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Conserved domains on  [gi|160707907|ref|NP_001104252|]
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synapsin-1 isoform b [Rattus norvegicus]

Protein Classification

ATP-grasp domain-containing protein; acetate--CoA ligase family protein( domain architecture ID 10301346)

ATP-grasp domain-containing protein may be related to carbamoyl phosphate synthetase and predicted to be involved in the biosynthesis of a ribonucleoside involved in stress response| acetate--CoA ligase family protein similar to ADP-forming acetate--CoA ligase that catalyzes the formation of acetate and ATP from acetyl-CoA by using ADP and phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSase_L_D2 super family cl17255
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 214-416 4.51e-138

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: 402.13  E-value: 4.51e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  214 NSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIAS 293
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  294 VVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVE 373
Cdd:pfam02750  81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 160707907  374 ALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMTQ 416
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
Synapsin pfam02078
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
 115-212 9.16e-61

Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.


:

Pssm-ID: 460438  Cd Length: 97  Bit Score: 197.87  E-value: 9.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  115 VLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFsmAR 194
Cdd:pfam02078   2 TLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVVRSFRPDFVLVRQHAR--DA 79

                          90
                  ....*....|....*...
gi 160707907  195 NGDYRSLVIGLQYAGIPS 212
Cdd:pfam02078  80 GEDYRNLLLGLQYGGVPS 97
Synapsin_N super family cl11206
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ...
 1-27 6.87e-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: 60.20  E-value: 6.87e-12
                          10        20
                  ....*....|....*....|....*..
gi 160707907    1 MNYLRRRLSDSNFMANLPNGYMTDLQR 27
Cdd:pfam10581   1 MNYLRRRLSDSNFMSNLPNGYMSDLQR 27
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 496-668 8.67e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  496 PPAG--SPLPQRLPSPTAAPQQSASQATPmtqgqgrqSRPVAGGPGAPPAARPPASPSPQRQAGP------PQATRQASI 567
Cdd:PHA03247 2771 PPAApaAGPPRRLTRPAVASLSESRESLP--------SPWDPADPPAAVLAPAAALPPAASPAGPlppptsAQPTAPPPP 2842

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  568 SGPAPPKVS---GASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPsQDVP 644
Cdd:PHA03247 2843 PGPPPPSLPlggSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP-QPQP 2921

                         170       180
                  ....*....|....*....|....
gi 160707907  645 PPIIAAAGGPPHPQLKASPAQAQP 668
Cdd:PHA03247 2922 QPPPPPQPQPPPPPPPRPQPPLAP 2945
 
Name Accession Description Interval E-value
Synapsin_C pfam02750
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ...
 214-416 4.51e-138

Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function unknown.


Pssm-ID: 308403  Cd Length: 203  Bit Score: 402.13  E-value: 4.51e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  214 NSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIAS 293
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  294 VVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVE 373
Cdd:pfam02750  81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 160707907  374 ALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMTQ 416
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
Synapsin pfam02078
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
 115-212 9.16e-61

Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.


Pssm-ID: 460438  Cd Length: 97  Bit Score: 197.87  E-value: 9.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  115 VLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFsmAR 194
Cdd:pfam02078   2 TLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVVRSFRPDFVLVRQHAR--DA 79

                          90
                  ....*....|....*...
gi 160707907  195 NGDYRSLVIGLQYAGIPS 212
Cdd:pfam02078  80 GEDYRNLLLGLQYGGVPS 97
Synapsin_N pfam10581
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ...
 1-27 6.87e-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: 60.20  E-value: 6.87e-12
                          10        20
                  ....*....|....*....|....*..
gi 160707907    1 MNYLRRRLSDSNFMANLPNGYMTDLQR 27
Cdd:pfam10581   1 MNYLRRRLSDSNFMSNLPNGYMSDLQR 27
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 161-420 1.64e-09

