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Conserved domains on  [gi|1907112372|ref|XP_006520050|]
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caspase recruitment domain-containing protein 6 isoform X1 [Mus musculus]

Protein Classification

CARD domain-containing protein( domain architecture ID 10109095)

CARD domain-containing protein

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
939-1316 2.63e-12

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.89  E-value: 2.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  939 SATPQQYHPNGP--FGRSQRQASPVQTHPKSRQmSRTLERSGTVVSRVGHGRSLGSQARRAAGKPQPEKAcaqglqLTKA 1016
Cdd:PHA03247  2615 SPLPPDTHAPDPppPSPSPAANEPDPHPPPTVP-PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP------RRRA 2687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1017 AGKSIRTLPHIKYPHPQPCQPAGASQERI----MPVSHQGAQQTTQGRPADFA--------FKPGSQSTSGSKLSSTSQS 1084
Cdd:PHA03247  2688 ARPTVGSLTSLADPPPPPPTPEPAPHALVsatpLPPGPAAARQASPALPAAPAppavpagpATPGGPARPARPPTTAGPP 2767
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1085 SAHQPKFQSKhfQPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSH 1164
Cdd:PHA03247  2768 APAPPAAPAA--GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP 2845
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1165 AKPSHQNPSHANPTHPQSSHAKPSHPQSSHAKPSHPQSSH-AKPSHPQSSHAKPsHPQSSQAKPSHPQSSQAKPTHPQSS 1243
Cdd:PHA03247  2846 PPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVSRSTESFA-LPPDQPERPPQPQAPPPPQPQPQPP 2924
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112372 1244 QANSHHPQ-ASQAKPSHPQSSHAKPS-HPHPSHAKPSPSQST----QCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQAR 1316
Cdd:PHA03247  2925 PPPQPQPPpPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGAlvpgRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSR 3003
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
161-229 2.11e-11

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 60.99  E-value: 2.11e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112372  161 IEKKRTKLLSVLqqDPDSILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRRFLRCL 229
Cdd:cd01671      1 LRKNRVELVEDL--DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEAL 67
 
Name Accession Description Interval E-value
PHA03247 PHA03247
large tegument protein UL36; Provisional
939-1316 2.63e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.89  E-value: 2.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  939 SATPQQYHPNGP--FGRSQRQASPVQTHPKSRQmSRTLERSGTVVSRVGHGRSLGSQARRAAGKPQPEKAcaqglqLTKA 1016
Cdd:PHA03247  2615 SPLPPDTHAPDPppPSPSPAANEPDPHPPPTVP-PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP------RRRA 2687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1017 AGKSIRTLPHIKYPHPQPCQPAGASQERI----MPVSHQGAQQTTQGRPADFA--------FKPGSQSTSGSKLSSTSQS 1084
Cdd:PHA03247  2688 ARPTVGSLTSLADPPPPPPTPEPAPHALVsatpLPPGPAAARQASPALPAAPAppavpagpATPGGPARPARPPTTAGPP 2767
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1085 SAHQPKFQSKhfQPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSH 1164
Cdd:PHA03247  2768 APAPPAAPAA--GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP 2845
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1165 AKPSHQNPSHANPTHPQSSHAKPSHPQSSHAKPSHPQSSH-AKPSHPQSSHAKPsHPQSSQAKPSHPQSSQAKPTHPQSS 1243
Cdd:PHA03247  2846 PPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVSRSTESFA-LPPDQPERPPQPQAPPPPQPQPQPP 2924
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112372 1244 QANSHHPQ-ASQAKPSHPQSSHAKPS-HPHPSHAKPSPSQST----QCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQAR 1316
Cdd:PHA03247  2925 PPPQPQPPpPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGAlvpgRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSR 3003
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1086-1320 1.84e-11

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: 69.03  E-value: 1.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1086 AHQPKFQSKHFQPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLT-QGQPSQATPTHSQASQAKPTHSQANSHHPHPSH 1164
Cdd:pfam03154  162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPpQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQR 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1165 AKPSHQNPSHANPTHPQSSHAKPSHPQSSH--AKPSHPQSSHAKPSHPQsshakpsHPQSSQAKPSHPQSSQAK------ 1236
Cdd:pfam03154  242 LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgQMPPMPHSLQTGPSHMQ-------HPVPPQPFPLTPQSSQSQvppgps 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1237 PTHPQSSQANSHHPqASQAKPSHPQSSHAKPSHPHP---SHAKPSPSQ------STQCKAHKAHQSQPKPFQPRPTQPKS 1307
Cdd:pfam03154  315 PAAPGQSQQRIHTP-PSQSQLQSQQPPREQPLPPAPlsmPHIKPPPTTpipqlpNPQSHKHPPHLSGPSPFQMNSNLPPP 393
                          250
                   ....*....|....
gi 1907112372 1308 SKTKP-SQARAFHP 1320
Cdd:pfam03154  394 PALKPlSSLSTHHP 407
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
161-229 2.11e-11

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 60.99  E-value: 2.11e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112372  161 IEKKRTKLLSVLqqDPDSILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRRFLRCL 229
Cdd:cd01671      1 LRKNRVELVEDL--DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEAL 67
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
159-238 5.65e-10

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 57.18  E-value: 5.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  159 ELIEKKRTKLLSVLQqDPDSILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRRFLRCLSNAFPESAS 238
Cdd:pfam00619    2 KLLKKNRVALVERLG-TLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
158-232 1.16e-08

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 53.50  E-value: 1.16e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907112372   158 SELIEKKRTKLLSVLQqdPDSILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRRFLRCLSNA 232
Cdd:smart00114    6 KRLLRRNRVRLGEELG--VDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQET 78
ARG80 COG5068
Regulator of arginine metabolism and related MADS box-containing transcription factors ...
1101-1305 1.23e-04

Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription];


Pssm-ID: 227400 [Multi-domain]  Cd Length: 412  Bit Score: 46.16  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1101 FQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQAT-PTHSQASQAKPTHSQANSHHPHP-SHakpSHQNPShanPT 1178
Cdd:COG5068    161 NAPSDSSEEPSSSASFSVDPNDNNPMGSFQHNGSPQTNFiPLQNPQTQQYQQHSSRKDHPTVPhSN---TNNGRP---PA 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1179 HPQSSHAKPSHPQSSHakPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHpqssQANSHHPQASQAKPS 1258
Cdd:COG5068    235 KFMIPELHSSHSTLDL--PSDFISDSGFPNQSSTSIFPLDSAIIQITPPHLPNNPPQENRH----ELYSNDSSMVSETPP 308
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907112372 1259 HPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQP 1305
Cdd:COG5068    309 PKNLPNGSPNQSPLNNLSRGNPASPNSIIRENNQVEDESFNGRQGSA 355
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1097-1317 3.06e-04

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: 45.14  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1097 QPQPFQPVPSQKKPSHSRPSQAKPPHLDPShanlTQGQPSQATPTHSQASQAKPTHSQANshhPHPSHAKPSHQnpshan 1176
Cdd:NF033839   300 QPSPQPEKKEVKPEPETPKPEVKPQLEKPK----PEVKPQPEKPKPEVKPQLETPKPEVK---PQPEKPKPEVK------ 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1177 pthPQSSHAKPS-HPQSSHAKPS-HPQSSHAKPS-HPQSSHAKPS-HPQSSQAKPS-HPQSSQAKP-THPQSSQANSH-H 1249
Cdd:NF033839   367 ---PQPEKPKPEvKPQPETPKPEvKPQPEKPKPEvKPQPEKPKPEvKPQPEKPKPEvKPQPEKPKPeVKPQPEKPKPEvK 443
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112372 1250 PQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKS-SKTKPSQARA 1317
Cdd:NF033839   444 PQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNlSKDKQPSNQA 512
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
1161-1274 1.43e-03

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: 42.34  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1161 HPSHAKPSHQnpshANPTHPQSSHAKPSHPQSSHAKPSHPQSSHAkPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHP 1240
Cdd:cd22056    203 FMGQQKPKHQ----MHSVHPQAFTHHQAAGPGALQGRGGRGGPDC-HLLHSSHHHHHHHHLQYQYMNAPYPPHYAHQGAP 277
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907112372 1241 QSSQANSHHPQASQAKPSHPQSSHAKPShPHPSH 1274
Cdd:cd22056    278 QFHGQYSVFREPMRVHHQGHPGSMLTPP-SSPPL 310
 
Name Accession Description Interval E-value
PHA03247 PHA03247
large tegument protein UL36; Provisional
939-1316 2.63e-12

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 71.89  E-value: 2.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  939 SATPQQYHPNGP--FGRSQRQASPVQTHPKSRQmSRTLERSGTVVSRVGHGRSLGSQARRAAGKPQPEKAcaqglqLTKA 1016
Cdd:PHA03247  2615 SPLPPDTHAPDPppPSPSPAANEPDPHPPPTVP-PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP------RRRA 2687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1017 AGKSIRTLPHIKYPHPQPCQPAGASQERI----MPVSHQGAQQTTQGRPADFA--------FKPGSQSTSGSKLSSTSQS 1084
Cdd:PHA03247  2688 ARPTVGSLTSLADPPPPPPTPEPAPHALVsatpLPPGPAAARQASPALPAAPAppavpagpATPGGPARPARPPTTAGPP 2767
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1085 SAHQPKFQSKhfQPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSH 1164
Cdd:PHA03247  2768 APAPPAAPAA--GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP 2845
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1165 AKPSHQNPSHANPTHPQSSHAKPSHPQSSHAKPSHPQSSH-AKPSHPQSSHAKPsHPQSSQAKPSHPQSSQAKPTHPQSS 1243
Cdd:PHA03247  2846 PPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlARPAVSRSTESFA-LPPDQPERPPQPQAPPPPQPQPQPP 2924
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112372 1244 QANSHHPQ-ASQAKPSHPQSSHAKPS-HPHPSHAKPSPSQST----QCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQAR 1316
Cdd:PHA03247  2925 PPPQPQPPpPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGAlvpgRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSR 3003
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1086-1320 1.84e-11

