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Conserved domains on  [gi|2750921207|gb|KAL0531070|]
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hypothetical protein Q4I32_000732 [Leishmania shawi]

Protein Classification

ATP-binding protein( domain architecture ID 10588955)

ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain may function as an ATPase

Gene Ontology:  GO:0005524
PubMed:  18208389|15037234

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 170-300 6.62e-06

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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 50.92  E-value: 6.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  170 QPPGMPHHHNPAGMTMPPPHQPGMMPVWMQSPQHTQQLQqapgmmmpmnsmmpmpMSMGAVSSPMSPGQRSSGPHSLPS- 248
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQ----------------VSPQPLPQPSLHGQMPPMPHSLQTg 285

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2750921207  249 QQHQQHPGMMMPFYPPPQAPHGTMPPLPNMTPPSPAMMMPRVPVPATGPASG 300
Cdd:pfam03154  286 PSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQ 337
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 401-487 6.16e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


:

Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 42.11  E-value: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  401 LAALNSNKPPKFSCVLLSGIPAVGKTTLGRELVNSLKTDGMGWAFFSGADFLTEQQGKRSVweTTRDVFDALSSRLDELL 480
Cdd:pfam13191   13 LDALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEAL--TREGLLRQLLDELESSL 90


                   ....*..
gi 2750921207  481 ERQHQAR 487
Cdd:pfam13191   91 LEAWRAA 97
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 6-335 8.37e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207    6 TDAGKPPRRQQRQQQASPPIPPALTETRLNANAKSFTPSAaeaPLPPSTPAAASGCAAAAAHLSAKQPPETDHAGSKTQP 85
Cdd:PHA03247  2696 TSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAL---PAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPP 2772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207   86 AGAGGKEPPAGGAQNLVPPVPQFPPAQSGKKESMMMPPPPPPPRFLEIPGMVPGMPPPMPGTASARYMMPPGLMPPPPPS 165
Cdd:PHA03247  2773 AAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL 2852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  166 EMMFQPPGMPHHHNPAGMTMPPPHQPGMMPV-WMQSPQHTQQLQQAPGMMMpmnsmmpmpmsmgavsSPMSPGQRSSGPH 244
Cdd:PHA03247  2853 GGSVAPGGDVRRRPPSRSPAAKPAAPARPPVrRLARPAVSRSTESFALPPD----------------QPERPPQPQAPPP 2916

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  245 SLPSQQHQQHPgmmMPFYPPPQAPHGTMPPLPNMTP-----PSPAMMMPRVP--VPATGPASGTIITPPAAGLMAPPPHH 317
Cdd:PHA03247  2917 PQPQPQPPPPP---QPQPPPPPPPRPQPPLAPTTDPagagePSGAVPQPWLGalVPGRVAVPRFRVPQPAPSREAPASST 2993

                          330
                   ....*....|....*...
gi 2750921207  318 LPFHPHSGSVITGGAHSI 335
Cdd:PHA03247  2994 PPLTGHSLSRVSSWASSL 3011
 
Name Accession Description Interval E-value
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 170-300 6.62e-06

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: 50.92  E-value: 6.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  170 QPPGMPHHHNPAGMTMPPPHQPGMMPVWMQSPQHTQQLQqapgmmmpmnsmmpmpMSMGAVSSPMSPGQRSSGPHSLPS- 248
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQ----------------VSPQPLPQPSLHGQMPPMPHSLQTg 285

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2750921207  249 QQHQQHPGMMMPFYPPPQAPHGTMPPLPNMTPPSPAMMMPRVPVPATGPASG 300
Cdd:pfam03154  286 PSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQ 337
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 172-297 1.80e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 43.62  E-value: 1.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207   172 PGMPHHhnPAGMTMPPPHQPGMMPvwmqsPQHTQQLQQapgmmmpmnsmmpmpmsmgavssPMSPgqrSSGPHSL-PSQQ 250
Cdd:smart00818   41 PVSQQH--PPTHTLQPHHHIPVLP-----AQQPVVPQQ-----------------------PLMP---VPGQHSMtPTQH 87

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 2750921207   251 HQqhPGMMMPFYPPPQAPHGT-MPPLPNMTPPSPAMMMPRVPVPATGP 297
Cdd:smart00818   88 HQ--PNLPQPAQQPFQPQPLQpPQPQQPMQPQPPVHPIPPLPPQPPLP 133
PHA03378 PHA03378
EBNA-3B; Provisional
 170-330 5.97e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 5.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  170 QPPGMPHHHNPAGMTM------------PPPHQPGMMPVWMQSPQHTQQLQQAPGMMMPMNSMMPMPMSMGAVSSPMSPG 237
Cdd:PHA03378   668 QIGHIPYQPSPTGANTmlpiqwapgtmqPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPP 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  238 QRSSGPHSLPsqqhQQHPGMMMPFYPPPQAPHGTMPPlpnMTPPSPaMMMPR-----VPVPATGPASgTIITPPAAGLMA 312
Cdd:PHA03378   748 AAAPGRARPP----AAAPGRARPPAAAPGAPTPQPPP---QAPPAP-QQRPRgaptpQPPPQAGPTS-MQLMPRAAPGQQ 818

