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Conserved domains on  [gi|28573157|ref|NP_731291|]
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polychaetoid, isoform A [Drosophila melanogaster]

Protein Classification

SH3_ZO and GuKc domain-containing protein( domain architecture ID 10097950)

protein containing domains PDZ_signaling, SH3_ZO, GuKc, and ZU5

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
604-780 1.21e-40

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


:

Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 148.60  E-value: 1.21e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     604 NWDDVVFSDSISKFP-AYERVVLRHPGFVRPVVLFGpvSDLARERlAKDFPDKFSTPLQDDdkSAATSGKCRIVRLSNIR 682
Cdd:smart00072    3 VGKGTLLAELIQEIPdAFERVVSHTTRPPRPGEVNG--VDYHFVS-KEEFEDDIKSGLFLE--WGEYEGNYYGTSKETIR 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     683 DVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLK-TDSKHVIKQLRHGLPKAAHKSSKKlLEQCQKLERVWsHIFSTQIA 761
Cdd:smart00072   78 QVAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIApPSSEELERRLRQRGTETSERIQKR-LAAAQKEAQEY-HLFDYVIV 155
                           170
                    ....*....|....*....
gi 28573157     762 LSDEESWYRKLRDSIDLQQ 780
Cdd:smart00072  156 NDDLEDAYEELKEILEAEQ 174
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
502-563 5.11e-35

Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212793  Cd Length: 62  Bit Score: 128.18  E-value: 5.11e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28573157  502 HIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAE 563
Cdd:cd11859    1 YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGTVGSWQAVRVGRNHQELERGVIPNKSRAE 62
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
1959-2046 1.56e-28

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


:

Pssm-ID: 425872  Cd Length: 96  Bit Score: 110.68  E-value: 1.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157   1959 SRGFFDSNGGTLADKLWHVSLQIPPGAIPAGVRQEIYFTVSDPRMgqavggPPLDMENGETMLSPLVMCGPQGLEFLVPV 2038
Cdd:pfam00791    1 ASGLFDSRGGRLVLPNSGVSLLIPPGAIPEGTRIEIYLAVLRDDT------SRPPLEEGETLLSPVVECGPPGLKFLKPV 74

                   ....*...
gi 28573157   2039 TLNIPHCA 2046
Cdd:pfam00791   75 ILEIPHCA 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
22-107 7.73e-21

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 88.39  E-value: 7.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157   22 HTVAVTRVPGYGFGIAVSGGRDNphfangDPSIAVSDVLKGGPAED-RLQVNDRIISVNGVSLENVEYATAVQVLRDSGN 100
Cdd:cd00992    2 RTVTLRKDPGGGLGFSLRGGKDS------GGGIFVSRVEPGGPAERgGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGD 75

                 ....*..
gi 28573157  101 TVQLVVK 107
Cdd:cd00992   76 EVTLTVR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
406-483 4.50e-18

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 80.69  E-value: 4.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157  406 PRFISFQKE--GSVGIRLTGGNEA--GIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLI 481
Cdd:cd00992    1 VRTVTLRKDpgGGLGFSLRGGKDSggGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLT 80

                 ..
gi 28573157  482 VQ 483
Cdd:cd00992   81 VR 82
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
169-250 9.13e-06

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


:

Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 45.64  E-value: 9.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157  169 PIKVTLTKGGKKDdYGVVL------GCRLFVKEIsskaREQLNANGYSLQEGDIITRIHNTNCGDtMSLKEAKKIIDGCK 242
Cdd:cd00992    1 VRTVTLRKDPGGG-LGFSLrggkdsGGGIFVSRV----EPGGPAERGGLRVGDRILEVNGVSVEG-LTHEEAVELLKNSG 74

                 ....*...
gi 28573157  243 ERLNLVVL 250
Cdd:cd00992   75 DEVTLTVR 82
 
Name Accession Description Interval E-value
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
604-780 1.21e-40

