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Conserved domains on  [gi|157820473|ref|NP_001101025|]
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zinc finger protein Pegasus [Rattus norvegicus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10603440)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  11361095|22803940|30718982
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
124-148 5.44e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.44e-05
                          10        20
                  ....*....|....*....|....*
gi 157820473  124 HLEAHMRSHTGEKPYKCELCSFRCS 148
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03269 super family cl29788
envelope glycoprotein C; Provisional
 251-361 1.06e-04

envelope glycoprotein C; Provisional


The actual alignment was detected with superfamily member PHA03269:

Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 44.33  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473 251 PLNQLSTLAG-QLSSLPPENQNPASPDVDP------CPDEKPFMIQQPSAQAVVSAVSASIPQSSSPTSPDPRP---SHS 320
Cdd:PHA03269  27 PIPELHTSAAtQKPDPAPAPHQAASRAPDPavaptsAASRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVapqLAA 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157820473 321 QRNYSPVAGPSSEPSAHTSTPSIGNSQPS-TPAPTLPVQDPQ 361
Cdd:PHA03269 107 APKPDAAEAFTSAAQAHEAPADAGTSAASkKPDPAAHTQHSP 148
zf-H2C2_2 pfam13465
Zinc-finger double domain;
96-121 7.03e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 7.03e-04
                          10        20
                  ....*....|....*....|....*.
gi 157820473   96 RLIEHIRIHTGEKPHRCHLCPFASAY 121
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
124-148 5.44e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.44e-05
                          10        20
                  ....*....|....*....|....*
gi 157820473  124 HLEAHMRSHTGEKPYKCELCSFRCS 148
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 251-361 1.06e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 44.33  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473 251 PLNQLSTLAG-QLSSLPPENQNPASPDVDP------CPDEKPFMIQQPSAQAVVSAVSASIPQSSSPTSPDPRP---SHS 320
Cdd:PHA03269  27 PIPELHTSAAtQKPDPAPAPHQAASRAPDPavaptsAASRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVapqLAA 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157820473 321 QRNYSPVAGPSSEPSAHTSTPSIGNSQPS-TPAPTLPVQDPQ 361
Cdd:PHA03269 107 APKPDAAEAFTSAAQAHEAPADAGTSAASkKPDPAAHTQHSP 148
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 248-373 1.25e-04

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 44.09  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473 248 VDNPLNQLSTL---AGQLSSLPPENQNPASPDVDPC----------PDEKPFM-----IQQPSAQAVVSAVSASIPQSSS 309
Cdd:cd23959  115 VPNPFSASSSTqreTHKTAQVAPPKAEPQTAPVTPFgqlpmfgqhpPPAKPLPaaaaaQQSSASPGEVASPFASGTVSAS 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157820473 310 PTSPDPRPSHSQRNYSPVAGPSSEPSAhTSTPSIGNSQPStpAPTLPVQDPQLLHHCQHCDMYF 373
Cdd:cd23959  195 PFATATDTAPSSGAPDGFPAEASAPSP-FAAPASAASFPA--APVANGEAATPTHACTICGKAF 255
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 220-360 2.09e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.75  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473  220 PNIQTDSYetmAKTTPTGGLPRD---PQELMVDNPLNQLSTLAGQLSSLPPENQNPASPDV-DPCPDEKPFMIQQPSAQA 295
Cdd:pfam05109 432 PTLNTTGF---AAPNTTTGLPSSthvPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTpSPSPRDNGTESKAPDMTS 508

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820473  296 VVSAVSASIPQSSSPTSPDPRPSHSQRnySPVAGPSS--------EPSAHTSTPSIGNSQPSTPAPTLPVQDP 360
Cdd:pfam05109 509 PTSAVTTPTPNATSPTPAVTTPTPNAT--SPTLGKTSptsavttpTPNATSPTPAVTTPTPNATIPTLGKTSP 579
zf-H2C2_2 pfam13465
Zinc-finger double domain;
96-121 7.03e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 7.03e-04
                          10        20
                  ....*....|....*....|....*.
gi 157820473   96 RLIEHIRIHTGEKPHRCHLCPFASAY 121
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
124-148 5.44e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.44e-05
                          10        20
                  ....*....|....*....|....*
gi 157820473  124 HLEAHMRSHTGEKPYKCELCSFRCS 148
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 251-361 1.06e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 44.33  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473 251 PLNQLSTLAG-QLSSLPPENQNPASPDVDP------CPDEKPFMIQQPSAQAVVSAVSASIPQSSSPTSPDPRP---SHS 320
Cdd:PHA03269  27 PIPELHTSAAtQKPDPAPAPHQAASRAPDPavaptsAASRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVapqLAA 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157820473 321 QRNYSPVAGPSSEPSAHTSTPSIGNSQPS-TPAPTLPVQDPQ 361
Cdd:PHA03269 107 APKPDAAEAFTSAAQAHEAPADAGTSAASkKPDPAAHTQHSP 148
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 248-373 1.25e-04

