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Conserved domains on  [gi|38569480|ref|NP_054767|]
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myocardin-related transcription factor B isoform 2 [Homo sapiens]

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 ...
 400-433 2.76e-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: 2.76e-10
                           10        20        30
                   ....*....|....*....|....*....|....
gi 38569480    400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLKPY 433
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEY 34
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
139-164 1.32e-05

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


:

Pssm-ID: 128947  Cd Length: 26  Bit Score: 42.85  E-value: 1.32e-05
                            10        20
                    ....*....|....*....|....*.
gi 38569480     139 DDLNEKIAQRPGPMELVEKNILPVDS 164
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILKELS 26
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 197-410 1.19e-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: 46.47  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   197 PDQPASQESQGSAASPSEPKVSESPSPVTTNTPAQFASVSPTVPEflkTPPTADQP--PPRPAAPVLPTNTV-SSAKPGP 273
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL---PPPTSAQPtaPPPPPGPPPPSLPLgGSVAPGG 2860

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   274 ALVK----QSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPDQKGEKNEPQmdsnyarLLQQQQLFLQLQILSQQKQHY 349
Cdd:PHA03247 2861 DVRRrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-------APPPPQPQPQPPPPPQPQPPP 2933

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38569480   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 1.81e-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: 1.81e-04
                           10        20
                   ....*....|....*....|....
gi 38569480     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 2.32e-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: 2.32e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 38569480    568 AEKDRKLQEKEKQIEELKR-KLEQEQKLV-EVLKMQLE 603
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 ...
 52-76 1.73e-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: 1.73e-03
                            10        20
                    ....*....|....*....|....*
gi 38569480      52 VLQLRLQQRRTREQLVDQGIMPPLK 76
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKELS 26
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 609-796 6.82e-03

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 6.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   609 QQQRPLEAQPSAPGHSVKSDQKHGSLGSSIKDEASLPDCSSSRQPIPVAShavgQPVSTGGQTLVAKKAVVIKQEVPvgQ 688
Cdd:PRK10263  707 QQQRYSGEQPAGANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQ----QPVAPQQQYQQPQQPVAPQPQYQ--Q 780

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   689 AEQQSVVSQFYTSPQAGMQTQPQIATAAQiptaalasglaPTVPQTQDTFPQHVLSQPQQvrkvftnsassntvlpYQRH 768
Cdd:PRK10263  781 PQQPVAPQPQYQQPQQPVAPQPQYQQPQQ-----------PVAPQPQYQQPQQPVAPQPQ----------------YQQP 833

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 38569480   769 PAPAVQQP--------FINKASNSVLQSRNAPLPSL 796
Cdd:PRK10263  834 QQPVAPQPqdtllhplLMRNGDSRPLHKPTTPLPSL 869
 
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 2.76e-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: 2.76e-10
                           10        20        30
                   ....*....|....*....|....*....|....
gi 38569480    400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLKPY 433
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEY 34
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
400-431 7.29e-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: 7.29e-09
                            10        20        30
                    ....*....|....*....|....*....|..
gi 38569480     400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLK 431
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLL 32
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
139-164 1.32e-05

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 42.85  E-value: 1.32e-05
                            10        20
                    ....*....|....*....|....*.
gi 38569480     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 3.45e-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: 3.45e-05
                           10        20
                   ....*....|....*....|....
gi 38569480    140 DLNEKIAQRPGPMELVEKNILPVD 163
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
PHA03247 PHA03247
large tegument protein UL36; Provisional
 197-410 1.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   197 PDQPASQESQGSAASPSEPKVSESPSPVTTNTPAQFASVSPTVPEflkTPPTADQP--PPRPAAPVLPTNTV-SSAKPGP 273
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL---PPPTSAQPtaPPPPPGPPPPSLPLgGSVAPGG 2860

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   274 ALVK----QSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPDQKGEKNEPQmdsnyarLLQQQQLFLQLQILSQQKQHY 349
Cdd:PHA03247 2861 DVRRrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-------APPPPQPQPQPPPPPQPQPPP 2933