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: 69.03  E-value: 1.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1086 AHQPKFQSKHFQPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLT-QGQPSQATPTHSQASQAKPTHSQANSHHPHPSH 1164
Cdd:pfam03154  162 AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPpQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQR 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1165 AKPSHQNPSHANPTHPQSSHAKPSHPQSSH--AKPSHPQSSHAKPSHPQsshakpsHPQSSQAKPSHPQSSQAK------ 1236
Cdd:pfam03154  242 LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLhgQMPPMPHSLQTGPSHMQ-------HPVPPQPFPLTPQSSQSQvppgps 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1237 PTHPQSSQANSHHPqASQAKPSHPQSSHAKPSHPHP---SHAKPSPSQ------STQCKAHKAHQSQPKPFQPRPTQPKS 1307
Cdd:pfam03154  315 PAAPGQSQQRIHTP-PSQSQLQSQQPPREQPLPPAPlsmPHIKPPPTTpipqlpNPQSHKHPPHLSGPSPFQMNSNLPPP 393
                          250
                   ....*....|....
gi 1907112372 1308 SKTKP-SQARAFHP 1320
Cdd:pfam03154  394 PALKPlSSLSTHHP 407
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
161-229 2.11e-11

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 60.99  E-value: 2.11e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112372  161 IEKKRTKLLSVLqqDPDSILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRRFLRCL 229
Cdd:cd01671      1 LRKNRVELVEDL--DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEAL 67
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
159-238 5.65e-10

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 57.18  E-value: 5.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  159 ELIEKKRTKLLSVLQqDPDSILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRRFLRCLSNAFPESAS 238
Cdd:pfam00619    2 KLLKKNRVALVERLG-TLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1088-1314 1.47e-09

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 62.75  E-value: 1.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1088 QPKFQSKHFQPQPFQPVPSQKKPSHSRPSQAKPP-----------------HLDPSHANLTQGQPSQATPTHSQASQAKP 1150
Cdd:pfam09770  106 QPAARAAQSSAQPPASSLPQYQYASQQSQQPSKPvrtgyekykepepipdlQVDASLWGVAPKKAAAPAPAPQPAAQPAS 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1151 THSQ---------------ANSHHPHPSHAKPSHQNPSHANPTHPQSSHAKPSHPQsshakpsHPQSSHAKPSHPQSsHA 1215
Cdd:pfam09770  186 LPAPsrkmmsleeveaamrAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQ-------QQQQPQQQPQQPQQ-HP 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1216 KPSHPQSSQakpSHPQSSQAKPTHPQSSQANSHHPQasQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQP 1295
Cdd:pfam09770  258 GQGHPVTIL---QRPQSPQPDPAQPSIQPQAQQFHQ--QPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQA 332
                          250
                   ....*....|....*....
gi 1907112372 1296 KPFQPRPTQPKSSKTKPSQ 1314
Cdd:pfam09770  333 HRQQGSFGRQAPIITHPQQ 351
PHA03247 PHA03247
large tegument protein UL36; Provisional
988-1320 4.17e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 61.49  E-value: 4.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  988 RSLGSQARRAAGKPQPEKACAQglqLTKAAGKSIRTlphiKYPHPQPCQPAGASQERIMPVSHQGAQQTTQGRPADfafk 1067
Cdd:PHA03247  2538 RGLEELASDDAGDPPPPLPPAA---PPAAPDRSVPP----PRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRG---- 2606
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1068 pgsqSTSGSKLSSTSQSSAHQPKfqskhfqPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHAnltqgQPSQATPTHSQASQ 1147
Cdd:PHA03247  2607 ----DPRGPAPPSPLPPDTHAPD-------PPPPSPSPAANEPDPHPPPTVPPPERPRDDP-----APGRVSRPRRARRL 2670
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1148 AKPTHSQANSHHPHPSHAKPshqnpshanPTHPQSSHAKPsHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQS----- 1222
Cdd:PHA03247  2671 GRAAQASSPPQRPRRRAARP---------TVGSLTSLADP-PPPPPTPEPAPHALVSATPLPPGPAAARQASPALpaapa 2740
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1223 ------------SQAKPSHPQSSqAKPTHPQSSQANSHHPQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKA 1290
Cdd:PHA03247  2741 ppavpagpatpgGPARPARPPTT-AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALP 2819
                          330       340       350
                   ....*....|....*....|....*....|
gi 1907112372 1291 HQSQPKPFQPRPTQPksSKTKPSQARAFHP 1320
Cdd:PHA03247  2820 PAASPAGPLPPPTSA--QPTAPPPPPGPPP 2847
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
158-232 1.16e-08

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 53.50  E-value: 1.16e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907112372   158 SELIEKKRTKLLSVLQqdPDSILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRRFLRCLSNA 232
Cdd:smart00114    6 KRLLRRNRVRLGEELG--VDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQET 78
PTZ00395 PTZ00395
Sec24-related protein; Provisional
1106-1282 1.33e-07

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 56.62  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1106 SQKKPSHSRPSQAKPPHLDPSHANLT---QGQPsQATPTHSQASQAKPTHS---QANSHHPHPSHAKPSHQNPSHANPTH 1179
Cdd:PTZ00395   351 SAGAPFNGLGNQADGGHINQVHPDARgawAGGP-HSNASYNCAAYSNAAQSnaaQSNAGFSNAGYSNPGNSNPGYNNAPN 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1180 PQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSH---PQSSQAKpsHPQSSQAKPTHPQSSQANSHHPQASQAK 1256
Cdd:PTZ00395   430 SNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNTPYSNAPLsnaPPSSAKD--HHSAYHAAYQHRAANQPAANLPTANQPA 507
                          170       180
                   ....*....|....*....|....*.
gi 1907112372 1257 PSHPQSSHAKpSHPHPSHAKPSPSQS 1282
Cdd:PTZ00395   508 ANNFHGAAGN-SVGNPFASRPFGSAP 532
PHA03378 PHA03378
EBNA-3B; Provisional
1098-1323 3.91e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 54.69  E-value: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1098 PQPFQPV--PSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSH-------AKPS 1168
Cdd:PHA03378   571 PLQIQPLtsPTTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQpitfnvlVFPT 650
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1169 HQNPSHANPTHPQSSHAKPSHPqsshakPSHPQSSHAKPSHPQSshAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSH 1248
Cdd:PHA03378   651 PHQPPQVEITPYKPTWTQIGHI------PYQPSPTGANTMLPIQ--WAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATG 722
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907112372 1249 HPQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQarafHPRAG 1323
Cdd:PHA03378   723 RARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQ----RPRGA 793
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1030-1222 4.67e-07

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 54.27  E-value: 4.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1030 PHPQPCQPAGASQER-IMPVSHQGAQQTTQgrpadfAFKPGSQSTSGSKLSSTSQSSAHQPKFQSKHFQPQPFQPVPSQK 1108
Cdd:pfam09770  177 PQPAAQPASLPAPSRkMMSLEEVEAAMRAQ------AKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQP 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1109 KPSHSRPSQAKPPHLdpshanLTQGQPSQATPTHSQASQAKPTHSQanshhphpsHAKPSHQNPSH--ANPTHPQSSHAK 1186
Cdd:pfam09770  251 QQPQQHPGQGHPVTI------LQRPQSPQPDPAQPSIQPQAQQFHQ---------QPPPVPVQPTQilQNPNRLSAARVG 315
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907112372 1187 PSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQS 1222
Cdd:pfam09770  316 YPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQ 351
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1032-1282 5.51e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.41  E-value: 5.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1032 PQPCQPAGASQERIMPVSHQGAQQTTQ-GRPADFAFKPGSQSTSGSKLSSTSQSSAHQPKFQSKHFQPQPFQPVPSQKKP 1110
Cdd:PHA03307   126 PPPSPAPDLSEMLRPVGSPGPPPAASPpAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPR 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1111 SHSRPSQAKPPHLDPSHANL-TQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHA----KPSHQNPSHANPTHPQSSHA 1185
Cdd:PHA03307   206 PPRRSSPISASASSPAPAPGrSAADDAGASSSDSSSSESSGCGWGPENECPLPRPApitlPTRIWEASGWNGPSSRPGPA 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1186 KPSHP---QSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSsqanSHHPQASQAKPSHPQS 1262
Cdd:PHA03307   286 SSSSSpreRSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGP----SPSRSPSPSRPPPPAD 361
                          250       260
                   ....*....|....*....|
gi 1907112372 1263 SHAKPSHPHPSHAKPSPSQS 1282
Cdd:PHA03307   362 PSSPRKRPRPSRAPSSPAAS 381
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1097-1325 6.92e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.02  E-value: 6.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1097 QPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQNPSHAN 1176
Cdd:PHA03307   171 QAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWG 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1177 PThpqsSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHP---QSSQAKPSHPQSSQAKPTHPQSSQANSHHPQAS 1253
Cdd:PHA03307   251 PE----NECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSpreRSPSPSPSSPGSGPAPSSPRASSSSSSSRESSS 326
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907112372 1254 QAKPSHPQSSHAKPSHPHPSHAKP----SPSQSTQCKAhKAHQSQPKPFQPRPTQPKSSKTKPSQARAFHPRAGRR 1325
Cdd:PHA03307   327 SSTSSSSESSRGAAVSPGPSPSRSpspsRPPPPADPSS-PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRR 401
AF-4 pfam05110
AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and ...
1086-1281 8.61e-07

AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and FMR2 (Fragile X E mental retardation syndrome) nuclear proteins. These proteins have been linked to human diseases such as acute lymphoblastic leukaemia and mental retardation. The family also contains a Drosophila AF4 protein homolog Lilliputian which contains an AT-hook domain. Lilliputian represents a novel pair-rule gene that acts in cytoskeleton regulation, segmentation and morphogenesis in Drosophila.