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 148.60  E-value: 1.21e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     604 NWDDVVFSDSISKFP-AYERVVLRHPGFVRPVVLFGpvSDLARERlAKDFPDKFSTPLQDDdkSAATSGKCRIVRLSNIR 682
Cdd:smart00072    3 VGKGTLLAELIQEIPdAFERVVSHTTRPPRPGEVNG--VDYHFVS-KEEFEDDIKSGLFLE--WGEYEGNYYGTSKETIR 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     683 DVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLK-TDSKHVIKQLRHGLPKAAHKSSKKlLEQCQKLERVWsHIFSTQIA 761
Cdd:smart00072   78 QVAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIApPSSEELERRLRQRGTETSERIQKR-LAAAQKEAQEY-HLFDYVIV 155
                           170
                    ....*....|....*....
gi 28573157     762 LSDEESWYRKLRDSIDLQQ 780
Cdd:smart00072  156 NDDLEDAYEELKEILEAEQ 174
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
502-563 5.11e-35

Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212793  Cd Length: 62  Bit Score: 128.18  E-value: 5.11e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28573157  502 HIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAE 563
Cdd:cd11859    1 YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGTVGSWQAVRVGRNHQELERGVIPNKSRAE 62
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
1959-2046 1.56e-28

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 425872  Cd Length: 96  Bit Score: 110.68  E-value: 1.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157   1959 SRGFFDSNGGTLADKLWHVSLQIPPGAIPAGVRQEIYFTVSDPRMgqavggPPLDMENGETMLSPLVMCGPQGLEFLVPV 2038
Cdd:pfam00791    1 ASGLFDSRGGRLVLPNSGVSLLIPPGAIPEGTRIEIYLAVLRDDT------SRPPLEEGETLLSPVVECGPPGLKFLKPV 74

                   ....*...
gi 28573157   2039 TLNIPHCA 2046
Cdd:pfam00791   75 ILEIPHCA 82
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
1957-2046 1.20e-22

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 94.34  E-value: 1.20e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157    1957 STSRGFFDSNGGTLADKLWHVSLQIPPGAIPAGVRQEIYFTVSDPRMGQavggPPldMENGETMLSPLVMCGPQGLEFLV 2036
Cdd:smart00218    3 FLVSGTFDARGGRLRGPRTGVRLIIPPGAIPQGTRYTCYLVVHKTLSTP----PP--LEEGETLLSPVVECGPHGALFLR 76
                            90
                    ....*....|
gi 28573157    2037 PVTLNIPHCA 2046
Cdd:smart00218   77 PVILEVPHCA 86
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
22-107 7.73e-21

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 88.39  E-value: 7.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157   22 HTVAVTRVPGYGFGIAVSGGRDNphfangDPSIAVSDVLKGGPAED-RLQVNDRIISVNGVSLENVEYATAVQVLRDSGN 100
Cdd:cd00992    2 RTVTLRKDPGGGLGFSLRGGKDS------GGGIFVSRVEPGGPAERgGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGD 75

                 ....*..
gi 28573157  101 TVQLVVK 107
Cdd:cd00992   76 EVTLTVR 82
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
23-107 3.12e-19

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 83.87  E-value: 3.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     23 TVAVTRVPGYGFGIAVSGGRDNphfanGDPSIAVSDVLKGGPAE-DRLQVNDRIISVNGVSLENVEYATAVQVLRDSGNT 101
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSDQ-----GDPGIFVSEVLPGGAAEaGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75

                   ....*.
gi 28573157    102 VQLVVK 107
Cdd:pfam00595   76 VTLTIL 81
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
406-483 4.50e-18

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 80.69  E-value: 4.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157  406 PRFISFQKE--GSVGIRLTGGNEA--GIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLI 481
Cdd:cd00992    1 VRTVTLRKDpgGGLGFSLRGGKDSggGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLT 80

                 ..
gi 28573157  482 VQ 483
Cdd:cd00992   81 VR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
405-486 7.46e-18

