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Conserved domains on  [gi|1723913134|ref|NP_001359060|]
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zinc finger protein Pegasus isoform 2 [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;
56-80 1.00e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.00e-04
                          10        20
                  ....*....|....*....|....*
gi 1723913134  56 HLEAHMRSHTGEKPYKCELCSFRCS 80
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03269 super family cl29788
envelope glycoprotein C; Provisional
 183-293 1.59e-04

envelope glycoprotein C; Provisional


The actual alignment was detected with superfamily member PHA03269:

Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 183 PLNQLSTLAGQLSSLP---PENQNPASPDVVPCP----DEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRP---SHS 252
Cdd:PHA03269   27 PIPELHTSAATQKPDPapaPHQAASRAPDPAVAPtsaaSRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVapqLAA 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1723913134 253 QRNYSPVAGPSSEPSAHTSTPSIGNSQPS-TPAPALPVQDPQ 293
Cdd:PHA03269  107 APKPDAAEAFTSAAQAHEAPADAGTSAASkKPDPAAHTQHSP 148
zf-H2C2_2 pfam13465
Zinc-finger double domain;
28-53 1.24e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|....*.
gi 1723913134  28 RLIEHIRIHTGEKPHRCHLCPFASAY 53
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
56-80 1.00e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.00e-04
                          10        20
                  ....*....|....*....|....*
gi 1723913134  56 HLEAHMRSHTGEKPYKCELCSFRCS 80
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 183-293 1.59e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 183 PLNQLSTLAGQLSSLP---PENQNPASPDVVPCP----DEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRP---SHS 252
Cdd:PHA03269   27 PIPELHTSAATQKPDPapaPHQAASRAPDPAVAPtsaaSRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVapqLAA 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1723913134 253 QRNYSPVAGPSSEPSAHTSTPSIGNSQPS-TPAPALPVQDPQ 293
Cdd:PHA03269  107 APKPDAAEAFTSAAQAHEAPADAGTSAASkKPDPAAHTQHSP 148
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 180-305 3.40e-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: 42.16  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 180 VDNPLNQLSTL---AGQLSSLPPENQNPASPDVVPC----------PDEKPFM-----IQQPSTQAVVSAVSASIPQSSS 241
Cdd:cd23959   115 VPNPFSASSSTqreTHKTAQVAPPKAEPQTAPVTPFgqlpmfgqhpPPAKPLPaaaaaQQSSASPGEVASPFASGTVSAS 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1723913134 242 PTSPEPRPSHSQRNYSPVAGPSSEPSAhTSTPSIGNSQPStpAPALPVQDPQLLHHCQHCDMYF 305
Cdd:cd23959   195 PFATATDTAPSSGAPDGFPAEASAPSP-FAAPASAASFPA--APVANGEAATPTHACTICGKAF 255
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 152-288 9.42e-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: 41.06  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 152 PNIQTDSYESMAKTTptgGLPRD---PQELMVDNPLNQLSTLAGQLSSLPPENQNPASPDV-VPCPDEKPFMIQQPSTQA 227
Cdd:pfam05109 432 PTLNTTGFAAPNTTT---GLPSSthvPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTpSPSPRDNGTESKAPDMTS 508

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1723913134 228 VVSAVSASIPQSSSPTSPEPRPSHSQRnySPVAGPSSePSAHTSTPSIGNSQPsTPAPALP 288
Cdd:pfam05109 509 PTSAVTTPTPNATSPTPAVTTPTPNAT--SPTLGKTS-PTSAVTTPTPNATSP-TPAVTTP 565
zf-H2C2_2 pfam13465
Zinc-finger double domain;
28-53 1.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|....*.
gi 1723913134  28 RLIEHIRIHTGEKPHRCHLCPFASAY 53
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 195-290 1.76e-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: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 195 SSLPPENQNPASPDVVPcpdEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQRNYSPVAGPSSEPSAHTSTPS 274
Cdd:COG3266   263 SASAPATTSLGEQQEVS---LPPAVAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAPA 339

