERLKALTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 153 FRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAP--DEY 230
Cdd:COG3186 83 WRVVAVPGLIPPDAFFELLANRRFPVATFIRTPEEIDYLPEPDIFHEVFGHVPLLTNPVFADFLQAYGEAGLKASklDSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 231 IEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL-SDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAK 309
Cdd:COG3186 163 LALLARLYWFTVEFGLIGTPEGLRIYGAGILSSPGESEYALeSDEPNRIPFDLERVMRTPYRIDIYQPTYFVIDSFDQLF 242
|
250
....*....|...
gi 1958787735 310 EKVRT-FAATIPR 321
Cdd:COG3186 243 EVLEEdFAALYDR 255
|
|
| phhA |
PRK11913 |
phenylalanine 4-monooxygenase; Reviewed |
64-307 |
1.69e-76 |
|
phenylalanine 4-monooxygenase; Reviewed
Pssm-ID: 237020 Cd Length: 275 Bit Score: 237.07 E-value: 1.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 64 DPVYRARRKQFADIAYNYRHGQPIprVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLekycGFREDNIPQLEDV 143
Cdd:PRK11913 1 DAAYRARRDAGMEKAADYTADQPW--IDYTAEEHAIWQTLYERQLALLPGRACDEFLEGLEAL----GLPKDRIPQLDEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 144 SQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLAS 223
Cdd:PRK11913 75 NRVLQAATGWQVVPVPGLIPFDVFFELLANRRFPVATFIRRPEELDYLQEPDIFHDVFGHVPLLTNPVFADFMQAYGKLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 224 LGAPDEY-IEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL-SDKPKLLPLELEKIACQEYSVTEFQPLYYV 301
Cdd:PRK11913 155 LRASKEGrLEFLARLYWFTVEFGLIRTPGGLRIYGAGILSSPGETLYALeSDSPNRRPFDLERVMRTPYRIDIFQPTYFV 234
|
....*.
gi 1958787735 302 AESFSD 307
Cdd:PRK11913 235 IDSFEQ 240
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Biopterin_H |
pfam00351 |
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ... |
32-362 |
0e+00 |
|
Biopterin-dependent aromatic amino acid hydroxylase; This family includes phenylalanine-4-hydroxylase, the phenylketonuria disease protein.
Pssm-ID: 459776 Cd Length: 331 Bit Score: 710.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 32 PWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALY 111
Cdd:pfam00351 1 PWFPRKISDLDKCAHLVLKYGPELDADHPGFTDPVYRKRRKEIADIAFNYKHGDPIPRVEYTEEEIKTWGTVYKKLTSLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 112 KTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYT 191
Cdd:pfam00351 81 PTHACREYLENFPLLEKNCGYREDNIPQLEDVSNFLKERTGFTLRPVAGLLSARDFLAGLAFRVFHCTQYIRHHSSPMYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 192 PEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL 271
Cdd:pfam00351 161 PEPDCCHELLGHVPLLADPDFAQFSQEIGLASLGASDEDIEKLATCYWFTVEFGLCKQNGELKAYGAGLLSSFGELEYAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 272 SDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSIN 351
Cdd:pfam00351 241 SDKPEYKPFDPEVTAVQKYPITTYQPVYFVAESFEDAKEKLRKFASTIKRPFSVRYNPYTQSVEVLDSKDKLKNLLSQIK 320
|
330
....*....|.
gi 1958787735 352 SEVGILCNALQ 362
Cdd:pfam00351 321 GDLDILTDALE 331
|
|
| Phe4hydrox_tetr |
TIGR01268 |
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form ... |
31-365 |
0e+00 |
|
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form of phenylalanine-4-hydroxylase, as found in metazoans. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. It is closely related to metazoan tyrosine 3-monooxygenase and tryptophan 5-monoxygenase, and more distantly to monomeric phenylalanine-4-hydroxylases of some Gram-negative bacteria. The member of this family from Drosophila has been described as having both phenylalanine-4-hydroxylase and tryptophan 5-monoxygenase activity (. However, a Drosophila member of the tryptophan 5-monoxygenase clade has subsequently been discovered.
