|
Name |
Accession |
Description |
Interval |
E-value |
| CPSase_L_D2 super family |
cl17255 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
192-394 |
3.70e-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: 3.70e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 192 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITS 271
Cdd:pfam02750 1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 272 VVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVK 351
Cdd:pfam02750 81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1624525551 352 AVHSKDGRDYIIEVMDSSMPLIGEHVEEDRQLMADLVVSKMSQ 394
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
|
|
| Synapsin |
pfam02078 |
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain. |
92-190 |
1.86e-60 |
|
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
:
Pssm-ID: 460438 Cd Length: 97 Bit Score: 195.17 E-value: 1.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVRSFKPDFILVRQHAYsmA 171
Cdd:pfam02078 1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVVRSFRPDFVLVRQHAR--D 78
|
90
....*....|....*....
gi 1624525551 172 LGEDYRSLVIGLQYGGLPA 190
Cdd:pfam02078 79 AGEDYRNLLLGLQYGGVPS 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 1624525551 1 MNFLRRRLSDSSFMANLPNGYMTDLQRPD 29
Cdd:pfam10581 1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
|
|
| PRK07764 super family |
cl35613 |
DNA polymerase III subunits gamma and tau; Validated |
393-535 |
1.89e-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: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 393 SQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQS 472
Cdd:PRK07764 605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525551 473 GSPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHL 535
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 ... |
192-394 |
3.70e-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: 3.70e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 192 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITS 271
Cdd:pfam02750 1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 272 VVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVK 351
Cdd:pfam02750 81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1624525551 352 AVHSKDGRDYIIEVMDSSMPLIGEHVEEDRQLMADLVVSKMSQ 394
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
|
|
| Synapsin |
pfam02078 |
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain. |
92-190 |
1.86e-60 |
|
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
Pssm-ID: 460438 Cd Length: 97 Bit Score: 195.17 E-value: 1.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVRSFKPDFILVRQHAYsmA 171
Cdd:pfam02078 1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVVRSFRPDFVLVRQHAR--D 78
|
90
....*....|....*....
gi 1624525551 172 LGEDYRSLVIGLQYGGLPA 190
Cdd:pfam02078 79 AGEDYRNLLLGLQYGGVPS 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 1624525551 1 MNFLRRRLSDSSFMANLPNGYMTDLQRPD 29
Cdd:pfam10581 1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
393-535 |
1.89e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.67 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 393 SQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQS 472
Cdd:PRK07764 605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525551 473 GSPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHL 535
Cdd:PRK07764 685 PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
91-365 |
8.41e-04 |
|
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: 41.46 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 91 PRILLVIDDAHTDWSKYFhgkkvngeieirveQAEFSELNLAAYV--TGGCMVDMQVVRNGTKVVRSFKPDFILVRQHAY 168
Cdd:COG0189 2 MKIAILTDPPDKDSTKAL--------------IEAAQRRGHEVEVidPDDLTLDLGRAPELYRGEDLSEFDAVLPRIDPP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 169 SMALGedyrsLVIGLQYGGLPAVNSLYSVYNFCSKpwVFSQLIKIFHSLG-PEkfplveqTFFPNHKPMVTAPH----FP 243
Cdd:COG0189 68 FYGLA-----LLRQLEAAGVPVVNDPEAIRRARDK--LFTLQLLARAGIPvPP-------TLVTRDPDDLRAFLeelgGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 244 VVVKLGHAHAGMGKIKVENQldfQDITSVVAMAKTYATTEA----FIDSK--YDIRI-----QKIGsnykAYMRTSISGN 312
Cdd:COG0189 134 VVLKPLDGSGGRGVFLVEDE---DALESILEALTELGSEPVlvqeFIPEEdgRDIRVlvvggEPVA----AIRRIPAEGE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1624525551 313 WKANT---GSAmlEQVAMTERYRLWVDSCSEMFgGLDICAVKAVHSKDGRdYIIEV 365
Cdd:COG0189 207 FRTNLargGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-LVLEV 258
