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Conserved domains on  [gi|1771357575|gb|QFW68530|]
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MAG: hypothetical protein NV1_52 [Nanoarchaeotal virus 1]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 178-257 3.90e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 3.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575  178 PTAER--PISMEPNPSITQPNEMATNPSPAINQPTSIAASARPLPPPQYIRRPQvpEQPNPELQPKPETPQPEITPPKPV 255
Cdd:PHA03247  2875 PAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPLAPTTDPAGA 2952


                   ..
gi 1771357575  256 LQ 257
Cdd:PHA03247  2953 GE 2954
 
Name Accession Description Interval E-value
PHA03247 PHA03247
large tegument protein UL36; Provisional
 178-257 3.90e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 3.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575  178 PTAER--PISMEPNPSITQPNEMATNPSPAINQPTSIAASARPLPPPQYIRRPQvpEQPNPELQPKPETPQPEITPPKPV 255
Cdd:PHA03247  2875 PAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPLAPTTDPAGA 2952


                   ..
gi 1771357575  256 LQ 257
Cdd:PHA03247  2953 GE 2954
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 174-259 1.29e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.14  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 174 VNFIPTAERP-ISMEPNPSITQPNEMATNPSPAInQPTSIAASARPLPPPQYiRRPQVPEQ---PNPELQPKPETPQPEI 249
Cdd:NF033839  288 GNKKPSAPKPgMQPSPQPEKKEVKPEPETPKPEV-KPQLEKPKPEVKPQPEK-PKPEVKPQletPKPEVKPQPEKPKPEV 365

                          90
                  ....*....|....*
gi 1771357575 250 TP----PKP-VLQQP 259
Cdd:NF033839  366 KPqpekPKPeVKPQP 380
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 179-261 1.73e-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: 40.14  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 179 TAERPISMEPNPSITQPNEMATNPSPAINQPTSIAAsarPLPPPQyirRPQVPEQPNPELQPKPETPQPEITPPKPVLQQ 258
Cdd:pfam03154 161 SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAAT---AGPTPS---APSVPPQGSPATSQPPNQTQSTAAPHTLIQQT 234


                  ...
gi 1771357575 259 PKI 261
Cdd:pfam03154 235 PTL 237
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 202-254 4.17e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 38.60  E-value: 4.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1771357575 202 PSPAIN-QPTSIAASARPLPPPQYIRRPQVPEQPNPELQPKPETPQPEITP----PKP 254
Cdd:NF033839  284 PKEPGNkKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPqpekPKP 341
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 178-260 5.68e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 38.21  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 178 PTAERPI-SMEPNPSITQPNemaTNPSPAINQPTSIAASARPLP---PPQYIRRPQV---PEQPNPELQPKPETPQPEIT 250
Cdd:NF033839  345 PQLETPKpEVKPQPEKPKPE---VKPQPEKPKPEVKPQPETPKPevkPQPEKPKPEVkpqPEKPKPEVKPQPEKPKPEVK 421

                          90
                  ....*....|....*...
gi 1771357575 251 PP--------KPVLQQPK 260
Cdd:NF033839  422 PQpekpkpevKPQPEKPK 439
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 178-298 6.31e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 38.21  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 178 PTAERPiSMEPNPSITQPN--EMATNPSPAIN-QPTSIAASARPLP-PPQYIRRPQvPEQPNPELQPKPETPQPEItPPK 253
Cdd:NF033839  380 PETPKP-EVKPQPEKPKPEvkPQPEKPKPEVKpQPEKPKPEVKPQPeKPKPEVKPQ-PEKPKPEVKPQPEKPKPEV-KPQ 456

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1771357575 254 PVLQQPKITPPPSVPNEPPQNPPTPPEENIPIPPEE-NKPKVPKNI 298
Cdd:NF033839  457 PETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADdKKPSTPNNL 502
 
