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Conserved domains on  [gi|1370992868|emb|SPJ10418|]
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Plasmodium exported protein (PHISTc), unknown function [Plasmodium sp. DRC-Itaito]

Protein Classification

PRESAN domain-containing protein( domain architecture ID 10560507)

PRESAN (Plasmodium RESA N-terminal) domain-containing protein, similar to Plasmodium falciparum PHIST protein that binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surface

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRESAN pfam09687
Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium ...
 97-221 4.66e-18

Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium export proteins PHISTa and PHISTc has been extended to become this six-helical PRESAN domain identified in the P. falciparum-specific RESA-type (Ring-infected erythrocyte surface antigen) proteins in association with the DnaJ domain. Overall, at least 67 proteins have been detected in P. falciparum with complete copies of the PRESAN domain. No versions of this domain were detected in other apicomplexan genera, suggesting that the domain was 'invented' after the divergence of the lineage leading to the genus Plasmodium undergoing a dramatic proliferation only in P. falciparum. A secondary structure-prediction derived from the multiple alignment of the PRESAN family reveals that it is composed of an all-helical fold with six conserved helical segments. There is some evidence it might localize to membranes.


:

Pssm-ID: 430754  Cd Length: 125  Bit Score: 79.63  E-value: 4.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  97 KYTAEEINQMIDNSNESISRNDMHIIFSFVHDAEIEKFKKVEENIFQFIESIVETYKISDEFKMKKFKYAHLEMEGHLIQ 176
Cdd:pfam09687   1 NLTEEEINKKINSLNEVVSKKDMYIIWNYVNKNEKKKYYNMIEKLWKYFEELAKKYNIPEEYKKKLWKECYKEITKELKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370992868 177 QEKFLLQYAFLSLNGKVCERKKFKEVLKYVKREWIEFRKLMFEVW 221
Cdd:pfam09687  81 KEKFYNKDFYSFLNKGKLSRDEFKEFINSCRKSWKKLRKELEKKW 125
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 270-397 5.75e-07

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.01  E-value: 5.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  270 LGEVESETIKKETEHHENEKITVEEVKPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPpklqQQKVEPPKLQQQKVKPPK 349
Cdd:PRK10263   724 LDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQP----QQPVAPQPQYQQPQQPVA 799

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370992868  350 VQQQKVKPpklqQQKVEPPKVQQQKVEPPKVQQQKLQNekgQKQVCPK 397
Cdd:PRK10263   800 PQPQYQQP----QQPVAPQPQYQQPQQPVAPQPQYQQP---QQPVAPQ 840
 
Name Accession Description Interval E-value
PRESAN pfam09687
Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium ...
 97-221 4.66e-18

Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium export proteins PHISTa and PHISTc has been extended to become this six-helical PRESAN domain identified in the P. falciparum-specific RESA-type (Ring-infected erythrocyte surface antigen) proteins in association with the DnaJ domain. Overall, at least 67 proteins have been detected in P. falciparum with complete copies of the PRESAN domain. No versions of this domain were detected in other apicomplexan genera, suggesting that the domain was 'invented' after the divergence of the lineage leading to the genus Plasmodium undergoing a dramatic proliferation only in P. falciparum. A secondary structure-prediction derived from the multiple alignment of the PRESAN family reveals that it is composed of an all-helical fold with six conserved helical segments. There is some evidence it might localize to membranes.


Pssm-ID: 430754  Cd Length: 125  Bit Score: 79.63  E-value: 4.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  97 KYTAEEINQMIDNSNESISRNDMHIIFSFVHDAEIEKFKKVEENIFQFIESIVETYKISDEFKMKKFKYAHLEMEGHLIQ 176
Cdd:pfam09687   1 NLTEEEINKKINSLNEVVSKKDMYIIWNYVNKNEKKKYYNMIEKLWKYFEELAKKYNIPEEYKKKLWKECYKEITKELKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370992868 177 QEKFLLQYAFLSLNGKVCERKKFKEVLKYVKREWIEFRKLMFEVW 221
Cdd:pfam09687  81 KEKFYNKDFYSFLNKGKLSRDEFKEFINSCRKSWKKLRKELEKKW 125
P_fal_TIGR01639 TIGR01639
Plasmodium falciparum uncharacterized domain TIGR01639; This model represents a conserved ...
 91-149 5.81e-10