                          170
                   ....*....|....*...
gi 2750921207  313 PPPHHLPFHPHSGSVITG 330
Cdd:PHA03378   819 GPTKQILRQLLTGGVKRG 836
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 401-487 6.16e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 42.11  E-value: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  401 LAALNSNKPPKFSCVLLSGIPAVGKTTLGRELVNSLKTDGMGWAFFSGADFLTEQQGKRSVweTTRDVFDALSSRLDELL 480
Cdd:pfam13191   13 LDALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEAL--TREGLLRQLLDELESSL 90


                   ....*..
gi 2750921207  481 ERQHQAR 487
Cdd:pfam13191   91 LEAWRAA 97
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
 170-288 6.38e-04

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 43.88  E-value: 6.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  170 QPPGMPHHHNPAGMTMPPPH---------QPGMM---------PVWMQSPQHTQQLQQAPGMMMPMNSMMPMPMSMgavs 231
Cdd:cd22056    163 RALPTAPPAHQPATSPPPLGykiktepveQSCMMaaggggfmgQQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGR---- 238

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750921207  232 sPMSPGQRSSGPHSLPSQQHQQHPGMMMPfYPPPQAPHGT-------------------MPPLPNMTPPSPAMMMP 288
Cdd:cd22056    239 -GGPDCHLLHSSHHHHHHHHLQYQYMNAP-YPPHYAHQGApqfhgqysvfrepmrvhhqGHPGSMLTPPSSPPLLE 312
PHA03247 PHA03247
large tegument protein UL36; Provisional
 6-335 8.37e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207    6 TDAGKPPRRQQRQQQASPPIPPALTETRLNANAKSFTPSAaeaPLPPSTPAAASGCAAAAAHLSAKQPPETDHAGSKTQP 85
Cdd:PHA03247  2696 TSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAL---PAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPP 2772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207   86 AGAGGKEPPAGGAQNLVPPVPQFPPAQSGKKESMMMPPPPPPPRFLEIPGMVPGMPPPMPGTASARYMMPPGLMPPPPPS 165
Cdd:PHA03247  2773 AAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL 2852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  166 EMMFQPPGMPHHHNPAGMTMPPPHQPGMMPV-WMQSPQHTQQLQQAPGMMMpmnsmmpmpmsmgavsSPMSPGQRSSGPH 244
Cdd:PHA03247  2853 GGSVAPGGDVRRRPPSRSPAAKPAAPARPPVrRLARPAVSRSTESFALPPD----------------QPERPPQPQAPPP 2916

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  245 SLPSQQHQQHPgmmMPFYPPPQAPHGTMPPLPNMTP-----PSPAMMMPRVP--VPATGPASGTIITPPAAGLMAPPPHH 317
Cdd:PHA03247  2917 PQPQPQPPPPP---QPQPPPPPPPRPQPPLAPTTDPagagePSGAVPQPWLGalVPGRVAVPRFRVPQPAPSREAPASST 2993

                          330
                   ....*....|....*...
gi 2750921207  318 LPFHPHSGSVITGGAHSI 335
Cdd:PHA03247  2994 PPLTGHSLSRVSSWASSL 3011
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 410-495 1.48e-03

Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 41.87  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  410 PKFSCVLLSGIPAVGKTTLGRE-LVNSLK--------------------TDGMGWAFFSGADFLTEQQGKRSVWETTRDV 468
Cdd:cd01124     17 PKGSVTLLTGGPGTGKTLFGLQfLYAGAKngepglfftfeesperllrnAKSFGWDFDEMEDEGKLIIVDAPPTEAGRFS 96

                           90       100
                   ....*....|....*....|....*..
gi 2750921207  469 FDALSSRLDELLErqhqARDIKGLVID 495
Cdd:cd01124     97 LDELLSRILSIIK----SFKAKRVVID 119
 
Name Accession Description Interval E-value
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 170-300 6.62e-06

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: 50.92  E-value: 6.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  170 QPPGMPHHHNPAGMTMPPPHQPGMMPVWMQSPQHTQQLQqapgmmmpmnsmmpmpMSMGAVSSPMSPGQRSSGPHSLPS- 248
Cdd:pfam03154  222 QSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQ----------------VSPQPLPQPSLHGQMPPMPHSLQTg 285