Pssm-ID: 461550 [Multi-domain]  Cd Length: 514  Bit Score: 53.20  E-value: 8.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1086 AHQPKFQSKHFQPQPfQPVPSQKKPSHSRPSQAKPPHLDPSHA--NLTQGQPSQATPT-----HSQASQAKPTHSQANSH 1158
Cdd:pfam05110  100 LPPSFHTSSHSQPMG-PPSSSSPSVSSSQSQKKSQARTEPAHGghSSSGSQSSQRSQGqsrskGGQESHSSSHHKRQERR 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1159 HPHPSHAKPSHQNPSHANPTHPQSSHAKPSHPQSShakpSHPQSSHAKPShpqsshAKPSHPQSSQAKPshpqssqakpt 1238
Cdd:pfam05110  179 EDLFSCASLSHSLEELSPLLSSLSSPVKPLSPSHS----RQHTGSKAQNS------SDHHGKEYSHSKS----------- 237
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907112372 1239 hPQSSQANSHHPQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQ 1281
Cdd:pfam05110  238 -PRDSEAGSHGPESPSTSLLASSSQLSSQTFPPSLPSKTSAMQ 279
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1114-1301 1.16e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 53.15  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1114 RPSQAKPPHLDPSHANLTQGQPSqaTPTHSQASQAKPTHSQANSHHPHPShaKPSHQNPSHANP-THPQSSHAKPSHPQS 1192
Cdd:PTZ00449   490 KKSKKKLAPIEEEDSDKHDEPPE--GPEASGLPPKAPGDKEGEEGEHEDS--KESDEPKEGGKPgETKEGEVGKKPGPAK 565
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1193 SHaKPSHPQSSHAKPSHPQsshaKPSHPQ--SSQAKPSHPQSSQaKPTHPQSSQanshHPQA-----SQAKPSHPQSSHA 1265
Cdd:PTZ00449   566 EH-KPSKIPTLSKKPEFPK----DPKHPKdpEEPKKPKRPRSAQ-RPTRPKSPK----LPELldipkSPKRPESPKSPKR 635
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907112372 1266 KPSHPHPSHAKpSPSQSTQCKAHKAHQSQPKPFQPR 1301
Cdd:PTZ00449   636 PPPPQRPSSPE-RPEGPKIIKSPKPPKSPKPPFDPK 670
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1030-1315 1.64e-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: 52.85  E-value: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1030 PHPQPCQPAGASQERIMPVSHQGAQQ----TTQGRPADF-------AFKPGSQSTSGSKLSSTSQSSAHQPkfQSKHFQP 1098
Cdd:pfam03154  251 PMTQPPPPSQVSPQPLPQPSLHGQMPpmphSLQTGPSHMqhpvppqPFPLTPQSSQSQVPPGPSPAAPGQS--QQRIHTP 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1099 qPFQPVPSQKKPSHSRPSQAKP---PHLDPSHANLTQGQPSQATPTHSqASQAKPTHSQANSHHPHPSHAKPSHQNPSHA 1175
Cdd:pfam03154  329 -PSQSQLQSQQPPREQPLPPAPlsmPHIKPPPTTPIPQLPNPQSHKHP-PHLSGPSPFQMNSNLPPPPALKPLSSLSTHH 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1176 NPT-HP---------QSSHAKPSHPQSSHAKPSHPQSShakpshpqSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQA 1245
Cdd:pfam03154  407 PPSaHPpplqlmpqsQQLPPPPAQPPVLTQSQSLPPPA--------ASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPP 478
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907112372 1246 NSHHPQASQAKPSHPQSSHAKPSHPHPSHAKPS-PSQSTQCKAHKAHQSQ----PKPFQPRPTQPKSSKTKPSQA 1315
Cdd:pfam03154  479 SGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVScPLPPVQIKEEALDEAEepesPPPPPRSPSPEPTVVNTPSHA 553
PHA03378 PHA03378
EBNA-3B; Provisional
1031-1322 1.69e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 52.76  E-value: 1.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1031 HPQPCQPAGASQERIMPVSHQGAQQTTQGRPADFA---FKPGSQSTSGSKLSSTSQSSAHQPKFQSKHFQPQPFQPVPSQ 1107
Cdd:PHA03378   560 HDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQtpwPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQ 639
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1108 KKPSH--SRPSQAKPPHLDPSHANLTQGQ----PSQATPTHSQAS---QAKPTHSQANSHHP-------------HPSHA 1165
Cdd:PHA03378   640 PITFNvlVFPTPHQPPQVEITPYKPTWTQighiPYQPSPTGANTMlpiQWAPGTMQPPPRAPtpmrppaappgraQRPAA 719
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1166 KPSHQNPSHANPTHPQSSHAKPSH---PQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQS 1242
Cdd:PHA03378   720 ATGRARPPAAAPGRARPPAAAPGRarpPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPP 799
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1243 SQANshhPQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQARAFHPRA 1322
Cdd:PHA03378   800 PQAG---PTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPSLKKPAALERQAAAGPTPSPGSGTSDKIVQAPVFYPPV 876
PHA03377 PHA03377
EBNA-3C; Provisional
952-1279 2.30e-06

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 52.36  E-value: 2.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  952 GRSQRQASPVQTHPKSRQMSRTLERSGTVVSRVGHGRSLGSQARRAAGKPQP-EKACAQGLQLTKAAGKSIRTLPHIKYP 1030
Cdd:PHA03377   544 GRRQKRATPPKVSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTgPRQQAKCKDGPPASGPHEKQPPSSAPR 623
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1031 HPQPCQPAGASQERIMPvshqgaqQTTQGRPADF-AFKPGSQSTSGSKLSSTSQSSAHQPKFQSKHFQPQPF-------- 1101
Cdd:PHA03377   624 DMAPSVVRMFLRERLLE-------QSTGPKPKSFwEMRAGRDGSGIQQEPSSRRQPATQSTPPRPSWLPSVFvlpsvdag 696
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1102 QPVPSQKKPSHS----RPS--QAKPPHLDPSHANLTQGQPSQATPTHSQA---SQAKPTHSQAnshhPHPSHAKP----- 1167
Cdd:PHA03377   697 RAQPSEESHLSSmsptQPIshEEQPRYEDPDDPLDLSLHPDQAPPPSHQApysGHEEPQAQQA----PYPGYWEPrppqa 772
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1168 --------------SHQNPSHANPTHPQSSHAKPSHP---QSSHAKPSHPQSSHA-KPSHPQ---SSHAKPSHPQSSQAK 1226
Cdd:PHA03377   773 pylgyqepqaqgvqVSSYPGYAGPWGLRAQHPRYRHSwayWSQYPGHGHPQGPWApRPPHLPpqwDGSAGHGQDQVSQFP 852
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907112372 1227 PSHPQSSQAKPTHPQSSQANSHHPQASQAKPSHPQSSHAKPSHPHPSHAKPSP 1279
Cdd:PHA03377   853 HLQSETGPPRLQLSQVPQLPYSQTLVSSSAPSWSSPQPRAPIRPIPTRFPPPP 905
CARD_NOD2_1_CARD15 cd08787
Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and ...
161-238 2.45e-06

Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 1. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176765  Cd Length: 87  Bit Score: 46.83  E-value: 2.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  161 IEKKRTKLLSVL----QQDP-DSILDTLTSRSLISEKEYETLEEITDPL-KKSRKLLILIQKKGEDSCRRFLRCLSNAFP 234
Cdd:cd08787      1 FLAQRSELLEVLcsggSLEPfESVLDWLLSQEVLSWEDYEGFHVLGQPLsHNARQLLDTVYNKGEWACQKFLAAAQQALA 80

                   ....
gi 1907112372  235 ESAS 238
Cdd:cd08787     81 EEQS 84
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1097-1287 3.61e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 51.62  E-value: 3.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1097 QPQPFQPVPSQKKPS--HSRPSQaKPPHLDPSHANLTQGQPSQATPTHSQASQAkpthsqANSHHPHPSHAKPSHQNPSH 1174
Cdd:PRK10263   376 APEGYPQQSQYAQPAvqYNEPLQ-QPVQPQQPYYAPAAEQPAQQPYYAPAPEQP------AQQPYYAPAPEQPVAGNAWQ 448
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1175 ANPTHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHP-----QSSQAKPTHPQSSQANSHH 1249
Cdd:PRK10263   449 AEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPplyyfEEVEEKRAREREQLAAWYQ 528
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907112372 1250 PQASQAKPSHPqsshAKPSHPHPSHAKPSPSQSTQCKA 1287
Cdd:PRK10263   529 PIPEPVKEPEP----IKSSLKAPSVAAVPPVEAAAAVS 562
PTZ00395 PTZ00395
Sec24-related protein; Provisional
1116-1323 4.11e-06

