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Conserved domains on  [gi|1624525583|ref|NP_001356837|]
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synapsin-3 isoform IIIa [Homo sapiens]

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 ...
 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 1624525583 193 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITS 272
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 273 VVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVK 352
Cdd:pfam02750  81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1624525583 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 1624525583  92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVsRSFKPDFILVRQHAYsm 171
Cdd:pfam02078   1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVV-RSFRPDFVLVRQHAR-- 77

                          90       100
                  ....*....|....*....|
gi 1624525583 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 1624525583   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 1624525583 394 SQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQS 473
Cdd:PRK07764  605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525583 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 1624525583 193 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITS 272
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 273 VVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVK 352
Cdd:pfam02750  81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1624525583 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 1624525583  92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVsRSFKPDFILVRQHAYsm 171
Cdd:pfam02078   1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVV-RSFRPDFVLVRQHAR-- 77

                          90       100
                  ....*....|....*....|
gi 1624525583 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 1624525583   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 1624525583 394 SQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQS 473
Cdd:PRK07764  605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525583 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 1624525583 447 SPQPQRSGSPSQ-QRLSPQGQQP-LSPQSGSPQQQRSPGSPQLSRASSG------SSPNQASKPGATLASQPRPPVQGRS 518
Cdd:pfam03154 150 SPQDNESDSDSSaQQQILQTQPPvLQAQSGAASPPSPPPPGTTQAATAGptpsapSVPPQGSPATSQPPNQTQSTAAPHT 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1624525583 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 1624525583 158 KPDFILVRQHAYSMALgedyrSLVIGLQYGGLPAVNSlYSVYNFCSKPWVFSQLIkifhslgpEKFPLVEQTFFPNHKP- 236
Cdd:TIGR00768  48 ELDVVIVRIVSMFRGL-----AVLRYLESLGVPVINS-SDAILNAGDKFLSHQLL--------AKAGIPLPRTGLAGSPe 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 237 --MVTAPH--FPVVVKLGHAHAGMGKIKVENQLDFQDITSVVAMAKTYATTeaFIDSKY-------DIRIQKIGSNYKAY 305
Cdd:TIGR00768 114 eaLKLIEEigFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQNL--FLVQEYikkpggrDIRVFVVGDEVVAA 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525583 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 1624525583  91 PRILLVIDDAHTDWSKYFhgkkvngeieirveQAEFSELNLAAYV--TGGCMVDMQVVRNGTKVVSRSfKPDFILVRQHA 168
Cdd:COG0189     2 MKIAILTDPPDKDSTKAL--------------IEAAQRRGHEVEVidPDDLTLDLGRAPELYRGEDLS-EFDAVLPRIDP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 169 YSMALGedyrsLVIGLQYGGLPAVNSLYSVYNFCSKpwVFSQLIKIFHSLG-PEkfplveqTFFPNHKPMVTAPH----F 243
Cdd:COG0189    67 PFYGLA-----LLRQLEAAGVPVVNDPEAIRRARDK--LFTLQLLARAGIPvPP-------TLVTRDPDDLRAFLeelgG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 244 PVVVKLGHAHAGMGKIKVENQldfQDITSVVAMAKTYATTEA----FIDSK--YDIRI-----QKIGsnykAYMRTSISG 312
Cdd:COG0189   133 PVVLKPLDGSGGRGVFLVEDE---DALESILEALTELGSEPVlvqeFIPEEdgRDIRVlvvggEPVA----AIRRIPAEG 205

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624525583 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 1624525583 193 NSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITS 272
Cdd:pfam02750   1 NSLESIYNFCDKPWVFAQLIAIFHSLGGEKFPLIEQTFFPNHKEMLTAPNFPVVIKIGHAHAGMGKIKVENHHDFQDIAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 273 VVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVK 352
Cdd:pfam02750  81 VVALAKTYATAEAFIDSKYDIRIQKIGNNYKAYMRTSISGNWKANTGSAMLEQIAMSDRYKLWVDSCSEMFGGLDICAVK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1624525583 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 1624525583  92 RILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVsRSFKPDFILVRQHAYsm 171
Cdd:pfam02078   1 KTLLVIDDQHTDWSKYFRGKKIHGDYDIRVEQAEFSELNLTAYADGGCVVDMQVIRNGTKVV-RSFRPDFVLVRQHAR-- 77

                          90       100
                  ....*....|....*....|
gi 1624525583 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 1624525583   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 1624525583 394 SQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQS 473
Cdd:PRK07764  605 SSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA 684

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525583 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 1624525583  409 PWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSPQQQRSPGSPQLS 488
Cdd:PRK10263   740 PHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ 819

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1624525583  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 1624525583 381 DRQLMADLVVSKMSQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQP--QRSGSPSQ 458
Cdd:PRK14971  347 NKRLLVELTLIQLAQLTQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSatQPAGTPPT 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 459 QRLSPQGQQPLSPQSGSPQQQRSPGSPQLSRAssgsSPNQASKPGATLASQPRPPVQGrstsQQGEESKKPAPPHPHLNK 538
Cdd:PRK14971  427 VSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKI----PVSKVSSLGPSTLRPIQEKAEQ----ATGNIKEAPTGTQKEIFT 498

