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Conserved domains on  [gi|568995287|ref|XP_006522171|]
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myocardin-related transcription factor B isoform X1 [Mus musculus]

Protein Classification

RPEL and SAP domain-containing protein( domain architecture ID 13233135)

protein containing domains RPEL, SAP, and GBP_C

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 ...
 415-448 2.92e-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: 2.92e-10
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568995287   415 LDDLKVSELKTELKLRGLPVSGTKPDLIERLKPY 448
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEY 34
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
160-185 1.47e-05

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


:

Pssm-ID: 128947  Cd Length: 26  Bit Score: 42.46  E-value: 1.47e-05
                            10        20
                    ....*....|....*....|....*.
gi 568995287    160 DDLNEKIAQRPGPMELVEKNILPVDS 185
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILKELS 26
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 117-140 1.80e-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: 1.80e-04
                           10        20
                   ....*....|....*....|....
gi 568995287   117 FLKHKIRSRPDRSELVRMHILEET 140
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
DUF2130 super family cl38307
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ...
 583-618 2.48e-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: 2.48e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568995287   583 AEKDRKLQEKEKQIEELKR-KLEQEQKLV-EVLKMQLE 618
Cdd:pfam09903    3 KEKEKQIKDLQEQIEELKRfKAEQSTKLQgEVLEQHCE 40
RPEL super family cl29414
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 73-97 1.90e-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: 1.90e-03
                            10        20
                    ....*....|....*....|....*
gi 568995287     73 VLQLRLQQRRTREQLVDQGIMPPLK 97
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKELS 26
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 218-342 6.22e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995287  218 PDQPASQESQGSAASPSEPKVSASPPPVTASTPAQFTSVSPAVPefLKTPLTADQ-PPTRSTAPVLPTNTV--SSAKSGP 294
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP--LPPPTSAQPtAPPPPPGPPPPSLPLggSVAPGGD 2861

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568995287  295 MLVK---QSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPNQKGEKSEPQ 342
Cdd:PHA03247 2862 VRRRppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912
 
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 ...
 415-448 2.92e-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: 2.92e-10
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568995287   415 LDDLKVSELKTELKLRGLPVSGTKPDLIERLKPY 448
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEY 34
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
415-446 7.73e-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: 7.73e-09
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568995287    415 LDDLKVSELKTELKLRGLPVSGTKPDLIERLK 446
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLL 32
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
160-185 1.47e-05

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 42.46  E-value: 1.47e-05
                            10        20
                    ....*....|....*....|....*.
gi 568995287    160 DDLNEKIAQRPGPMELVEKNILPVDS 185
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILKELS 26
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 161-184 3.38e-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: 3.38e-05
                           10        20
                   ....*....|....*....|....
gi 568995287   161 DLNEKIAQRPGPMELVEKNILPVD 184
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 117-140 1.80e-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: 1.80e-04
                           10        20
                   ....*....|....*....|....
gi 568995287   117 FLKHKIRSRPDRSELVRMHILEET 140
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
DUF2130 pfam09903
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ...
 583-618 2.48e-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: 2.48e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568995287   583 AEKDRKLQEKEKQIEELKR-KLEQEQKLV-EVLKMQLE 618
Cdd:pfam09903    3 KEKEKQIKDLQEQIEELKRfKAEQSTKLQgEVLEQHCE 40
COG4487 COG4487
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
579-618 3.58e-04

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


Pssm-ID: 443580 [Multi-domain]  Cd Length: 425  Bit Score: 44.17  E-value: 3.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568995287  579 ELDAAEKDRKLQEKEKQIEELKRKLEQ-EQKLV-EVLKMQLE 618
Cdd:COG4487   167 SLKVAEYEKQLKDMQEQIEELKRKKEQgSTQLQgEVLELEFE 208
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 586-626 1.85e-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: 41.79  E-value: 1.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568995287  586 DRKLQEKEKQIEELKRK---LEQEQKLVEVLKMQLEVEKRGQQR 626
Cdd:cd16269   190 DQALTEKEKEIEAERAKaeaAEQERKLLEEQQRELEQKLEDQER 233
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
73-97 1.90e-03