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
446-557 |
2.07e-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: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 446 SPQPQRSGSPSQ-QRLSPQGQQP-LSPQSGSPQQQRSPGSPQLSRASSG------SSPNQASKPGATLASQPRPPVQGRS 517
Cdd:pfam03154 150 SPQDNESDSDSSaQQQILQTQPPvLQAQSGAASPPSPPPPGTTQAATAGptpsapSVPPQGSPATSQPPNQTQSTAAPHT 229
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1624525551 518 TSQQGEESKKPAPPHPHlNKSQSLTNSLSTSDTSQRGTPS 557
Cdd:pfam03154 230 LIQQTPTLHPQRLPSPH-PPLQPMTQPPPPSQVSPQPLPQ 268
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
157-374 |
4.83e-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: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 157 KPDFILVRQHAYSMALgedyrSLVIGLQYGGLPAVNSlYSVYNFCSKPWVFSQLIkifhslgpEKFPLVEQTFFPNHKP- 235
Cdd:TIGR00768 48 ELDVVIVRIVSMFRGL-----AVLRYLESLGVPVINS-SDAILNAGDKFLSHQLL--------AKAGIPLPRTGLAGSPe 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 236 --MVTAPH--FPVVVKLGHAHAGMGKIKVENQLDFQDITSVVAMAKTYATTeaFIDSKY-------DIRIQKIGSNYKAY 304
Cdd:TIGR00768 114 eaLKLIEEigFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQNL--FLVQEYikkpggrDIRVFVVGDEVVAA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525551 305 MRTSISGNWKANT---GSAMLEQVAMTERyRLWVDSCSEMfgGLDICAVKAVHSKDGrdYIIEVMDSSMPLIG 374
Cdd:TIGR00768 192 IYRITSGHWRSNLargGKAEPCSLTEEIE-ELAIKAAKAL--GLDVAGVDLLESEDG--LLVNEVNANPEFKN 259
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Synapsin_C |
pfam02750 |
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ... |
192-394 |
3.70e-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: 3.70e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 192 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITS 271
Cdd:pfam02750 1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 272 VVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVK 351
Cdd:pfam02750 81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1624525551 352 AVHSKDGRDYIIEVMDSSMPLIGEHVEEDRQLMADLVVSKMSQ 394
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
|
|
| Synapsin |
pfam02078 |
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain. |
92-190 |
1.86e-60 |
|
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
Pssm-ID: 460438 Cd Length: 97 Bit Score: 195.17 E-value: 1.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVRSFKPDFILVRQHAYsmA 171
Cdd:pfam02078 1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVVRSFRPDFVLVRQHAR--D 78
|
90
....*....|....*....
gi 1624525551 172 LGEDYRSLVIGLQYGGLPA 190
Cdd:pfam02078 79 AGEDYRNLLLGLQYGGVPS 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 1624525551 1 MNFLRRRLSDSSFMANLPNGYMTDLQRPD 29
Cdd:pfam10581 1 MNYLRRRLSDSNFMSNLPNGYMSDLQRPD 29
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
393-535 |
1.89e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 47.67 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 393 SQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQS 472
Cdd:PRK07764 605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525551 473 GSPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHL 535
Cdd:PRK07764 685 PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
408-536 |
2.51e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.39 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 408 PWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSPQQQRSPGSPQLS 487
Cdd:PRK10263 740 PHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ 819
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1624525551 488 RASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEES--KKPAPPHPHLN 536
Cdd:PRK10263 820 PQQPVAPQPQYQQPQQPVAPQPQDTLLHPLLMRNGDSRplHKPTTPLPSLD 870
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
380-570 |
8.08e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 45.54 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 380 DRQLMADLVVSKMSQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQP--QRSGSPSQ 457
Cdd:PRK14971 347 NKRLLVELTLIQLAQLTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSatQPAGTPPT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 458 QRLSPQGQQPLSPQSGSPQQQRSPGSPQLSRAssgsSPNQASKPGATLASQPRPPVQGrstsQQGEESKKPAPPHPHLNK 537
Cdd:PRK14971 427 VSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKI----PVSKVSSLGPSTLRPIQEKAEQ----ATGNIKEAPTGTQKEIFT 498
|
170 180 190
....*....|....*....|....*....|...