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: 59.57  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 161 FSVDMEVLRNGVKVVRSLKPDFVLIRQ----HAFSMARNgdyrslvigLQYAGIPSVNSLHSVYNFCDKpwvFAQMVRLH 236
Cdd:COG0189   38 LTLDLGRAPELYRGEDLSEFDAVLPRIdppfYGLALLRQ---------LEAAGVPVVNDPEAIRRARDK---LFTLQLLA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 237 KK-LGTeefP--LIdqTFYPNH-KEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQD-IASVVALTKTYATAEPFIDAK 311
Cdd:COG0189  106 RAgIPV---PptLV--TRDPDDlRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESiLEALTELGSEPVLVQEFIPEE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 312 --YDVRVqkI---GQNYKAYMRTSVSGNWKTNT---GSAmlEQIAMSDRYKLWVDTCSEIFgGLDICAVEALHGKDGRdH 383
Cdd:COG0189  181 dgRDIRV--LvvgGEPVAAIRRIPAEGEFRTNLargGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-L 254

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 160707907 384 IIEVvgSSMPLIGDHQDEDKQLIVELVVNKMTQALPR 420
Cdd:COG0189  255 VLEV--NVTPGFRGLERATGVDIAEAIADYLEARAAR 289
PHA03247 PHA03247
large tegument protein UL36; Provisional
 496-668 8.67e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  496 PPAG--SPLPQRLPSPTAAPQQSASQATPmtqgqgrqSRPVAGGPGAPPAARPPASPSPQRQAGP------PQATRQASI 567
Cdd:PHA03247 2771 PPAApaAGPPRRLTRPAVASLSESRESLP--------SPWDPADPPAAVLAPAAALPPAASPAGPlppptsAQPTAPPPP 2842

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  568 SGPAPPKVS---GASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPsQDVP 644
Cdd:PHA03247 2843 PGPPPPSLPlggSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP-QPQP 2921

                         170       180
                  ....*....|....*....|....
gi 160707907  645 PPIIAAAGGPPHPQLKASPAQAQP 668
Cdd:PHA03247 2922 QPPPPPQPQPPPPPPPRPQPPLAP 2945
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 491-668 2.05e-05

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: 47.84  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  491 LSGLGPPAGSPL--PQRLPSPTAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAgPPQATRQASIS 568
Cdd:pfam03154 194 AATAGPTPSAPSvpPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV-SPQPLPQPSLH 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  569 GPAPPKVSGASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKPQLAQK---PSQDVPP 645
Cdd:pfam03154 273 GQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREqplPPAPLSM 352

                         170       180
                  ....*....|....*....|...
gi 160707907  646 PIIAAAGGPPHPQLKASPAQAQP 668
Cdd:pfam03154 353 PHIKPPPTTPIPQLPNPQSHKHP 375
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 179-396 3.44e-04

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: 43.10  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  179 KPDFVLIR----QHAFSMARNgdyrslvigLQYAGIPSVNSLHSVYNFCDKPWVFAqmvrlhkKLGTEEFPLIDQTFYPN 254
Cdd:TIGR00768  48 ELDVVIVRivsmFRGLAVLRY---------LESLGVPVINSSDAILNAGDKFLSHQ-------LLAKAGIPLPRTGLAGS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  255 HKE---MLSSTTYPVVVKMGHAHSGMGKVKVDnqhDFQDIASVV-ALTKTYATAEPFIDAKY-------DVRVQKIGQNY 323
Cdd:TIGR00768 112 PEEalkLIEEIGFPVVLKPVFGSWGRGVSLAR---DRQAAESLLeHFEQLNGPQNLFLVQEYikkpggrDIRVFVVGDEV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  324 KAYMRTSVSGNWKTNT---GSAM-------LEQIAMSdryklwvdtCSEIFgGLDICAVEALHGKDGrdHIIEVVGSSMP 393
Cdd:TIGR00768 189 VAAIYRITSGHWRSNLargGKAEpcslteeIEELAIK---------AAKAL-GLDVAGVDLLESEDG--LLVNEVNANPE 256


                  ...
gi 160707907  394 LIG 396
Cdd:TIGR00768 257 FKN 259
 
Name Accession Description Interval E-value
Synapsin_C pfam02750
Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function ...
 214-416 4.51e-138

Synapsin, ATP binding domain; Ca dependent ATP binding in this ATP grasp fold. Function unknown.