Pssm-ID: 130335 [Multi-domain] Cd Length: 436 Bit Score: 700.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 31 VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKAL 110
Cdd:TIGR01268 102 VPWFPRKINDIDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAFNYKHGQPIPRVEYTDEEIATWRTVFNNLTVL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 111 YKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY 190
Cdd:TIGR01268 182 YPTHACQEYNHIFPLLQQNCGFREDNIPQLEDVSQFLQDCTGFTLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHHSKPMY 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 191 TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYC 270
Cdd:TIGR01268 262 TPEPDICHELLGHVPLFADVEFAQFSQEIGLASLGAPDDYIEKLATLYWFTIEFGLCKQDGEKKAYGAGLLSSFGELQYC 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 271 LSDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSI 350
Cdd:TIGR01268 342 LSDKPEVVDFDPEVTCVTKYPITEFQPLYFLAESFEDAKEKLKSFAATIPRPFSVRYNAYTQRVEILDKKAQLQRLADDI 421
|
330
....*....|....*
gi 1958787735 351 NSEVGILCNALQKIK 365
Cdd:TIGR01268 422 RSEISILQEALGKLN 436
|
|
| eu_PheOH |
cd03347 |
Eukaryotic phenylalanine-4-hydroxylase (eu_PheOH); a member of the biopterin-dependent ... |
32-337 |
0e+00 |
|
Eukaryotic phenylalanine-4-hydroxylase (eu_PheOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic phenylalanine-4-hydroxylase (pro_PheOH), eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH catalyzes the first and rate-limiting step in the metabolism of the amino acid L-phenylalanine (L-Phe), the hydroxylation of L-Phe to L-tyrosine (L-Tyr). It uses (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) as the physiological electron donor. The catalytic activity of the tetrameric enzyme is tightly regulated by the binding of L-Phe and BH4 as well as by phosphorylation. Mutations in the human enzyme are linked to a severe variant of phenylketonuria.
Pssm-ID: 239463 Cd Length: 306 Bit Score: 649.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 32 PWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALY 111
Cdd:cd03347 1 PWFPRTIQDLDRFANQILSYGAELDADHPGFKDPVYRARRKEFADIAYNYKHGQPIPRVEYTEEEKKTWGTVFRELKSLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 112 KTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYT 191
Cdd:cd03347 81 PTHACYEYNHVFPLLEKNCGFSEDNIPQLEDVSNFLQTCTGFRLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHPSKPMYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 192 PEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL 271
Cdd:cd03347 161 PEPDICHELLGHVPLFADPSFAQFSQEIGLASLGAPDEYIEKLATVYWFTVEFGLCKQGGSIKAYGAGLLSSFGELQYCL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958787735 272 SDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVL 337
Cdd:cd03347 241 SDKPELLPFEPEKTAVTKYPITEFQPLYYVAESFEDAKEKLRNFAATIPRPFSVRYNPYTQRIEVL 306
|
|
| Trp_5_monoox |
TIGR01270 |
tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a ... |
31-364 |
0e+00 |
|
tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tyrosine 3-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130337 [Multi-domain] Cd Length: 464 Bit Score: 524.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 31 VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKAL 110
Cdd:TIGR01270 129 VPWFPKKISDLDKCANRVLMYGSELDADHPGFKDTEYRKRRMMFADLALNYKHGEPIPRVEYTEEERKTWGTIYRELRRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 111 YKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY 190
Cdd:TIGR01270 209 YKTHACKEFLDNLPLLEKYCGYREDNIPQLEDVSKFLKAKTGFRLRPVAGYLSARDFLSGLAFRVFHCTQYVRHSADPFY 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 191 TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDS-IKAYGAGLLSSFGELQY 269
Cdd:TIGR01270 289 TPEPDTCHELLGHMPLLADPSFAQFSQEIGLASLGASEEDIKKLATLYFFTIEFGLCKQDDEqFKVYGAGLLSSVAELQH 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 270 CLSDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADS 349
Cdd:TIGR01270 369 ALSGSAKIKPFDPDRVCEQECLITTFQNAYFYTRSFEEAKEKMREFTNTIKRPFGVRYNPYTESVEVLKNSKSITLAVNE 448
|
330
....*....|....*
gi 1958787735 350 INSEVGILCNALQKI 364
Cdd:TIGR01270 449 LRSDLNLVAGALHKI 463
|
|
| eu_TyrOH |
cd03345 |
Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino ... |
33-330 |
0e+00 |
|
Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tryptophan hydroxylase (TrpOH). TyrOH catalyzes the conversion of tyrosine to L-dihydroxyphenylalanine (L-DOPA), the rate-limiting step in the biosynthesis of the catecholamines dopamine, noradrenaline, and adrenaline.