gi 1624525551 538 SQSLtNSLSTSDTSQRgtPSEDEAKAETIRNLR 570
Cdd:PRK14971 499 EEDL-QYYWQEFAGTR--PQEEKALKETMINCR 528
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
393-538 |
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 1624525551 393 SQLPMPGGTAP-------SPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQrsgSPSQQRLSPQGQ 465
Cdd:PHA03247 2848 PSLPLGGSVAPggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ---APPPPQPQPQPP 2924
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624525551 466 QPLSPQSGSPQQQR--SPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHLNKS 538
Cdd:PHA03247 2925 PPPQPQPPPPPPPRpqPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGH 2999
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
396-564 |
3.44e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 396 PMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSP 475
Cdd:PRK07764 627 PAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 476 QQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHlnksqsltNSLSTSDTSQRGT 555
Cdd:PRK07764 707 ATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPA--------PAAAPAAAPPPSP 778
|
....*....
gi 1624525551 556 PSEDEAKAE 564
Cdd:PRK07764 779 PSEEEEMAE 787
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
396-570 |
6.67e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 396 PMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQP-LSPQSGS 474
Cdd:PHA03247 2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRrLTRPAVA 2789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 475 PQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHLNKSQSLTNSlstSDTSQRG 554
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG---GDVRRRP 2866
|
170
....*....|....*.
gi 1624525551 555 TPSEDEAKAETIRNLR 570
Cdd:PHA03247 2867 PSRSPAAKPAAPARPP 2882
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
91-365 |
8.41e-04 |
|
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: 41.46 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 91 PRILLVIDDAHTDWSKYFhgkkvngeieirveQAEFSELNLAAYV--TGGCMVDMQVVRNGTKVVRSFKPDFILVRQHAY 168
Cdd:COG0189 2 MKIAILTDPPDKDSTKAL--------------IEAAQRRGHEVEVidPDDLTLDLGRAPELYRGEDLSEFDAVLPRIDPP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 169 SMALGedyrsLVIGLQYGGLPAVNSLYSVYNFCSKpwVFSQLIKIFHSLG-PEkfplveqTFFPNHKPMVTAPH----FP 243
Cdd:COG0189 68 FYGLA-----LLRQLEAAGVPVVNDPEAIRRARDK--LFTLQLLARAGIPvPP-------TLVTRDPDDLRAFLeelgGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 244 VVVKLGHAHAGMGKIKVENQldfQDITSVVAMAKTYATTEA----FIDSK--YDIRI-----QKIGsnykAYMRTSISGN 312
Cdd:COG0189 134 VVLKPLDGSGGRGVFLVEDE---DALESILEALTELGSEPVlvqeFIPEEdgRDIRVlvvggEPVA----AIRRIPAEGE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1624525551 313 WKANT---GSAmlEQVAMTERYRLWVDSCSEMFgGLDICAVKAVHSKDGRdYIIEV 365
Cdd:COG0189 207 FRTNLargGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-LVLEV 258
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
396-531 |
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 1624525551 396 PMPGGTAPSP--LRPWAPQIKSAKSPGQAQlgpqlgqPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSG 473
Cdd:PRK10263 375 PAPEGYPQQSqyAQPAVQYNEPLQQPVQPQ-------QPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAW 447
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1624525551 474 SPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPP 531
Cdd:PRK10263 448 QAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPP 505
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
446-557 |