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38569480   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 1.81e-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: 1.81e-04
                           10        20
                   ....*....|....*....|....
gi 38569480     96 FLKHKIRSRPDRSELVRMHILEET 119
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
DUF2130 pfam09903
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ...
 568-603 2.32e-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: 2.32e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 38569480    568 AEKDRKLQEKEKQIEELKR-KLEQEQKLV-EVLKMQLE 603
Cdd:pfam09903    3 KEKEKQIKDLQEQIEELKRfKAEQSTKLQgEVLEQHCE 40
COG4487 COG4487
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
564-603 3.31e-04

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


Pssm-ID: 443580 [Multi-domain]  Cd Length: 425  Bit Score: 44.17  E-value: 3.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 38569480  564 ELDAAEKDRKLQEKEKQIEELKRKLEQ-EQKLV-EVLKMQLE 603
Cdd:COG4487  167 SLKVAEYEKQLKDMQEQIEELKRKKEQgSTQLQgEVLELEFE 208
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
52-76 1.73e-03

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 36.69  E-value: 1.73e-03
                            10        20
                    ....*....|....*....|....*
gi 38569480      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 2.24e-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: 2.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 38569480  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 3.05e-03

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 35.92  E-value: 3.05e-03
                            10        20
                    ....*....|....*....|....
gi 38569480      96 FLKHKIRSRPDRSELVRMHILEET 119
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKEL 25
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 609-796 6.82e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 6.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   609 QQQRPLEAQPSAPGHSVKSDQKHGSLGSSIKDEASLPDCSSSRQPIPVAShavgQPVSTGGQTLVAKKAVVIKQEVPvgQ 688
Cdd:PRK10263  707 QQQRYSGEQPAGANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQ----QPVAPQQQYQQPQQPVAPQPQYQ--Q 780

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   689 AEQQSVVSQFYTSPQAGMQTQPQIATAAQiptaalasglaPTVPQTQDTFPQHVLSQPQQvrkvftnsassntvlpYQRH 768
Cdd:PRK10263  781 PQQPVAPQPQYQQPQQPVAPQPQYQQPQQ-----------PVAPQPQYQQPQQPVAPQPQ----------------YQQP 833

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 38569480   769 PAPAVQQP--------FINKASNSVLQSRNAPLPSL 796
Cdd:PRK10263  834 QQPVAPQPqdtllhplLMRNGDSRPLHKPTTPLPSL 869
 
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 2.76e-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: 2.76e-10
                           10        20        30
                   ....*....|....*....|....*....|....
gi 38569480    400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLKPY 433
Cdd:pfam02037    1 LSKLTVAELKEELRKRGLPTSGKKAELIERLQEY 34
SAP smart00513
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation;
400-431 7.29e-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: 7.29e-09
                            10        20        30
                    ....*....|....*....|....*....|..
gi 38569480     400 LDDLKVSELKTELKLRGLPVSGTKPDLIERLK 431
Cdd:smart00513    1 LAKLKVSELKDELKKRGLSTSGTKAELVDRLL 32
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
139-164 1.32e-05

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 42.85  E-value: 1.32e-05
                            10        20
                    ....*....|....*....|....*.
gi 38569480     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 3.45e-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: 3.45e-05
                           10        20
                   ....*....|....*....|....
gi 38569480    140 DLNEKIAQRPGPMELVEKNILPVD 163
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
PHA03247 PHA03247
large tegument protein UL36; Provisional
 197-410 1.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   197 PDQPASQESQGSAASPSEPKVSESPSPVTTNTPAQFASVSPTVPEflkTPPTADQP--PPRPAAPVLPTNTV-SSAKPGP 273
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL---PPPTSAQPtaPPPPPGPPPPSLPLgGSVAPGG 2860

