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Conserved domains on  [gi|1034595424|ref|XP_016878990|]
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myocardin-related transcription factor B isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 400-433 2.89e-10

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


:

Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 56.25  E-value: 2.89e-10
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034595424  400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLKPY 433
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEY 34
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
139-164 1.28e-05

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;


:

Pssm-ID: 128947  Cd Length: 26  Bit Score: 42.85  E-value: 1.28e-05
                            10        20
                    ....*....|....*....|....*.
gi 1034595424   139 DDLNEKIAQRPGPMELVEKNILPVDS 164
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILKELS 26
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 197-410 1.48e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  197 PDQPASQESQGSAASPSEPKVSESPSPVTTNTPAQFASVSPTVPEflkTPPTADQP--PPRPAAPVLPTNTV-SSAKPGP 273
Cdd:PHA03247  2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL---PPPTSAQPtaPPPPPGPPPPSLPLgGSVAPGG 2860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  274 ALVK----QSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPDQKGEKNEPQmdsnyarLLQQQQLFLQLQILSQQKQHY 349
Cdd:PHA03247  2861 DVRRrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-------APPPPQPQPQPPPPPQPQPPP 2933

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034595424  350 NYQTILPAPFKPLNDKNSNSG---------NSALNNATPNTPRQNTSTP---VRKPGPLPSSLDDLKVSELKT 410
Cdd:PHA03247  2934 PPPPRPQPPLAPTTDPAGAGEpsgavpqpwLGALVPGRVAVPRFRVPQPapsREAPASSTPPLTGHSLSRVSS 3006
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 96-119 1.72e-04

RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin.


:

Pssm-ID: 460677  Cd Length: 24  Bit Score: 39.56  E-value: 1.72e-04
                           10        20
                   ....*....|....*....|....
gi 1034595424   96 FLKHKIRSRPDRSELVRMHILEET 119
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
DUF2130 super family cl38307
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ...
 568-603 2.45e-04

Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various hypothetical prokaryotic proteins, has no known function.


The actual alignment was detected with superfamily member pfam09903:

Pssm-ID: 430914 [Multi-domain]  Cd Length: 248  Bit Score: 44.15  E-value: 2.45e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034595424  568 AEKDRKLQEKEKQIEELKR-KLEQEQKLV-EVLKMQLE 603
Cdd:pfam09903    3 KEKEKQIKDLQEQIEELKRfKAEQSTKLQgEVLEQHCE 40
SP1-4_N super family cl41773
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 649-826 1.44e-03

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; 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. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong 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 SP1-4.


The actual alignment was detected with superfamily member cd22540:

Pssm-ID: 425404 [Multi-domain]  Cd Length: 511  Bit Score: 42.61  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  649 SSRQPIPVASHAVGQPVSTGGQTLVAKKAVVIKQEVPVGQAEQQSVVSQFYVSSQ------------GQPPPAVVAQPQA 716
Cdd:cd22540    176 APLQTSNTNSASLQVPGNVIKLQSGGNVALTLPVNNLVGTQDGATQLQLAAAPSKpskkirkksaqaAQPAVTVAEQVET 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  717 LLTTQTAqlllPVSIQ-GSSVTSVQLPVGSLKLQTSPQAGMQTQpQIATAAQIPTAAL-----ASGLAPTVPQTQDTFPQ 790
Cdd:cd22540    256 VLIETTA----DNIIQaGNNLLIVQSPGTGQPAVLQQVQVLQPK-QEQQVVQIPQQALrvvqaASATLPTVPQKPLQNIQ 330

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034595424  791 HVLSQPQQVRKVF-TNSASSNTVLpYQRHPAPAVQQP 826
Cdd:cd22540    331 IQNSEPTPTQVYIkTPSGEVQTVL-LQEAPAATATPS 366
RPEL super family cl29414
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 52-76 1.69e-03

RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin.