2.07e-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: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 446 SPQPQRSGSPSQ-QRLSPQGQQP-LSPQSGSPQQQRSPGSPQLSRASSG------SSPNQASKPGATLASQPRPPVQGRS 517
Cdd:pfam03154 150 SPQDNESDSDSSaQQQILQTQPPvLQAQSGAASPPSPPPPGTTQAATAGptpsapSVPPQGSPATSQPPNQTQSTAAPHT 229
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1624525551 518 TSQQGEESKKPAPPHPHlNKSQSLTNSLSTSDTSQRGTPS 557
Cdd:pfam03154 230 LIQQTPTLHPQRLPSPH-PPLQPMTQPPPPSQVSPQPLPQ 268
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
395-533 |
2.21e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 395 LPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQprpppqggprqAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGS 474
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-----------AASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 475 PQQQRSPGSPQLSRASSGSSPNQASKPGATLASQ-PRPPVQgRSTSQQGEESKKPAPPHP 533
Cdd:PHA03247 2852 LGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVS-RSTESFALPPDQPERPPQ 2910
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
396-533 |
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 1624525551 396 PMPGGTAPSPLRPWAPqiKSAKSPGQAqlgpqlgqPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSP 475
Cdd:PHA03378 676 PSPTGANTMLPIQWAP--GTMQPPPRA--------PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRAR 745
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1624525551 476 QQQRSPGSPQLSRASSGSSPNQASKPGatlASQPRPPVQGRSTSQQgEESKKPAPPHP 533
Cdd:PHA03378 746 PPAAAPGRARPPAAAPGRARPPAAAPG---APTPQPPPQAPPAPQQ-RPRGAPTPQPP 799
|
|
| Androgen_recep |
pfam02166 |
Androgen receptor; |
445-531 |
3.46e-03 |
|
Androgen receptor;
Pssm-ID: 426632 [Multi-domain] Cd Length: 501 Bit Score: 40.30 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 445 QSPQPQRSGSPSQQRLSPQGQQplspQSGSPQQQRSPGSPQLSRA----------SSGSSPNQASKPGAT-----LASQP 509
Cdd:pfam02166 54 QQQQQQVPQQPQQQESSPRQPQ----ASVQPQQAGDDGSPPAHNRgpagylaledDEQPQPSQAQPAAECcpengCVPEP 129
|
90 100
....*....|....*....|..
gi 1624525551 510 RPPVQGRSTSQQgeESKKPAPP 531
Cdd:pfam02166 130 GAAAAAGKGLPQ--QAVAPAAP 149
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
157-374 |
4.83e-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: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 157 KPDFILVRQHAYSMALgedyrSLVIGLQYGGLPAVNSlYSVYNFCSKPWVFSQLIkifhslgpEKFPLVEQTFFPNHKP- 235
Cdd:TIGR00768 48 ELDVVIVRIVSMFRGL-----AVLRYLESLGVPVINS-SDAILNAGDKFLSHQLL--------AKAGIPLPRTGLAGSPe 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 236 --MVTAPH--FPVVVKLGHAHAGMGKIKVENQLDFQDITSVVAMAKTYATTeaFIDSKY-------DIRIQKIGSNYKAY 304
Cdd:TIGR00768 114 eaLKLIEEigFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQNL--FLVQEYikkpggrDIRVFVVGDEVVAA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525551 305 MRTSISGNWKANT---GSAMLEQVAMTERyRLWVDSCSEMfgGLDICAVKAVHSKDGrdYIIEVMDSSMPLIG 374
Cdd:TIGR00768 192 IYRITSGHWRSNLargGKAEPCSLTEEIE-ELAIKAAKAL--GLDVAGVDLLESEDG--LLVNEVNANPEFKN 259
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
449-553 |
6.30e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.92 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525551 449 PQRSGSPSQQRLS-PQGQQPLSPQSGSPQQQRSpgspqlSRASSGSSPnqASKPGATLASQPRPPVQGRSTSQQGEESKK 527
Cdd:PHA03247 375 PKRASLPTRKRRSaRHAATPFARGPGGDDQTRP------AAPVPASVP--TPAPTPVPASAPPPPATPLPSAEPGSDDGP 446
|
90 100
....*....|....*....|....*.
gi 1624525551 528 PAPPHPHLNKSQSLTNSLSTSDTSQR 553
Cdd:PHA03247 447 APPPERQPPAPATEPAPDDPDDATRK 472
|
|
| |