                          90       100
                  ....*....|....*....|
gi 1723913134 275 ----IGNSQPSTPAPALPVQ 290
Cdd:COG3266   340 peaaAAAAAPAAPAVAKKLA 359
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
56-80 1.00e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.89  E-value: 1.00e-04
                          10        20
                  ....*....|....*....|....*
gi 1723913134  56 HLEAHMRSHTGEKPYKCELCSFRCS 80
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 183-293 1.59e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 183 PLNQLSTLAGQLSSLP---PENQNPASPDVVPCP----DEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRP---SHS 252
Cdd:PHA03269   27 PIPELHTSAATQKPDPapaPHQAASRAPDPAVAPtsaaSRKPDLAQAPTPAASEKFDPAPAPHQAASRAPDPAVapqLAA 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1723913134 253 QRNYSPVAGPSSEPSAHTSTPSIGNSQPS-TPAPALPVQDPQ 293
Cdd:PHA03269  107 APKPDAAEAFTSAAQAHEAPADAGTSAASkKPDPAAHTQHSP 148
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 180-305 3.40e-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: 42.16  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 180 VDNPLNQLSTL---AGQLSSLPPENQNPASPDVVPC----------PDEKPFM-----IQQPSTQAVVSAVSASIPQSSS 241
Cdd:cd23959   115 VPNPFSASSSTqreTHKTAQVAPPKAEPQTAPVTPFgqlpmfgqhpPPAKPLPaaaaaQQSSASPGEVASPFASGTVSAS 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1723913134 242 PTSPEPRPSHSQRNYSPVAGPSSEPSAhTSTPSIGNSQPStpAPALPVQDPQLLHHCQHCDMYF 305
Cdd:cd23959   195 PFATATDTAPSSGAPDGFPAEASAPSP-FAAPASAASFPA--APVANGEAATPTHACTICGKAF 255
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 152-288 9.42e-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: 41.06  E-value: 9.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 152 PNIQTDSYESMAKTTptgGLPRD---PQELMVDNPLNQLSTLAGQLSSLPPENQNPASPDV-VPCPDEKPFMIQQPSTQA 227
Cdd:pfam05109 432 PTLNTTGFAAPNTTT---GLPSSthvPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTpSPSPRDNGTESKAPDMTS 508

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1723913134 228 VVSAVSASIPQSSSPTSPEPRPSHSQRnySPVAGPSSePSAHTSTPSIGNSQPsTPAPALP 288
Cdd:pfam05109 509 PTSAVTTPTPNATSPTPAVTTPTPNAT--SPTLGKTS-PTSAVTTPTPNATSP-TPAVTTP 565
zf-H2C2_2 pfam13465
Zinc-finger double domain;
28-53 1.24e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.24e-03
                          10        20
                  ....*....|....*....|....*.
gi 1723913134  28 RLIEHIRIHTGEKPHRCHLCPFASAY 53
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PRK10856 PRK10856
cytoskeleton protein RodZ;
176-287 1.48e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.01  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 176 QEL--MVDNPLNQLSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQ 253
Cdd:PRK10856  141 EEIttMADQSSAELSQNSGQSVPLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTA 220

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1723913134 254 RNYSPVAGPSSEPSAHTSTPSIGNSQPSTPAPAL 287
Cdd:PRK10856  221 ATPAPAAPATPDGAAPLPTDQAGVSTPAADPNAL 254
PHA03247 PHA03247
large tegument protein UL36; Provisional
 181-292 1.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134  181 DNPLNQLSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPST---------QAVVSAVSASIPQSSSPTSPEPRPSH 251
Cdd:PHA03247  2754 PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLpspwdpadpPAAVLAPAAALPPAASPAGPLPPPTS 2833

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1723913134  252 SQrnysPVAGPSSEPSAHTSTPSIGN------------SQPSTPAPALPVQDP 292
Cdd:PHA03247  2834 AQ----PTAPPPPPGPPPPSLPLGGSvapggdvrrrppSRSPAAKPAAPARPP 2882
motB PRK12799
flagellar motor protein MotB; Reviewed
 189-288 1.53e-03

