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Conserved domains on  [gi|1723913129|ref|NP_001359056|]
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zinc finger protein Pegasus isoform 1 [Homo sapiens]

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 5.28e-05

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.28e-05
                          10        20
                  ....*....|....*....|....*
gi 1723913129 124 HLEAHMRSHTGEKPYKCELCSFRCS 148
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03269 super family cl29788
envelope glycoprotein C; Provisional
 251-361 8.49e-05

envelope glycoprotein C; Provisional


The actual alignment was detected with superfamily member PHA03269:

Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 44.72  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 251 PLNQLSTLAGQLSSLP---PENQNPASPDVVPCP----DEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRP---SHS 320
Cdd:PHA03269   27 PIPELHTSAATQKPDPapaPHQAASRAPDPAVAPtsaaSRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVapqLAA 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1723913129 321 QRNYSPVAGPSSEPSAHTSTPSIGNSQPS-TPAPALPVQDPQ 361
Cdd:PHA03269  107 APKPDAAEAFTSAAQAHEAPADAGTSAASkKPDPAAHTQHSP 148
zf-H2C2_2 pfam13465
Zinc-finger double domain;
96-121 6.89e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 6.89e-04
                          10        20
                  ....*....|....*....|....*.
gi 1723913129  96 RLIEHIRIHTGEKPHRCHLCPFASAY 121
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
124-148 5.28e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.28e-05
                          10        20
                  ....*....|....*....|....*
gi 1723913129 124 HLEAHMRSHTGEKPYKCELCSFRCS 148
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 251-361 8.49e-05

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 44.72  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 251 PLNQLSTLAGQLSSLP---PENQNPASPDVVPCP----DEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRP---SHS 320
Cdd:PHA03269   27 PIPELHTSAATQKPDPapaPHQAASRAPDPAVAPtsaaSRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVapqLAA 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1723913129 321 QRNYSPVAGPSSEPSAHTSTPSIGNSQPS-TPAPALPVQDPQ 361
Cdd:PHA03269  107 APKPDAAEAFTSAAQAHEAPADAGTSAASkKPDPAAHTQHSP 148
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 248-373 3.56e-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: 42.55  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 248 VDNPLNQLSTL---AGQLSSLPPENQNPASPDVVPC----------PDEKPFM-----IQQPSTQAVVSAVSASIPQSSS 309
Cdd:cd23959   115 VPNPFSASSSTqreTHKTAQVAPPKAEPQTAPVTPFgqlpmfgqhpPPAKPLPaaaaaQQSSASPGEVASPFASGTVSAS 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1723913129 310 PTSPEPRPSHSQRNYSPVAGPSSEPSAhTSTPSIGNSQPStpAPALPVQDPQLLHHCQHCDMYF 373
Cdd:cd23959   195 PFATATDTAPSSGAPDGFPAEASAPSP-FAAPASAASFPA--APVANGEAATPTHACTICGKAF 255
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 220-356 5.55e-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: 42.21  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 220 PNIQTDSYESMAKTTptgGLPRD---PQELMVDNPLNQLSTLAGQLSSLPPENQNPASPDV-VPCPDEKPFMIQQPSTQA 295
Cdd:pfam05109 432 PTLNTTGFAAPNTTT---GLPSSthvPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTpSPSPRDNGTESKAPDMTS 508

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1723913129 296 VVSAVSASIPQSSSPTSPEPRPSHSQRnySPVAGPSSePSAHTSTPSIGNSQPsTPAPALP 356
Cdd:pfam05109 509 PTSAVTTPTPNATSPTPAVTTPTPNAT--SPTLGKTS-PTSAVTTPTPNATSP-TPAVTTP 565
zf-H2C2_2 pfam13465
Zinc-finger double domain;
96-121 6.89e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 6.89e-04
                          10        20
                  ....*....|....*....|....*.
gi 1723913129  96 RLIEHIRIHTGEKPHRCHLCPFASAY 121
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 263-358 2.33e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 40.22  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 263 SSLPPENQNPASPDVVPcpdEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQRNYSPVAGPSSEPSAHTSTPS 342
Cdd:COG3266   263 SASAPATTSLGEQQEVS---LPPAVAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAPA 339

                          90       100
                  ....*....|....*....|
gi 1723913129 343 ----IGNSQPSTPAPALPVQ 358
Cdd:COG3266   340 peaaAAAAAPAAPAVAKKLA 359
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
108-350 8.73e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.14  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 108 KPHRCHLCPFASAYERHLEAHMRSHTGEKPYKCELCSFRC--SDRSNLSHHRRRKHK-----------MVPIKGTRSSLS 174
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKsfSRPLELSRHLRTHHNnpsdlnskslpLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 175 SKKMWGVLQKKTSNLGYSrrALINLSPPSMVVQKPDYLNDFTHEIPNIQTDSYESMAKTTPTGGLPRDPQELMVDNPLNQ 254
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLP--PSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 255 LSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQ------RNYSPVA 328
Cdd:COG5048   190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSasesprSSLPTAS 269