Pssm-ID: 308403  Cd Length: 203  Bit Score: 402.13  E-value: 4.51e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  214 NSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIAS 293
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  294 VVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVE 373
Cdd:pfam02750  81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 160707907  374 ALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMTQ 416
Cdd:pfam02750 161 AVHGKDGKDYIFEVMDCSMPLIGEHQEEDKQLIADLVISKMNQ 203
Synapsin pfam02078
Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.
 115-212 9.16e-61

Synapsin, N-terminal domain; This family is structurally related to the PreATP-grasp domain.


Pssm-ID: 460438  Cd Length: 97  Bit Score: 197.87  E-value: 9.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  115 VLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFsmAR 194
Cdd:pfam02078   2 TLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVVRSFRPDFVLVRQHAR--DA 79

                          90
                  ....*....|....*...
gi 160707907  195 NGDYRSLVIGLQYAGIPS 212
Cdd:pfam02078  80 GEDYRNLLLGLQYGGVPS 97
Synapsin_N pfam10581
Synapsin N-terminal; This highly conserved domain of synapsin proteins has a serine at ...
 1-27 6.87e-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: 60.20  E-value: 6.87e-12
                          10        20
                  ....*....|....*....|....*..
gi 160707907    1 MNYLRRRLSDSNFMANLPNGYMTDLQR 27
Cdd:pfam10581   1 MNYLRRRLSDSNFMSNLPNGYMSDLQR 27
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 161-420 1.64e-09

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: 59.57  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 161 FSVDMEVLRNGVKVVRSLKPDFVLIRQ----HAFSMARNgdyrslvigLQYAGIPSVNSLHSVYNFCDKpwvFAQMVRLH 236
Cdd:COG0189   38 LTLDLGRAPELYRGEDLSEFDAVLPRIdppfYGLALLRQ---------LEAAGVPVVNDPEAIRRARDK---LFTLQLLA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 237 KK-LGTeefP--LIdqTFYPNH-KEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQD-IASVVALTKTYATAEPFIDAK 311
Cdd:COG0189  106 RAgIPV---PptLV--TRDPDDlRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESiLEALTELGSEPVLVQEFIPEE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 312 --YDVRVqkI---GQNYKAYMRTSVSGNWKTNT---GSAmlEQIAMSDRYKLWVDTCSEIFgGLDICAVEALHGKDGRdH 383
Cdd:COG0189  181 dgRDIRV--LvvgGEPVAAIRRIPAEGEFRTNLargGRA--EPVELTDEERELALRAAPAL-GLDFAGVDLIEDDDGP-L 254

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 160707907 384 IIEVvgSSMPLIGDHQDEDKQLIVELVVNKMTQALPR 420
Cdd:COG0189  255 VLEV--NVTPGFRGLERATGVDIAEAIADYLEARAAR 289
PHA03247 PHA03247
large tegument protein UL36; Provisional
 496-668 8.67e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  496 PPAG--SPLPQRLPSPTAAPQQSASQATPmtqgqgrqSRPVAGGPGAPPAARPPASPSPQRQAGP------PQATRQASI 567
Cdd:PHA03247 2771 PPAApaAGPPRRLTRPAVASLSESRESLP--------SPWDPADPPAAVLAPAAALPPAASPAGPlppptsAQPTAPPPP 2842

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  568 SGPAPPKVS---GASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPsQDVP 644
Cdd:PHA03247 2843 PGPPPPSLPlggSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP-QPQP 2921

                         170       180
                  ....*....|....*....|....
gi 160707907  645 PPIIAAAGGPPHPQLKASPAQAQP 668
Cdd:PHA03247 2922 QPPPPPQPQPPPPPPPRPQPPLAP 2945
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 492-668 2.34e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.75  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 492 SGLGPPAGSPLPQRLPSPTAAPQQSASQATPMTQGQGRQSrpVAGGPGAPPAARPPASPSPQRQAGPPQATRQASISGPA 571
Cdd:PRK07764 592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAG--AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 572 PPKVSGASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPSQDVPP-----P 646
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPepddpP 749