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 51.61  E-value: 4.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1116 SQAKPPHLDPSHANLTQGQPSQaTPTHSQASQaKPTHSQANSHHPHPSHAKPSHQNPS--------HANPTHPQSSHAKP 1187
Cdd:PTZ00395   303 NNTNDAQRNAIQGDLVRGAPND-KNSFDRGNE-KTYQIYGGFHDGSPNAASAGAPFNGlgnqadggHINQVHPDARGAWA 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1188 SHPQS----SHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAkpthPQSSQANSHHPQASQAKPSHPQS- 1262
Cdd:PTZ00395   381 GGPHSnasyNCAAYSNAAQSNAAQSNAGFSNAGYSNPGNSNPGYNNAPNSNT----PYNNPPNSNTPYSNPPNSNPPYSn 456
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907112372 1263 ---SHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPfQPRPTQPKSSKtkpSQARAFHPRAG 1323
Cdd:PTZ00395   457 lpySNTPYSNAPLSNAPPSSAKDHHSAYHAAYQHRAAN-QPAANLPTANQ---PAANNFHGAAG 516
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1164-1320 6.22e-06

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 50.80  E-value: 6.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1164 HAKPSHQNP----SHANPTHPQSSHAKPSHPQSSHAKPSHPQSS--------------HAKPS----HPQSSHAKPSHPQ 1221
Cdd:pfam09770   99 QVRFNRQQPaaraAQSSAQPPASSLPQYQYASQQSQQPSKPVRTgyekykepepipdlQVDASlwgvAPKKAAAPAPAPQ 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1222 SSQAKPSHPQSS---------------QAKPTHPQSSQANSHHPQASQAKPSHPQSSHAKP-SHPHPSHAKPSPSQSTQC 1285
Cdd:pfam09770  179 PAAQPASLPAPSrkmmsleeveaamraQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQiQQQQQPQQQPQQPQQHPG 258
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907112372 1286 KAHKAHQSQ-PKPFQPRPTQPKSSKTKPSQARAFHP 1320
Cdd:pfam09770  259 QGHPVTILQrPQSPQPDPAQPSIQPQAQQFHQQPPP 294
PHA03247 PHA03247
large tegument protein UL36; Provisional
862-1319 7.16e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 7.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  862 PYPAHPWPLPIEAGSNFYHVPLRAPRAISSHFRSQQKAewffPFPHQNTSVHSRGqnfaiKYLQPWRFYSRERFTRCSAT 941
Cdd:PHA03247  2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTV----PPPERPRDDPAPG-----RVSRPRRARRLGRAAQASSP 2679
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  942 PQQYHPN------GPFGRSQRQASPVQThPKSRQMSRTLERSGTVVSRVGHGRSLGSQARRAAgKPQPEKACAQGLQLTK 1015
Cdd:PHA03247  2680 PQRPRRRaarptvGSLTSLADPPPPPPT-PEPAPHALVSATPLPPGPAAARQASPALPAAPAP-PAVPAGPATPGGPARP 2757
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1016 AAGKSIRTLPHikyPHPqPCQPAGASQERIMPVSHQGAQQTTQGRPADFAFKPGSQSTSGSKLSSTSQSSAHQPKFQSKH 1095
Cdd:PHA03247  2758 ARPPTTAGPPA---PAP-PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS 2833
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1096 FQPQPfQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQ-ATPTHSQASQ-AKPTHSQANSHHPHPSHAKPSHQNPS 1173
Cdd:PHA03247  2834 AQPTA-PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKpAAPARPPVRRlARPAVSRSTESFALPPDQPERPPQPQ 2912
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1174 HANPTHPQSSHAKPSHPQSSHAKPSHPQSshakPSHPQSSHAKPSHPQSSQAKPSH---------------PQSSQAKPT 1238
Cdd:PHA03247  2913 APPPPQPQPQPPPPPQPQPPPPPPPRPQP----PLAPTTDPAGAGEPSGAVPQPWLgalvpgrvavprfrvPQPAPSREA 2988
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1239 HPQSSQANSHHPQ----------ASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKSS 1308
Cdd:PHA03247  2989 PASSTPPLTGHSLsrvsswasslALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAH 3068
                          490
                   ....*....|.
gi 1907112372 1309 KTKPSQARAFH 1319
Cdd:PHA03247  3069 EPDPATPEAGA 3079
PHA03247 PHA03247
large tegument protein UL36; Provisional
1020-1267 1.93e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1020 SIRTLPHIKYPHPQPCQPAGASQERIMPVSHQGAQQTTQGRPA--------DFAFKPGSQSTSGSKLSSTSQSSAHQPKF 1091
Cdd:PHA03247  2834 AQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAaparppvrRLARPAVSRSTESFALPPDQPERPPQPQA 2913
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1092 QSKHfQPQPFQPVPSQKKPSHSRPSQAKPPhLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQN 1171
Cdd:PHA03247  2914 PPPP-QPQPQPPPPPQPQPPPPPPPRPQPP-LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPAS 2991
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1172 PSHANPTHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQS--SHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHH 1249
Cdd:PHA03247  2992 STPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDdtEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPD 3071
                          250
                   ....*....|....*...
gi 1907112372 1250 PQASQAKPSHPQSSHAKP 1267
Cdd:PHA03247  3072 PATPEAGARESPSSQFGP 3089
AF-4 pfam05110
AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and ...
1186-1312 2.62e-05

AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and FMR2 (Fragile X E mental retardation syndrome) nuclear proteins. These proteins have been linked to human diseases such as acute lymphoblastic leukaemia and mental retardation. The family also contains a Drosophila AF4 protein homolog Lilliputian which contains an AT-hook domain. Lilliputian represents a novel pair-rule gene that acts in cytoskeleton regulation, segmentation and morphogenesis in Drosophila.


Pssm-ID: 461550 [Multi-domain]  Cd Length: 514  Bit Score: 48.58  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1186 KPSHPQSSHAKPSHP----QSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHHPQASQAKPSHPQ 1261
Cdd:pfam05110   77 KNSVPQTPQEKPDQPffpdKTSGLPPSFHTSSHSQPMGPPSSSSPSVSSSQSQKKSQARTEPAHGGHSSSGSQSSQRSQG 156
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907112372 1262 SSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKSSKTKP 1312
Cdd:pfam05110  157 QSRSKGGQESHSSSHHKRQERREDLFSCASLSHSLEELSPLLSSLSSPVKP 207
AF-4 pfam05110
AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and ...
1124-1320 3.60e-05

AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and FMR2 (Fragile X E mental retardation syndrome) nuclear proteins. These proteins have been linked to human diseases such as acute lymphoblastic leukaemia and mental retardation. The family also contains a Drosophila AF4 protein homolog Lilliputian which contains an AT-hook domain. Lilliputian represents a novel pair-rule gene that acts in cytoskeleton regulation, segmentation and morphogenesis in Drosophila.


Pssm-ID: 461550 [Multi-domain]  Cd Length: 514  Bit Score: 48.20  E-value: 3.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1124 DPSHANLTqGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQ--NPSHANPTHPQSSHakpsHPQSSHAKPSHPQ 1201
Cdd:pfam05110   66 NKSNQHLV-GIPKNSVPQTPQEKPDQPFFPDKTSGLPPSFHTSSHSQpmGPPSSSSPSVSSSQ----SQKKSQARTEPAH 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1202 SSHAKP-SHPQSSHAKPSHPQSSQAK-PSHPQSSQAKPTHPQSSQANSHhpQASQAKPSHP-QSSHAKPSHPHPS----H 1274
Cdd:pfam05110  141 GGHSSSgSQSSQRSQGQSRSKGGQEShSSSHHKRQERREDLFSCASLSH--SLEELSPLLSsLSSPVKPLSPSHSrqhtG 218
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907112372 1275 AKPSPSQSTQCKAHKAHQSqPKPFQPRPTQPKSSKTKPSQARAFHP 1320
Cdd:pfam05110  219 SKAQNSSDHHGKEYSHSKS-PRDSEAGSHGPESPSTSLLASSSQLS 263
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1190-1308 3.65e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.54  E-value: 3.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1190 PQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQaKPTHPQSSQANSHHPQASQAKPSHPQsshaKPSH 1269
Cdd:PRK10263   751 PVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQ-QPVAPQPQYQQPQQPVAPQPQYQQPQ----QPVA 825
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907112372 1270 PHPSHAKPSPSQSTQCKAHKAH-----QSQPKPFQpRPTQPKSS 1308
Cdd:PRK10263   826 PQPQYQQPQQPVAPQPQDTLLHpllmrNGDSRPLH-KPTTPLPS 868
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1107-1280 4.04e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.16  E-value: 4.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1107 QKKPSHSRPSQAKPPHLD-----PSHANLTQGqPSQATPTHSQASQAKPTHSQAnshhphpshakPSHQNPSHANPTHPQ 1181
Cdd:PRK10263   708 QQRYSGEQPAGANPFSLDdfefsPMKALLDDG-PHEPLFTPIVEPVQQPQQPVA-----------PQQQYQQPQQPVAPQ 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1182 SSHAKPSHPqsshAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPthPQSSQANSHHPQASQAKPSHPQ 1261
Cdd:PRK10263   776 PQYQQPQQP----VAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQ--PQYQQPQQPVAPQPQDTLLHPL 849
                          170
                   ....*....|....*....
gi 1907112372 1262 SSHAKPSHPHPSHAKPSPS 1280
Cdd:PRK10263   850 LMRNGDSRPLHKPTTPLPS 868
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1130-1321 5.18e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 47.76  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1130 LTQGQPSQATPTHSQASQAK--PTHSQANSHHPHPshakPSHQNPSHANPTHPQSSHAKPSHPQSShaKPSHPQSSHAKP 1207
Cdd:PTZ00449   476 ISKIQFTQEIKKLIKKSKKKlaPIEEEDSDKHDEP----PEGPEASGLPPKAPGDKEGEEGEHEDS--KESDEPKEGGKP 549
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1208 SHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQssqanshhpqasqaKPSHPQsshaKPSHPHPSHAKPSPSQSTQCKA 1287
Cdd:PTZ00449   550 GETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPK--------------DPKHPK----DPEEPKKPKRPRSAQRPTRPKS 611
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1907112372 1288 HKAHQSQPKPFQP-RPTQPKSSKTKPSQARAFHPR 1321
Cdd:PTZ00449   612 PKLPELLDIPKSPkRPESPKSPKRPPPPQRPSSPE 646
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
942-1233 6.62e-05