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2750921207  249 QQHQQHPGMMMPFYPPPQAPHGTMPPLPNMTPPSPAMMMPRVPVPATGPASG 300
Cdd:pfam03154  286 PSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQ 337
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 172-297 1.80e-04

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 43.62  E-value: 1.80e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207   172 PGMPHHhnPAGMTMPPPHQPGMMPvwmqsPQHTQQLQQapgmmmpmnsmmpmpmsmgavssPMSPgqrSSGPHSL-PSQQ 250
Cdd:smart00818   41 PVSQQH--PPTHTLQPHHHIPVLP-----AQQPVVPQQ-----------------------PLMP---VPGQHSMtPTQH 87

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 2750921207   251 HQqhPGMMMPFYPPPQAPHGT-MPPLPNMTPPSPAMMMPRVPVPATGP 297
Cdd:smart00818   88 HQ--PNLPQPAQQPFQPQPLQpPQPQQPMQPQPPVHPIPPLPPQPPLP 133
PHA03378 PHA03378
EBNA-3B; Provisional
 170-330 5.97e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 5.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  170 QPPGMPHHHNPAGMTM------------PPPHQPGMMPVWMQSPQHTQQLQQAPGMMMPMNSMMPMPMSMGAVSSPMSPG 237
Cdd:PHA03378   668 QIGHIPYQPSPTGANTmlpiqwapgtmqPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPP 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  238 QRSSGPHSLPsqqhQQHPGMMMPFYPPPQAPHGTMPPlpnMTPPSPaMMMPR-----VPVPATGPASgTIITPPAAGLMA 312
Cdd:PHA03378   748 AAAPGRARPP----AAAPGRARPPAAAPGAPTPQPPP---QAPPAP-QQRPRgaptpQPPPQAGPTS-MQLMPRAAPGQQ 818

                          170
                   ....*....|....*...
gi 2750921207  313 PPPHHLPFHPHSGSVITG 330
Cdd:PHA03378   819 GPTKQILRQLLTGGVKRG 836
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 401-487 6.16e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 42.11  E-value: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  401 LAALNSNKPPKFSCVLLSGIPAVGKTTLGRELVNSLKTDGMGWAFFSGADFLTEQQGKRSVweTTRDVFDALSSRLDELL 480
Cdd:pfam13191   13 LDALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEAL--TREGLLRQLLDELESSL 90


                   ....*..
gi 2750921207  481 ERQHQAR 487
Cdd:pfam13191   91 LEAWRAA 97
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
 170-288 6.38e-04

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 43.88  E-value: 6.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  170 QPPGMPHHHNPAGMTMPPPH---------QPGMM---------PVWMQSPQHTQQLQQAPGMMMPMNSMMPMPMSMgavs 231
Cdd:cd22056    163 RALPTAPPAHQPATSPPPLGykiktepveQSCMMaaggggfmgQQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGR---- 238

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2750921207  232 sPMSPGQRSSGPHSLPSQQHQQHPGMMMPfYPPPQAPHGT-------------------MPPLPNMTPPSPAMMMP 288
Cdd:cd22056    239 -GGPDCHLLHSSHHHHHHHHLQYQYMNAP-YPPHYAHQGApqfhgqysvfrepmrvhhqGHPGSMLTPPSSPPLLE 312
PHA03247 PHA03247
large tegument protein UL36; Provisional
 6-335 8.37e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207    6 TDAGKPPRRQQRQQQASPPIPPALTETRLNANAKSFTPSAaeaPLPPSTPAAASGCAAAAAHLSAKQPPETDHAGSKTQP 85
Cdd:PHA03247  2696 TSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAL---PAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPP 2772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207   86 AGAGGKEPPAGGAQNLVPPVPQFPPAQSGKKESMMMPPPPPPPRFLEIPGMVPGMPPPMPGTASARYMMPPGLMPPPPPS 165
Cdd:PHA03247  2773 AAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL 2852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  166 EMMFQPPGMPHHHNPAGMTMPPPHQPGMMPV-WMQSPQHTQQLQQAPGMMMpmnsmmpmpmsmgavsSPMSPGQRSSGPH 244
Cdd:PHA03247  2853 GGSVAPGGDVRRRPPSRSPAAKPAAPARPPVrRLARPAVSRSTESFALPPD----------------QPERPPQPQAPPP 2916

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  245 SLPSQQHQQHPgmmMPFYPPPQAPHGTMPPLPNMTP-----PSPAMMMPRVP--VPATGPASGTIITPPAAGLMAPPPHH 317
Cdd:PHA03247  2917 PQPQPQPPPPP---QPQPPPPPPPRPQPPLAPTTDPagagePSGAVPQPWLGalVPGRVAVPRFRVPQPAPSREAPASST 2993