Plasmodium falciparum uncharacterized domain TIGR01639; This model represents a conserved sequence region of about 60 amino acids found in over 40 predicted proteins of Plasmodium falciparum. It is not found elsewhere, including closely related species such as Plasmodium yoelii. No member of this family is characterized.


Pssm-ID: 130700  Cd Length: 61  Bit Score: 54.95  E-value: 5.81e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  91 NKCDMQK-YTAEEINQMIDNSNESISRNDMHIIFSFVHDAEIEKFKKVEENIFQFIESIV 149
Cdd:TIGR01639   2 KYNDLSKkLTKEELNEMINSLDEIPNRNDMLIIWNQVHGIERDKFVKMQENLKEYIQKLV 61
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 270-397 5.75e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.01  E-value: 5.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  270 LGEVESETIKKETEHHENEKITVEEVKPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPpklqQQKVEPPKLQQQKVKPPK 349
Cdd:PRK10263   724 LDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQP----QQPVAPQPQYQQPQQPVA 799

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370992868  350 VQQQKVKPpklqQQKVEPPKVQQQKVEPPKVQQQKLQNekgQKQVCPK 397
Cdd:PRK10263   800 PQPQYQQP----QQPVAPQPQYQQPQQPVAPQPQYQQP---QQPVAPQ 840
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 281-378 1.53e-06

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 50.30  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 281 ETEHHENEKITVEEVKPPKLQEQkVEPPKLQQQKVEPPKLQQ-QKVEPPKLQQQKVEPPKLQQQKVKPPKVQQ-QKVKPP 358
Cdd:cd22536   328 SSERTEEEPQTSAAESEAQSSSQ-LQSNGLQNVQDQSNSLQQvQIVGQPILQQIQIQQPQQQIIQAIQPQSFQlQSGQTI 406

                          90       100
                  ....*....|....*....|
gi 1370992868 359 KLQQQKVEpPKVQQQKVEPP 378
Cdd:cd22536   407 QTIQQQPL-QNVQLQAVQSP 425
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 296-379 3.49e-05

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 45.82  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 296 KPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPklQQQKVEPPKLQQQK--VKPPKVQQQKVKPPKLQQQKVEPPKVQ-Q 372
Cdd:COG5180   175 PPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVK--DEAQEEPPDLTGGAdhPRPEAASSPKVDPPSTSEARSRPATVDaQ 252


                  ....*..
gi 1370992868 373 QKVEPPK 379
Cdd:COG5180   253 PEMRPPA 259
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 287-407 7.15e-05

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 43.10  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 287 NEKITVEEVkPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKVQQQKVKPPklqQQKVE 366
Cdd:pfam15240  20 SEDVSQEDS-PSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPP---QGGPR 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370992868 367 PPKVQQQKVEPPKVQQQ-------KLQNEKGQKQVCPKVKGNNQRKQT 407
Cdd:pfam15240  96 PPPGKPQGPPPQGGNQQqgppppgKPQGPPPQGGGPPPQGGNQQGPPP 143
 
Name Accession Description Interval E-value
PRESAN pfam09687
Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium ...
 97-221 4.66e-18

Plasmodium RESA N-terminal; The short, four-helical domain first identified in the Plasmodium export proteins PHISTa and PHISTc has been extended to become this six-helical PRESAN domain identified in the P. falciparum-specific RESA-type (Ring-infected erythrocyte surface antigen) proteins in association with the DnaJ domain. Overall, at least 67 proteins have been detected in P. falciparum with complete copies of the PRESAN domain. No versions of this domain were detected in other apicomplexan genera, suggesting that the domain was 'invented' after the divergence of the lineage leading to the genus Plasmodium undergoing a dramatic proliferation only in P. falciparum. A secondary structure-prediction derived from the multiple alignment of the PRESAN family reveals that it is composed of an all-helical fold with six conserved helical segments. There is some evidence it might localize to membranes.