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 44.09  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473 248 VDNPLNQLSTL---AGQLSSLPPENQNPASPDVDPC----------PDEKPFM-----IQQPSAQAVVSAVSASIPQSSS 309
Cdd:cd23959  115 VPNPFSASSSTqreTHKTAQVAPPKAEPQTAPVTPFgqlpmfgqhpPPAKPLPaaaaaQQSSASPGEVASPFASGTVSAS 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157820473 310 PTSPDPRPSHSQRNYSPVAGPSSEPSAhTSTPSIGNSQPStpAPTLPVQDPQLLHHCQHCDMYF 373
Cdd:cd23959  195 PFATATDTAPSSGAPDGFPAEASAPSP-FAAPASAASFPA--APVANGEAATPTHACTICGKAF 255
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 220-360 2.09e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.75  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473  220 PNIQTDSYetmAKTTPTGGLPRD---PQELMVDNPLNQLSTLAGQLSSLPPENQNPASPDV-DPCPDEKPFMIQQPSAQA 295
Cdd:pfam05109 432 PTLNTTGF---AAPNTTTGLPSSthvPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTpSPSPRDNGTESKAPDMTS 508

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157820473  296 VVSAVSASIPQSSSPTSPDPRPSHSQRnySPVAGPSS--------EPSAHTSTPSIGNSQPSTPAPTLPVQDP 360
Cdd:pfam05109 509 PTSAVTTPTPNATSPTPAVTTPTPNAT--SPTLGKTSptsavttpTPNATSPTPAVTTPTPNATIPTLGKTSP 579
zf-H2C2_2 pfam13465
Zinc-finger double domain;
96-121 7.03e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 7.03e-04
                          10        20
                  ....*....|....*....|....*.
gi 157820473   96 RLIEHIRIHTGEKPHRCHLCPFASAY 121
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
261-360 9.45e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.30  E-value: 9.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473 261 QLSSLPPENQNpASPDVDPCPDEKPFMIQQpsaqavvsavsASIPQSSSPTSPDPRPSHSQRNYSPVAGPSSePSAHTST 340
Cdd:PRK14971 358 QLAQLTQKGDD-ASGGRGPKQHIKPVFTQP-----------AAAPQPSAAAAASPSPSQSSAAAQPSAPQSA-TQPAGTP 424

                         90       100
                 ....*....|....*....|
gi 157820473 341 PSIgNSQPSTPAPTLPVQDP 360
Cdd:PRK14971 425 PTV-SVDPPAAVPVNPPSTA 443
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 263-360 2.08e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473  263 SSLPPENQNPASPDVDPCPDEKPFMIQQPS--AQAVVSAVSASIPQSSSPTSPDPRPSHSQRNYSPVAGPSsePSAHTST 340
Cdd:PHA03307  238 DSSSSESSGCGWGPENECPLPRPAPITLPTriWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPA--PSSPRAS 315

                          90       100
                  ....*....|....*....|
gi 157820473  341 PSIGNSQPSTPAPTLPVQDP 360
Cdd:PHA03307  316 SSSSSSRESSSSSTSSSSES 335
PRK10856 PRK10856
cytoskeleton protein RodZ;
244-352 2.51e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 39.62  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473 244 QEL--MVDNPLNQLSTLAGQLSSLPPENQNPASPDVDPCPDEKPFMIQQPSAQAVVSAVSASIPQSSSPTSPDPRPSHSQ 321
Cdd:PRK10856 141 EEIttMADQSSAELSQNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTA 220

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157820473 322 RNysPVAGPSSEPSAHTSTPSiGNSQPSTPA 352
Cdd:PRK10856 221 AT--PAPAAPATPDGAAPLPT-DQAGVSTPA 248
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 201-360 2.83e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473  201 PPSMVVQKPDYLNDFTHEIPNIQTDSYETMAKTTPTGGLPRDPQELMVDNPLNQLSTLAGQLSSL-------------PP 267
Cdd:PHA03307   39 SQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREgsptppgpsspdpPP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473  268 ENQNPASPDVDPCPDekpfmiQQPSAQAVVSAVSASIPQSSSPTSPDPRPSHSQRNYSPVAGPSSEPSAHTSTpsignsq 347
Cdd:PHA03307  119 PTPPPASPPPSPAPD------LSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARA------- 185

                         170
                  ....*....|...
gi 157820473  348 PSTPAPTLPVQDP 360
Cdd:PHA03307  186 PSSPPAEPPPSTP 198
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 251-360 7.09e-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: 38.98  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820473  251 PLNQLSTLAGQLSSLPPENQNPASPDVDPCPDEKPFMIQQPSaqavVSAVSASIPQSSSPTSPDPRPSHSQRNY----SP 326
Cdd:pfam03154 398 PLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQS----LPPPAASHPPTSGLHQVPSQSPFPQHPFvpggPP 473

                          90       100       110
                  ....*....|....*....|....*....|....
gi 157820473  327 VAGPSSEPSAHTSTPSIGNSQPSTPAPTLPVQDP 360
Cdd:pfam03154 474 PITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVP 507
 
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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