|
Name |
Accession |
Description |
Interval |
E-value |
| CPSase_L_D2 super family |
cl17255 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
193-395 |
3.83e-157 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
The actual alignment was detected with superfamily member pfam02750:
Pssm-ID: 473076 Cd Length: 203 Bit Score: 447.58 E-value: 3.83e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 193 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITS 272
Cdd:pfam02750 1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 273 VVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVK 352
Cdd:pfam02750 81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034629533 353 AVHSKDGRDYIIEVMDSSMPLIGEHVEEDRQLMADLVVSKMSQ 395
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
|
|
| Synapsin |
pfam02078 |
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain. |
92-191 |
1.09e-58 |
|
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
:
Pssm-ID: 460438 Cd Length: 97 Bit Score: 190.55 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVsRSFKPDFILVRQHAYsm 171
Cdd:pfam02078 1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVV-RSFRPDFVLVRQHAR-- 77
|
90 100
....*....|....*....|
gi 1034629533 172 ALGEDYRSLVIGLQYGGLPA 191
Cdd:pfam02078 78 DAGEDYRNLLLGLQYGGVPS 97
|
|
| Synapsin_N super family |
cl11206 |
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ... |
1-29 |
2.46e-12 |
|
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at position 9 or 10 which is a phosphorylation site. The domain appears to be the part of the molecule that binds to calmodulin.
The actual alignment was detected with superfamily member pfam10581:
Pssm-ID: 463155 Cd Length: 32 Bit Score: 61.35 E-value: 2.46e-12
10 20
....*....|....*....|....*....
gi 1034629533 1 MNFLRRRLSDSSFMANLPNGYMTDLQRPD 29
Cdd:pfam10581 1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
|
|
| PRK07764 super family |
cl35613 |
DNA polymerase III subunits gamma and tau; Validated |
394-536 |
1.87e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
The actual alignment was detected with superfamily member PRK07764:
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.67 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 394 SQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQS 473
Cdd:PRK07764 605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629533 474 GSPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHL 536
Cdd:PRK07764 685 PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Synapsin_C |
pfam02750 |
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ... |
193-395 |
3.83e-157 |
|
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function unknown.
Pssm-ID: 308403 Cd Length: 203 Bit Score: 447.58 E-value: 3.83e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 193 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITS 272
Cdd:pfam02750 1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 273 VVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVK 352
Cdd:pfam02750 81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034629533 353 AVHSKDGRDYIIEVMDSSMPLIGEHVEEDRQLMADLVVSKMSQ 395
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
|
|
| Synapsin |
pfam02078 |
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain. |
92-191 |
1.09e-58 |
|
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
Pssm-ID: 460438 Cd Length: 97 Bit Score: 190.55 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVsRSFKPDFILVRQHAYsm 171
Cdd:pfam02078 1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVV-RSFRPDFVLVRQHAR-- 77
|
90 100
....*....|....*....|
gi 1034629533 172 ALGEDYRSLVIGLQYGGLPA 191
Cdd:pfam02078 78 DAGEDYRNLLLGLQYGGVPS 97
|
|
| Synapsin_N |
pfam10581 |
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ... |
1-29 |
2.46e-12 |
|
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at position 9 or 10 which is a phosphorylation site. The domain appears to be the part of the molecule that binds to calmodulin.
Pssm-ID: 463155 Cd Length: 32 Bit Score: 61.35 E-value: 2.46e-12
10 20
....*....|....*....|....*....