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1624525583 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 1624525583  394 SQLPMPGGTAP-------SPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQrsgSPSQQRLSPQGQ 466
Cdd:PHA03247  2848 PSLPLGGSVAPggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ---APPPPQPQPQPP 2924

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624525583  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 1624525583 397 PMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSP 476
Cdd:PRK07764  627 PAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA 706

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 477 QQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHlnksqsltNSLSTSDTSQRGT 556
Cdd:PRK07764  707 ATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPA--------PAAAPAAAPPPSP 778


                  ....*....
gi 1624525583 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 1624525583  397 PMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQP-LSPQSGS 475
Cdd:PHA03247  2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRrLTRPAVA 2789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583  476 PQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHLNKSQSLTNSlstSDTSQRG 555
Cdd:PHA03247  2790 SLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG---GDVRRRP 2866

                          170
                   ....*....|....*.
gi 1624525583  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 1624525583  397 PMPGGTAPSP--LRPWAPQIKSAKSPGQAQlgpqlgqPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSG 474
Cdd:PRK10263   375 PAPEGYPQQSqyAQPAVQYNEPLQQPVQPQ-------QPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAW 447

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1624525583  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 1624525583 447 SPQPQRSGSPSQ-QRLSPQGQQP-LSPQSGSPQQQRSPGSPQLSRASSG------SSPNQASKPGATLASQPRPPVQGRS 518
Cdd:pfam03154 150 SPQDNESDSDSSaQQQILQTQPPvLQAQSGAASPPSPPPPGTTQAATAGptpsapSVPPQGSPATSQPPNQTQSTAAPHT 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1624525583 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 1624525583  396 LPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQprpppqggprqAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGS 475
Cdd:PHA03247  2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-----------AASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583  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 1624525583 397 PMPGGTAPSPLRPWAPqiKSAKSPGQAqlgpqlgqPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSP 476
Cdd:PHA03378  676 PSPTGANTMLPIQWAP--GTMQPPPRA--------PTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRAR 745

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1624525583 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 1624525583 446 QSPQPQRSGSPSQQRLSPQGQQplspQSGSPQQQRSPGSPQLSRA----------SSGSSPNQASKPGAT-----LASQP 510
Cdd:pfam02166  54 QQQQQQVPQQPQQQESSPRQPQ----ASVQPQQAGDDGSPPAHNRgpagylaledDEQPQPSQAQPAAECcpengCVPEP 129

                          90       100
                  ....*....|....*....|..
gi 1624525583 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 1624525583 158 KPDFILVRQHAYSMALgedyrSLVIGLQYGGLPAVNSlYSVYNFCSKPWVFSQLIkifhslgpEKFPLVEQTFFPNHKP- 236
Cdd:TIGR00768  48 ELDVVIVRIVSMFRGL-----AVLRYLESLGVPVINS-SDAILNAGDKFLSHQLL--------AKAGIPLPRTGLAGSPe 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 237 --MVTAPH--FPVVVKLGHAHAGMGKIKVENQLDFQDITSVVAMAKTYATTeaFIDSKY-------DIRIQKIGSNYKAY 305
Cdd:TIGR00768 114 eaLKLIEEigFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQLNGPQNL--FLVQEYikkpggrDIRVFVVGDEVVAA 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525583 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 1624525583  91 PRILLVIDDAHTDWSKYFhgkkvngeieirveQAEFSELNLAAYV--TGGCMVDMQVVRNGTKVVSRSfKPDFILVRQHA 168
Cdd:COG0189     2 MKIAILTDPPDKDSTKAL--------------IEAAQRRGHEVEVidPDDLTLDLGRAPELYRGEDLS-EFDAVLPRIDP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 169 YSMALGedyrsLVIGLQYGGLPAVNSLYSVYNFCSKpwVFSQLIKIFHSLG-PEkfplveqTFFPNHKPMVTAPH----F 243
Cdd:COG0189    67 PFYGLA-----LLRQLEAAGVPVVNDPEAIRRARDK--LFTLQLLARAGIPvPP-------TLVTRDPDDLRAFLeelgG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525583 244 PVVVKLGHAHAGMGKIKVENQldfQDITSVVAMAKTYATTEA----FIDSK--YDIRI-----QKIGsnykAYMRTSISG 312
Cdd:COG0189   133 PVVLKPLDGSGGRGVFLVEDE---DALESILEALTELGSEPVlvqeFIPEEdgRDIRVlvvggEPVA----AIRRIPAEG 205

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1624525583 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 1624525583  450 PQRSGSPSQQRLS-PQGQQPLSPQSGSPQQQRSpgspqlSRASSGSSPnqASKPGATLASQPRPPVQGRSTSQQGEESKK 528
Cdd:PHA03247   375 PKRASLPTRKRRSaRHAATPFARGPGGDDQTRP------AAPVPASVP--TPAPTPVPASAPPPPATPLPSAEPGSDDGP 446

                           90       100
                   ....*....|....*....|....*.
gi 1624525583  529 PAPPHPHLNKSQSLTNSLSTSDTSQR 554
Cdd:PHA03247   447 APPPERQPPAPATEPAPDDPDDATRK 472
 
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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