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Conserved domains on  [gi|303324568|ref|NP_957462|]
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splicing factor, suppressor of white-apricot homolog [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DRY_EERY pfam09750
Alternative splicing regulator; This entry represents the conserved N-terminal region of SWAP ...
 27-143 1.53e-43

Alternative splicing regulator; This entry represents the conserved N-terminal region of SWAP (suppressor-of-white-apricot protein) proteins. This region contains two highly conserved motifs, viz: DRY and EERY, which appear to be the sites for alternative splicing of exons 2 and 3 of the SWAP mRNA. These proteins are thus thought to be involved in auto-regulation of pre-mRNA splicing. Most family members are associated with two Surp domains pfam01805 and an Arginine- serine-rich binding region towards the C-terminus.


:

Pssm-ID: 462881  Cd Length: 129  Bit Score: 154.01  E-value: 1.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303324568   27 LLVFGYACKLFRDDERAFYHDQGKHLIPWMGDKNIMIDRYDGRGHLHDLSEYDAGSWNHDYQLSEEEARIEALCDEERYL 106
Cdd:pfam09750   1 LQVFGRRCKLFRDDAIAAAAESGKHLVPWQGDPDLLIDRFDVRALLDDIPEYEAGRSARLSELTSEEEEEERECNYERYR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 303324568  107 AMHTD----------LLEEEARQEEEYKRLSEALADEGTYNAVAFRY 143
Cdd:pfam09750  81 DLIKNefegvseeeeLKRIYQEEQFGAKRLSAAKKSSGSYAAIGFSY 127
SWAP smart00648
Suppressor-of-White-APricot splicing regulator; domain present in regulators which are ...
 197-250 4.26e-16

Suppressor-of-White-APricot splicing regulator; domain present in regulators which are responsible for pre-mRNA splicing processes


:

Pssm-ID: 197818 [Multi-domain]  Cd Length: 54  Bit Score: 73.01  E-value: 4.26e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 303324568   197 HAIIERTANFVCKQGAQFEIVLKAKQAGNSQFDFLRFDHYLNPYYKHILRAMKE 250
Cdd:smart00648   1 LDIIDKTAQFVARNGPEFEAKLMERERNNPQFDFLKPNDPYHAYYRKKLAEYRQ 54
SWAP smart00648
Suppressor-of-White-APricot splicing regulator; domain present in regulators which are ...
 480-521 1.49e-12

Suppressor-of-White-APricot splicing regulator; domain present in regulators which are responsible for pre-mRNA splicing processes


:

Pssm-ID: 197818 [Multi-domain]  Cd Length: 54  Bit Score: 62.99  E-value: 1.49e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 303324568   480 DKLAEYVARNGVKFETSVRAK--NDPRFDFLQSWHQYNSYYEFK 521
Cdd:smart00648   5 DKTAQFVARNGPEFEAKLMERerNNPQFDFLKPNDPYHAYYRKK 48
ERM_helical super family cl48646
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 603-697 7.26e-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.


The actual alignment was detected with superfamily member pfam20492:

Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.59  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303324568  603 LEGMELAIGLLEAPREVpqpplAEEKKPVLSQEELEAKQAKQKLEDRLAAAAREklaqasKESKERQLqAERKRKAALFL 682
Cdd:pfam20492  29 LEESEETAEELEEERRQ-----AEEEAERLEQKRQEAEEEKERLEESAEMEAEE------KEQLEAEL-AEAQEEIARLE 96

                          90
                  ....*....|....*
gi 303324568  683 QTLRGPEAEVKRTEE 697
Cdd:pfam20492  97 EEVERKEEEARRLQE 111
 
Name Accession Description Interval E-value
DRY_EERY pfam09750
Alternative splicing regulator; This entry represents the conserved N-terminal region of SWAP ...
 27-143 1.53e-43

Alternative splicing regulator; This entry represents the conserved N-terminal region of SWAP (suppressor-of-white-apricot protein) proteins. This region contains two highly conserved motifs, viz: DRY and EERY, which appear to be the sites for alternative splicing of exons 2 and 3 of the SWAP mRNA. These proteins are thus thought to be involved in auto-regulation of pre-mRNA splicing. Most family members are associated with two Surp domains pfam01805 and an Arginine- serine-rich binding region towards the C-terminus.