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: 80.12  E-value: 7.46e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     405 EPRFISFQKE-GSVGIRLTGGNE--AGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLI 481
Cdd:smart00228    1 EPRLVELEKGgGGLGFSLVGGKDegGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80

                    ....*
gi 28573157     482 VQYCK 486
Cdd:smart00228   81 VLRGG 85
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
20-109 2.33e-17

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: 78.57  E-value: 2.33e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157      20 EYHTVAVTRVPGyGFGIAVSGGRDNPHFangdpsIAVSDVLKGGPAE-DRLQVNDRIISVNGVSLENVEYATAVQVLRDS 98
Cdd:smart00228    1 EPRLVELEKGGG-GLGFSLVGGKDEGGG------VVVSSVVPGSPAAkAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
                            90
                    ....*....|.
gi 28573157      99 GNTVQLVVKRR 109
Cdd:smart00228   74 GGKVTLTVLRG 84
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
409-483 2.45e-14

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 70.00  E-value: 2.45e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28573157    409 ISFQKEGSVGIRLTGGNEA---GIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQ 483
Cdd:pfam00595    4 LEKDGRGGLGFSLKGGSDQgdpGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
502-564 5.40e-09

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 53.75  E-value: 5.40e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28573157    502 HIKTHFHCDNPSKGEMAFKAGDVFRVIDTlhnGVVGSWQVLKIGRghqemqRGVIPNKSRAEE 564
Cdd:pfam07653    1 YGRVIFDYVGTDKNGLTLKKGDVVKVLGK---DNDGWWEGETGGR------VGLVPSTAVEEI 54
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
415-471 1.69e-07

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 55.80  E-value: 1.69e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 28573157  415 GSVGIRLTGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFL 471
Cdd:COG0793  100 GGIGIELQMEDIGGVKVVSPIDGSPAAKAGIKPGDVIIKIDGKSVGGVSLDEAVKLI 156
Guanylate_kin pfam00625
Guanylate kinase;
678-777 1.85e-07

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 53.15  E-value: 1.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157    678 LSNIRDVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLKTDSKHVIKQLRHGLPKaahKSSKKLLEQCQKLERVWSH-IF 756
Cdd:pfam00625   83 VETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGK---EQEEKINKRMAAAEQEFQHyEF 159
                           90       100
                   ....*....|....*....|.
gi 28573157    757 STQIALSDEESWYRKLRDSID 777
Cdd:pfam00625  160 DVIIVNDDLEEAYKKLKEALE 180
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
169-250 9.13e-06

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 45.64  E-value: 9.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157  169 PIKVTLTKGGKKDdYGVVL------GCRLFVKEIsskaREQLNANGYSLQEGDIITRIHNTNCGDtMSLKEAKKIIDGCK 242
Cdd:cd00992    1 VRTVTLRKDPGGG-LGFSLrggkdsGGGIFVSRV----EPGGPAERGGLRVGDRILEVNGVSVEG-LTHEEAVELLKNSG 74

                 ....*...
gi 28573157  243 ERLNLVVL 250
Cdd:cd00992   75 DEVTLTVR 82
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
424-483 1.40e-04

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 46.45  E-value: 1.40e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157    424 GNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQ 483
Cdd:TIGR02037  359 GDVKGVVVTKVVSGSPAARAGLQPGDVILSVNQQPVSSVAELRKVLARAKKGGRVALLIL 418
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
56-108 1.47e-03

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 43.09  E-value: 1.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28573157   56 VSDVLKGGPAE-DRLQVNDRIISVNGVSLENVEYATAVQVLR-DSGNTVQLVVKR 108
Cdd:COG0793  116 VVSPIDGSPAAkAGIKPGDVIIKIDGKSVGGVSLDEAVKLIRgKPGTKVTLTILR 170
 
Name Accession Description Interval E-value
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
604-780 1.21e-40