                         250       260
                  ....*....|....*....|..
gi 1723913129 329 GPSSEPSAHTSTPSIGNSQPST 350
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSLPIK 291
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
124-148 5.28e-05

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 5.28e-05
                          10        20
                  ....*....|....*....|....*
gi 1723913129 124 HLEAHMRSHTGEKPYKCELCSFRCS 148
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 251-361 8.49e-05

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 44.72  E-value: 8.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 251 PLNQLSTLAGQLSSLP---PENQNPASPDVVPCP----DEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRP---SHS 320
Cdd:PHA03269   27 PIPELHTSAATQKPDPapaPHQAASRAPDPAVAPtsaaSRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVapqLAA 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1723913129 321 QRNYSPVAGPSSEPSAHTSTPSIGNSQPS-TPAPALPVQDPQ 361
Cdd:PHA03269  107 APKPDAAEAFTSAAQAHEAPADAGTSAASkKPDPAAHTQHSP 148
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 248-373 3.56e-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: 42.55  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 248 VDNPLNQLSTL---AGQLSSLPPENQNPASPDVVPC----------PDEKPFM-----IQQPSTQAVVSAVSASIPQSSS 309
Cdd:cd23959   115 VPNPFSASSSTqreTHKTAQVAPPKAEPQTAPVTPFgqlpmfgqhpPPAKPLPaaaaaQQSSASPGEVASPFASGTVSAS 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1723913129 310 PTSPEPRPSHSQRNYSPVAGPSSEPSAhTSTPSIGNSQPStpAPALPVQDPQLLHHCQHCDMYF 373
Cdd:cd23959   195 PFATATDTAPSSGAPDGFPAEASAPSP-FAAPASAASFPA--APVANGEAATPTHACTICGKAF 255
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 220-356 5.55e-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: 42.21  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 220 PNIQTDSYESMAKTTptgGLPRD---PQELMVDNPLNQLSTLAGQLSSLPPENQNPASPDV-VPCPDEKPFMIQQPSTQA 295
Cdd:pfam05109 432 PTLNTTGFAAPNTTT---GLPSSthvPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTpSPSPRDNGTESKAPDMTS 508

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1723913129 296 VVSAVSASIPQSSSPTSPEPRPSHSQRnySPVAGPSSePSAHTSTPSIGNSQPsTPAPALP 356
Cdd:pfam05109 509 PTSAVTTPTPNATSPTPAVTTPTPNAT--SPTLGKTS-PTSAVTTPTPNATSP-TPAVTTP 565
zf-H2C2_2 pfam13465
Zinc-finger double domain;
96-121 6.89e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 6.89e-04
                          10        20
                  ....*....|....*....|....*.
gi 1723913129  96 RLIEHIRIHTGEKPHRCHLCPFASAY 121
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PHA03247 PHA03247
large tegument protein UL36; Provisional
 249-360 1.29e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129  249 DNPLNQLSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPST---------QAVVSAVSASIPQSSSPTSPEPRPSH 319
Cdd:PHA03247  2754 PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLpspwdpadpPAAVLAPAAALPPAASPAGPLPPPTS 2833

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1723913129  320 SQrnysPVAGPSSEPSAHTSTPSIGN------------SQPSTPAPALPVQDP 360
Cdd:PHA03247  2834 AQ----PTAPPPPPGPPPPSLPLGGSvapggdvrrrppSRSPAAKPAAPARPP 2882
PRK10856 PRK10856
cytoskeleton protein RodZ;
244-355 1.94e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.01  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 244 QEL--MVDNPLNQLSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQ 321
Cdd:PRK10856  141 EEIttMADQSSAELSQNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTA 220

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1723913129 322 RNYSPVAGPSSEPSAHTSTPSIGNSQPSTPAPAL 355
Cdd:PRK10856  221 ATPAPAAPATPDGAAPLPTDQAGVSTPAADPNAL 254
motB PRK12799
flagellar motor protein MotB; Reviewed
 257-356 2.09e-03

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 40.08  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 257 TLAGQLSSLPPENQNPAS-PDVVPCPDEKPfmiQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQRNYSPVAGPSSEP- 334
Cdd:PRK12799  307 SSAVTQSSAITPSSAAIPsPAVIPSSVTTQ---SATTTQASAVALSSAGVLPSDVTLPGTVALPAAEPVNMQPQPMSTTe 383