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 36.69  E-value: 1.90e-03
                            10        20
                    ....*....|....*....|....*
gi 568995287     73 VLQLRLQQRRTREQLVDQGIMPPLK 97
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKELS 26
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
117-140 3.40e-03

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 35.92  E-value: 3.40e-03
                            10        20
                    ....*....|....*....|....
gi 568995287    117 FLKHKIRSRPDRSELVRMHILEET 140
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKEL 25
PHA03247 PHA03247
large tegument protein UL36; Provisional
 218-342 6.22e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995287  218 PDQPASQESQGSAASPSEPKVSASPPPVTASTPAQFTSVSPAVPefLKTPLTADQ-PPTRSTAPVLPTNTV--SSAKSGP 294
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP--LPPPTSAQPtAPPPPPGPPPPSLPLggSVAPGGD 2861

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568995287  295 MLVK---QSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPNQKGEKSEPQ 342
Cdd:PHA03247 2862 VRRRppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912
 
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 ...
 415-448 2.92e-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: 2.92e-10
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568995287   415 LDDLKVSELKTELKLRGLPVSGTKPDLIERLKPY 448
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEY 34
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
415-446 7.73e-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: 7.73e-09
                            10        20        30
                    ....*....|....*....|....*....|..
gi 568995287    415 LDDLKVSELKTELKLRGLPVSGTKPDLIERLK 446
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLL 32
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
160-185 1.47e-05

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 42.46  E-value: 1.47e-05
                            10        20
                    ....*....|....*....|....*.
gi 568995287    160 DDLNEKIAQRPGPMELVEKNILPVDS 185
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILKELS 26
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 161-184 3.38e-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: 3.38e-05
                           10        20
                   ....*....|....*....|....
gi 568995287   161 DLNEKIAQRPGPMELVEKNILPVD 184
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
RPEL pfam02755
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ...
 117-140 1.80e-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: 1.80e-04
                           10        20
                   ....*....|....*....|....
gi 568995287   117 FLKHKIRSRPDRSELVRMHILEET 140
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
DUF2130 pfam09903
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ...
 583-618 2.48e-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: 2.48e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568995287   583 AEKDRKLQEKEKQIEELKR-KLEQEQKLV-EVLKMQLE 618
Cdd:pfam09903    3 KEKEKQIKDLQEQIEELKRfKAEQSTKLQgEVLEQHCE 40
COG4487 COG4487
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
579-618 3.58e-04

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


Pssm-ID: 443580 [Multi-domain]  Cd Length: 425  Bit Score: 44.17  E-value: 3.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568995287  579 ELDAAEKDRKLQEKEKQIEELKRKLEQ-EQKLV-EVLKMQLE 618
Cdd:COG4487   167 SLKVAEYEKQLKDMQEQIEELKRKKEQgSTQLQgEVLELEFE 208
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 586-626 1.85e-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: 41.79  E-value: 1.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568995287  586 DRKLQEKEKQIEELKRK---LEQEQKLVEVLKMQLEVEKRGQQR 626
Cdd:cd16269   190 DQALTEKEKEIEAERAKaeaAEQERKLLEEQQRELEQKLEDQER 233
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
73-97 1.90e-03

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 36.69  E-value: 1.90e-03
                            10        20
                    ....*....|....*....|....*
gi 568995287     73 VLQLRLQQRRTREQLVDQGIMPPLK 97
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKELS 26
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
117-140 3.40e-03

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 35.92  E-value: 3.40e-03
                            10        20
                    ....*....|....*....|....
gi 568995287    117 FLKHKIRSRPDRSELVRMHILEET 140
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKEL 25
PHA03247 PHA03247
large tegument protein UL36; Provisional
 218-342 6.22e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568995287  218 PDQPASQESQGSAASPSEPKVSASPPPVTASTPAQFTSVSPAVPefLKTPLTADQ-PPTRSTAPVLPTNTV--SSAKSGP 294
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP--LPPPTSAQPtAPPPPPGPPPPSLPLggSVAPGGD 2861

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568995287  295 MLVK---QSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPNQKGEKSEPQ 342
Cdd:PHA03247 2862 VRRRppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912
 
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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