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: 47.45  E-value: 6.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  942 PQQYHPNGPFGRSQRQASPVQTHPKSRQMSRTLERSGTVVSRVGHGRSLGSQARRAAGKPQPEKACAQGLQ-LTKAAGKS 1020
Cdd:pfam03154  269 PSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPpREQPLPPA 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1021 IRTLPHIKYPHPQPCQPAGASQERIMP--VSHQGAQQTTQGRPADFAFKPGSQSTSgsklssTSQSSAHQPKFQSKHfQP 1098
Cdd:pfam03154  349 PLSMPHIKPPPTTPIPQLPNPQSHKHPphLSGPSPFQMNSNLPPPPALKPLSSLST------HHPPSAHPPPLQLMP-QS 421
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1099 QPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQNPSHANPT 1178
Cdd:pfam03154  422 QQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVS 501
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907112372 1179 HPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSS 1233
Cdd:pfam03154  502 SSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSHASQS 556
PHA03378 PHA03378
EBNA-3B; Provisional
1097-1325 1.03e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.98  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1097 QPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQA-----TPTHSQAS-----QAKPTHSQANSHHPHPSHAK 1166
Cdd:PHA03378   552 EPASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAqtpwpVPHPSQTPeppttQSHIPETSAPRQWPMPLRPI 631
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1167 PSHQNPSHANPTHPQsshAKPSHPQSSHAKPSHPQSSHAKPSHP--QSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQ 1244
Cdd:PHA03378   632 PMRPLRMQPITFNVL---VFPTPHQPPQVEITPYKPTWTQIGHIpyQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPA 708
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1245 ANSHHPQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQARAFHPRAGR 1324
Cdd:PHA03378   709 APPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQ 788

                   .
gi 1907112372 1325 R 1325
Cdd:PHA03378   789 R 789
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
1025-1169 1.22e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 46.57  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1025 PHIKYPHPQPCQPAGASQERIMPVSHQGAQQTTQGRPADFAFK--PGSQSTSGSKLSSTSQSSAHQPKFQSKHFQPQPFQ 1102
Cdd:pfam09770  217 APAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQghPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVP 296
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907112372 1103 PVPSQKKPSHSRPSqakpphldPSHANLTQGQPSQATPTHSQASQakptHSQANSHHPHPSHAKPSH 1169
Cdd:pfam09770  297 VQPTQILQNPNRLS--------AARVGYPQNPQPGVQPAPAHQAH----RQQGSFGRQAPIITHPQQ 351
ARG80 COG5068
Regulator of arginine metabolism and related MADS box-containing transcription factors ...
1101-1305 1.23e-04

Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription];


Pssm-ID: 227400 [Multi-domain]  Cd Length: 412  Bit Score: 46.16  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1101 FQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQAT-PTHSQASQAKPTHSQANSHHPHP-SHakpSHQNPShanPT 1178
Cdd:COG5068    161 NAPSDSSEEPSSSASFSVDPNDNNPMGSFQHNGSPQTNFiPLQNPQTQQYQQHSSRKDHPTVPhSN---TNNGRP---PA 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1179 HPQSSHAKPSHPQSSHakPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHpqssQANSHHPQASQAKPS 1258
Cdd:COG5068    235 KFMIPELHSSHSTLDL--PSDFISDSGFPNQSSTSIFPLDSAIIQITPPHLPNNPPQENRH----ELYSNDSSMVSETPP 308
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1907112372 1259 HPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQP 1305
Cdd:COG5068    309 PKNLPNGSPNQSPLNNLSRGNPASPNSIIRENNQVEDESFNGRQGSA 355
dnaA PRK14086
chromosomal replication initiator protein DnaA;
1131-1302 1.86e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 45.97  E-value: 1.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1131 TQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQnpsHANPTHPQSSHAKPSHPQ-SSHAKP-SHPQSSHAKPS 1208
Cdd:PRK14086    91 SAGEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRADDRP---PGLPRQDQLPTARPAYPAyQQRPEPgAWPRAADDYGW 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1209 HPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHHPQASQAKPSHPQSSHAKPSHP-------HPSHAKPSPSQ 1281
Cdd:PRK14086   168 QQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRPepppgagHVHRGGPGPPE 247
                          170       180
                   ....*....|....*....|.
gi 1907112372 1282 STQCKAHKAHQSQPKPFQPRP 1302
Cdd:PRK14086   248 RDDAPVVPIRPSAPGPLAAQP 268
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1089-1277 2.21e-04

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 45.65  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1089 PKFQSKHFQPQPFQPVPSQKKpSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPS-HAKP 1167
Cdd:COG5422     80 PKLFQRRNSAGPITHSPSATS-STSSLNSNDGDQFSPASDSLSFNPSSTQSRKDSGPGDGSPVQKRKNPLLPSSStHGTH 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1168 SHQNPSHANPTHPQSSHAK-PSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQAN 1246
Cdd:COG5422    159 PPIVFTDNNGSHAGAPNARsRKEIPSLGSQSMQLPSPHFRQKFSSSDTSNGFSYPSIRKNSRHSSNSMPSFPHSSTAVLL 238
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907112372 1247 SHHPQASQAkpsHPQSSHAKPSHPH-----PSHAKP 1277
Cdd:COG5422    239 KRHSGSSGA---SLISSNITPSSSNseamsTSSKRP 271
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1111-1300 2.42e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1111 SHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQNPSHANPTHPQSSHAKPS-- 1188
Cdd:PRK10263   295 SGNRATQPEYDEYDPLLNGAPITEPVAVAAAATTATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVia 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1189 ------HPQSSHAKPSHPQSSH-AKPSHPQSSHAKPSHPQSSQAKPSHPQSSQA--------KPTHPQSSQANSHHPQAS 1253
Cdd:PRK10263   375 papegyPQQSQYAQPAVQYNEPlQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPaqqpyyapAPEQPVAGNAWQAEEQQS 454
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1254 --QAKPSH-PQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQP 1300
Cdd:PRK10263   455 tfAPQSTYqTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARP 504
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1097-1317 3.06e-04

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: 45.14  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1097 QPQPFQPVPSQKKPSHSRPSQAKPPHLDPShanlTQGQPSQATPTHSQASQAKPTHSQANshhPHPSHAKPSHQnpshan 1176
Cdd:NF033839   300 QPSPQPEKKEVKPEPETPKPEVKPQLEKPK----PEVKPQPEKPKPEVKPQLETPKPEVK---PQPEKPKPEVK------ 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1177 pthPQSSHAKPS-HPQSSHAKPS-HPQSSHAKPS-HPQSSHAKPS-HPQSSQAKPS-HPQSSQAKP-THPQSSQANSH-H 1249
Cdd:NF033839   367 ---PQPEKPKPEvKPQPETPKPEvKPQPEKPKPEvKPQPEKPKPEvKPQPEKPKPEvKPQPEKPKPeVKPQPEKPKPEvK 443
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907112372 1250 PQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKS-SKTKPSQARA 1317
Cdd:NF033839   444 PQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPQADDKKPSTPNNlSKDKQPSNQA 512
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
149-229 3.80e-04

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260038  Cd Length: 94  Bit Score: 40.89  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  149 EAMATEGASseLIEKKRTKLL----SVLqqdpdSILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRR 224
Cdd:cd08329      1 EEMASDDLS--LIRKNRMALFqhltCVL-----PILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEV 73

                   ....*
gi 1907112372  225 FLRCL 229
Cdd:cd08329     74 FRNCL 78
dnaA PRK14086
chromosomal replication initiator protein DnaA;
1182-1321 4.01e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 44.82  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1182 SSHAKPSHPQSSHAKPSHPQSSHAKPShPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQAN--SHHPQASQAKPSH 1259
Cdd:PRK14086    90 PSAGEPAPPPPHARRTSEPELPRPGRR-PYEGYGGPRADDRPPGLPRQDQLPTARPAYPAYQQRPepGAWPRAADDYGWQ 168
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907112372 1260 PQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQARAFHPR 1321
Cdd:PRK14086   169 QQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRPE 230
PRK11901 PRK11901
hypothetical protein; Reviewed
1131-1313 4.33e-04

