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Conserved domains on  [gi|1207171491|ref|XP_021330718|]
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serine/threonine-protein phosphatase 6 regulatory subunit 2a isoform X1 [Danio rerio]

Protein Classification

SAPS family protein( domain architecture ID 10517350)

SAPS (SIT4-associating proteins) family protein

Gene Ontology:  GO:0019888|GO:0043666
PubMed:  8649382

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SAPS pfam04499
SIT4 phosphatase-associated protein; This family includes a conserved region from a group of ...
 128-537 6.45e-149

SIT4 phosphatase-associated protein; This family includes a conserved region from a group of yeast proteins that associate with the SIT4 phosphatase. This association is required for SIT4's role in G1 cyclin transcription and for bud formation. This family also includes homologous regions from other eukaryotes.


:

Pssm-ID: 398279  Cd Length: 383  Bit Score: 443.61  E-value: 6.45e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 128 IGNLIARKTDQVISFLRKKHNFISLVLNHIDASAMMDLLLRLISCVEPaPLRMEVLNWLNEERLIQRLTELMHTGRDEER 207
Cdd:pfam04499   1 NENLLDRKTDQMIEFIRKQENFVDKFLKHIDTPAIMDLLLKLISTDKP-ELPTGVIEWLNEQNLIPKLLDLLSPSYDEDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 208 QSNASQTLCDIIRLSRDQANQLSEVTDSDPLLAVLESQENVAELLKNMFEGeRSEASVVNGTQVLLTLLESRRSGLEGLM 287
Cdd:pfam04499  80 QSNASDFLKAIITISRNAPLQLQSSIGPNELTRELVSEESVEKLLDNMLKG-KSGSALVNGVGIIIELIRKNNSDYDPVQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 288 DLYSQGCERSYTVNSSI-----LRAIEPHLKDFQQLLLNPPTRSAILTTVGVLEQPLGSARLHVARLVASLLQTCDLSIC 362
Cdd:pfam04499 159 LLYTTLEEHPPSDRDPIylghlLRAFSPHLPDFHQLLLDPPKDSPLQTTLGVLIEPLGFERFKIVELIAELLHCSNMSLL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 363 QE---------ICRLNTMDLLLDLFFKYTWNNFLHLQVELCVASILNhsahadvqnpglqnheerpatdnqteegtpgqn 433
Cdd:pfam04499 239 NEkkgeklkikLVDLGIIPTILDLFFKYPWNNFLHNVVEDIIQQILN--------------------------------- 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 434 sssDPANTPIQDALVANLFQHCRLVQRILDAWEENDKIQTEGGRRRGNMGHLTRIANTVVQNLEKGLAHSQINDLIKELp 513
Cdd:pfam04499 286 ---GPMDFSYNSFLVVDLFTDCNLTQRILEGQKESDRFQAEKGPRLGYMGHLTLIAEEVVKFSEKYPPELISPDILEIL- 361

                         410       420
                  ....*....|....*....|....
gi 1207171491 514 edCRGRWESFVGETLRETNRRNTV 537
Cdd:pfam04499 362 --ENEEWEEYVEETLEETRERYNV 383
Glutenin_hmw super family cl26620
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 699-766 2.01e-04

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


The actual alignment was detected with superfamily member pfam03157:

Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 45.32  E-value: 2.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207171491 699 QQSAGAQTQNPGWTASFGEAEvsaSGSWGNSPQQGSEGQQDTGWASFTEFQPFSSTESSQTEGQPQQG 766
Cdd:pfam03157 573 QPGQGQQGQQPGQGQQPGQGQ---PGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGQGQQG 637
 
Name Accession Description Interval E-value
SAPS pfam04499
SIT4 phosphatase-associated protein; This family includes a conserved region from a group of ...
 128-537 6.45e-149

SIT4 phosphatase-associated protein; This family includes a conserved region from a group of yeast proteins that associate with the SIT4 phosphatase. This association is required for SIT4's role in G1 cyclin transcription and for bud formation. This family also includes homologous regions from other eukaryotes.