gi 1034629533 1 MNFLRRRLSDSSFMANLPNGYMTDLQRPD 29
Cdd:pfam10581 1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
394-536 |
1.87e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.67 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 394 SQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQS 473
Cdd:PRK07764 605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629533 474 GSPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHL 536
Cdd:PRK07764 685 PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
447-558 |
2.08e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 41.29 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 447 SPQPQRSGSPSQ-QRLSPQGQQP-LSPQSGSPQQQRSPGSPQLSRASSG------SSPNQASKPGATLASQPRPPVQGRS 518
Cdd:pfam03154 150 SPQDNESDSDSSaQQQILQTQPPvLQAQSGAASPPSPPPPGTTQAATAGptpsapSVPPQGSPATSQPPNQTQSTAAPHT 229
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034629533 519 TSQQGEESKKPAPPHPHlNKSQSLTNSLSTSDTSQRGTPS 558
Cdd:pfam03154 230 LIQQTPTLHPQRLPSPH-PPLQPMTQPPPPSQVSPQPLPQ 268
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
158-375 |
4.84e-03 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 39.25 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 158 KPDFILVRQHAYSMALgedyrSLVIGLQYGGLPAVNSlYSVYNFCSKPWVFSQLIkifhslgpEKFPLVEQTFFPNHKP- 236
Cdd:TIGR00768 48 ELDVVIVRIVSMFRGL-----AVLRYLESLGVPVINS-SDAILNAGDKFLSHQLL--------AKAGIPLPRTGLAGSPe 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 237 --MVTAPH--FPVVVKLGHAHAGMGKIKVENQLDFQDITSVVAMAKTYATTeaFIDSKY-------DIRIQKIGSNYKAY 305
Cdd:TIGR00768 114 eaLKLIEEigFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQNL--FLVQEYikkpggrDIRVFVVGDEVVAA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629533 306 MRTSISGNWKANT---GSAMLEQVAMTERyRLWVDSCSEMfgGLDICAVKAVHSKDGrdYIIEVMDSSMPLIG 375
Cdd:TIGR00768 192 IYRITSGHWRSNLargGKAEPCSLTEEIE-ELAIKAAKAL--GLDVAGVDLLESEDG--LLVNEVNANPEFKN 259
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
91-366 |
5.87e-03 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 39.15 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 91 PRILLVIDDAHTDWSKYFhgkkvngeieirveQAEFSELNLAAYV--TGGCMVDMQVVRNGTKVVSRSfKPDFILVRQHA 168
Cdd:COG0189 2 MKIAILTDPPDKDSTKAL--------------IEAAQRRGHEVEVidPDDLTLDLGRAPELYRGEDLS-EFDAVLPRIDP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 169 YSMALGedyrsLVIGLQYGGLPAVNSLYSVYNFCSKpwVFSQLIKIFHSLG-PEkfplveqTFFPNHKPMVTAPH----F 243
Cdd:COG0189 67 PFYGLA-----LLRQLEAAGVPVVNDPEAIRRARDK--LFTLQLLARAGIPvPP-------TLVTRDPDDLRAFLeelgG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 244 PVVVKLGHAHAGMGKIKVENQldfQDITSVVAMAKTYATTEA----FIDSK--YDIRI-----QKIGsnykAYMRTSISG 312
Cdd:COG0189 133 PVVLKPLDGSGGRGVFLVEDE---DALESILEALTELGSEPVlvqeFIPEEdgRDIRVlvvggEPVA----AIRRIPAEG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629533 313 NWKANT---GSAmlEQVAMTERYRLWVDSCSEMFgGLDICAVKAVHSKDGRdYIIEV 366
Cdd:COG0189 206 EFRTNLargGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-LVLEV 258
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Synapsin_C |
pfam02750 |
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ... |
193-395 |
3.83e-157 |
|
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function unknown.
Pssm-ID: 308403 Cd Length: 203 Bit Score: 447.58 E-value: 3.83e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 193 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITS 272
Cdd:pfam02750 1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 273 VVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVK 352
Cdd:pfam02750 81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034629533 353 AVHSKDGRDYIIEVMDSSMPLIGEHVEEDRQLMADLVVSKMSQ 395
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
|
|
| Synapsin |
pfam02078 |
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain. |
92-191 |
1.09e-58 |
|
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
Pssm-ID: 460438 Cd Length: 97 Bit Score: 190.55 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVsRSFKPDFILVRQHAYsm 171
Cdd:pfam02078 1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVV-RSFRPDFVLVRQHAR-- 77
|
90 100
....*....|....*....|
gi 1034629533 172 ALGEDYRSLVIGLQYGGLPA 191
Cdd:pfam02078 78 DAGEDYRNLLLGLQYGGVPS 97
|
|
| Synapsin_N |
pfam10581 |
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ... |
1-29 |
2.46e-12 |
|
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at position 9 or 10 which is a phosphorylation site. The domain appears to be the part of the molecule that binds to calmodulin.