Pssm-ID: 239461 Cd Length: 298 Bit Score: 505.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 33 WFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYK 112
Cdd:cd03345 1 WFPRHISELDKCHHLVTKYEPDLDLDHPGFSDKVYRERRKLIAEIAFQYKHGDPIPRVEYTAEEIATWKEVYKTLKDLHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 113 THACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTP 192
Cdd:cd03345 81 THACKEYLDAFQLLEKECGYSEDRIPQLEDVSEFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 193 EPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCLS 272
Cdd:cd03345 161 EPDCCHELLGHVPMLADPTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKENGELKAYGAGLLSSYGELLHALS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958787735 273 DKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPY 330
Cdd:cd03345 241 DEPEHRPFDPAATAVQPYQDQTYQPIYFVSESFSDAKDKLRNYASTMKRPFSVRYDPY 298
|
|
| eu_TrpOH |
cd03346 |
Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino ... |
32-318 |
2.92e-172 |
|
Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tyrosine hydroxylase (TyrOH). TrpOH oxidizes L-tryptophan to 5-hydroxy-L-tryptophan, the rate-limiting step in the biosynthesis of serotonin (5-hydroxytryptamine), a widely distributed hormone and neurotransmitter.
Pssm-ID: 239462 Cd Length: 287 Bit Score: 480.84 E-value: 2.92e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 32 PWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALY 111
Cdd:cd03346 1 PWFPKKISDLDKCANRVLMYGSELDADHPGFKDNVYRKRRKYFADVAMNYKHGDPIPRVEYTEEEIKTWGTVYRELNRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 112 KTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYT 191
Cdd:cd03346 81 PTHACREYLKNLPLLEKHCGYREDNIPQLEDVSRFLKERTGFTIRPVAGYLSPRDFLAGLAFRVFHCTQYVRHSSDPFYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 192 PEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL 271
Cdd:cd03346 161 PEPDTCHELLGHVPLLADPSFAQFSQEIGLASLGASDEDIQKLATCYFFTVEFGLCKQDGQLKVYGAGLLSSIGELKHAL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1958787735 272 SDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAAT 318
Cdd:cd03346 241 SGEAKVKPFDPKVTCKQECLITTFQEAYFVSESFEEAKEKMREFAKT 287
|
|
| Tyr_3_monoox |
TIGR01269 |
tyrosine 3-monooxygenase, tetrameric; This model describes tyrosine 3-monooxygenase, a member ... |
32-365 |
2.95e-171 |
|
tyrosine 3-monooxygenase, tetrameric; This model describes tyrosine 3-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tryptophan 5-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria.
Pssm-ID: 130336 [Multi-domain] Cd Length: 457 Bit Score: 485.21 E-value: 2.95e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 32 PWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALY 111
Cdd:TIGR01269 124 DWFPKHISELDKCQHLLTKFQPDLDTDHPGFHDKVYRQRREAIAEIAFQYKYGDPIPEVEYTKEEIETWRLVFTTMKDLH 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 112 KTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYT 191
Cdd:TIGR01269 204 ASHACREYIDAFQLLEKYCNYNSESIPQLQTISEFLHRTTGFRLRPVAGLLSARDFLASLAFRVFQCTQYIRHHSSPMHT 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 192 PEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL 271
Cdd:TIGR01269 284 PEPDCIHELLGHMPMLADRQFAQFSQEIGLASLGASEEEIEKLSTLYWFTVEFGLCKENGETKAYGAGLLSSYGELEHAF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 272 SDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNTQQLKILADSIN 351
Cdd:TIGR01269 364 SDLSEKRPFNPNDAAVQPYQDQGYQKIYFVTESFEDAKRKLRNYINTSGRPFIVRFDPITETVEVLDRFSKRKELLKHVK 443
|
330
....*....|....
gi 1958787735 352 SEVGILCNALQKIK 365
Cdd:TIGR01269 444 EEIGQLTTALNHLN 457
|
|
| arom_aa_hydroxylase |
cd00361 |
Biopterin-dependent aromatic amino acid hydroxylase; a family of non-heme, iron(II)-dependent ... |
88-311 |
2.32e-133 |
|
Biopterin-dependent aromatic amino acid hydroxylase; a family of non-heme, iron(II)-dependent enzymes that includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH), eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH converts L-phenylalanine to L-tyrosine, an important step in phenylalanine catabolism and neurotransmitter biosynthesis, and is linked to a severe variant of phenylketonuria in humans. TyrOH and TrpOH are involved in the biosynthesis of catecholamine and serotonin, respectively. The eukaryotic enzymes are all homotetramers.