Pssm-ID: 430754  Cd Length: 125  Bit Score: 79.63  E-value: 4.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  97 KYTAEEINQMIDNSNESISRNDMHIIFSFVHDAEIEKFKKVEENIFQFIESIVETYKISDEFKMKKFKYAHLEMEGHLIQ 176
Cdd:pfam09687   1 NLTEEEINKKINSLNEVVSKKDMYIIWNYVNKNEKKKYYNMIEKLWKYFEELAKKYNIPEEYKKKLWKECYKEITKELKK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370992868 177 QEKFLLQYAFLSLNGKVCERKKFKEVLKYVKREWIEFRKLMFEVW 221
Cdd:pfam09687  81 KEKFYNKDFYSFLNKGKLSRDEFKEFINSCRKSWKKLRKELEKKW 125
P_fal_TIGR01639 TIGR01639
Plasmodium falciparum uncharacterized domain TIGR01639; This model represents a conserved ...
 91-149 5.81e-10

Plasmodium falciparum uncharacterized domain TIGR01639; This model represents a conserved sequence region of about 60 amino acids found in over 40 predicted proteins of Plasmodium falciparum. It is not found elsewhere, including closely related species such as Plasmodium yoelii. No member of this family is characterized.


Pssm-ID: 130700  Cd Length: 61  Bit Score: 54.95  E-value: 5.81e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  91 NKCDMQK-YTAEEINQMIDNSNESISRNDMHIIFSFVHDAEIEKFKKVEENIFQFIESIV 149
Cdd:TIGR01639   2 KYNDLSKkLTKEELNEMINSLDEIPNRNDMLIIWNQVHGIERDKFVKMQENLKEYIQKLV 61
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 270-397 5.75e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.01  E-value: 5.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  270 LGEVESETIKKETEHHENEKITVEEVKPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPpklqQQKVEPPKLQQQKVKPPK 349
Cdd:PRK10263   724 LDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQP----QQPVAPQPQYQQPQQPVA 799

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1370992868  350 VQQQKVKPpklqQQKVEPPKVQQQKVEPPKVQQQKLQNekgQKQVCPK 397
Cdd:PRK10263   800 PQPQYQQP----QQPVAPQPQYQQPQQPVAPQPQYQQP---QQPVAPQ 840
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 281-378 1.53e-06

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 50.30  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 281 ETEHHENEKITVEEVKPPKLQEQkVEPPKLQQQKVEPPKLQQ-QKVEPPKLQQQKVEPPKLQQQKVKPPKVQQ-QKVKPP 358
Cdd:cd22536   328 SSERTEEEPQTSAAESEAQSSSQ-LQSNGLQNVQDQSNSLQQvQIVGQPILQQIQIQQPQQQIIQAIQPQSFQlQSGQTI 406

                          90       100
                  ....*....|....*....|
gi 1370992868 359 KLQQQKVEpPKVQQQKVEPP 378
Cdd:cd22536   407 QTIQQQPL-QNVQLQAVQSP 425
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 288-384 3.31e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.70  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  288 EKITVEEVKPPKLQEQKVEPPKLQQQKVEPpklqQQKVEPPKLQQQKVEP--PKLQQQKVKPPKVQQQKVKPPklqQQKV 365
Cdd:PRK10263   752 VQQPQQPVAPQQQYQQPQQPVAPQPQYQQP----QQPVAPQPQYQQPQQPvaPQPQYQQPQQPVAPQPQYQQP---QQPV 824

                           90
                   ....*....|....*....
gi 1370992868  366 EPPKVQQQKVEPPKVQQQK 384
Cdd:PRK10263   825 APQPQYQQPQQPVAPQPQD 843
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 291-387 9.99e-06