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 148.60  E-value: 1.21e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     604 NWDDVVFSDSISKFP-AYERVVLRHPGFVRPVVLFGpvSDLARERlAKDFPDKFSTPLQDDdkSAATSGKCRIVRLSNIR 682
Cdd:smart00072    3 VGKGTLLAELIQEIPdAFERVVSHTTRPPRPGEVNG--VDYHFVS-KEEFEDDIKSGLFLE--WGEYEGNYYGTSKETIR 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     683 DVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLK-TDSKHVIKQLRHGLPKAAHKSSKKlLEQCQKLERVWsHIFSTQIA 761
Cdd:smart00072   78 QVAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIApPSSEELERRLRQRGTETSERIQKR-LAAAQKEAQEY-HLFDYVIV 155
                           170
                    ....*....|....*....
gi 28573157     762 LSDEESWYRKLRDSIDLQQ 780
Cdd:smart00072  156 NDDLEDAYEELKEILEAEQ 174
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
502-563 5.11e-35

Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO proteins are scaffolding proteins that associate with each other and with other proteins of the tight junction, zonula adherens, and gap junctions. They play roles in regulating cytoskeletal dynamics at these cell junctions. They are considered members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. Vertebrates contain three ZO proteins (ZO-1, ZO-2, and ZO-3) with redundant and non-redundant roles. They contain three PDZ domains, followed by SH3 and GuK domains; in addition, ZO-1 and ZO-2 contains a proline-rich (PR) actin binding domain at the C-terminus while ZO-3 contains this PR domain between the second and third PDZ domains. The C-terminal regions of the three ZO proteins are unique. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212793  Cd Length: 62  Bit Score: 128.18  E-value: 5.11e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28573157  502 HIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAE 563
Cdd:cd11859    1 YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGTVGSWQAVRVGRNHQELERGVIPNKSRAE 62
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
1959-2046 1.56e-28

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 425872  Cd Length: 96  Bit Score: 110.68  E-value: 1.56e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157   1959 SRGFFDSNGGTLADKLWHVSLQIPPGAIPAGVRQEIYFTVSDPRMgqavggPPLDMENGETMLSPLVMCGPQGLEFLVPV 2038
Cdd:pfam00791    1 ASGLFDSRGGRLVLPNSGVSLLIPPGAIPEGTRIEIYLAVLRDDT------SRPPLEEGETLLSPVVECGPPGLKFLKPV 74

                   ....*...
gi 28573157   2039 TLNIPHCA 2046
Cdd:pfam00791   75 ILEIPHCA 82
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
1957-2046 1.20e-22

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 94.34  E-value: 1.20e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157    1957 STSRGFFDSNGGTLADKLWHVSLQIPPGAIPAGVRQEIYFTVSDPRMGQavggPPldMENGETMLSPLVMCGPQGLEFLV 2036
Cdd:smart00218    3 FLVSGTFDARGGRLRGPRTGVRLIIPPGAIPQGTRYTCYLVVHKTLSTP----PP--LEEGETLLSPVVECGPHGALFLR 76
                            90
                    ....*....|
gi 28573157    2037 PVTLNIPHCA 2046
Cdd:smart00218   77 PVILEVPHCA 86
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
22-107 7.73e-21

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 88.39  E-value: 7.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157   22 HTVAVTRVPGYGFGIAVSGGRDNphfangDPSIAVSDVLKGGPAED-RLQVNDRIISVNGVSLENVEYATAVQVLRDSGN 100
Cdd:cd00992    2 RTVTLRKDPGGGLGFSLRGGKDS------GGGIFVSRVEPGGPAERgGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGD 75

                 ....*..
gi 28573157  101 TVQLVVK 107
Cdd:cd00992   76 EVTLTVR 82
SH3_ZO-1 cd12026
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ...
499-563 9.76e-21

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-1 plays an essential role in embryonic development. It regulates the assembly and dynamics of the cortical cytoskeleton at cell-cell junctions. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-1 is the largest of the three ZO proteins and contains an actin-binding region and domains of unknown function designated alpha and ZU5. The SH3 domain of ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212959  Cd Length: 65  Bit Score: 87.44  E-value: 9.76e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28573157  499 DSFHIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAE 563
Cdd:cd12026    1 DSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNKNRAE 65
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
23-107 3.12e-19