                        170       180
                 ....*....|....*....|..
gi 160707907 647 IIAAAGGPPHPQLKASPAQAQP 668
Cdd:PRK07764 750 DPAGAPAQPPPPPAPAPAAAPA 771
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
513-663 2.39e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 50.64  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 513 PQQSASQATPMTQGQGRQSRPVAGGPGappaarppaspspQRQAGPPQATRQASisGPAPPKVSGASPGGQQRQGPPQKP 592
Cdd:PRK12323 365 PGQSGGGAGPATAAAAPVAQPAPAAAA-------------PAAAAPAPAAPPAA--PAAAPAAAAAARAVAAAPARRSPA 429

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160707907 593 PGPAGPIRQASQAGPGPRTGPPTTQqprPSGPGPAGRPTKPQLAQKPSQDVPPPIIAAAGGPPHPQLKASP 663
Cdd:PRK12323 430 PEALAAARQASARGPGGAPAPAPAP---AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPP 497
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 491-668 2.05e-05

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: 47.84  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  491 LSGLGPPAGSPL--PQRLPSPTAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAgPPQATRQASIS 568
Cdd:pfam03154 194 AATAGPTPSAPSvpPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQV-SPQPLPQPSLH 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  569 GPAPPKVSGASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKPQLAQK---PSQDVPP 645
Cdd:pfam03154 273 GQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREqplPPAPLSM 352

                         170       180
                  ....*....|....*....|...
gi 160707907  646 PIIAAAGGPPHPQLKASPAQAQP 668
Cdd:pfam03154 353 PHIKPPPTTPIPQLPNPQSHKHP 375
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 503-658 1.02e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 45.80  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  503 PQRLPSPTAAPQQSAsQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQASISGPAPPKVSGASPGG 582
Cdd:pfam09770 208 KKPAQQPAPAPAQPP-AAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQPSIQPQAQ 286

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160707907  583 QQRQGPPQKPPgpagpirQASQAGPGP-RTGPPTTQQPRPSGPGPAGRPTKPQLAQKPSQDVPPPIIAaaggppHPQ 658
Cdd:pfam09770 287 QFHQQPPPVPV-------QPTQILQNPnRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIIT------HPQ 350
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 510-668 2.57e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 510 TAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQASISGPAPPK-------VSGASPGG 582
Cdd:PRK07764 587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEhhpkhvaVPDASDGG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 583 QQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKP--QLAQKPSQDVPPPIIAAAGGPPHPQLK 660
Cdd:PRK07764 667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPaaQPPQAAQGASAPSPAADDPVPLPPEPD 746


                 ....*...
gi 160707907 661 ASPAQAQP 668
Cdd:PRK07764 747 DPPDPAGA 754
PHA03247 PHA03247
large tegument protein UL36; Provisional
 498-668 3.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  498 AGSPLPQRLPSPTAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATrqasiSGPAPPKVSG 577
Cdd:PHA03247 2699 ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT-----AGPPAPAPPA 2773

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  578 ASPGGQQRQGPPQKPPGPAGPIRQA---------SQAGPGPRTGPPTTQQPR-PSGPGPAGRPTKPQLAQKPSQDVPPPI 647
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASLSESRESLpspwdpadpPAAVLAPAAALPPAASPAgPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853

                         170       180
                  ....*....|....*....|..
gi 160707907  648 IAAA-GGPPHPQLKASPAQAQP 668
Cdd:PHA03247 2854 GSVApGGDVRRRPPSRSPAAKP 2875
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 179-396 3.44e-04