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 47.60  E-value: 9.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 291 TVEEVKPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEppklQQQKVEPPKLQQQKVKPPKVQQQKVKPPK-LQQQKVEPPK 369
Cdd:cd22536   332 TEEEPQTSAAESEAQSSSQLQSNGLQNVQDQSNSLQ----QVQIVGQPILQQIQIQQPQQQIIQAIQPQsFQLQSGQTIQ 407

                          90
                  ....*....|....*...
gi 1370992868 370 VQQQKVEpPKVQQQKLQN 387
Cdd:cd22536   408 TIQQQPL-QNVQLQAVQS 424
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 296-379 3.49e-05

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 45.82  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 296 KPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPklQQQKVEPPKLQQQK--VKPPKVQQQKVKPPKLQQQKVEPPKVQ-Q 372
Cdd:COG5180   175 PPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVK--DEAQEEPPDLTGGAdhPRPEAASSPKVDPPSTSEARSRPATVDaQ 252


                  ....*..
gi 1370992868 373 QKVEPPK 379
Cdd:COG5180   253 PEMRPPA 259
PRK12757 PRK12757
cell division protein FtsN; Provisional
 317-403 4.99e-05

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 44.65  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 317 PPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKVQQQKVKPPKLQQQKVEPPKVQQQKVEPPKVQQQKlqnEKGQKQV-- 394
Cdd:PRK12757  112 PQVPRSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEK---EKEQRWMvq 188


                  ....*....
gi 1370992868 395 CPKVKGNNQ 403
Cdd:PRK12757  189 CGSFKGTEQ 197
PHA03377 PHA03377
EBNA-3C; Provisional
 301-382 5.67e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 45.43  E-value: 5.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  301 QEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKV---QQQKVK--PPKLQQQKVEPPKVQQQKV 375
Cdd:PHA03377   546 RQKRATPPKVSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTgprQQAKCKdgPPASGPHEKQPPSSAPRDM 625


                   ....*..
gi 1370992868  376 EPPKVQQ 382
Cdd:PHA03377   626 APSVVRM 632
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 287-407 7.15e-05

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 43.10  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 287 NEKITVEEVkPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKVQQQKVKPPklqQQKVE 366
Cdd:pfam15240  20 SEDVSQEDS-PSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPP---QGGPR 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370992868 367 PPKVQQQKVEPPKVQQQ-------KLQNEKGQKQVCPKVKGNNQRKQT 407
Cdd:pfam15240  96 PPPGKPQGPPPQGGNQQqgppppgKPQGPPPQGGGPPPQGGNQQGPPP 143
PRK11633 PRK11633
cell division protein DedD; Provisional
 294-384 7.38e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 43.84  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 294 EVKPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVePPKLQQQKVKPPKVQQQKVKPPKLQQQKVEPPKVQQQ 373
Cdd:PRK11633   54 DMMPAATQALPTQPPEGAAEAVRAGDAAAPSLDPATVAPPNT-PVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAPK 132

                          90
                  ....*....|.
gi 1370992868 374 KVEPPKVQQQK 384
Cdd:PRK11633  133 PEPKPVVEEKA 143
PHA03377 PHA03377
EBNA-3C; Provisional
 297-372 1.17e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 44.66  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  297 PPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKL---QQQKVK--PPKVQQQKVKPPKLQQQKVEPPKVQ 371
Cdd:PHA03377   552 PPKVSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTgprQQAKCKdgPPASGPHEKQPPSSAPRDMAPSVVR 631


                   .
gi 1370992868  372 Q 372
Cdd:PHA03377   632 M 632
PHA03378 PHA03378
EBNA-3B; Provisional
 296-392 1.34e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 296 KPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKV-------QQQKVKPPKLQQQKVEPP 368
Cdd:PHA03378  715 QRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAapgaptpQPPPQAPPAPQQRPRGAP 794