Pssm-ID: 238215 Cd Length: 221 Bit Score: 379.59 E-value: 2.32e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 88 PRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLekycGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDF 167
Cdd:cd00361 1 PRVDYTEEEHATWRTLYRRLKKLLPTHACREYLEGLELL----GLPEDRIPQLEDVSEFLKALTGWTLVPVAGLISPRDF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 168 LGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPD-EYIEKLATIYWFTVEFGL 246
Cdd:cd00361 77 FALLAFRVFPVTQYIRHPEEPDYTPEPDIFHELFGHVPLLADPSFADFSQEYGLASLGASDlEEIEKLARLYWFTVEFGL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958787735 247 CKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAKEK 311
Cdd:cd00361 157 IKEDGELKAYGAGLLSSYGELQHALSDKPKRIPFDPERVARTPYDITSFQPTYFVIESFEQLKEK 221
|
|
| PhhA |
COG3186 |
Phenylalanine-4-hydroxylase [Amino acid transport and metabolism]; |
73-321 |
8.50e-82 |
|
Phenylalanine-4-hydroxylase [Amino acid transport and metabolism];
Pssm-ID: 442419 Cd Length: 279 Bit Score: 250.88 E-value: 8.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 73 QFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLekycGFREDNIPQLEDVSQFLQTCTG 152
Cdd:COG3186 7 LARDPAYLARYTDPQGYIDYTAEEHAVWRRLYRRQVALLPGRACDEYLDGLEKL----GLPADRIPQLDEVNERLKALTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 153 FRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAP--DEY 230
Cdd:COG3186 83 WRVVAVPGLIPPDAFFELLANRRFPVATFIRTPEEIDYLPEPDIFHEVFGHVPLLTNPVFADFLQAYGEAGLKASklDSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 231 IEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL-SDKPKLLPLELEKIACQEYSVTEFQPLYYVAESFSDAK 309
Cdd:COG3186 163 LALLARLYWFTVEFGLIGTPEGLRIYGAGILSSPGESEYALeSDEPNRIPFDLERVMRTPYRIDIYQPTYFVIDSFDQLF 242
|
250
....*....|...
gi 1958787735 310 EKVRT-FAATIPR 321
Cdd:COG3186 243 EVLEEdFAALYDR 255
|
|
| phhA |
PRK11913 |
phenylalanine 4-monooxygenase; Reviewed |
64-307 |
1.69e-76 |
|
phenylalanine 4-monooxygenase; Reviewed
Pssm-ID: 237020 Cd Length: 275 Bit Score: 237.07 E-value: 1.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 64 DPVYRARRKQFADIAYNYRHGQPIprVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLekycGFREDNIPQLEDV 143
Cdd:PRK11913 1 DAAYRARRDAGMEKAADYTADQPW--IDYTAEEHAIWQTLYERQLALLPGRACDEFLEGLEAL----GLPKDRIPQLDEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 144 SQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLAS 223
Cdd:PRK11913 75 NRVLQAATGWQVVPVPGLIPFDVFFELLANRRFPVATFIRRPEELDYLQEPDIFHDVFGHVPLLTNPVFADFMQAYGKLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 224 LGAPDEY-IEKLATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCL-SDKPKLLPLELEKIACQEYSVTEFQPLYYV 301
Cdd:PRK11913 155 LRASKEGrLEFLARLYWFTVEFGLIRTPGGLRIYGAGILSSPGETLYALeSDSPNRRPFDLERVMRTPYRIDIFQPTYFV 234
|
....*.
gi 1958787735 302 AESFSD 307
Cdd:PRK11913 235 IDSFEQ 240
|
|
| pro_PheOH |
cd03348 |
Prokaryotic phenylalanine-4-hydroxylase (pro_PheOH); a member of the biopterin-dependent ... |
82-307 |
1.65e-55 |
|
Prokaryotic phenylalanine-4-hydroxylase (pro_PheOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes the eukaryotic proteins, phenylalanine-4-hydroxylase (eu_PheOH), tyrosine hydroxylase (TyrOH) and tryptophan hydroxylase (TrpOH). PheOH catalyzes the hydroxylation of L-Phe to L-tyrosine (L-Tyr). It uses (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) as the physiological electron donor.