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: 43.10  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  179 KPDFVLIR----QHAFSMARNgdyrslvigLQYAGIPSVNSLHSVYNFCDKPWVFAqmvrlhkKLGTEEFPLIDQTFYPN 254
Cdd:TIGR00768  48 ELDVVIVRivsmFRGLAVLRY---------LESLGVPVINSSDAILNAGDKFLSHQ-------LLAKAGIPLPRTGLAGS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  255 HKE---MLSSTTYPVVVKMGHAHSGMGKVKVDnqhDFQDIASVV-ALTKTYATAEPFIDAKY-------DVRVQKIGQNY 323
Cdd:TIGR00768 112 PEEalkLIEEIGFPVVLKPVFGSWGRGVSLAR---DRQAAESLLeHFEQLNGPQNLFLVQEYikkpggrDIRVFVVGDEV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  324 KAYMRTSVSGNWKTNT---GSAM-------LEQIAMSdryklwvdtCSEIFgGLDICAVEALHGKDGrdHIIEVVGSSMP 393
Cdd:TIGR00768 189 VAAIYRITSGHWRSNLargGKAEpcslteeIEELAIK---------AAKAL-GLDVAGVDLLESEDG--LLVNEVNANPE 256


                  ...
gi 160707907  394 LIG 396
Cdd:TIGR00768 257 FKN 259
PHA03247 PHA03247
large tegument protein UL36; Provisional
 496-668 3.71e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  496 PPAGSPLPQRLPSPTAAPQQSASQATPMTQGqGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQASISGPAPPKV 575
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPP 2706

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907  576 S----------------GASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPgPAGRPTKPqlaqkp 639
Cdd:PHA03247 2707 TpepaphalvsatplppGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAP-PAAPAAGP------ 2779

                         170       180
                  ....*....|....*....|....*....
gi 160707907  640 sqdvPPPIIAAAGGPPHPQLKASPAQAQP 668
Cdd:PHA03247 2780 ----PRRLTRPAVASLSESRESLPSPWDP 2804
dnaA PRK14086
chromosomal replication initiator protein DnaA;
496-661 6.25e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 42.89  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 496 PPAGSPLPQRLPSPTAA-------PQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPP----------ASPSPQRQAGP 558
Cdd:PRK14086  95 PAPPPPHARRTSEPELPrpgrrpyEGYGGPRADDRPPGLPRQDQLPTARPAYPAYQQRPepgawpraadDYGWQQQRLGF 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 559 PQATRQASISGPAPPKVSGASPGGQQRQGPPQkppgpagpiRQASQAGPGPRTGPP---TTQQPRPS---------GPGP 626
Cdd:PRK14086 175 PPRAPYASPASYAPEQERDREPYDAGRPEYDQ---------RRRDYDHPRPDWDRPrrdRTDRPEPPpgaghvhrgGPGP 245

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 160707907 627 AGRPTKPQLAQKPSQDVPP---PIIAAAGGPPHPQLKA 661
Cdd:PRK14086 246 PERDDAPVVPIRPSAPGPLaaqPAPAPGPGEPTARLNP 283
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 553-668 1.27e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 553 QRQAGP-PQATRQASISGPAPPKVSGASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPT 631
Cdd:PRK07764 401 AAAAAPaAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP 480

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 160707907 632 KPQLAQKPSQDVPPPIIAAAGGPPHPQLKASPAQAQP 668
Cdd:PRK07764 481 APAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWP 517
PHA03378 PHA03378
EBNA-3B; Provisional
 497-667 1.33e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 497 PAGSPLPQRLPSPTAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQAT-----RQASISGPA 571
Cdd:PHA03378 645 VLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPpgraqRPAAATGRA 724

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 572 PPkvSGASPGGQQRQGPPQKPPGPAGPI---RQASQAGPGPRTGP------PTTQQPRPSGPGPAGRPTKPQLAQKPSQD 642
Cdd:PHA03378 725 RP--PAAAPGRARPPAAAPGRARPPAAApgrARPPAAAPGRARPPaaapgaPTPQPPPQAPPAPQQRPRGAPTPQPPPQA 802

                        170       180
                 ....*....|....*....|....*
gi 160707907 643 VPPPIIAAAGGPPHPQLKASPAQAQ 667
Cdd:PHA03378 803 GPTSMQLMPRAAPGQQGPTKQILRQ 827
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 493-624 3.39e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 493 GLGPPAGSPLPQRLPSPTAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQASISGPAP 572
Cdd:PRK07764 386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 160707907 573 PKVSGASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGP 624
Cdd:PRK07764 466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWP 517
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 495-668 4.13e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 495 GPPAGSPLPQRLPSPTAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQASISGPAPPK 574
Cdd:PRK07764 632 AAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPA 711