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 83.87  E-value: 3.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     23 TVAVTRVPGYGFGIAVSGGRDNphfanGDPSIAVSDVLKGGPAE-DRLQVNDRIISVNGVSLENVEYATAVQVLRDSGNT 101
Cdd:pfam00595    1 QVTLEKDGRGGLGFSLKGGSDQ-----GDPGIFVSEVLPGGAAEaGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGK 75

                   ....*.
gi 28573157    102 VQLVVK 107
Cdd:pfam00595   76 VTLTIL 81
SH3_ZO-2 cd12027
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a ...
498-563 8.68e-19

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-2 plays an essential role in embryonic development. It is critical for the blood-testis barrier integrity and male fertility. It also regulates the expression of cyclin D1 and cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-2 contains an actin-binding region and a domain of unknown function designated beta. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212960  Cd Length: 63  Bit Score: 81.89  E-value: 8.68e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28573157  498 GDSFHIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGrghQEMQRGVIPNKSRAE 563
Cdd:cd12027    1 GDSFFIRTHFEYEKELPQSLAFTRGEIFRVVDTLYDGKLGNWLAVRIG---NELEKGLIPNKSRAE 63
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
406-483 4.50e-18

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 80.69  E-value: 4.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157  406 PRFISFQKE--GSVGIRLTGGNEA--GIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLI 481
Cdd:cd00992    1 VRTVTLRKDpgGGLGFSLRGGKDSggGIFVSRVEPGGPAERGGLRVGDRILEVNGVSVEGLTHEEAVELLKNSGDEVTLT 80

                 ..
gi 28573157  482 VQ 483
Cdd:cd00992   81 VR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
405-486 7.46e-18

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: 80.12  E-value: 7.46e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157     405 EPRFISFQKE-GSVGIRLTGGNE--AGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLI 481
Cdd:smart00228    1 EPRLVELEKGgGGLGFSLVGGKDegGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLT 80

                    ....*
gi 28573157     482 VQYCK 486
Cdd:smart00228   81 VLRGG 85
SH3_ZO-3 cd12028
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ...
499-563 8.67e-18

Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a scaffolding protein that associates with other ZO proteins and other proteins of the tight junction, zonula adherens, and gap junctions. ZO proteins play roles in regulating cytoskeletal dynamics at these cell junctions. ZO-3 is critical for epidermal barrier function. It regulates cyclin D1-dependent cell proliferation. It is considered a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. The C-terminal region of ZO-3 is the smallest of the three ZO proteins. The SH3 domain of the related protein ZO-1 has been shown to bind ZONAB, ZAK, afadin, and Galpha12. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212961  Cd Length: 65  Bit Score: 79.14  E-value: 8.67e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28573157  499 DSFHIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAE 563
Cdd:cd12028    1 DSFYIRTHFDYEPDPPSGLSFTRGEVFHVLDTMHRGKLGSWLAVRMGRDLREMEKGIIPNQSRAE 65
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
20-109 2.33e-17

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: 78.57  E-value: 2.33e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157      20 EYHTVAVTRVPGyGFGIAVSGGRDNPHFangdpsIAVSDVLKGGPAE-DRLQVNDRIISVNGVSLENVEYATAVQVLRDS 98
Cdd:smart00228    1 EPRLVELEKGGG-GLGFSLVGGKDEGGG------VVVSSVVPGSPAAkAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
                            90
                    ....*....|.
gi 28573157      99 GNTVQLVVKRR 109
Cdd:smart00228   74 GGKVTLTVLRG 84
PDZ pfam00595
PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.
409-483 2.45e-14

PDZ domain (Also known as DHR or GLGF); PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 70.00  E-value: 2.45e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28573157    409 ISFQKEGSVGIRLTGGNEA---GIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQ 483
Cdd:pfam00595    4 LEKDGRGGLGFSLKGGSDQgdpGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
415-468 2.03e-12