Pssm-ID: 463155 Cd Length: 32 Bit Score: 61.35 E-value: 2.46e-12
10 20
....*....|....*....|....*....
gi 1034629533 1 MNFLRRRLSDSSFMANLPNGYMTDLQRPD 29
Cdd:pfam10581 1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
394-536 |
1.87e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.67 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 394 SQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQS 473
Cdd:PRK07764 605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629533 474 GSPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHL 536
Cdd:PRK07764 685 PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
409-537 |
2.52e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.39 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 409 PWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSPQQQRSPGSPQLS 488
Cdd:PRK10263 740 PHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ 819
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034629533 489 RASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEES--KKPAPPHPHLN 537
Cdd:PRK10263 820 PQQPVAPQPQYQQPQQPVAPQPQDTLLHPLLMRNGDSRplHKPTTPLPSLD 870
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
381-571 |
8.10e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 45.54 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 381 DRQLMADLVVSKMSQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQP--QRSGSPSQ 458
Cdd:PRK14971 347 NKRLLVELTLIQLAQLTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSatQPAGTPPT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 459 QRLSPQGQQPLSPQSGSPQQQRSPGSPQLSRAssgsSPNQASKPGATLASQPRPPVQGrstsQQGEESKKPAPPHPHLNK 538
Cdd:PRK14971 427 VSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKI----PVSKVSSLGPSTLRPIQEKAEQ----ATGNIKEAPTGTQKEIFT 498
|
170 180 190
....*....|....*....|....*....|...
gi 1034629533 539 SQSLtNSLSTSDTSQRgtPSEDEAKAETIRNLR 571
Cdd:PRK14971 499 EEDL-QYYWQEFAGTR--PQEEKALKETMINCR 528
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
394-539 |
1.73e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 394 SQLPMPGGTAP-------SPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQrsgSPSQQRLSPQGQ 466
Cdd:PHA03247 2848 PSLPLGGSVAPggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ---APPPPQPQPQPP 2924
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629533 467 QPLSPQSGSPQQQR--SPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHLNKS 539
Cdd:PHA03247 2925 PPPQPQPPPPPPPRpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGH 2999
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
397-565 |
3.42e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 397 PMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSP 476
Cdd:PRK07764 627 PAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 477 QQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHlnksqsltNSLSTSDTSQRGT 556
Cdd:PRK07764 707 ATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPA--------PAAAPAAAPPPSP 778
|
....*....
gi 1034629533 557 PSEDEAKAE 565
Cdd:PRK07764 779 PSEEEEMAE 787
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
397-571 |
6.69e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 397 PMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQP-LSPQSGS 475
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRrLTRPAVA 2789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 476 PQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHLNKSQSLTNSlstSDTSQRG 555
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG---GDVRRRP 2866
|
170
....*....|....*.
gi 1034629533 556 TPSEDEAKAETIRNLR 571
Cdd:PHA03247 2867 PSRSPAAKPAAPARPP 2882
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
397-532 |
1.40e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.61 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 397 PMPGGTAPSP--LRPWAPQIKSAKSPGQAQlgpqlgqPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSG 474
Cdd:PRK10263 375 PAPEGYPQQSqyAQPAVQYNEPLQQPVQPQ-------QPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAW 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629533 475 SPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPP 532
Cdd:PRK10263 448 QAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPP 505
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
447-558 |
2.08e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 41.29 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 447 SPQPQRSGSPSQ-QRLSPQGQQP-LSPQSGSPQQQRSPGSPQLSRASSG------SSPNQASKPGATLASQPRPPVQGRS 518
Cdd:pfam03154 150 SPQDNESDSDSSaQQQILQTQPPvLQAQSGAASPPSPPPPGTTQAATAGptpsapSVPPQGSPATSQPPNQTQSTAAPHT 229
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1034629533 519 TSQQGEESKKPAPPHPHlNKSQSLTNSLSTSDTSQRGTPS 558
Cdd:pfam03154 230 LIQQTPTLHPQRLPSPH-PPLQPMTQPPPPSQVSPQPLPQ 268
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
396-534 |
2.22e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 396 LPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQprpppqggprqAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGS 475
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-----------AASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 476 PQQQRSPGSPQLSRASSGSSPNQASKPGATLASQ-PRPPVQgRSTSQQGEESKKPAPPHP 534
Cdd:PHA03247 2852 LGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVS-RSTESFALPPDQPERPPQ 2910
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
397-534 |
2.59e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 40.82 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 397 PMPGGTAPSPLRPWAPqiKSAKSPGQAqlgpqlgqPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSP 476
Cdd:PHA03378 676 PSPTGANTMLPIQWAP--GTMQPPPRA--------PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRAR 745
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629533 477 QQQRSPGSPQLSRASSGSSPNQASKPGatlASQPRPPVQGRSTSQQgEESKKPAPPHP 534
Cdd:PHA03378 746 PPAAAPGRARPPAAAPGRARPPAAAPG---APTPQPPPQAPPAPQQ-RPRGAPTPQPP 799
|
|
| Androgen_recep |
pfam02166 |
Androgen receptor; |
446-532 |
3.47e-03 |
|
Androgen receptor;
Pssm-ID: 426632 [Multi-domain] Cd Length: 501 Bit Score: 40.30 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 446 QSPQPQRSGSPSQQRLSPQGQQplspQSGSPQQQRSPGSPQLSRA----------SSGSSPNQASKPGAT-----LASQP 510
Cdd:pfam02166 54 QQQQQQVPQQPQQQESSPRQPQ----ASVQPQQAGDDGSPPAHNRgpagylaledDEQPQPSQAQPAAECcpengCVPEP 129
|
90 100
....*....|....*....|..