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 575 VSGASPGGQQRqgppqkppgpagpirqASQAGPGPRTGPPTTQQPRPSGPGPAGRPtkpqlAQKPSQDVPPPIIAAAGGP 654
Cdd:PRK07764 712 GQADDPAAQPP----------------QAAQGASAPSPAADDPVPLPPEPDDPPDP-----AGAPAQPPPPPAPAPAAAP 770

                        170
                 ....*....|....
gi 160707907 655 PHPQLKASPAQAQP 668
Cdd:PRK07764 771 AAAPPPSPPSEEEE 784
PHA03378 PHA03378
EBNA-3B; Provisional
 496-658 5.39e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 496 PPAGSPLPQRLPS-PTAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPpaspspqrQAGPPQATRQASISGPAPPk 574
Cdd:PHA03378 696 PPPRAPTPMRPPAaPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPP--------AAAPGRARPPAAAPGRARP- 766

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 575 vSGASPGGQQRQGPPQKPPGPagpiRQASQAGPGPR---TGPPTTQQPRPSGPGPAGRPTKPQLAQ---------KPSQD 642
Cdd:PHA03378 767 -PAAAPGAPTPQPPPQAPPAP----QQRPRGAPTPQpppQAGPTSMQLMPRAAPGQQGPTKQILRQlltggvkrgRPSLK 841

                        170
                 ....*....|....*...
gi 160707907 643 VPPPI--IAAAGGPPHPQ 658
Cdd:PHA03378 842 KPAALerQAAAGPTPSPG 859
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 573-668 8.03e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 8.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 573 PKVSGASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKP-----SQDVPPPI 647
Cdd:PRK07764 365 PSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPapapaPAPAPPSP 444

                         90       100
                 ....*....|....*....|.
gi 160707907 648 IAAAGGPPHPQLKASPAQAQP 668
Cdd:PRK07764 445 AGNAPAGGAPSPPPAAAPSAQ 465
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
496-668 9.39e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.09  E-value: 9.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 496 PPAGSPLPQRLPSPTAAPQQSASQATPMTQGQGRQSRPvaggpgappaarppaspspqrqAGPPQATRQASISG------ 569
Cdd:PRK12323 392 PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPA----------------------PEALAAARQASARGpggapa 449

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 570 ----PAPPKVSGASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPrPSGPGPAGRPTKPQLAQKPSQDVPP 645
Cdd:PRK12323 450 papaPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELP-PEFASPAPAQPDAAPAGWVAESIPD 528

                        170       180
                 ....*....|....*....|...
gi 160707907 646 PIIAAAGGPPHPQLKASPAQAQP 668
Cdd:PRK12323 529 PATADPDDAFETLAPAPAAAPAP 551
PRK11901 PRK11901
hypothetical protein; Reviewed
 499-668 9.52e-03

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 38.51  E-value: 9.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 499 GSPL--PQRLPSPTAAPQQSA------SQATPMTQGQGRQSRPVAGGPGAPPAARPPaspspqrQAGPPQATRQASISGP 570
Cdd:PRK11901  55 GSALksPTEHESQQSSNNAGAeknidlSGSSSLSSGNQSSPSAANNTSDGHDASGVK-------NTAPPQDISAPPISPT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160707907 571 APPKVSGASPGGQQRQG----PPQKPPGPAGPIRQASQAGPGPRTGPPT---TQQPRPSGPGPAGRPTKPQLAQKPSQDV 643
Cdd:PRK11901 128 PTQAAPPQTPNGQQRIElpgnISDALSQQQGQVNAASQNAQGNTSTLPTapaTVAPSKGAKVPATAETHPTPPQKPATKK 207

                        170       180
                 ....*....|....*....|....*
gi 160707907 644 PPPIIAAAggPPHPQLKASPAQAQP 668
Cdd:PRK11901 208 PAVNHHKT--ATVAVPPATSGKPKS 230
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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