Name Accession Description Interval E-value
PHA03247 PHA03247
large tegument protein UL36; Provisional
 178-257 3.90e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 3.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575  178 PTAER--PISMEPNPSITQPNEMATNPSPAINQPTSIAASARPLPPPQYIRRPQvpEQPNPELQPKPETPQPEITPPKPV 255
Cdd:PHA03247  2875 PAAPArpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ--PQPPPPPPPRPQPPLAPTTDPAGA 2952


                   ..
gi 1771357575  256 LQ 257
Cdd:PHA03247  2953 GE 2954
PRK11633 PRK11633
cell division protein DedD; Provisional
 180-257 1.21e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 42.68  E-value: 1.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771357575 180 AERPISMEPNPSITQPNEMATNPSPAINQPTSIA-ASARPLPPPQyiRRPQVPEQPNPELQPKPETPQPEITPPKPVLQ 257
Cdd:PRK11633   72 AEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEpPKPKPVEKPK--PKPKPQQKVEAPPAPKPEPKPVVEEKAAPTGK 148
PHA03247 PHA03247
large tegument protein UL36; Provisional
 178-259 1.41e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575  178 PTAERPISMEPNPSITQPNEMATN--PSPAINQPTSiaasARPLPPPQyirrPQVPEQPNPELQPKPETPQPEITPPKPV 255
Cdd:PHA03247  2861 DVRRRPPSRSPAAKPAAPARPPVRrlARPAVSRSTE----SFALPPDQ----PERPPQPQAPPPPQPQPQPPPPPQPQPP 2932


                   ....
gi 1771357575  256 LQQP 259
Cdd:PHA03247  2933 PPPP 2936
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 198-259 5.19e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.33  E-value: 5.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771357575 198 MATNPSPAINQPTSIA-ASARPLPPPqyIRRPQVPE-QPNPELQPKPETPQPEITPPKPVLQQP 259
Cdd:PRK14950  360 LVPVPAPQPAKPTAAApSPVRPTPAP--STRPKAAAaANIPPKEPVRETATPPPVPPRPVAPPV 421
PRK11633 PRK11633
cell division protein DedD; Provisional
 177-260 1.25e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 39.60  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 177 IPTAERPISMEPNPSITQPNEMATNPSPAINQPTSIAASARPLPPPQYIRRPQVPEQPNPELQPKPE---TPQPEITP-P 252
Cdd:PRK11633   56 MPAATQALPTQPPEGAAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQqkvEAPPAPKPeP 135


                  ....*...
gi 1771357575 253 KPVLQQPK 260
Cdd:PRK11633  136 KPVVEEKA 143
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 174-259 1.29e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.14  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 174 VNFIPTAERP-ISMEPNPSITQPNEMATNPSPAInQPTSIAASARPLPPPQYiRRPQVPEQ---PNPELQPKPETPQPEI 249
Cdd:NF033839  288 GNKKPSAPKPgMQPSPQPEKKEVKPEPETPKPEV-KPQLEKPKPEVKPQPEK-PKPEVKPQletPKPEVKPQPEKPKPEV 365

                          90
                  ....*....|....*
gi 1771357575 250 TP----PKP-VLQQP 259
Cdd:NF033839  366 KPqpekPKPeVKPQP 380
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 179-261 1.73e-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: 40.14  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 179 TAERPISMEPNPSITQPNEMATNPSPAINQPTSIAAsarPLPPPQyirRPQVPEQPNPELQPKPETPQPEITPPKPVLQQ 258
Cdd:pfam03154 161 SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAAT---AGPTPS---APSVPPQGSPATSQPPNQTQSTAAPHTLIQQT 234


                  ...
gi 1771357575 259 PKI 261
Cdd:pfam03154 235 PTL 237
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 180-261 2.00e-03

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: 39.90  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 180 AERPISMEPNPSITQPNEMATNPSPAINQPTSIAASAR--PLPPPQYIRRPqvpeqpnpelQPKPETPQPEITPPKPVLQ 257
Cdd:pfam05109 501 SKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTlgKTSPTSAVTTP----------TPNATSPTPAVTTPTPNAT 570