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   274 ALVK----QSHPKNPNDKHRSKKCKDPKPRVKKLKYHQYIPPDQKGEKNEPQmdsnyarLLQQQQLFLQLQILSQQKQHY 349
Cdd:PHA03247 2861 DVRRrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-------APPPPQPQPQPPPPPQPQPPP 2933

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38569480   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 1.81e-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: 1.81e-04
                           10        20
                   ....*....|....*....|....
gi 38569480     96 FLKHKIRSRPDRSELVRMHILEET 119
Cdd:pfam02755    1 SLERKLSHRPTREELVERNILPED 24
DUF2130 pfam09903
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ...
 568-603 2.32e-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: 2.32e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 38569480    568 AEKDRKLQEKEKQIEELKR-KLEQEQKLV-EVLKMQLE 603
Cdd:pfam09903    3 KEKEKQIKDLQEQIEELKRfKAEQSTKLQgEVLEQHCE 40
COG4487 COG4487
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
564-603 3.31e-04

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


Pssm-ID: 443580 [Multi-domain]  Cd Length: 425  Bit Score: 44.17  E-value: 3.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 38569480  564 ELDAAEKDRKLQEKEKQIEELKRKLEQ-EQKLV-EVLKMQLE 603
Cdd:COG4487  167 SLKVAEYEKQLKDMQEQIEELKRKKEQgSTQLQgEVLELEFE 208
RPEL smart00707
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;
52-76 1.73e-03

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 36.69  E-value: 1.73e-03
                            10        20
                    ....*....|....*....|....*
gi 38569480      52 VLQLRLQQRRTREQLVDQGIMPPLK 76
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKELS 26
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
185-323 1.77e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.07  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   185 FSFDEDSSDALSPDQPASQESQGSAASPSEP-KVSESPSPVTTNTPAQfASVSPTVPEFLKTPPTADQPPPRPaAPVLPT 263
Cdd:PRK14971  363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSaAAAASPSPSQSSAAAQ-PSAPQSATQPAGTPPTVSVDPPAA-VPVNPP 440

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38569480   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 2.24e-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: 2.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 38569480  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 3.05e-03

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


Pssm-ID: 128947  Cd Length: 26  Bit Score: 35.92  E-value: 3.05e-03
                            10        20
                    ....*....|....*....|....
gi 38569480      96 FLKHKIRSRPDRSELVRMHILEET 119
Cdd:smart00707    2 VLNRKLSQRPTREELEERNILKEL 25
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 609-796 6.82e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 6.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   609 QQQRPLEAQPSAPGHSVKSDQKHGSLGSSIKDEASLPDCSSSRQPIPVAShavgQPVSTGGQTLVAKKAVVIKQEVPvgQ 688
Cdd:PRK10263  707 QQQRYSGEQPAGANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQ----QPVAPQQQYQQPQQPVAPQPQYQ--Q 780

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   689 AEQQSVVSQFYTSPQAGMQTQPQIATAAQiptaalasglaPTVPQTQDTFPQHVLSQPQQvrkvftnsassntvlpYQRH 768
Cdd:PRK10263  781 PQQPVAPQPQYQQPQQPVAPQPQYQQPQQ-----------PVAPQPQYQQPQQPVAPQPQ----------------YQQP 833

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 38569480   769 PAPAVQQP--------FINKASNSVLQSRNAPLPSL 796
Cdd:PRK10263  834 QQPVAPQPqdtllhplLMRNGDSRPLHKPTTPLPSL 869
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 193-295 7.76e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 40.44  E-value: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38569480   193 DALSPDQPASQESQGSAASPSEPKVSESPS-PVTTNTPAqfasvSPTVPEFLKTPPTAdQPPPRPAAPVLPTNTVSSAKP 271
Cdd:PTZ00449  584 DPKHPKDPEEPKKPKRPRSAQRPTRPKSPKlPELLDIPK-----SPKRPESPKSPKRP-PPPQRPSSPERPEGPKIIKSP 657

                          90       100
                  ....*....|....*....|....
gi 38569480   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 9.69e-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: 37.21  E-value: 9.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 38569480    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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