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Conserved domains on  [gi|1958747064|ref|XP_038953828|]
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signal-induced proliferation-associated 1-like protein 2 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rap_GAP pfam02145
Rap/ran-GAP;
626-806 3.29e-89

Rap/ran-GAP;


:

Pssm-ID: 460463  Cd Length: 179  Bit Score: 287.49  E-value: 3.29e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064  626 YNNETAGPAFEEFLDLLGQRVRLKGFSKYRAQLDNKTDSTGTHSLYTTYKDFELMFHVSTLLPYMPNNRQQLLRKRHIGN 705
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064  706 DIVTIIFQEPGaLPFTPKNIRSHFQHVFVIVKVHNPCTENVCYSVGVSRSKDVPPFGPPIPKGVTFPKS--AVFRDFLLa 783
Cdd:pfam02145   81 DIVNIVFNESG-GPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDnlPEFVRFLA- 158

                          170       180
                   ....*....|....*....|...
gi 1958747064  784 kvINAENAAHKSEKFRAMATRTR 806
Cdd:pfam02145  159 --INAERAALKSSSFAERLRRIR 179
SPAR_C pfam11881
C-terminal domain of SPAR protein; This domain is found st the C-terminus of many ...
 1423-1685 2.17e-74

C-terminal domain of SPAR protein; This domain is found st the C-terminus of many spine-associated Rap GTPase-activating - SPAR - proteins in eukaryotes. This domain is found associated with pfam02145, pfam00595. The exact function is not known.


:

Pssm-ID: 463383  Cd Length: 242  Bit Score: 247.79  E-value: 2.17e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064 1423 EMDIMSTASQHPAVVGD--SVPEAQHVLSKDDFLKLMLPDSPLVEEGRRKFSFYGNLSPRRSLYRTLSDESVCSNrRGSS 1500
Cdd:pfam11881    5 SDGNVSGQPRLRASLRDlrSPQKNYKSTIEEDLKKLIIMDSPPPEEQERKPSFPGNPSPRRSLQRTLSDESICSG-QREP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064 1501 FASSRSSILDQALPNDILFSTT------PPYHSTLPPRTHPAPSMGSLRNEFWFSDGSLSD-----KSKCADPGLMPLPD 1569
Cdd:pfam11881   84 SFSSRDSVLDQALPSDVLFSCTstlprsPTTRSAPLRRASYALGMKSLHGDLSASDLSLTDlrdrrPLRRLDPGLMPLPD 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064 1570 TAAGLDWSHLVDAARAFEghcgeegqqipfsklvctksrglvaltnllsicssspDQRVASFCTLTDLQHGQE-LEGAPE 1648
Cdd:pfam11881  164 TAAGLDWSHLVDAAKAFE-------------------------------------VQRAASFFSLDDNHRSPDaASSPQQ 206

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1958747064 1649 LSLCVDPTSGKEFMdTPGERSPSTLTGKVNQLELILR 1685
Cdd:pfam11881  207 LSLQVAPQTPRTTS-TSSEESPADLTGKVYQLEAMLK 242
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 951-1023 6.70e-45

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


:

Pssm-ID: 467227 [Multi-domain]  Cd Length: 73  Bit Score: 156.67  E-value: 6.70e-45
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747064  951 EMTLRRNGLGQLGFHVNFEGIVADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTSVTVKVVII 1023
Cdd:cd06745      1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73
 
Name Accession Description Interval E-value
Rap_GAP pfam02145
Rap/ran-GAP;
626-806 3.29e-89

Rap/ran-GAP;


Pssm-ID: 460463  Cd Length: 179  Bit Score: 287.49  E-value: 3.29e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064  626 YNNETAGPAFEEFLDLLGQRVRLKGFSKYRAQLDNKTDSTGTHSLYTTYKDFELMFHVSTLLPYMPNNRQQLLRKRHIGN 705
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064  706 DIVTIIFQEPGaLPFTPKNIRSHFQHVFVIVKVHNPCTENVCYSVGVSRSKDVPPFGPPIPKGVTFPKS--AVFRDFLLa 783
Cdd:pfam02145   81 DIVNIVFNESG-GPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDnlPEFVRFLA- 158

                          170       180
                   ....*....|....*....|...
gi 1958747064  784 kvINAENAAHKSEKFRAMATRTR 806
Cdd:pfam02145  159 --INAERAALKSSSFAERLRRIR 179
SPAR_C pfam11881
C-terminal domain of SPAR protein; This domain is found st the C-terminus of many ...
 1423-1685 2.17e-74

C-terminal domain of SPAR protein; This domain is found st the C-terminus of many spine-associated Rap GTPase-activating - SPAR - proteins in eukaryotes. This domain is found associated with pfam02145, pfam00595. The exact function is not known.