                  ....
gi 1771357575 258 QPKI 261
Cdd:pfam05109 571 IPTL 574
PHA03247 PHA03247
large tegument protein UL36; Provisional
 177-273 2.66e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575  177 IPTAERPISMEPNPSITQPNEMATNPSP--------------------AINQPTSIAASARPLPPPQYIRRPQVPEQPNP 236
Cdd:PHA03247  2818 LPPAASPAGPLPPPTSAQPTAPPPPPGPpppslplggsvapggdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTES 2897

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1771357575  237 ELQPkPETPQPEITPPKPVLQQPKITPPPSVPNE-PPQ 273
Cdd:PHA03247  2898 FALP-PDQPERPPQPQAPPPPQPQPQPPPPPQPQpPPP 2934
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 202-254 4.17e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 38.60  E-value: 4.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1771357575 202 PSPAIN-QPTSIAASARPLPPPQYIRRPQVPEQPNPELQPKPETPQPEITP----PKP 254
Cdd:NF033839  284 PKEPGNkKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPqpekPKP 341
PHA03247 PHA03247
large tegument protein UL36; Provisional
 180-260 4.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.77  E-value: 4.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575  180 AERPiSMEPNPSITQPNEMATNPSPAINQPTSIAASARPLPPPQYIRRPQVPEQPNPELQPKPETPQPEITPPKPVLQQP 259
Cdd:PHA03247  2586 ARRP-DAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRP 2664


                   .
gi 1771357575  260 K 260
Cdd:PHA03247  2665 R 2665
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 178-260 5.15e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 37.92  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 178 PTAERPISmePNPSITQPNEMATNPSPAINQPTSIAASARPLPPPQyirrpQVPEQPNPELQPKPETPQP------EITP 251
Cdd:PHA02682   76 PSGQSPLA--PSPACAAPAPACPACAPAAPAPAVTCPAPAPACPPA-----TAPTCPPPAVCPAPARPAPacppstRQCP 148


                  ....*....
gi 1771357575 252 PKPVLQQPK 260
Cdd:PHA02682  149 PAPPLPTPK 157
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 178-260 5.68e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 38.21  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 178 PTAERPI-SMEPNPSITQPNemaTNPSPAINQPTSIAASARPLP---PPQYIRRPQV---PEQPNPELQPKPETPQPEIT 250
Cdd:NF033839  345 PQLETPKpEVKPQPEKPKPE---VKPQPEKPKPEVKPQPETPKPevkPQPEKPKPEVkpqPEKPKPEVKPQPEKPKPEVK 421

                          90
                  ....*....|....*...
gi 1771357575 251 PP--------KPVLQQPK 260
Cdd:NF033839  422 PQpekpkpevKPQPEKPK 439
PHA03247 PHA03247
large tegument protein UL36; Provisional
 178-254 5.69e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.38  E-value: 5.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771357575  178 PTAERPISMEPNPSITQPNematnPSPAINQPTSIAASARPLPPPQYiRRPQVPEQP--NPELQPKPETPQPEITPPKP 254
Cdd:PHA03247  2554 PLPPAAPPAAPDRSVPPPR-----PAPRPSEPAVTSRARRPDAPPQS-ARPRAPVDDrgDPRGPAPPSPLPPDTHAPDP 2626
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 178-298 6.31e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 38.21  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771357575 178 PTAERPiSMEPNPSITQPN--EMATNPSPAIN-QPTSIAASARPLP-PPQYIRRPQvPEQPNPELQPKPETPQPEItPPK 253
Cdd:NF033839  380 PETPKP-EVKPQPEKPKPEvkPQPEKPKPEVKpQPEKPKPEVKPQPeKPKPEVKPQ-PEKPKPEVKPQPEKPKPEV-KPQ 456

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1771357575 254 PVLQQPKITPPPSVPNEPPQNPPTPPEENIPIPPEE-NKPKVPKNI 298
Cdd:NF033839  457 PETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADdKKPSTPNNL 502
 
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.
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