                          90       100
                  ....*....|....*....|....
gi 1723913129 335 SAHTSTPSI--GNSQPSTPAPALP 356
Cdd:PRK12799  384 TQQSSTGNItsTANGPTTSLPAAP 407
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 263-358 2.33e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 40.22  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 263 SSLPPENQNPASPDVVPcpdEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQRNYSPVAGPSSEPSAHTSTPS 342
Cdd:COG3266   263 SASAPATTSLGEQQEVS---LPPAVAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAPA 339

                          90       100
                  ....*....|....*....|
gi 1723913129 343 ----IGNSQPSTPAPALPVQ 358
Cdd:COG3266   340 peaaAAAAAPAAPAVAKKLA 359
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
261-360 3.82e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 39.37  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 261 QLSSLPPENQNpASPDVVPCPDEKPFMIQQpstqavvsavsASIPQSSSPTSPEPRPSHSQRNYSPVAGPSSePSAHTST 340
Cdd:PRK14971  358 QLAQLTQKGDD-ASGGRGPKQHIKPVFTQP-----------AAAPQPSAAAAASPSPSQSSAAAQPSAPQSA-TQPAGTP 424

                          90       100
                  ....*....|....*....|
gi 1723913129 341 PSIgNSQPSTPAPALPVQDP 360
Cdd:PRK14971  425 PTV-SVDPPAAVPVNPPSTA 443
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 266-361 4.63e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 266 PPENQNPASPDVVPCPDEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPshsqrnySPVAGPSSEPSAHTSTPsign 345
Cdd:PRK07764  429 PQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP-------APAPPAAPAPAAAPAAP---- 497

                          90
                  ....*....|....*.
gi 1723913129 346 SQPSTPAPALPVQDPQ 361
Cdd:PRK07764  498 AAPAAPAGADDAATLR 513
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 201-360 4.91e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.38  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129  201 PPSMVVQKPDYLNDFTHEIPNIQTDSYESMAKTTPTGGLPRDPQELMVDNPLNQLSTLAGQLSSL-------------PP 267
Cdd:PHA03307    39 SQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREgsptppgpsspdpPP 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129  268 ENQNPASPDVVPCPDEKPfmiQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQRNYSPVAgPSSEPSAHTSTPSIGNSQ 347
Cdd:PHA03307   119 PTPPPASPPPSPAPDLSE---MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPL-SSPEETARAPSSPPAEPP 194

                          170
                   ....*....|...
gi 1723913129  348 PSTPAPALPVQDP 360
Cdd:PHA03307   195 PSTPPAAASPRPP 207
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
253-356 5.59e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 38.88  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 253 NQLSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPSTQAVVSAVSASIP------QSSSPTSPEPRPSHSQRNYSP 326
Cdd:pfam05539 168 PKTAVTTSKTTSWPTEVSHPTYPSQVTPQSQPATQGHQTATANQRLSSTEPVGtqgtttSSNPEPQTEPPPSQRGPSGSP 247

                          90       100       110
                  ....*....|....*....|....*....|
gi 1723913129 327 VAgPSSEPSAHTSTPsiGNSQPSTPAPALP 356
Cdd:pfam05539 248 QH-PPSTTSQDQSTT--GDGQEHTQRRKTP 274
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 251-360 6.34e-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: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 251 PLNQLSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPStqavVSAVSASIPQSSSPTSPEPRPSHSQRNY----SP 326
Cdd:pfam03154 398 PLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQS----LPPPAASHPPTSGLHQVPSQSPFPQHPFvpggPP 473

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1723913129 327 VAGPSSEPSAHTSTPSIGNSQPSTPAPALPVQDP 360
Cdd:pfam03154 474 PITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVP 507
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
108-350 8.73e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.14  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 108 KPHRCHLCPFASAYERHLEAHMRSHTGEKPYKCELCSFRC--SDRSNLSHHRRRKHK-----------MVPIKGTRSSLS 174
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKsfSRPLELSRHLRTHHNnpsdlnskslpLSNSKASSSSLS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 175 SKKMWGVLQKKTSNLGYSrrALINLSPPSMVVQKPDYLNDFTHEIPNIQTDSYESMAKTTPTGGLPRDPQELMVDNPLNQ 254
Cdd:COG5048   112 SSSSNSNDNNLLSSHSLP--PSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLIS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913129 255 LSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQ------RNYSPVA 328
Cdd:COG5048   190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSasesprSSLPTAS 269

                         250       260
                  ....*....|....*....|..
gi 1723913129 329 GPSSEPSAHTSTPSIGNSQPST 350
Cdd:COG5048   270 SQSSSPNESDSSSEKGFSLPIK 291
 
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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