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 40.08  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 189 TLAGQLSSLPPENQNPAS-PDVVPCPDEKPfmiQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQRNYSPVAGPSSEP- 266
Cdd:PRK12799  307 SSAVTQSSAITPSSAAIPsPAVIPSSVTTQ---SATTTQASAVALSSAGVLPSDVTLPGTVALPAAEPVNMQPQPMSTTe 383

                          90       100
                  ....*....|....*....|....
gi 1723913134 267 SAHTSTPSI--GNSQPSTPAPALP 288
Cdd:PRK12799  384 TQQSSTGNItsTANGPTTSLPAAP 407
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 195-290 1.76e-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: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 195 SSLPPENQNPASPDVVPcpdEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQRNYSPVAGPSSEPSAHTSTPS 274
Cdd:COG3266   263 SASAPATTSLGEQQEVS---LPPAVAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAPA 339

                          90       100
                  ....*....|....*....|
gi 1723913134 275 ----IGNSQPSTPAPALPVQ 290
Cdd:COG3266   340 peaaAAAAAPAAPAVAKKLA 359
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
193-292 3.26e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 39.37  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 193 QLSSLPPENQNpASPDVVPCPDEKPFMIQQpstqavvsavsASIPQSSSPTSPEPRPSHSQRNYSPVAGPSSePSAHTST 272
Cdd:PRK14971  358 QLAQLTQKGDD-ASGGRGPKQHIKPVFTQP-----------AAAPQPSAAAAASPSPSQSSAAAQPSAPQSA-TQPAGTP 424

                          90       100
                  ....*....|....*....|
gi 1723913134 273 PSIgNSQPSTPAPALPVQDP 292
Cdd:PRK14971  425 PTV-SVDPPAAVPVNPPSTA 443
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 198-293 3.83e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 198 PPENQNPASPDVVPCPDEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPshsqrnySPVAGPSSEPSAHTSTPsign 277
Cdd:PRK07764  429 PQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP-------APAPPAAPAPAAAPAAP---- 497

                          90
                  ....*....|....*.
gi 1723913134 278 SQPSTPAPALPVQDPQ 293
Cdd:PRK07764  498 AAPAAPAGADDAATLR 513
PHA03247 PHA03247
large tegument protein UL36; Provisional
 167-291 4.61e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 4.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134  167 PTGGLPRDPQELMVDNPLNQLSTLAGQLSSLPPENQNPASPDVVPCPDEKPfmiQQPSTQAVVSAVSASIPQSSSPTSPE 246
Cdd:PHA03247  2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP---RRRAARPTVGSLTSLADPPPPPPTPE 2709

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1723913134  247 PRPSHSQRNYSPVAGPSSEPSAHTSTPSIGNSQPSTPAPALPVQD 291
Cdd:PHA03247  2710 PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGP 2754
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 133-292 7.38e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 38.23  E-value: 7.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134  133 PPSMVVQKPDYLNDFTHEIPNIQTDSYESMAKTTPTGGLPRDPQELMVDNPLNQLSTLAGQLSSL-------------PP 199
Cdd:PHA03307    39 SQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREgsptppgpsspdpPP 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134  200 ENQNPASPDVVPCPDEKPfmiQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQRNYSPVAgPSSEPSAHTSTPSIGNSQ 279
Cdd:PHA03307   119 PTPPPASPPPSPAPDLSE---MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPL-SSPEETARAPSSPPAEPP 194

                          170
                   ....*....|...
gi 1723913134  280 PSTPAPALPVQDP 292
Cdd:PHA03307   195 PSTPPAAASPRPP 207
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
185-288 9.01e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 37.72  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723913134 185 NQLSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPSTQAVVSAVSASIP------QSSSPTSPEPRPSHSQRNYSP 258
Cdd:pfam05539 168 PKTAVTTSKTTSWPTEVSHPTYPSQVTPQSQPATQGHQTATANQRLSSTEPVGtqgtttSSNPEPQTEPPPSQRGPSGSP 247

                          90       100       110
                  ....*....|....*....|....*....|
gi 1723913134 259 VAgPSSEPSAHTSTPsiGNSQPSTPAPALP 288
Cdd:pfam05539 248 QH-PPSTTSQDQSTT--GDGQEHTQRRKTP 274
 
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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