Pssm-ID: 462881  Cd Length: 129  Bit Score: 154.01  E-value: 1.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303324568   27 LLVFGYACKLFRDDERAFYHDQGKHLIPWMGDKNIMIDRYDGRGHLHDLSEYDAGSWNHDYQLSEEEARIEALCDEERYL 106
Cdd:pfam09750   1 LQVFGRRCKLFRDDAIAAAAESGKHLVPWQGDPDLLIDRFDVRALLDDIPEYEAGRSARLSELTSEEEEEERECNYERYR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 303324568  107 AMHTD----------LLEEEARQEEEYKRLSEALADEGTYNAVAFRY 143
Cdd:pfam09750  81 DLIKNefegvseeeeLKRIYQEEQFGAKRLSAAKKSSGSYAAIGFSY 127
SWAP smart00648
Suppressor-of-White-APricot splicing regulator; domain present in regulators which are ...
 197-250 4.26e-16

Suppressor-of-White-APricot splicing regulator; domain present in regulators which are responsible for pre-mRNA splicing processes


Pssm-ID: 197818 [Multi-domain]  Cd Length: 54  Bit Score: 73.01  E-value: 4.26e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 303324568   197 HAIIERTANFVCKQGAQFEIVLKAKQAGNSQFDFLRFDHYLNPYYKHILRAMKE 250
Cdd:smart00648   1 LDIIDKTAQFVARNGPEFEAKLMERERNNPQFDFLKPNDPYHAYYRKKLAEYRQ 54
Surp pfam01805
Surp module; This domain is also known as the SWAP domain. SWAP stands for ...
 198-248 8.74e-15

Surp module; This domain is also known as the SWAP domain. SWAP stands for Suppressor-of-White-APricot. It has been suggested that these domains may be RNA binding.


Pssm-ID: 460339 [Multi-domain]  Cd Length: 52  Bit Score: 69.08  E-value: 8.74e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 303324568  198 AIIERTANFVCKQGAQFEIVLKAKQAGNSQFDFLR-FDHYLNPYYKHILRAM 248
Cdd:pfam01805   1 DIIKKTAQFVARNGPEFEALLMEREERNPQFDFLFdPDDPLHAYYRWKLEEY 52
SWAP smart00648
Suppressor-of-White-APricot splicing regulator; domain present in regulators which are ...
 480-521 1.49e-12

Suppressor-of-White-APricot splicing regulator; domain present in regulators which are responsible for pre-mRNA splicing processes


Pssm-ID: 197818 [Multi-domain]  Cd Length: 54  Bit Score: 62.99  E-value: 1.49e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 303324568   480 DKLAEYVARNGVKFETSVRAK--NDPRFDFLQSWHQYNSYYEFK 521
Cdd:smart00648   5 DKTAQFVARNGPEFEAKLMERerNNPQFDFLKPNDPYHAYYRKK 48
Surp pfam01805
Surp module; This domain is also known as the SWAP domain. SWAP stands for ...
 480-521 2.40e-11

Surp module; This domain is also known as the SWAP domain. SWAP stands for Suppressor-of-White-APricot. It has been suggested that these domains may be RNA binding.


Pssm-ID: 460339 [Multi-domain]  Cd Length: 52  Bit Score: 59.45  E-value: 2.40e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 303324568  480 DKLAEYVARNGVKFETSVRAK--NDPRFDFL-QSWHQYNSYYEFK 521
Cdd:pfam01805   4 KKTAQFVARNGPEFEALLMEReeRNPQFDFLfDPDDPLHAYYRWK 48
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 603-697 7.26e-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: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303324568  603 LEGMELAIGLLEAPREVpqpplAEEKKPVLSQEELEAKQAKQKLEDRLAAAAREklaqasKESKERQLqAERKRKAALFL 682
Cdd:pfam20492  29 LEESEETAEELEEERRQ-----AEEEAERLEQKRQEAEEEKERLEESAEMEAEE------KEQLEAEL-AEAQEEIARLE 96

                          90
                  ....*....|....*
gi 303324568  683 QTLRGPEAEVKRTEE 697
Cdd:pfam20492  97 EEVERKEEEARRLQE 111
rpsP PRK14521
30S ribosomal protein S16; Provisional
 628-704 9.28e-03

30S ribosomal protein S16; Provisional


Pssm-ID: 237744 [Multi-domain]  Cd Length: 186  Bit Score: 38.22  E-value: 9.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303324568 628 KKPVLSQEELEAKQA--KQKLEDRLAAAArEKLAQASKESKERQLQAERKRKAAlflqtlRGPEAEVKRTEETTAAPEP 704
Cdd:PRK14521  90 AKGAFTEAQAEAKFEawKEEKEGKVNAKK-DKLSKAKKAAKKAALEAEKKVNEA------RAEAVAEKKAAEAAAVAAE 161
 
Name Accession Description Interval E-value
DRY_EERY pfam09750
Alternative splicing regulator; This entry represents the conserved N-terminal region of SWAP ...
 27-143 1.53e-43

Alternative splicing regulator; This entry represents the conserved N-terminal region of SWAP (suppressor-of-white-apricot protein) proteins. This region contains two highly conserved motifs, viz: DRY and EERY, which appear to be the sites for alternative splicing of exons 2 and 3 of the SWAP mRNA. These proteins are thus thought to be involved in auto-regulation of pre-mRNA splicing. Most family members are associated with two Surp domains pfam01805 and an Arginine- serine-rich binding region towards the C-terminus.