Pssm-ID: 463383  Cd Length: 242  Bit Score: 247.79  E-value: 2.17e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064 1423 EMDIMSTASQHPAVVGD--SVPEAQHVLSKDDFLKLMLPDSPLVEEGRRKFSFYGNLSPRRSLYRTLSDESVCSNrRGSS 1500
Cdd:pfam11881    5 SDGNVSGQPRLRASLRDlrSPQKNYKSTIEEDLKKLIIMDSPPPEEQERKPSFPGNPSPRRSLQRTLSDESICSG-QREP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064 1501 FASSRSSILDQALPNDILFSTT------PPYHSTLPPRTHPAPSMGSLRNEFWFSDGSLSD-----KSKCADPGLMPLPD 1569
Cdd:pfam11881   84 SFSSRDSVLDQALPSDVLFSCTstlprsPTTRSAPLRRASYALGMKSLHGDLSASDLSLTDlrdrrPLRRLDPGLMPLPD 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064 1570 TAAGLDWSHLVDAARAFEghcgeegqqipfsklvctksrglvaltnllsicssspDQRVASFCTLTDLQHGQE-LEGAPE 1648
Cdd:pfam11881  164 TAAGLDWSHLVDAAKAFE-------------------------------------VQRAASFFSLDDNHRSPDaASSPQQ 206

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1958747064 1649 LSLCVDPTSGKEFMdTPGERSPSTLTGKVNQLELILR 1685
Cdd:pfam11881  207 LSLQVAPQTPRTTS-TSSEESPADLTGKVYQLEAMLK 242
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 951-1023 6.70e-45

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467227 [Multi-domain]  Cd Length: 73  Bit Score: 156.67  E-value: 6.70e-45
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747064  951 EMTLRRNGLGQLGFHVNFEGIVADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTSVTVKVVII 1023
Cdd:cd06745      1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 948-1025 2.15e-10

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 58.54  E-value: 2.15e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064   948 ETVEMTLRRNGlGQLGFHV-----NFEGI-VADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLR-TSVTVKV 1020
Cdd:smart00228    1 EPRLVELEKGG-GGLGFSLvggkdEGGGVvVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKkAGGKVTL 79


                    ....*
gi 1958747064  1021 VIIQP 1025
Cdd:smart00228   80 TVLRG 84
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 951-1023 1.24e-06

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 47.66  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064  951 EMTLRRNGLGQLGF-------HVNFEGIVADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTSV-TVKVVI 1022
Cdd:pfam00595    1 QVTLEKDGRGGLGFslkggsdQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGgKVTLTI 80


                   .
gi 1958747064 1023 I 1023
Cdd:pfam00595   81 L 81
 
Name Accession Description Interval E-value
Rap_GAP pfam02145
Rap/ran-GAP;
626-806 3.29e-89

Rap/ran-GAP;


Pssm-ID: 460463  Cd Length: 179  Bit Score: 287.49  E-value: 3.29e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064  626 YNNETAGPAFEEFLDLLGQRVRLKGFSKYRAQLDNKTDSTGTHSLYTTYKDFELMFHVSTLLPYMPNNRQQLLRKRHIGN 705
Cdd:pfam02145    1 LSNEEGSPAYEEFLNLLGWLVELKGFKGYRGGLDTKNNTTGEYSYYWADRGTEIMFHVSTLMPTTENDPQQLEKKRHIGN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064  706 DIVTIIFQEPGaLPFTPKNIRSHFQHVFVIVKVHNPCTENVCYSVGVSRSKDVPPFGPPIPKGVTFPKS--AVFRDFLLa 783
Cdd:pfam02145   81 DIVNIVFNESG-GPFDPSTIKSQFNHVFIVVQPNLPDTDNTLYRVSVVRKDDVPPFGPLLPDPKIFSKDnlPEFVRFLA- 158

                          170       180
                   ....*....|....*....|...
gi 1958747064  784 kvINAENAAHKSEKFRAMATRTR 806
Cdd:pfam02145  159 --INAERAALKSSSFAERLRRIR 179
SPAR_C pfam11881
C-terminal domain of SPAR protein; This domain is found st the C-terminus of many ...
 1423-1685 2.17e-74

C-terminal domain of SPAR protein; This domain is found st the C-terminus of many spine-associated Rap GTPase-activating - SPAR - proteins in eukaryotes. This domain is found associated with pfam02145, pfam00595. The exact function is not known.