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 43.90  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1131 TQGQPSQATPTHSQA-----SQAKPTHSQANSHHPHPSHAKPSHQNPSHANPTHPQSSHAKPSHPQSSHAKPSHPQSSHA 1205
Cdd:PRK11901    62 TEHESQQSSNNAGAEknidlSGSSSLSSGNQSSPSAANNTSDGHDASGVKNTAPPQDISAPPISPTPTQAAPPQTPNGQQ 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1206 KPSHPQSSHAKPSHPQS--SQAKPSHPQSSQAKPTHPQSsQANSHHPQASQAKPSHPQSshakpsHPHPSHAKPSPSQST 1283
Cdd:PRK11901   142 RIELPGNISDALSQQQGqvNAASQNAQGNTSTLPTAPAT-VAPSKGAKVPATAETHPTP------PQKPATKKPAVNHHK 214
                          170       180       190
                   ....*....|....*....|....*....|
gi 1907112372 1284 QCKAHKAHQSQPKPFQPRPTQPKSSKTKPS 1313
Cdd:PRK11901   215 TATVAVPPATSGKPKSGAASARALSSAPAS 244
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
1175-1281 5.59e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 44.38  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1175 ANPTHPQSSHAKPSHPQSsHAKPSHPQSshAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHHPQASQ 1254
Cdd:PRK14971   360 AQLTQKGDDASGGRGPKQ-HIKPVFTQP--AAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVP 436
                           90       100
                   ....*....|....*....|....*..
gi 1907112372 1255 AKPSHPQSSHAKPShPHPSHAKPSPSQ 1281
Cdd:PRK14971   437 VNPPSTAPQAVRPA-QFKEEKKIPVSK 462
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1200-1320 5.63e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.69  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1200 PQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQssqaKPTHPQSSQANSHHPQASQAKPSHPQsshaKPSHPHPSHAKPSp 1279
Cdd:PRK10263   751 PVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQ----QPVAPQPQYQQPQQPVAPQPQYQQPQ----QPVAPQPQYQQPQ- 821
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907112372 1280 sqstqckahkahqsQPKPFQPRPTQPKSSKTKPSQARAFHP 1320
Cdd:PRK10263   822 --------------QPVAPQPQYQQPQQPVAPQPQDTLLHP 848
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
1179-1317 6.10e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 44.09  E-value: 6.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1179 HPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHHPQASQAKPS 1258
Cdd:PRK07994   360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAK 439
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907112372 1259 HPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQP----KSSKTKPSQARA 1317
Cdd:PRK07994   440 KSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPvevkKEPVATPKALKK 502
PHA03269 PHA03269
envelope glycoprotein C; Provisional
1111-1244 6.23e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.95  E-value: 6.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1111 SHSRPSQAKPPHLDPSHANLTQGQPSQA-TPTHSQASQAKPTHSQANSHHPHPSHAKPSHQNPShanpthpqsshakpsh 1189
Cdd:PHA03269    46 PHQAASRAPDPAVAPTSAASRKPDLAQApTPAASEKFDPAPAPHQAASRAPDPAVAPQLAAAPK---------------- 109
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907112372 1190 PQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPqssqakPSHPQSSQAKPTHPQSSQ 1244
Cdd:PHA03269   110 PDAAEAFTSAAQAHEAPADAGTSAASKKPDP------AAHTQHSPPPFAYTRSME 158
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1158-1320 6.78e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.31  E-value: 6.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1158 HHPHPSHAKPSHQNPSHANPTHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKP 1237
Cdd:PRK10263   367 QTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNA 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1238 THPQSSQANSHHPQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQARA 1317
Cdd:PRK10263   447 WQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAW 526

                   ...
gi 1907112372 1318 FHP 1320
Cdd:PRK10263   527 YQP 529
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1106-1320 8.33e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.91  E-value: 8.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1106 SQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQaTPTHSQasqaKPTHSQANSHHPHPSHAKPSHQNPSHANPTHPQSsha 1185
Cdd:PTZ00449   540 SDEPKEGGKPGETKEGEVGKKPGPAKEHKPSK-IPTLSK----KPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKS--- 611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1186 kPSHPQS-----SHAKPSHPQSSHAKPShPQSShAKPSHPQSSQA-KPSHPQSSQAKPTHPQSSQA--NSHHPQASQAKP 1257
Cdd:PTZ00449   612 -PKLPELldipkSPKRPESPKSPKRPPP-PQRP-SSPERPEGPKIiKSPKPPKSPKPPFDPKFKEKfyDDYLDAAAKSKE 688
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907112372 1258 ShpqsshakPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQP-RPTQPKSSKTKPSQARAFHP 1320
Cdd:PTZ00449   689 T--------KTTVVLDESFESILKETLPETPGTPFTTPRPLPPkLPRDEEFPFEPIGDPDAEQP 744
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
1176-1290 9.46e-04

Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.


Pssm-ID: 462833 [Multi-domain]  Cd Length: 183  Bit Score: 41.86  E-value: 9.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1176 NPTHPQSSHAKPSHPQSShAKPSHPQSSHAKPSHPQSSHakpSHPQSSQAKPSHPQS----SQAKPTHPQSSQANSHHPQ 1251
Cdd:pfam09595   56 NKQHPEQEHHENPPLNEA-AKEAPSESEDAPDIDPNNQH---PSQDRSEAPPLEPAAktkpSEHEPANPPDASNRLSPPD 131
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1907112372 1252 ASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKA 1290
Cdd:pfam09595  132 ASTAAIREARTFRKPSTGKRNNPSSAQSDQSPPRANHEA 170
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
1089-1320 1.06e-03

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 43.73  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1089 PKFQSKhfQPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKP---THSQANSHHPHPSHA 1165
Cdd:COG5422     24 DAFVSK--QLLPPRRLQRKLNPISIRNGADNDIINSESKESFGKYALGHQIFSSFSSSPKLFqrrNSAGPITHSPSATSS 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1166 KPS-------HQNPSHA----NPTHPQSS------HAKPSHPQSSHAKPSHPQSSHAKP---SHPQSSHAKPSHPQSSQA 1225
Cdd:COG5422    102 TSSlnsndgdQFSPASDslsfNPSSTQSRkdsgpgDGSPVQKRKNPLLPSSSTHGTHPPivfTDNNGSHAGAPNARSRKE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1226 KPSH-PQSSQAKPTHPQSSQANSHHPQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQ 1304
Cdd:COG5422    182 IPSLgSQSMQLPSPHFRQKFSSSDTSNGFSYPSIRKNSRHSSNSMPSFPHSSTAVLLKRHSGSSGASLISSNITPSSSNS 261
                          250
                   ....*....|....*.
gi 1907112372 1305 PKSSKTkpSQARAFHP 1320
Cdd:COG5422    262 EAMSTS--SKRPYIYP 275
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
1197-1325 1.11e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 43.52  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1197 PSHPQSSHAKPSHPQSSHAKPSHPQSSqaKPSHPQSSQAKPTHPQSSQANSHHPQASQAKPSHPQSSHAKPSHPHPSHAK 1276
Cdd:PTZ00449   511 PEGPEASGLPPKAPGDKEGEEGEHEDS--KESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHP 588
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907112372 1277 PSPSQSTQCKAHKAHQSQPKPfqPRPTQPKSSKTKPSQARAFHPRAGRR 1325
Cdd:PTZ00449   589 KDPEEPKKPKRPRSAQRPTRP--KSPKLPELLDIPKSPKRPESPKSPKR 635
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
1161-1274 1.43e-03

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: 42.34  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1161 HPSHAKPSHQnpshANPTHPQSSHAKPSHPQSSHAKPSHPQSSHAkPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHP 1240
Cdd:cd22056    203 FMGQQKPKHQ----MHSVHPQAFTHHQAAGPGALQGRGGRGGPDC-HLLHSSHHHHHHHHLQYQYMNAPYPPHYAHQGAP 277
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907112372 1241 QSSQANSHHPQASQAKPSHPQSSHAKPShPHPSH 1274
Cdd:cd22056    278 QFHGQYSVFREPMRVHHQGHPGSMLTPP-SSPPL 310
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
1115-1317 1.49e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.99  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1115 PSQAKPPHlDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQN---PSHANPTHPQSSHAKPShPQ 1191
Cdd:PLN03209   324 PSQRVPPK-ESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDlkpPTSPIPTPPSSSPASSK-SV 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1192 SSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAK---PTHPQSSQANSHHPQASQAkPSHPQSSHAKPS 1268
Cdd:PLN03209   402 DAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDlkpPTSPSPTAPTGVSPSVSST-SSVPAVPDTAPA 480
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907112372 1269 HPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQARA 1317
Cdd:PLN03209   481 TAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEV 529
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
1117-1223 1.55e-03

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: 42.34  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1117 QAKPPHLDPSHANLTQGQPSQATPTHSQASQA--KPTHSQANSHHPHPSHakPSHQNPSHANPTHPQssHAKPSHPQ--- 1191
Cdd:cd22056    206 QQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGrgGPDCHLLHSSHHHHHH--HHLQYQYMNAPYPPH--YAHQGAPQfhg 281
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1907112372 1192 --SSHAKPSHPQSSHakpsHPQSSHAKPSHPQSS 1223
Cdd:cd22056    282 qySVFREPMRVHHQG----HPGSMLTPPSSPPLL 311
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1170-1324 1.84e-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: 42.83  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1170 QNPSHANPTHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPsHPQSSQAKPTHPQssQANSHH 1249
Cdd:pfam03154  170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAP-HTLIQQTPTLHPQ--RLPSPH 246
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907112372 1250 PQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKA---HKAHQSQPKPFQPRPTQPKSSKTKPSQARAFHPRAGR 1324
Cdd:pfam03154  247 PPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTgpsHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1030-1244 2.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1030 PHPQPCQPAGASQErimpvshqgaqqtTQGRPADFAFKPGSQSTSGSKLSSTSQSSAHQPKFQSKHFQPQPFQPVPSQKK 1109
Cdd:PRK07764   590 PAPGAAGGEGPPAP-------------ASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKH 656
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1110 PSHSRPSQAKpphlDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQNPSHANPTHPQSSHAKPSH 1189
Cdd:PRK07764   657 VAVPDASDGG----DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPS 732
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907112372 1190 PQSSHAKPSHPqsshAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQ 1244
Cdd:PRK07764   733 PAADDPVPLPP----EPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
PRK11901 PRK11901
hypothetical protein; Reviewed
1181-1320 2.82e-03