gi 1034629533 511 RPPVQGRSTSQQgeESKKPAPP 532
Cdd:pfam02166 130 GAAAAAGKGLPQ--QAVAPAAP 149
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
158-375 |
4.84e-03 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 39.25 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 158 KPDFILVRQHAYSMALgedyrSLVIGLQYGGLPAVNSlYSVYNFCSKPWVFSQLIkifhslgpEKFPLVEQTFFPNHKP- 236
Cdd:TIGR00768 48 ELDVVIVRIVSMFRGL-----AVLRYLESLGVPVINS-SDAILNAGDKFLSHQLL--------AKAGIPLPRTGLAGSPe 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 237 --MVTAPH--FPVVVKLGHAHAGMGKIKVENQLDFQDITSVVAMAKTYATTeaFIDSKY-------DIRIQKIGSNYKAY 305
Cdd:TIGR00768 114 eaLKLIEEigFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQNL--FLVQEYikkpggrDIRVFVVGDEVVAA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629533 306 MRTSISGNWKANT---GSAMLEQVAMTERyRLWVDSCSEMfgGLDICAVKAVHSKDGrdYIIEVMDSSMPLIG 375
Cdd:TIGR00768 192 IYRITSGHWRSNLargGKAEPCSLTEEIE-ELAIKAAKAL--GLDVAGVDLLESEDG--LLVNEVNANPEFKN 259
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
91-366 |
5.87e-03 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 39.15 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 91 PRILLVIDDAHTDWSKYFhgkkvngeieirveQAEFSELNLAAYV--TGGCMVDMQVVRNGTKVVSRSfKPDFILVRQHA 168
Cdd:COG0189 2 MKIAILTDPPDKDSTKAL--------------IEAAQRRGHEVEVidPDDLTLDLGRAPELYRGEDLS-EFDAVLPRIDP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 169 YSMALGedyrsLVIGLQYGGLPAVNSLYSVYNFCSKpwVFSQLIKIFHSLG-PEkfplveqTFFPNHKPMVTAPH----F 243
Cdd:COG0189 67 PFYGLA-----LLRQLEAAGVPVVNDPEAIRRARDK--LFTLQLLARAGIPvPP-------TLVTRDPDDLRAFLeelgG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 244 PVVVKLGHAHAGMGKIKVENQldfQDITSVVAMAKTYATTEA----FIDSK--YDIRI-----QKIGsnykAYMRTSISG 312
Cdd:COG0189 133 PVVLKPLDGSGGRGVFLVEDE---DALESILEALTELGSEPVlvqeFIPEEdgRDIRVlvvggEPVA----AIRRIPAEG 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629533 313 NWKANT---GSAmlEQVAMTERYRLWVDSCSEMFgGLDICAVKAVHSKDGRdYIIEV 366
Cdd:COG0189 206 EFRTNLargGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-LVLEV 258
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
450-554 |
6.31e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.92 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629533 450 PQRSGSPSQQRLS-PQGQQPLSPQSGSPQQQRSpgspqlSRASSGSSPnqASKPGATLASQPRPPVQGRSTSQQGEESKK 528
Cdd:PHA03247 375 PKRASLPTRKRRSaRHAATPFARGPGGDDQTRP------AAPVPASVP--TPAPTPVPASAPPPPATPLPSAEPGSDDGP 446
|
90 100
....*....|....*....|....*.
gi 1034629533 529 PAPPHPHLNKSQSLTNSLSTSDTSQR 554
Cdd:PHA03247 447 APPPERQPPAPATEPAPDDPDDATRK 472
|
|
| |