The actual alignment was detected with superfamily member smart00707:

Pssm-ID: 475195  Cd Length: 26  Bit Score: 36.69  E-value: 1.69e-03
                            10        20
                    ....*....|....*....|....*
gi 1034595424    52 VLQLRLQQRRTREQLVDQGIMPPLK 76
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKELS 26
 
Name Accession Description Interval E-value
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 400-433 2.89e-10

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 56.25  E-value: 2.89e-10
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034595424  400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLKPY 433
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEY 34
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
400-431 7.64e-09

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 52.10  E-value: 7.64e-09
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1034595424   400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLK 431
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLL 32
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
139-164 1.28e-05

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;


Pssm-ID: 128947  Cd Length: 26  Bit Score: 42.85  E-value: 1.28e-05
                            10        20
                    ....*....|....*....|....*.
gi 1034595424   139 DDLNEKIAQRPGPMELVEKNILPVDS 164
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILKELS 26
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 140-163 3.27e-05

RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin.


Pssm-ID: 460677  Cd Length: 24  Bit Score: 41.49  E-value: 3.27e-05
                           10        20
                   ....*....|....*....|....
gi 1034595424  140 DLNEKIAQRPGPMELVEKNILPVD 163
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
PHA03247 PHA03247
large tegument protein UL36; Provisional
 197-410 1.48e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  197 PDQPASQESQGSAASPSEPKVSESPSPVTTNTPAQFASVSPTVPEflkTPPTADQP--PPRPAAPVLPTNTV-SSAKPGP 273
Cdd:PHA03247  2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL---PPPTSAQPtaPPPPPGPPPPSLPLgGSVAPGG 2860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  274 ALVK----QSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPDQKGEKNEPQmdsnyarLLQQQQLFLQLQILSQQKQHY 349
Cdd:PHA03247  2861 DVRRrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-------APPPPQPQPQPPPPPQPQPPP 2933

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034595424  350 NYQTILPAPFKPLNDKNSNSG---------NSALNNATPNTPRQNTSTP---VRKPGPLPSSLDDLKVSELKT 410
Cdd:PHA03247  2934 PPPPRPQPPLAPTTDPAGAGEpsgavpqpwLGALVPGRVAVPRFRVPQPapsREAPASSTPPLTGHSLSRVSS 3006
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 96-119 1.72e-04

RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin.


Pssm-ID: 460677  Cd Length: 24  Bit Score: 39.56  E-value: 1.72e-04
                           10        20
                   ....*....|....*....|....
gi 1034595424   96 FLKHKIRSRPDRSELVRMHILEET 119
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
DUF2130 pfam09903
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ...
 568-603 2.45e-04

Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various hypothetical prokaryotic proteins, has no known function.


Pssm-ID: 430914 [Multi-domain]  Cd Length: 248  Bit Score: 44.15  E-value: 2.45e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034595424  568 AEKDRKLQEKEKQIEELKR-KLEQEQKLV-EVLKMQLE 603
Cdd:pfam09903    3 KEKEKQIKDLQEQIEELKRfKAEQSTKLQgEVLEQHCE 40
COG4487 COG4487
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
564-603 3.10e-04

Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 443580 [Multi-domain]  Cd Length: 425  Bit Score: 44.55  E-value: 3.10e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034595424  564 ELDAAEKDRKLQEKEKQIEELKRKLEQ-EQKLV-EVLKMQLE 603
Cdd:COG4487    167 SLKVAEYEKQLKDMQEQIEELKRKKEQgSTQLQgEVLELEFE 208
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 649-826 1.44e-03

N-terminal domain of transcription factor Specificity Protein (SP) 2; 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. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 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 SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 42.61  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  649 SSRQPIPVASHAVGQPVSTGGQTLVAKKAVVIKQEVPVGQAEQQSVVSQFYVSSQ------------GQPPPAVVAQPQA 716
Cdd:cd22540    176 APLQTSNTNSASLQVPGNVIKLQSGGNVALTLPVNNLVGTQDGATQLQLAAAPSKpskkirkksaqaAQPAVTVAEQVET 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  717 LLTTQTAqlllPVSIQ-GSSVTSVQLPVGSLKLQTSPQAGMQTQpQIATAAQIPTAAL-----ASGLAPTVPQTQDTFPQ 790
Cdd:cd22540    256 VLIETTA----DNIIQaGNNLLIVQSPGTGQPAVLQQVQVLQPK-QEQQVVQIPQQALrvvqaASATLPTVPQKPLQNIQ 330