Pssm-ID: 462881  Cd Length: 129  Bit Score: 154.01  E-value: 1.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303324568   27 LLVFGYACKLFRDDERAFYHDQGKHLIPWMGDKNIMIDRYDGRGHLHDLSEYDAGSWNHDYQLSEEEARIEALCDEERYL 106
Cdd:pfam09750   1 LQVFGRRCKLFRDDAIAAAAESGKHLVPWQGDPDLLIDRFDVRALLDDIPEYEAGRSARLSELTSEEEEEERECNYERYR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 303324568  107 AMHTD----------LLEEEARQEEEYKRLSEALADEGTYNAVAFRY 143
Cdd:pfam09750  81 DLIKNefegvseeeeLKRIYQEEQFGAKRLSAAKKSSGSYAAIGFSY 127
SWAP smart00648
Suppressor-of-White-APricot splicing regulator; domain present in regulators which are ...
 197-250 4.26e-16

Suppressor-of-White-APricot splicing regulator; domain present in regulators which are responsible for pre-mRNA splicing processes


Pssm-ID: 197818 [Multi-domain]  Cd Length: 54  Bit Score: 73.01  E-value: 4.26e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 303324568   197 HAIIERTANFVCKQGAQFEIVLKAKQAGNSQFDFLRFDHYLNPYYKHILRAMKE 250
Cdd:smart00648   1 LDIIDKTAQFVARNGPEFEAKLMERERNNPQFDFLKPNDPYHAYYRKKLAEYRQ 54
Surp pfam01805
Surp module; This domain is also known as the SWAP domain. SWAP stands for ...
 198-248 8.74e-15

Surp module; This domain is also known as the SWAP domain. SWAP stands for Suppressor-of-White-APricot. It has been suggested that these domains may be RNA binding.


Pssm-ID: 460339 [Multi-domain]  Cd Length: 52  Bit Score: 69.08  E-value: 8.74e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 303324568  198 AIIERTANFVCKQGAQFEIVLKAKQAGNSQFDFLR-FDHYLNPYYKHILRAM 248
Cdd:pfam01805   1 DIIKKTAQFVARNGPEFEALLMEREERNPQFDFLFdPDDPLHAYYRWKLEEY 52
SWAP smart00648
Suppressor-of-White-APricot splicing regulator; domain present in regulators which are ...
 480-521 1.49e-12

Suppressor-of-White-APricot splicing regulator; domain present in regulators which are responsible for pre-mRNA splicing processes


Pssm-ID: 197818 [Multi-domain]  Cd Length: 54  Bit Score: 62.99  E-value: 1.49e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 303324568   480 DKLAEYVARNGVKFETSVRAK--NDPRFDFLQSWHQYNSYYEFK 521
Cdd:smart00648   5 DKTAQFVARNGPEFEAKLMERerNNPQFDFLKPNDPYHAYYRKK 48
Surp pfam01805
Surp module; This domain is also known as the SWAP domain. SWAP stands for ...
 480-521 2.40e-11

Surp module; This domain is also known as the SWAP domain. SWAP stands for Suppressor-of-White-APricot. It has been suggested that these domains may be RNA binding.


Pssm-ID: 460339 [Multi-domain]  Cd Length: 52  Bit Score: 59.45  E-value: 2.40e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 303324568  480 DKLAEYVARNGVKFETSVRAK--NDPRFDFL-QSWHQYNSYYEFK 521
Cdd:pfam01805   4 KKTAQFVARNGPEFEALLMEReeRNPQFDFLfDPDDPLHAYYRWK 48
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 603-697 7.26e-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: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 303324568  603 LEGMELAIGLLEAPREVpqpplAEEKKPVLSQEELEAKQAKQKLEDRLAAAAREklaqasKESKERQLqAERKRKAALFL 682
Cdd:pfam20492  29 LEESEETAEELEEERRQ-----AEEEAERLEQKRQEAEEEKERLEESAEMEAEE------KEQLEAEL-AEAQEEIARLE 96

                          90
                  ....*....|....*
gi 303324568  683 QTLRGPEAEVKRTEE 697
Cdd:pfam20492  97 EEVERKEEEARRLQE 111
rpsP PRK14521
30S ribosomal protein S16; Provisional
 628-704 9.28e-03

30S ribosomal protein S16; Provisional


Pssm-ID: 237744 [Multi-domain]  Cd Length: 186  Bit Score: 38.22  E-value: 9.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 303324568 628 KKPVLSQEELEAKQA--KQKLEDRLAAAArEKLAQASKESKERQLQAERKRKAAlflqtlRGPEAEVKRTEETTAAPEP 704
Cdd:PRK14521  90 AKGAFTEAQAEAKFEawKEEKEGKVNAKK-DKLSKAKKAAKKAALEAEKKVNEA------RAEAVAEKKAAEAAAVAAE 161
 
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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