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 41.59  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1181 QSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHP---------QSSQANsHHPQ 1251
Cdd:PRK11901    87 LSSGNQSSPSAANNTSDGHDASGVKNTAPPQDISAPPISPTPTQAAPPQTPNGQQRIELPgnisdalsqQQGQVN-AASQ 165
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907112372 1252 ASQAKPSH--------PQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPRPTQPKSSKTKPSQARAFHP 1320
Cdd:PRK11901   166 NAQGNTSTlptapatvAPSKGAKVPATAETHPTPPQKPATKKPAVNHHKTATVAVPPATSGKPKSGAASARALSSAP 242
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
1204-1302 2.96e-03

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: 41.57  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1204 HAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHHPQasqakPSHPQSSHAKPSHPHPSHAKPSPSQ-- 1281
Cdd:cd22056    206 QQKPKHQMHSVHPQAFTHHQAAGPGALQGRGGRGGPDCHLLHSSHHHH-----HHHHLQYQYMNAPYPPHYAHQGAPQfh 280
                           90       100
                   ....*....|....*....|....
gi 1907112372 1282 ---STQCKAHKAHQSQPKPFQPRP 1302
Cdd:cd22056    281 gqySVFREPMRVHHQGHPGSMLTP 304
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1210-1325 3.08e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.01  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1210 PQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHHPQASQAKPSHPQSSHAKPSHPHPSHAKPSPSqSTQCKAHK 1289
Cdd:PRK14951   373 AAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA-AVALAPAP 451
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907112372 1290 AHQSQPKPFQ-PRPTQPKSSKTKPSQARAFHPRAGRR 1325
Cdd:PRK14951   452 PAQAAPETVAiPVRVAPEPAVASAAPAPAAAPAAARL 488
CARD_NOD1_CARD4 cd08324
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ...
179-229 3.23e-03

Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260035  Cd Length: 85  Bit Score: 37.84  E-value: 3.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907112372  179 ILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRRFLRCL 229
Cdd:cd08324     20 LLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYIL 70
PHA02666 PHA02666
hypothetical protein; Provisional
1107-1278 3.35e-03

hypothetical protein; Provisional


Pssm-ID: 222914 [Multi-domain]  Cd Length: 287  Bit Score: 41.07  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1107 QKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQNPSHANPTHPQSSHAK 1186
Cdd:PHA02666    43 KSRPSRQHRSAERTPTTASSLTHENNTAPSRHGKQHSCKASSRSSHNRGSTSSSHNHHAHRGPHQSAHRRSKHDAVRDTY 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1187 PSHPQSshakPSHPQSSHAKPSHPQSSHAKPSH----PQSSQAKPSHPQSSQAKPthpqssqaNSHHPQASQAKPSHPQS 1262
Cdd:PHA02666   123 QPCPQS----PETDLYKGRLPGETERHYETPDHiydvPEDVRCAAVEPRRDLALP--------PLHIPSSKPARRMRPGS 190
                          170
                   ....*....|....*.
gi 1907112372 1263 SHAKPSHpHPSHAKPS 1278
Cdd:PHA02666   191 MGDFPMK-HTSAGKPN 205
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1015-1201 3.84e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1015 KAAGKSIRTLPHIKYPHPQPCQPAGASQERIMPVSHQGAQQTTQGRPADFAFKPGSQSTSGSKLSSTSQSSAHQPKFQSK 1094
Cdd:PRK07764   593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1095 HFQPQPFQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPS-HQNPS 1173
Cdd:PRK07764   673 AGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDdPPDPA 752
                          170       180
                   ....*....|....*....|....*...
gi 1907112372 1174 HANPTHPQSSHAKPSHPQSSHAKPSHPQ 1201
Cdd:PRK07764   753 GAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
PTZ00395 PTZ00395
Sec24-related protein; Provisional
1062-1244 3.86e-03

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 41.98  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1062 ADFAFKPGSQSTSGSKLSSTSQSSAHQPKFQSKHFQPQPFQPVPSQKKPsHSRPSQAKPPhldpsHANLTQGQPSQATPT 1141
Cdd:PTZ00395   395 SNAAQSNAAQSNAGFSNAGYSNPGNSNPGYNNAPNSNTPYNNPPNSNTP-YSNPPNSNPP-----YSNLPYSNTPYSNAP 468
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1142 HSQASQAKPThsqansHHPHPSHAKPSHQN---PSHANPTHPQSShAKPSH--PQSSHAKP--SHPQSSHAKPSHPQSSh 1214
Cdd:PTZ00395   469 LSNAPPSSAK------DHHSAYHAAYQHRAanqPAANLPTANQPA-ANNFHgaAGNSVGNPfaSRPFGSAPYGGNAATT- 540
                          170       180       190
                   ....*....|....*....|....*....|
gi 1907112372 1215 akpSHPQSSQAKPSHPQSSQAKPTHPQSSQ 1244
Cdd:PTZ00395   541 ---ADPNGIAKREDHPEGGTNRQKYEQSDE 567
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
1086-1305 3.87e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.45  E-value: 3.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1086 AHQPKFQSKHFQPQPFQPVPSQKKPShsRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHhPHPSHA 1165
Cdd:PLN03209   336 ADGPKPVPTKPVTPEAPSPPIEEEPP--QPKAVVPRPLSPYTAYEDLKPPTSPIPTPPSSSPASSKSVDAVAK-PAEPDV 412
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1166 KPSHQNPSHANPTHPQSSHAKPSHPQSSHA-----KPshpqsshakPSHPQSSHAKPSHPQSSQAkPSHPQSSQAKPthP 1240
Cdd:PLN03209   413 VPSPGSASNVPEVEPAQVEAKKTRPLSPYAryedlKP---------PTSPSPTAPTGVSPSVSST-SSVPAVPDTAP--A 480
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1241 QSSQANSHHPQA------------SQAKPSHPQSSHAKPSHPHPSHAKPSPSQST---QCKAHKAHQSQPKpfqPRPTQP 1305
Cdd:PLN03209   481 TAATDAAAPPPAnmrplspyavydDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSappTALADEQHHAQPK---PRPLSP 557
ARG80 COG5068
Regulator of arginine metabolism and related MADS box-containing transcription factors ...
1032-1280 4.20e-03

Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription];


Pssm-ID: 227400 [Multi-domain]  Cd Length: 412  Bit Score: 41.15  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1032 PQPCQPAGASQERIMPVSHQGAQQTTQGRPADFAFKPGSQSTSGSKLSSTSQSSAHQPKFQSKHFQPQPFQPVPSQKKPS 1111
Cdd:COG5068    144 SVVKSLEGKSLIQSPCSNAPSDSSEEPSSSASFSVDPNDNNPMGSFQHNGSPQTNFIPLQNPQTQQYQQHSSRKDHPTVP 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1112 HSRPSQAKPPHLdPSHANLTQGQPSQATPTHSQASQAKPTHSQAnshhphpSHAKPSHQNPSHANPTHPQSSHAKPSHPQ 1191
Cdd:COG5068    224 HSNTNNGRPPAK-FMIPELHSSHSTLDLPSDFISDSGFPNQSST-------SIFPLDSAIIQITPPHLPNNPPQENRHEL 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1192 SSHakPSHPQSSHAKPshPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHHPQASQAKPSHPQSSHAKPSHPH 1271
Cdd:COG5068    296 YSN--DSSMVSETPPP--KNLPNGSPNQSPLNNLSRGNPASPNSIIRENNQVEDESFNGRQGSAIWNALISTTQPNSGLH 371

                   ....*....
gi 1907112372 1272 PSHAKPSPS 1280
Cdd:COG5068    372 TEASTAPSS 380
PRK11901 PRK11901
hypothetical protein; Reviewed
1105-1295 4.32e-03

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 40.82  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1105 PSQKKPSHSRPSQ--AKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANShhPHPSHAKPSHQNPSHANPTHPQS 1182
Cdd:PRK11901    61 PTEHESQQSSNNAgaEKNIDLSGSSSLSSGNQSSPSAANNTSDGHDASGVKNTAP--PQDISAPPISPTPTQAAPPQTPN 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1183 SHAKPSHPQSSHAKPSHPQSshakpshpQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSH---HPQASQAKPsh 1259
Cdd:PRK11901   139 GQQRIELPGNISDALSQQQG--------QVNAASQNAQGNTSTLPTAPATVAPSKGAKVPATAETHptpPQKPATKKP-- 208
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907112372 1260 PQSSHAKPSHPHPSHAKPSPSQSTqcKAHKAHQSQP 1295
Cdd:PRK11901   209 AVNHHKTATVAVPPATSGKPKSGA--ASARALSSAP 242
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
1143-1313 4.73e-03