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 63.86  E-value: 2.03e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 28573157  415 GSVGIRLTGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAV 468
Cdd:cd00136    1 GGLGFSIRGGTEGGVVVLSVEPGSPAERAGLQAGDVILAVNGTDVKNLTLEDVA 54
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
415-471 5.37e-09

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 54.92  E-value: 5.37e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 28573157  415 GSVGIRLtGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFL 471
Cdd:cd00988    2 GGIGLEL-KYDDGGLVITSVLPGSPAAKAGIKAGDIIVAIDGEPVDGLSLEDVVKLL 57
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
502-564 5.40e-09

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 53.75  E-value: 5.40e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28573157    502 HIKTHFHCDNPSKGEMAFKAGDVFRVIDTlhnGVVGSWQVLKIGRghqemqRGVIPNKSRAEE 564
Cdd:pfam07653    1 YGRVIFDYVGTDKNGLTLKKGDVVKVLGK---DNDGWWEGETGGR------VGLVPSTAVEEI 54
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
514-564 1.31e-08

Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein that is located at sites of cell-cell contact and is involved in the maintenance of cell shape and polarity. Mutations in the DLG5 gene are associated with Crohn's disease (CD) and inflammatory bowel disease (IBD). DLG5 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG5 contains 4 PDZ domains as well as an N-terminal domain of unknown function. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212794  Cd Length: 63  Bit Score: 53.11  E-value: 1.31e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 28573157  514 KGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAEE 564
Cdd:cd11860   13 EDELSFKKDDILYVDNTMFNGVFGQWRAWLVDEEGRKRKCGIIPSKYKVEE 63
PDZ cd00136
PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). ...
33-107 1.41e-08

PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. Heterodimerization through PDZ-PDZ domain interactions adds to the domain's versatility, and PDZ domain-mediated interactions may be modulated dynamically through target phosphorylation. Some PDZ domains play a role in scaffolding supramolecular complexes. PDZ domains are found in diverse signaling proteins in bacteria, archebacteria, and eurkayotes. This CD contains two distinct structural subgroups with either a N- or C-terminal beta-strand forming the peptide-binding groove base. The circular permutation placing the strand on the N-terminus appears to be found in Eumetazoa only, while the C-terminal variant is found in all three kingdoms of life, and seems to co-occur with protease domains. PDZ domains have been named after PSD95(post synaptic density protein), DlgA (Drosophila disc large tumor suppressor), and ZO1, a mammalian tight junction protein.


Pssm-ID: 238080 [Multi-domain]  Cd Length: 70  Bit Score: 53.08  E-value: 1.41e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28573157   33 GFGIAVSGGRDNPhfangdpsIAVSDVLKGGPAED-RLQVNDRIISVNGVSLENVEYATAVQVLRDS-GNTVQLVVK 107
Cdd:cd00136    2 GLGFSIRGGTEGG--------VVVLSVEPGSPAERaGLQAGDVILAVNGTDVKNLTLEDVAELLKKEvGEKVTLTVR 70
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
415-471 1.69e-07

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 55.80  E-value: 1.69e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 28573157  415 GSVGIRLTGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFL 471
Cdd:COG0793  100 GGIGIELQMEDIGGVKVVSPIDGSPAAKAGIKPGDVIIKIDGKSVGGVSLDEAVKLI 156
Guanylate_kin pfam00625
Guanylate kinase;
678-777 1.85e-07

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 53.15  E-value: 1.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157    678 LSNIRDVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLKTDSKHVIKQLRHGLPKaahKSSKKLLEQCQKLERVWSH-IF 756
Cdd:pfam00625   83 VETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGK---EQEEKINKRMAAAEQEFQHyEF 159
                           90       100
                   ....*....|....*....|.
gi 28573157    757 STQIALSDEESWYRKLRDSID 777
Cdd:pfam00625  160 DVIIVNDDLEEAYKKLKEALE 180
PDZ_CTP_protease cd00988
PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in ...
56-111 2.57e-07