Pssm-ID: 239464 Cd Length: 228 Bit Score: 181.31 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 82 RHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLekycGFREDNIPQLEDVSQFLQTCTGFRLRPVAGL 161
Cdd:cd03348 1 DVPDEQGQIDYTPEEHAVWRTLYERQAKLLPGRACDAFLEGLEKL----GLPTDRIPDFADVSERLKAATGWTVVAVPGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 162 LSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAP-DEYIEKLATIYWF 240
Cdd:cd03348 77 IPDDEFFEHLANRRFPVTNFIRRPEELDYLQEPDIFHDIFGHVPMLTNPVFADFMQAYGKGGLKATgLEDRALLARLYWY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958787735 241 TVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDK-PKLLPLELEKIACQEYSVTEFQPLYYVAESFSD 307
Cdd:cd03348 157 TVEFGLIQEPGGLRIYGAGILSSPGETLYALESPdPNRIPFDLERVMRTPYRIDSFQPTYFVIDSFEQ 224
|
|
| Phe4hydrox_mono |
TIGR01267 |
phenylalanine-4-hydroxylase, monomeric form; This model describes the smaller, monomeric form ... |
86-305 |
2.39e-44 |
|
phenylalanine-4-hydroxylase, monomeric form; This model describes the smaller, monomeric form of phenylalanine-4-hydroxylase, as found in a small number of Gram-negative bacteria. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. This family is of biopterin and metal-dependent hydroxylases is related to a family of longer, multimeric aromatic amino acid hydroxylases that have additional N-terminal regulatory sequences. These include tyrosine 3-monooxygenase, phenylalanine-4-hydroxylase, and tryptophan 5-monoxygenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130334 Cd Length: 248 Bit Score: 153.10 E-value: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 86 PIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHnhiFPLLEKYcGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSR 165
Cdd:TIGR01267 5 DQGFDHYSEEEHAVWNTLITRQLKLIEGRACQEY---LDGIEQL-GLPHDRIPDFDEINRKLQATTGWRIAAVPGLIPFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 166 DFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGA-PDEYIEKLATIYWFTVEF 244
Cdd:TIGR01267 81 TFFEHLANRRFPVTTWLRTPEELDYLQEPDIFHDIFGHVPLLTNPVFADFTHTYGKLGLKAsALGRVEMLARLYWYTIEF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958787735 245 GLCKEGDSIKAYGAGLLSSFGELQYCL-SDKPKLLPLELEKIACQEYSVTEFQPLYYVAESF 305
Cdd:TIGR01267 161 GLVETDQGKRIYGAGILSSPKETVYSLeSDEPLHVAFDLLEAMRTPYRIDIFQPLYFVLPSF 222
|
|
| PRK14056 |
PRK14056 |
aromatic amino acid hydroxylase; |
91-318 |
1.56e-29 |
|
aromatic amino acid hydroxylase;
Pssm-ID: 237598 Cd Length: 578 Bit Score: 119.39 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 91 EYTEEEKQTWGTVFRTLKALYKTHAcyeHNHIFPLLEKyCGFREDNIPQLEDVSQFLQTcTGFRLRPVAGLLSSRDFLGG 170
Cdd:PRK14056 20 QYTPVDHAVWRYVMRQNHSFLKDVA---HPAYLNGLQS-TGINIERIPKVEEMNECLAE-IGWGAVAVDGFIPPVAFFEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 171 LAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQ---EIGLASL----------------------G 225
Cdd:PRK14056 95 QGHGVLPIATDIRKVENIEYTPAPDIIHEAAGHAPILADPTYAEYLRrfgEIGAKAIsskedhdvfeavrtlsivkespT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 226 APDEYIEK--------------------LATIYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKI 285
Cdd:PRK14056 175 STPEEVAAaenrviekqnlvsglseaeqISRLFWWTVEYGLIGTLDNPKIYGAGLLSSVGESKHCLTDAVEKVPFSIEAC 254
|
250 260 270
....*....|....*....|....*....|...
gi 1958787735 286 ACQEYSVTEFQPLYYVAESFSDAKEKVRTFAAT 318
Cdd:PRK14056 255 TSTTYDITKMQPQLFVCPDFEELSEVLEEFAET 287
|
|
| PRK14055 |
PRK14055 |
aromatic amino acid hydroxylase; Provisional |
141-310 |
1.24e-16 |
|
aromatic amino acid hydroxylase; Provisional
Pssm-ID: 172547 [Multi-domain] Cd Length: 362 Bit Score: 80.10 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 141 EDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIG 220
Cdd:PRK14055 143 QAVIKFFELETHFSYYPVSGFVAPHQYLSLLQDRYFPIASVMRTLDKDNFSLTPDLIHDLLGHVPWLLHPSFSEFFINMG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787735 221 ---------LASLGAPDEYIEKLAT-------IYWFTVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEK 284
Cdd:PRK14055 223 rlftkviekVQALPSKKQRIQTLQSnliaivrCFWFTVESGLIENHEGRKAYGAVLISSPQELGHAFIDNVRVLPLELDQ 302
|
170 180
....*....|....*....|....*.
gi 1958787735 285 IACQEYSVTEFQPLYYVAESFSDAKE 310
Cdd:PRK14055 303 IIRLPFNTSTPQETLFSIRHFDELVE 328
|
|
| |