Pssm-ID: 463383  Cd Length: 242  Bit Score: 247.79  E-value: 2.17e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064 1423 EMDIMSTASQHPAVVGD--SVPEAQHVLSKDDFLKLMLPDSPLVEEGRRKFSFYGNLSPRRSLYRTLSDESVCSNrRGSS 1500
Cdd:pfam11881    5 SDGNVSGQPRLRASLRDlrSPQKNYKSTIEEDLKKLIIMDSPPPEEQERKPSFPGNPSPRRSLQRTLSDESICSG-QREP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064 1501 FASSRSSILDQALPNDILFSTT------PPYHSTLPPRTHPAPSMGSLRNEFWFSDGSLSD-----KSKCADPGLMPLPD 1569
Cdd:pfam11881   84 SFSSRDSVLDQALPSDVLFSCTstlprsPTTRSAPLRRASYALGMKSLHGDLSASDLSLTDlrdrrPLRRLDPGLMPLPD 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064 1570 TAAGLDWSHLVDAARAFEghcgeegqqipfsklvctksrglvaltnllsicssspDQRVASFCTLTDLQHGQE-LEGAPE 1648
Cdd:pfam11881  164 TAAGLDWSHLVDAAKAFE-------------------------------------VQRAASFFSLDDNHRSPDaASSPQQ 206

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1958747064 1649 LSLCVDPTSGKEFMdTPGERSPSTLTGKVNQLELILR 1685
Cdd:pfam11881  207 LSLQVAPQTPRTTS-TSSEESPADLTGKVYQLEAMLK 242
PDZ_SIPA1-like cd06745
PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; ...
 951-1023 6.70e-45

PDZ domain of signal-induced proliferation-associated protein 1 (SIPA1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SIPA1, and related domains. The Rap-GTPase activating protein SIPA1 (also known as GTPase-activating protein Spa-1, p130 SPA1) is a metastasis promoter; a polymorphism in a region of the Sipa1 gene encoding the PDZ domain is associated with metastasis. The SIPA1 PDZ domain binds ribosomal RNA processing 1 homolog B (Rrp1b). SIPA1 also forms a complex with water channel aquaporin-2 (AQP2) and plays a role in trafficking of AQP2, targeted positioning of which strictly regulates body water homeostasis; the SIPA1 PDZ domain binds AQP2. Rrp1b or AQP2 binding inhibits the RapGAP activity of SIPA1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SIPA1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467227 [Multi-domain]  Cd Length: 73  Bit Score: 156.67  E-value: 6.70e-45
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958747064  951 EMTLRRNGLGQLGFHVNFEGIVADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTSVTVKVVII 1023
Cdd:cd06745      1 ELTLRRNGLGQLGFHVNYEGFVTEVERFGFAWQAGLRQGSRLVEICKVPVATLTHEQMIDLLRTSVKVKVTVI 73
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 948-1025 2.15e-10

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 58.54  E-value: 2.15e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064   948 ETVEMTLRRNGlGQLGFHV-----NFEGI-VADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLR-TSVTVKV 1020
Cdd:smart00228    1 EPRLVELEKGG-GGLGFSLvggkdEGGGVvVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKkAGGKVTL 79


                    ....*
gi 1958747064  1021 VIIQP 1025
Cdd:smart00228   80 TVLRG 84
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 951-1021 9.54e-10

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 56.78  E-value: 9.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064  951 EMTLRRNGLGQLGFHV-----NFEGI-VADVEPFGFAWKAG-LRQGSRLVEICKVAVATLTHEQMIDLLRTS---VTVKV 1020
Cdd:cd00136      1 TVTLEKDPGGGLGFSIrggkdGGGGIfVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTHEEAVELLKSAggeVTLTV 80


                   .
gi 1958747064 1021 V 1021
Cdd:cd00136     81 R 81
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 963-1021 7.99e-07

PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 48.20  E-value: 7.99e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958747064  963 GFHVNFEG-----IVADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTS---VTVKVV 1021
Cdd:cd06768     13 GFNLHAEKgrpghFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQVVEKIKASgnqVTLLVV 79
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 951-1023 1.24e-06

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 47.66  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958747064  951 EMTLRRNGLGQLGF-------HVNFEGIVADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTSV-TVKVVI 1022
Cdd:pfam00595    1 QVTLEKDGRGGLGFslkggsdQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGgKVTLTI 80


                   .
gi 1958747064 1023 I 1023
Cdd:pfam00595   81 L 81
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
 974-1021 1.61e-06

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 47.97  E-value: 1.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958747064  974 DVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTS---VTVKVV 1021
Cdd:cd06746     48 SVDPGGVADKAGLKKGDFLLEINGEDVVKASHEQVVNLIRQSgntLVLKVV 98
PDZ2_APBA1_3-like cd06793
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ...
 950-1016 2.37e-06

PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking, and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2) which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins, APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467255 [Multi-domain]  Cd Length: 78  Bit Score: 47.01  E-value: 2.37e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958747064  950 VEMTLRRNGLG-QLGFHVNfEGIVADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTSV 1016
Cdd:cd06793      3 TTVLIRRPDLKyQLGFSVQ-NGIICSLLRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVQLLSNSV 69
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 949-1021 3.18e-04

PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 41.03  E-value: 3.18e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958747064  949 TVEMTLRRNGLGqlgFHVNFEG--IVADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRT----SVTVKVV 1021
Cdd:cd06712      3 TVHLTKEEGGFG---FTLRGDSpvQVASVDPGSCAAEAGLKEGDYIVSVGGVDCKWSKHSEVVKLLKSageeGLELQVV 78
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 972-1016 7.38e-04

PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 40.47  E-value: 7.38e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958747064  972 VADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTSV 1016
Cdd:cd23070     40 VSAVLEGGAADKAGVRKGDRILEVNGVNVEGATHKQVVDLIKSGG 84
PDZ5_DrPTPN13-like cd23060
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ...
 951-1022 1.94e-03

PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467273 [Multi-domain]  Cd Length: 80  Bit Score: 38.87  E-value: 1.94e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958747064  951 EMTLRRNGLGQLGFHV----NFEGI-VADVEPFGFAWKAG-LRQGSRLVEICKVAVATLTHEQMIDLLR-TSVTVKVVI 1022
Cdd:cd23060      1 QIELEKPANGGLGFSLvggeGGSGIfVKSISPGGVADRDGrLQVGDRLLQVNGESVIGLSHSKAVNILRkAKGTVQLTV 79
PDZ_ARHGEF11-12-like cd23069
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 952-1020 3.49e-03

PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGEF11, ARHGEF12, and related domains. This subfamily includes the GEFs (guanine exchange factors) ARHGEF11 (Rho guanine nucleotide exchange factor 11, known as PDZ-RhoGEF) and ARHGEF12 (Rho guanine nucleotide exchange factor 12, also known as leukemia-associated RhoGEF). GEFs activate Rho GTPases by promoting GTP binding. ARHGEF11/12 are regulators of G protein signaling (RGS) domain-containing GEFs; the RGS domain mediates their binding to and activation of Galpha (and Gq also in the case of ARHGEF12), in response to G-protein coupled receptor activation. ARHGEF11 and 12 are involved in serum-signaling, and regulate Yes-Associated Protein (YAP1)-dependent transcription. The ARHGEF12 PDZ domain binds plexin-B1 and the receptor tyrosine kinase insulin-like growth factor receptor (IGF-R1) beta-subunit. ARHGEF12 also interacts with glutamate receptor delta-1(GluD1), a postsynaptic organizer of inhibitory synapses in cortical pyramidal neurons. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGEF11-12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467282 [Multi-domain]  Cd Length: 76  Bit Score: 37.76  E-value: 3.49e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958747064  952 MTLRRNGLGqLGFHVNFEGI--VADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTSVTVKV 1020
Cdd:cd23069      4 VVIQRDENG-YGLTVSGDNPvfVQSVKEGGAAYRAGVQEGDRIIKVNGTLVTHSNHLEVVKLIKSGSYVAL 73
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 981-1020 4.07e-03

circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 38.23  E-value: 4.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958747064  981 AWKAGLRQGSRLVEICKVAVATLTHEQMIDLLR----TSVTVKV 1020
Cdd:cd06782     27 AEKAGIKPGDVIVAVDGESVRGMSLDEVVKLLRgpkgTKVKLTI 70
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
 951-1020 6.04e-03

PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 37.62  E-value: 6.04e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958747064  951 EMTLRRNGLGQLGFHV--NFE---GI-VADVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRT--SVTVKV 1020
Cdd:cd06737      4 LVRLDRRGPESLGFSVrgGLEhgcGLfVSHVSPGSQADNKGLRVGDEIVRINGYSISQCTHEEVINLIKTkkTVSLKV 81
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
 940-1015 7.27e-03

PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467226 [Multi-domain]  Cd Length: 75  Bit Score: 36.87  E-value: 7.27e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958747064  940 LVIVTRGCETVEMTLRRNGlgqlgfHVNFEgivaDVEPFGFAWKAGLRQGSRLVEICKVAVATLTHEQMIDLLRTS 1015
Cdd:cd06744      1 TVRVYRGNGSFGFTLRGHA------PVYIE----SVDPGSAAERAGLKPGDRILFLNGLDVRNCSHDKVVSLLQGS 66
 
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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