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034595424  791 HVLSQPQQVRKVF-TNSASSNTVLpYQRHPAPAVQQP 826
Cdd:cd22540    331 IQNSEPTPTQVYIkTPSGEVQTVL-LQEAPAATATPS 366
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
52-76 1.69e-03

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;


Pssm-ID: 128947  Cd Length: 26  Bit Score: 36.69  E-value: 1.69e-03
                            10        20
                    ....*....|....*....|....*
gi 1034595424    52 VLQLRLQQRRTREQLVDQGIMPPLK 76
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKELS 26
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 571-617 2.36e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.41  E-value: 2.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034595424  571 DRKLQEKEKQIEELKRK---LEQEQKLVEVLKMQLEvEKRGQQQRPLEAQ 617
Cdd:cd16269    190 DQALTEKEKEIEAERAKaeaAEQERKLLEEQQRELE-QKLEDQERSYEEH 238
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
96-119 3.04e-03

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;


Pssm-ID: 128947  Cd Length: 26  Bit Score: 35.92  E-value: 3.04e-03
                            10        20
                    ....*....|....*....|....
gi 1034595424    96 FLKHKIRSRPDRSELVRMHILEET 119
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKEL 25
 
Name Accession Description Interval E-value
SAP pfam02037
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ...
 400-433 2.89e-10

SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.


Pssm-ID: 460424 [Multi-domain]  Cd Length: 35  Bit Score: 56.25  E-value: 2.89e-10
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1034595424  400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLKPY 433
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEY 34
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
400-431 7.64e-09

Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;


Pssm-ID: 128789 [Multi-domain]  Cd Length: 35  Bit Score: 52.10  E-value: 7.64e-09
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1034595424   400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLK 431
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLL 32
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
139-164 1.28e-05

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;


Pssm-ID: 128947  Cd Length: 26  Bit Score: 42.85  E-value: 1.28e-05
                            10        20
                    ....*....|....*....|....*.
gi 1034595424   139 DDLNEKIAQRPGPMELVEKNILPVDS 164
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILKELS 26
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 140-163 3.27e-05

RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin.


Pssm-ID: 460677  Cd Length: 24  Bit Score: 41.49  E-value: 3.27e-05
                           10        20
                   ....*....|....*....|....
gi 1034595424  140 DLNEKIAQRPGPMELVEKNILPVD 163
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
PHA03247 PHA03247
large tegument protein UL36; Provisional
 197-410 1.48e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  197 PDQPASQESQGSAASPSEPKVSESPSPVTTNTPAQFASVSPTVPEflkTPPTADQP--PPRPAAPVLPTNTV-SSAKPGP 273
Cdd:PHA03247  2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL---PPPTSAQPtaPPPPPGPPPPSLPLgGSVAPGG 2860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  274 ALVK----QSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPDQKGEKNEPQmdsnyarLLQQQQLFLQLQILSQQKQHY 349
Cdd:PHA03247  2861 DVRRrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-------APPPPQPQPQPPPPPQPQPPP 2933

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034595424  350 NYQTILPAPFKPLNDKNSNSG---------NSALNNATPNTPRQNTSTP---VRKPGPLPSSLDDLKVSELKT 410
Cdd:PHA03247  2934 PPPPRPQPPLAPTTDPAGAGEpsgavpqpwLGALVPGRVAVPRFRVPQPapsREAPASSTPPLTGHSLSRVSS 3006
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 96-119 1.72e-04

RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin.


Pssm-ID: 460677  Cd Length: 24  Bit Score: 39.56  E-value: 1.72e-04
                           10        20
                   ....*....|....*....|....
gi 1034595424   96 FLKHKIRSRPDRSELVRMHILEET 119
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
DUF2130 pfam09903
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ...
 568-603 2.45e-04

Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various hypothetical prokaryotic proteins, has no known function.