                          90       100
                  ....*....|....*....|....
gi 1370992868 369 KVQQQKVEPPKVQQQKLQNEKGQK 392
Cdd:PHA03378  795 TPQPPPQAGPTSMQLMPRAAPGQQ 818
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 293-377 1.71e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.92  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  293 EEVKPPKLQEQKVEPPKLQQQKVEPpklqQQKVEPPKLQQQKVEPPKLQQQKVKPpkvQQQKVKPPKLQQ-QKVEPPKVQ 371
Cdd:PRK10263   770 QPVAPQPQYQQPQQPVAPQPQYQQP----QQPVAPQPQYQQPQQPVAPQPQYQQP---QQPVAPQPQYQQpQQPVAPQPQ 842


                   ....*.
gi 1370992868  372 QQKVEP 377
Cdd:PRK10263   843 DTLLHP 848
ECM1 pfam05782
Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic ...
 281-377 1.75e-04

Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic extracellular matrix protein 1 (ECM1) sequences. ECM1 has been shown to regulate endochondral bone formation, stimulate the proliferation of endothelial cells and induce angiogenesis. Mutations in the ECM1 gene can cause lipoid proteinosis, a disorder which causes generalized thickening of skin, mucosae and certain viscera. Classical features include beaded eyelid papules and laryngeal infiltration leading to hoarseness.


Pssm-ID: 461739  Cd Length: 518  Bit Score: 43.68  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 281 ETEHHENEKITVEEVKPPKLQEQkvepPKLQQQKVEPPKLQ-QQKVEPPKLQ-----QQKVEPPKLQ-QQKVKPPKVQQQ 353
Cdd:pfam05782  21 DTSQHDPPFEGQSEVQPPPSQEA----IPVQEEELPPPQLPvEKKVDPPLPQeaiplQEELPPPQLPiEQKEIDPPFPQQ 96

                          90       100
                  ....*....|....*....|....
gi 1370992868 354 KVKPPKLQQQKVEPPKVQQQKVEP 377
Cdd:pfam05782  97 EEITPSKQREEKPAPLVGQGHPEP 120
PHA03377 PHA03377
EBNA-3C; Provisional
 276-378 1.79e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 43.89  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868  276 ETIKKETEhhENEKITVEEVKPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKVQQQKV 355
Cdd:PHA03377   513 EVIDVETT--EEEESVTQPAKPHRKVQDGFQRSGRRQKRATPPKVSPSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDM 590

                           90       100
                   ....*....|....*....|....*...
gi 1370992868  356 KPP-----KLQQQKVEPPKVQQQKVEPP 378
Cdd:PHA03377   591 APPstgprQQAKCKDGPPASGPHEKQPP 618
PHA03378 PHA03378
EBNA-3B; Provisional
 296-383 2.92e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 296 KPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKVQQQKVKPPKLQQQKVEPPKV----- 370
Cdd:PHA03378  695 QPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAapgap 774

                          90
                  ....*....|....*
gi 1370992868 371 --QQQKVEPPKVQQQ 383
Cdd:PHA03378  775 tpQPPPQAPPAPQQR 789
ECM1 pfam05782
Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic ...
 297-396 8.70e-04

Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic extracellular matrix protein 1 (ECM1) sequences. ECM1 has been shown to regulate endochondral bone formation, stimulate the proliferation of endothelial cells and induce angiogenesis. Mutations in the ECM1 gene can cause lipoid proteinosis, a disorder which causes generalized thickening of skin, mucosae and certain viscera. Classical features include beaded eyelid papules and laryngeal infiltration leading to hoarseness.