PDZ domain of C-terminal processing-, tail-specific-, and tricorn proteases, which function in posttranslational protein processing, maturation, and disassembly or degradation, in Bacteria, Archaea, and plant chloroplasts. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238488 [Multi-domain]  Cd Length: 85  Bit Score: 49.92  E-value: 2.57e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 28573157   56 VSDVLKGGPAEDR-LQVNDRIISVNGVSLENVEYATAVQVLR-DSGNTVQLVVKRRVP 111
Cdd:cd00988   17 ITSVLPGSPAAKAgIKAGDIIVAIDGEPVDGLSLEDVVKLLRgKAGTKVRLTLKRGDG 74
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
420-483 2.79e-07

PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 49.95  E-value: 2.79e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28573157  420 RLTGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQ 483
Cdd:cd00987   17 ELGLKDTKGVLVASVDPGSPAAKAGLKPGDVILAVNGKPVKSVADLRRALAELKPGDKVTLTVL 80
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
56-108 2.56e-06

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 46.37  E-value: 2.56e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 28573157     56 VSDVLKGGPAEDR-LQVNDRIISVNGVSLENVEyaTAVQVLRDSGNT-VQLVVKR 108
Cdd:pfam17820    2 VTAVVPGSPAERAgLRVGDVILAVNGKPVRSLE--DVARLLQGSAGEsVTLTVRR 54
PDZ_signaling cd00992
PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. ...
169-250 9.13e-06

PDZ domain found in a variety of Eumetazoan signaling molecules, often in tandem arrangements. May be responsible for specific protein-protein interactions, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of PDZ domains an N-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in proteases.


Pssm-ID: 238492 [Multi-domain]  Cd Length: 82  Bit Score: 45.64  E-value: 9.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157  169 PIKVTLTKGGKKDdYGVVL------GCRLFVKEIsskaREQLNANGYSLQEGDIITRIHNTNCGDtMSLKEAKKIIDGCK 242
Cdd:cd00992    1 VRTVTLRKDPGGG-LGFSLrggkdsGGGIFVSRV----EPGGPAERGGLRVGDRILEVNGVSVEG-LTHEEAVELLKNSG 74

                 ....*...
gi 28573157  243 ERLNLVVL 250
Cdd:cd00992   75 DEVTLTVR 82
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
430-472 1.86e-05

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 43.67  E-value: 1.86e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 28573157    430 FVTAVQPGSPASLQGLMPGDKILKVNDMDmngVTREEAVLFLL 472
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGKP---VRSLEDVARLL 40
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
415-456 2.46e-05

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 44.15  E-value: 2.46e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 28573157  415 GSVGIRLtGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVND 456
Cdd:cd00989    1 AILGFVP-GGPPIEPVIGEVVPGSPAAKAGLKAGDRILAING 41
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
426-480 5.97e-05

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223343 [Multi-domain]  Cd Length: 347  Bit Score: 47.58  E-value: 5.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28573157  426 EAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDL 480
Cdd:COG0265  269 AAGAVVLGVLPGSPAAKAGIKAGDIITAVNGKPVASLSDLVAAVASNRPGDEVAL 323
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
424-483 1.40e-04

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 46.45  E-value: 1.40e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573157    424 GNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQ 483
Cdd:TIGR02037  359 GDVKGVVVTKVVSGSPAARAGLQPGDVILSVNQQPVSSVAELRKVLARAKKGGRVALLIL 418
PDZ_serine_protease cd00987
PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins ...
56-108 1.85e-04

PDZ domain of trypsin-like serine proteases, such as DegP/HtrA, which are oligomeric proteins involved in heat-shock response, chaperone function, and apoptosis. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238487 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 1.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 28573157   56 VSDVLKGGPAEDR-LQVNDRIISVNGVSLENVeyATAVQVLRDS--GNTVQLVVKR 108
Cdd:cd00987   28 VASVDPGSPAAKAgLKPGDVILAVNGKPVKSV--ADLRRALAELkpGDKVTLTVLR 81
PDZ_LON_protease cd00986
PDZ domain of ATP-dependent LON serine proteases. Most PDZ domains bind C-terminal ...
54-108 3.21e-04