Pssm-ID: 430914 [Multi-domain]  Cd Length: 248  Bit Score: 44.15  E-value: 2.45e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034595424  568 AEKDRKLQEKEKQIEELKR-KLEQEQKLV-EVLKMQLE 603
Cdd:pfam09903    3 KEKEKQIKDLQEQIEELKRfKAEQSTKLQgEVLEQHCE 40
COG4487 COG4487
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
564-603 3.10e-04

Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];


Pssm-ID: 443580 [Multi-domain]  Cd Length: 425  Bit Score: 44.55  E-value: 3.10e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034595424  564 ELDAAEKDRKLQEKEKQIEELKRKLEQ-EQKLV-EVLKMQLE 603
Cdd:COG4487    167 SLKVAEYEKQLKDMQEQIEELKRKKEQgSTQLQgEVLELEFE 208
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 649-826 1.44e-03

N-terminal domain of transcription factor Specificity Protein (SP) 2; 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. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 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 SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 42.61  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  649 SSRQPIPVASHAVGQPVSTGGQTLVAKKAVVIKQEVPVGQAEQQSVVSQFYVSSQ------------GQPPPAVVAQPQA 716
Cdd:cd22540    176 APLQTSNTNSASLQVPGNVIKLQSGGNVALTLPVNNLVGTQDGATQLQLAAAPSKpskkirkksaqaAQPAVTVAEQVET 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  717 LLTTQTAqlllPVSIQ-GSSVTSVQLPVGSLKLQTSPQAGMQTQpQIATAAQIPTAAL-----ASGLAPTVPQTQDTFPQ 790
Cdd:cd22540    256 VLIETTA----DNIIQaGNNLLIVQSPGTGQPAVLQQVQVLQPK-QEQQVVQIPQQALrvvqaASATLPTVPQKPLQNIQ 330

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034595424  791 HVLSQPQQVRKVF-TNSASSNTVLpYQRHPAPAVQQP 826
Cdd:cd22540    331 IQNSEPTPTQVYIkTPSGEVQTVL-LQEAPAATATPS 366
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
52-76 1.69e-03

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;


Pssm-ID: 128947  Cd Length: 26  Bit Score: 36.69  E-value: 1.69e-03
                            10        20
                    ....*....|....*....|....*
gi 1034595424    52 VLQLRLQQRRTREQLVDQGIMPPLK 76
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKELS 26
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
185-323 2.04e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.07  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  185 FSFDEDSSDALSPDQPASQESQGSAASPSEP-KVSESPSPVTTNTPAQfASVSPTVPEFLKTPPTADQPPPRPaAPVLPT 263
Cdd:PRK14971   363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSaAAAASPSPSQSSAAAQ-PSAPQSATQPAGTPPTVSVDPPAA-VPVNPP 440

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034595424  264 NTVSSAKPGPalVKQSHPKNPNDKHRS-----KKCKDPKPRVKKLKYHQYIPPDQKGEKNEPQMD 323
Cdd:PRK14971   441 STAPQAVRPA--QFKEEKKIPVSKVSSlgpstLRPIQEKAEQATGNIKEAPTGTQKEIFTEEDLQ 503
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 571-617 2.36e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.41  E-value: 2.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034595424  571 DRKLQEKEKQIEELKRK---LEQEQKLVEVLKMQLEvEKRGQQQRPLEAQ 617
Cdd:cd16269    190 DQALTEKEKEIEAERAKaeaAEQERKLLEEQQRELE-QKLEDQERSYEEH 238
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
96-119 3.04e-03

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;


Pssm-ID: 128947  Cd Length: 26  Bit Score: 35.92  E-value: 3.04e-03
                            10        20
                    ....*....|....*....|....
gi 1034595424    96 FLKHKIRSRPDRSELVRMHILEET 119
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKEL 25
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 193-295 7.92e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 7.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034595424  193 DALSPDQPASQESQGSAASPSEPKVSESPS-PVTTNTPAqfasvSPTVPEFLKTPPTAdQPPPRPAAPVLPTNTVSSAKP 271
Cdd:PTZ00449   584 DPKHPKDPEEPKKPKRPRSAQRPTRPKSPKlPELLDIPK-----SPKRPESPKSPKRP-PPPQRPSSPERPEGPKIIKSP 657

                           90       100
                   ....*....|....*....|....
gi 1034595424  272 GPAlvkqSHPKNPNDKHRSKKCKD 295
Cdd:PTZ00449   658 KPP----KSPKPPFDPKFKEKFYD 677
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 565-617 8.08e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.59  E-value: 8.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034595424  565 LDAAEKDRKLQEKEKQIEELKRKLEQEQKLVEVLKMQLEVEKRGQQ--QRPLEAQ 617
Cdd:pfam20492   30 EESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAeeKEQLEAE 84
 
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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