                          330
                   ....*....|....*...
gi 2750921207  318 LPFHPHSGSVITGGAHSI 335
Cdd:PHA03247  2994 PPLTGHSLSRVSSWASSL 3011
AAA_18 pfam13238
AAA domain;
415-547 9.70e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.87  E-value: 9.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  415 VLLSGIPAVGKTTLGRELVNSLKTDGMGWAFFSGADFLTEQQGKrsvWETTRDVFDALSSRLDELLERQHQARDIKGLVI 494
Cdd:pfam13238    1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLGDDPE---TRESKRLDEDKLDRLLDLLEENAALEEGGNLII 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2750921207  495 DknckgiediyYLNALLLSKDIPFVGIVGLECaDDDVLVKRMGGDDYLREKLK 547
Cdd:pfam13238   78 D----------GHLAELEPERAKDLVGIVLRA-SPEELLERLEKRGYEEAKIK 119
KaiC-like cd01124
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ...
 410-495 1.48e-03

Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.


Pssm-ID: 410869 [Multi-domain]  Cd Length: 222  Bit Score: 41.87  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  410 PKFSCVLLSGIPAVGKTTLGRE-LVNSLK--------------------TDGMGWAFFSGADFLTEQQGKRSVWETTRDV 468
Cdd:cd01124     17 PKGSVTLLTGGPGTGKTLFGLQfLYAGAKngepglfftfeesperllrnAKSFGWDFDEMEDEGKLIIVDAPPTEAGRFS 96

                           90       100
                   ....*....|....*....|....*..
gi 2750921207  469 FDALSSRLDELLErqhqARDIKGLVID 495
Cdd:cd01124     97 LDELLSRILSIIK----SFKAKRVVID 119
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 165-308 2.22e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  165 SEMMFQPPGMPHHHNPAGMTMPPPHQPGMMPVwmQSPQHTQQLQQAPGMMMPMNSMMPMPMSMGAVSSPMSPGQRSsgph 244
Cdd:PRK10263   741 HEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPV--APQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQ---- 814

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  245 slPSQQHQQHPGMMMPFYPPPQAPHGTMP------PLPNMTPPSPAMMMPRVPVPatgpaSGTIITPPAA 308
Cdd:PRK10263   815 --PQYQQPQQPVAPQPQYQQPQQPVAPQPqdtllhPLLMRNGDSRPLHKPTTPLP-----SLDLLTPPPS 877
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 9-295 2.29e-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: 42.45  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207    9 GKPPRRQQRQQQASPPIPPALTETRL-NANAKSFTPSAAEAPLPPSTPAAASGCAAAAAHLSAKQ-----PPETDHAGSK 82
Cdd:pfam03154  169 TQPPVLQAQSGAASPPSPPPPGTTQAaTAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQtptlhPQRLPSPHPP 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207   83 TQPAgAGGKEPPAGGAQNLVPPV---PQFPPAQSGKKESMMMPPPPPPPRFLEIPGMVPGMPPPMPGTASARYMMPPGLM 159
Cdd:pfam03154  249 LQPM-TQPPPPSQVSPQPLPQPSlhgQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHT 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  160 PPPPPSEMMFQPP----------GMPH-----------------HHNPAGMTMPPPHQ--------PGMMPVWMQSPQH- 203
Cdd:pfam03154  328 PPSQSQLQSQQPPreqplppaplSMPHikpppttpipqlpnpqsHKHPPHLSGPSPFQmnsnlpppPALKPLSSLSTHHp 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  204 ----------TQQLQQAPGMMMPMNSMMPMPMSMGAVSSPMSPGQRSSGPHSLPSQQHQQHPGMMMPFYPPPQAPHGTMP 273
Cdd:pfam03154  408 psahppplqlMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSS 487

                          330       340
                   ....*....|....*....|..
gi 2750921207  274 PLPNMTPPSPAMMMPRVPVPAT 295
Cdd:pfam03154  488 AMPGIQPPSSASVSSSGPVPAA 509
AAA_17 pfam13207
AAA domain;
418-537 4.50e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 39.14  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2750921207  418 SGIPAVGKTTLGRELVNSLktdgmGWAFFSGADFLTEQQGKRSvWETTRDVFDALSSRLDELLeRQHQARDI------KG 491
Cdd:pfam13207    1 TGVPGSGKTTQLKKLAEKL-----GFPHISAGDLLREEAKERG-LVEDRDEMRKLPLEPQKEL-QKLAAERIaeeageGG 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2750921207  492 LVIDKNCKGIEDIYYLNALL--LSKDIPFVGIVGLECADDDVLVKRMG 537
Cdd:pfam13207   74 VIVDGHPRIKTPAGYLPGLPveVLRELKPDAIILLEADPEEILERRLK 121
 
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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