PDZ domain of ATP-dependent LON serine proteases. Most PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this bacterial subfamily of protease-associated PDZ domains a C-terminal beta-strand is thought to form the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238486 [Multi-domain]  Cd Length: 79  Bit Score: 41.29  E-value: 3.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 28573157   54 IAVSDVLKGGPAEDRLQVNDRIISVNGVSLEN----VEYATAvqvlRDSGNTVQLVVKR 108
Cdd:cd00986   10 VYVTSVVEGMPAAGKLKAGDHIIAVDGKPFKEaeelIDYIQS----KKEGDTVKLKVKR 64
PDZ_metalloprotease cd00989
PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or ...
56-108 4.30e-04

PDZ domain of bacterial and plant zinc metalloprotases, presumably membrane-associated or integral membrane proteases, which may be involved in signalling and regulatory mechanisms. May be responsible for substrate recognition and/or binding, as most PDZ domains bind C-terminal polypeptides, and binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. In this subfamily of protease-associated PDZ domains a C-terminal beta-strand forms the peptide-binding groove base, a circular permutation with respect to PDZ domains found in Eumetazoan signaling proteins.


Pssm-ID: 238489 [Multi-domain]  Cd Length: 79  Bit Score: 40.68  E-value: 4.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28573157   56 VSDVLKGGPAEDR-LQVNDRIISVNGVSLENVEyaTAVQVLRDS-GNTVQLVVKR 108
Cdd:cd00989   16 IGEVVPGSPAAKAgLKAGDRILAINGQKIKSWE--DLVDAVQENpGKPLTLTVER 68
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
56-108 1.47e-03

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223864 [Multi-domain]  Cd Length: 406  Bit Score: 43.09  E-value: 1.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28573157   56 VSDVLKGGPAE-DRLQVNDRIISVNGVSLENVEYATAVQVLR-DSGNTVQLVVKR 108
Cdd:COG0793  116 VVSPIDGSPAAkAGIKPGDVIIKIDGKSVGGVSLDEAVKLIRgKPGTKVTLTILR 170
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
408-468 2.47e-03

C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair]


Pssm-ID: 272970 [Multi-domain]  Cd Length: 334  Bit Score: 42.35  E-value: 2.47e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28573157    408 FISFQKEGS-----VGIRLtGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAV 468
Cdd:TIGR00225   39 AKSFSETTSgslegIGIQV-GMDDGKIVIVSPFEGSPAEKAGIKPGDKIIKINGKSVAGMSLDDAV 103
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
428-460 2.76e-03

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 42.59  E-value: 2.76e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 28573157    428 GIFVTAVQPGSPASLQGLMPGDKILKVNDMDMN 460
Cdd:TIGR02037  258 GALVAQVLPGSPAEKAGLKAGDVITSVNGKPIS 290
PDZ_2 pfam13180
PDZ domain;
47-109 4.21e-03

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 37.64  E-value: 4.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28573157     47 FANGDPSIAVSDVLKGGPAEDR-LQVNDRIISVNGV---SLENVEYAtavqVLRDS-GNTVQLVVKRR 109
Cdd:pfam13180    1 FVDLEGGVVVVSVKSSGPAAKAgLKAGDVILSIDGRkinDLTDLESA----LYGHKpGDTVTLQVYRD 64
PDZ_2 pfam13180
PDZ domain;
425-456 4.97e-03

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 37.64  E-value: 4.97e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 28573157    425 NEAGIFVTAVQPGSPASLQGLMPGDKILKVND 456
Cdd:pfam13180    4 LEGGVVVVSVKSSGPAAKAGLKAGDVILSIDG 35
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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