Pssm-ID: 461739  Cd Length: 518  Bit Score: 41.36  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 297 PPKLQEQKVEPPKLQQQkvEPPKLQQQKVEPPKLQqqkvEPPKLQQQKVKPPKVQ-QQKVKPPKLQ-----QQKVEPPKV 370
Cdd:pfam05782   9 PPQTRGLPVDHPDTSQH--DPPFEGQSEVQPPPSQ----EAIPVQEEELPPPQLPvEKKVDPPLPQeaiplQEELPPPQL 82

                          90       100
                  ....*....|....*....|....*..
gi 1370992868 371 Q-QQKVEPPKVQQQKLQNEKGQKQVCP 396
Cdd:pfam05782  83 PiEQKEIDPPFPQQEEITPSKQREEKP 109
PRK12757 PRK12757
cell division protein FtsN; Provisional
 307-374 9.08e-04

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 40.80  E-value: 9.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370992868 307 PPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKVQQQKVKPPKLQQQKVEPPKVQQQK 374
Cdd:PRK12757  112 PQVPRSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEK 179
PRK11633 PRK11633
cell division protein DedD; Provisional
 296-377 9.12e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 40.37  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 296 KPPKLQEQKVEPPKLQQQKVEPPKLQQQKVePPKLQQQKVEPPKLQQQKVKPPKVQQQKVKPPKLQQqKVEPPKVQQQKV 375
Cdd:PRK11633   66 QPPEGAAEAVRAGDAAAPSLDPATVAPPNT-PVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAP-KPEPKPVVEEKA 143


                  ..
gi 1370992868 376 EP 377
Cdd:PRK11633  144 AP 145
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 317-393 1.82e-03

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (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. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 40.67  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370992868 317 PPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKVQQ-QKVKPPKLQQQKVEPPKVQQQKVEPPKVQQQKLQNEKGQKQ 393
Cdd:cd22536   333 EEEPQTSAAESEAQSSSQLQSNGLQNVQDQSNSLQQvQIVGQPILQQIQIQQPQQQIIQAIQPQSFQLQSGQTIQTIQ 410
PRK11633 PRK11633
cell division protein DedD; Provisional
 279-389 2.27e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 39.22  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 279 KKeteHHENEKITVEEV-KPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVkPPKVQQQKVKP 357
Cdd:PRK11633   31 KK---HYQDEFAAIPLVpKPGDRDEPDMMPAATQALPTQPPEGAAEAVRAGDAAAPSLDPATVAPPNT-PVEPEPAPVEP 106

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1370992868 358 PKLQQQKVEPPKVQ-QQKVEP---PKVQQQKLQNEK 389
Cdd:PRK11633  107 PKPKPVEKPKPKPKpQQKVEAppaPKPEPKPVVEEK 142
PRK12757 PRK12757
cell division protein FtsN; Provisional
 294-364 3.87e-03

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 38.87  E-value: 3.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370992868 294 EVKPPKLQEQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKVQQQKVKPPKLQQQK 364
Cdd:PRK12757  109 EQTPQVPRSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAPVRTQPAAPVTQAVEAPKVEAEK 179
Activator_LAG-3 pfam11498
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ...
 303-391 6.11e-03

Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.


Pssm-ID: 151935 [Multi-domain]  Cd Length: 476  Bit Score: 38.79  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 303 QKVEPPKLQQQKVEppKLQQQKVEPPKLQQQKVEPPKLQQQKVKPPKVQQQKVKPPKLQQQKVEPPKVQQQKveppKVQQ 382
Cdd:pfam11498 310 QSAPPPAMNPQHIA--QLAQQQNKMRLLQQQEMEMQRIEQQRQQQIMHQHQQQQQQEHQQQQMLLQQQQQMH----QLQQ 383


                  ....*....
gi 1370992868 383 QKLQNEKGQ 391
Cdd:pfam11498 384 HHQMNGGGQ 392
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 270-387 7.19e-03

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: 38.86  E-value: 7.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370992868 270 LGEVE---SETIKKETEHHENEKITVEEVKPPKLQEQKVEPPKLQQQkvePPKLQQQKVEPPKLQQQKVEPPKLQQQKVK 346
Cdd:pfam09770 196 LEEVEaamRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQ---QQQPQQQPQQPQQHPGQGHPVTILQRPQSP 272

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370992868 347 PPKVQQQKVkPPKLQQQKVEPPKVQQQKVeppkvqqQKLQN 387
Cdd:pfam09770 273 QPDPAQPSI-QPQAQQFHQQPPPVPVQPT-------QILQN 305
 
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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