Pssm-ID: 398279  Cd Length: 383  Bit Score: 443.61  E-value: 6.45e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 128 IGNLIARKTDQVISFLRKKHNFISLVLNHIDASAMMDLLLRLISCVEPaPLRMEVLNWLNEERLIQRLTELMHTGRDEER 207
Cdd:pfam04499   1 NENLLDRKTDQMIEFIRKQENFVDKFLKHIDTPAIMDLLLKLISTDKP-ELPTGVIEWLNEQNLIPKLLDLLSPSYDEDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 208 QSNASQTLCDIIRLSRDQANQLSEVTDSDPLLAVLESQENVAELLKNMFEGeRSEASVVNGTQVLLTLLESRRSGLEGLM 287
Cdd:pfam04499  80 QSNASDFLKAIITISRNAPLQLQSSIGPNELTRELVSEESVEKLLDNMLKG-KSGSALVNGVGIIIELIRKNNSDYDPVQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 288 DLYSQGCERSYTVNSSI-----LRAIEPHLKDFQQLLLNPPTRSAILTTVGVLEQPLGSARLHVARLVASLLQTCDLSIC 362
Cdd:pfam04499 159 LLYTTLEEHPPSDRDPIylghlLRAFSPHLPDFHQLLLDPPKDSPLQTTLGVLIEPLGFERFKIVELIAELLHCSNMSLL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 363 QE---------ICRLNTMDLLLDLFFKYTWNNFLHLQVELCVASILNhsahadvqnpglqnheerpatdnqteegtpgqn 433
Cdd:pfam04499 239 NEkkgeklkikLVDLGIIPTILDLFFKYPWNNFLHNVVEDIIQQILN--------------------------------- 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 434 sssDPANTPIQDALVANLFQHCRLVQRILDAWEENDKIQTEGGRRRGNMGHLTRIANTVVQNLEKGLAHSQINDLIKELp 513
Cdd:pfam04499 286 ---GPMDFSYNSFLVVDLFTDCNLTQRILEGQKESDRFQAEKGPRLGYMGHLTLIAEEVVKFSEKYPPELISPDILEIL- 361

                         410       420
                  ....*....|....*....|....
gi 1207171491 514 edCRGRWESFVGETLRETNRRNTV 537
Cdd:pfam04499 362 --ENEEWEEYVEETLEETRERYNV 383
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 699-766 2.01e-04

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 45.32  E-value: 2.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207171491 699 QQSAGAQTQNPGWTASFGEAEvsaSGSWGNSPQQGSEGQQDTGWASFTEFQPFSSTESSQTEGQPQQG 766
Cdd:pfam03157 573 QPGQGQQGQQPGQGQQPGQGQ---PGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGQGQQG 637
 
Name Accession Description Interval E-value
SAPS pfam04499
SIT4 phosphatase-associated protein; This family includes a conserved region from a group of ...
 128-537 6.45e-149

SIT4 phosphatase-associated protein; This family includes a conserved region from a group of yeast proteins that associate with the SIT4 phosphatase. This association is required for SIT4's role in G1 cyclin transcription and for bud formation. This family also includes homologous regions from other eukaryotes.


Pssm-ID: 398279  Cd Length: 383  Bit Score: 443.61  E-value: 6.45e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 128 IGNLIARKTDQVISFLRKKHNFISLVLNHIDASAMMDLLLRLISCVEPaPLRMEVLNWLNEERLIQRLTELMHTGRDEER 207
Cdd:pfam04499   1 NENLLDRKTDQMIEFIRKQENFVDKFLKHIDTPAIMDLLLKLISTDKP-ELPTGVIEWLNEQNLIPKLLDLLSPSYDEDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 208 QSNASQTLCDIIRLSRDQANQLSEVTDSDPLLAVLESQENVAELLKNMFEGeRSEASVVNGTQVLLTLLESRRSGLEGLM 287
Cdd:pfam04499  80 QSNASDFLKAIITISRNAPLQLQSSIGPNELTRELVSEESVEKLLDNMLKG-KSGSALVNGVGIIIELIRKNNSDYDPVQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 288 DLYSQGCERSYTVNSSI-----LRAIEPHLKDFQQLLLNPPTRSAILTTVGVLEQPLGSARLHVARLVASLLQTCDLSIC 362
Cdd:pfam04499 159 LLYTTLEEHPPSDRDPIylghlLRAFSPHLPDFHQLLLDPPKDSPLQTTLGVLIEPLGFERFKIVELIAELLHCSNMSLL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 363 QE---------ICRLNTMDLLLDLFFKYTWNNFLHLQVELCVASILNhsahadvqnpglqnheerpatdnqteegtpgqn 433
Cdd:pfam04499 239 NEkkgeklkikLVDLGIIPTILDLFFKYPWNNFLHNVVEDIIQQILN--------------------------------- 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171491 434 sssDPANTPIQDALVANLFQHCRLVQRILDAWEENDKIQTEGGRRRGNMGHLTRIANTVVQNLEKGLAHSQINDLIKELp 513
Cdd:pfam04499 286 ---GPMDFSYNSFLVVDLFTDCNLTQRILEGQKESDRFQAEKGPRLGYMGHLTLIAEEVVKFSEKYPPELISPDILEIL- 361

                         410       420
                  ....*....|....*....|....
gi 1207171491 514 edCRGRWESFVGETLRETNRRNTV 537
Cdd:pfam04499 362 --ENEEWEEYVEETLEETRERYNV 383
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 699-766 2.01e-04

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 45.32  E-value: 2.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207171491 699 QQSAGAQTQNPGWTASFGEAEvsaSGSWGNSPQQGSEGQQDTGWASFTEFQPFSSTESSQTEGQPQQG 766
Cdd:pfam03157 573 QPGQGQQGQQPGQGQQPGQGQ---PGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSSLQLGQGQQG 637
 
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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