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 41.19  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1143 SQASQAKPTHSQANSHHPhpshAKPSHQNP-SHANPTHPQSSHAKpshpQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQ 1221
Cdd:pfam05539  170 TAVTTSKTTSWPTEVSHP----TYPSQVTPqSQPATQGHQTATAN----QRLSSTEPVGTQGTTTSSNPEPQTEPPPSQR 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1222 SSQAKPSHPQSsqakpTHPQSSQANSHHPQASQAKPSHPQSSHAKPSHPHPSHAKPSPSQSTQCKAHKAHQSQPKPFQPR 1301
Cdd:pfam05539  242 GPSGSPQHPPS-----TTSQDQSTTGDGQEHTQRRKTPPATSNRRSPHSTATPPPTTKRQETGRPTPRPTATTQSGSSPP 316
                          170
                   ....*....|..
gi 1907112372 1302 PTQPKSSKTKPS 1313
Cdd:pfam05539  317 HSSPPGVQANPT 328
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
1158-1264 5.08e-03

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: 40.80  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1158 HHPHPSHAKPSHQNPSHANPTHPQSSHAKPSHPQSSHAKPSHPQSSHakpsHPQSSHAKPSHPQSSQAKPSHPQ-----S 1232
Cdd:cd22056    209 PKHQMHSVHPQAFTHHQAAGPGALQGRGGRGGPDCHLLHSSHHHHHH----HHLQYQYMNAPYPPHYAHQGAPQfhgqyS 284
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1907112372 1233 SQAKPTHPQssqaNSHHPQASQAKPSHPQSSH 1264
Cdd:cd22056    285 VFREPMRVH----HQGHPGSMLTPPSSPPLLE 312
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
1106-1264 6.34e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 40.86  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1106 SQKKPSHSR----PSQAKPPhLDPSHANltqgqpSQATPTHSQASQAKPTHSQANSHHPHPSHAKPSHQNPSHANPTHP- 1180
Cdd:PRK14949   635 DGKKSSADRkpktPPSRAPP-ASLSKPA------SSPDASQTSASFDLDPDFELATHQSVPEAALASGSAPAPPPVPDPy 707
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1181 -------QSSHAKPSHPQSSHAKPSHPQSSH-AKPSHPQSSHAKPSHPQSSQAKPshpQSSQAKPTHPQSSQANSHHPQA 1252
Cdd:PRK14949   708 drppweeAPEVASANDGPNNAAEGNLSESVEdASNSELQAVEQQATHQPQVQAEA---QSPASTTALTQTSSEVQDTELN 784
                          170
                   ....*....|..
gi 1907112372 1253 SQAKPSHPQSSH 1264
Cdd:PRK14949   785 LVLLSSGSITGH 796
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1028-1213 6.97e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 6.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1028 KYPHPQPCQPAGASQERIMPVSHQGA---QQTTQG-RPA--------DFAFKP-------GSQSTSGSKLSSTSQSSAHQ 1088
Cdd:PRK10263   679 QYQHDVPVNAEDADAAAEAELARQFAqtqQQRYSGeQPAganpfsldDFEFSPmkallddGPHEPLFTPIVEPVQQPQQP 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1089 PKFQSKHFQPQpfQPVPSQKKpsHSRPSQAKPPhldpSHANLTQGQPSQATPTHSQASQakPTHSQANSHHPH-PSHAKP 1167
Cdd:PRK10263   759 VAPQQQYQQPQ--QPVAPQPQ--YQQPQQPVAP----QPQYQQPQQPVAPQPQYQQPQQ--PVAPQPQYQQPQqPVAPQP 828
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907112372 1168 SHQNPSHANPTHPQSSHAKPSHPQSSHAKPSHpqsshaKPSHPQSS 1213
Cdd:PRK10263   829 QYQQPQQPVAPQPQDTLLHPLLMRNGDSRPLH------KPTTPLPS 868
PRK10263 PRK10263
DNA translocase FtsK; Provisional
994-1246 7.15e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 7.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372  994 ARRAAGKPQPEKACAQGLQLTKAagkSIRTLPHIKYPHPQPCQPAGASQE--------RIMPVSHQGAQQTTQGRPADFA 1065
Cdd:PRK10263   349 VDVPPAQPTVAWQPVPGPQTGEP---VIAPAPEGYPQQSQYAQPAVQYNEplqqpvqpQQPYYAPAAEQPAQQPYYAPAP 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1066 FKPGSQSTSGSKLSSTSQSSAHQPKFQSKHFQPQP-FQPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQPSQATPTHS- 1143
Cdd:PRK10263   426 EQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQStYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPp 505
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1144 -------QASQAKPTHSQANSHHPHPSHAK-PSHQNPSHANPTHPQSSHAKPSHPQSSHAKPSHPQSSHAkpshpqSSHA 1215
Cdd:PRK10263   506 lyyfeevEEKRAREREQLAAWYQPIPEPVKePEPIKSSLKAPSVAAVPPVEAAAAVSPLASGVKKATLAT------GAAA 579
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907112372 1216 KPSHPQSSQAKPSHPQSSQAKPTHPQSSQAN 1246
Cdd:PRK10263   580 TVAAPVFSLANSGGPRPQVKEGIGPQLPRPK 610
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1116-1314 7.65e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.84  E-value: 7.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1116 SQAKPPHLDpSHANLTQGQPSQA---------TPTHSQASQAKPTHSQANSHHPHPSHAKPS--------HQNPSHANPT 1178
Cdd:PRK10263   297 NRATQPEYD-EYDPLLNGAPITEpvavaaaatTATQSWAAPVEPVTQTPPVASVDVPPAQPTvawqpvpgPQTGEPVIAP 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1179 HPQS--SHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHHPQaSQAK 1256
Cdd:PRK10263   376 APEGypQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAE-EQQS 454
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907112372 1257 PSHPQSSHaKPSHPHPSHAKPSPSqstqckaHKAHQSQPKPFQPRPtQPKSSKTKPSQ 1314
Cdd:PRK10263   455 TFAPQSTY-QTEQTYQQPAAQEPL-------YQQPQPVEQQPVVEP-EPVVEETKPAR 503
PRK10263 PRK10263
DNA translocase FtsK; Provisional
1113-1320 8.76e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 8.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1113 SRPSQAKPPHLDPSHANLTQGQPSQATPTHSQASQAKPTHSQANSHHPHPSHAKPShqNPSHANPTHPqSSHAKPSHPQS 1192
Cdd:PRK10263   282 ARGVAADPDDVLFSGNRATQPEYDEYDPLLNGAPITEPVAVAAAATTATQSWAAPV--EPVTQTPPVA-SVDVPPAQPTV 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1193 SHAKPSHPQSshAKPSHPQSSHAKPSHPQSSQakpshPQSSQAKPTHPQSSQANSHHPQASQAKPSHPQSSHAKPSHPHP 1272
Cdd:PRK10263   359 AWQPVPGPQT--GEPVIAPAPEGYPQQSQYAQ-----PAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQ 431
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1273 SHAKPSPSQSTQCKAHKAHQSQPkPFQPRPT-QPKSSKTKP-SQARAFHP 1320
Cdd:PRK10263   432 PYYAPAPEQPVAGNAWQAEEQQS-TFAPQSTyQTEQTYQQPaAQEPLYQQ 480
PRK10905 PRK10905
cell division protein DamX; Validated
1102-1282 9.48e-03

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 39.92  E-value: 9.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1102 QPVPSQKKPSHSRPSQAKPPHLDPSHANLTQGQpsqaTPTHSQASQAKPTHSQANShhphpshAKPSHQNPSHAN----- 1176
Cdd:PRK10905    52 QPAPGTTSAEQTAGNTQQDVSLPPISSTPTQGQ----TPVATDGQQRVEVQGDLNN-------ALTQPQNQQQLNnvavn 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112372 1177 ---PTHPqSSHAKPSHPQSSHAKPSHPQSSHAKPSHPQSSHA--KPSHPQSSQAKPSHPQSSQAKPTHPQSSQANSHHPQ 1251
Cdd:PRK10905   121 stlPTEP-ATVAPVRNGNASRQTAKTQTAERPATTRPARKQAviEPKKPQATAKTEPKPVAQTPKRTEPAAPVASTKAPA 199
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1907112372 1252 ASQAKPSHPQSSHAKPSHPHPSHAKPSPSQS 1282
Cdd:PRK10905   200 ATSTPAPKETATTAPVQTASPAQTTATPAAG 230
CARD_RIP2_CARD3 cd08786
Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase ...
159-229 9.57e-03

Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase activation and recruitment domain (CARD) of Receptor Interacting Protein 2 (RIP2/RIPK2/RICK/CARDIAK/CARD3). RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP2 harbors a C-terminal CARD domain and functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR)-family, NOD1 and NOD2, which recognizes bacterial peptidoglycans released upon infection. This cascade is implicated in inflammatory immune responses and the clearance of intracellular pathogens. RIP2 associates with NOD1 and NOD2 via CARD-CARD interactions. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176764  Cd Length: 87  Bit Score: 36.82  E-value: 9.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907112372  159 ELIEKKRTKLLSVLQQDP-DSILDTLTSRSLISEKEYETLEEITDPLKKSRKLLILIQKKGEDSCRRFLRCL 229
Cdd:cd08786      1 QWIASKREEIVSQMTEAClNQSLDALLSRQLLMREDYELISTKPTRTSKVRQLLDTCDCQGEEFARVVVQKL 72
 
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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