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Conserved domains on  [gi|300669666|sp|Q8TF72|]
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RecName: Full=Protein Shroom3; AltName: Full=Shroom-related protein; Short=hShrmL

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
1670-1956 5.32e-146

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


:

Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 453.64  E-value: 5.32e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  1670 ALAKEIVHQDKSLADILDPDSRLKTTMDLMEGLFPRDVNLLKENSVKRKAIQRTVsssgcEGKRNEDKEAVSMLVNCPAY 1749
Cdd:pfam08687    1 ELVKELVPKDKSLADILDPKPSRKTTMDLMEGLFPEDTLRAMKPDLGEAYKKAPS-----EEGSEEEASGTSSLSSCSAY 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  1750 YSVSAPKAELLNKIKEM--------PAEVNEEEEQADVNEKKAELIGSLTHKLETLQEAKGSLLTDIKLNNALGEEVEAL 1821
Cdd:pfam08687   76 YTTSAPKAELLTKMKDLttlpspdqPEEQGEEELDNDLQQKKVELIESLQRKLQVLREEQEALQEEIQANAALGAEVEAL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  1822 ISELCKPNEFDKYRMFIGDLDKVVNLLLSLSGRLARVENVLSGLGEDASNEERSSLYEKRKILAGQHEDARELKENLDRR 1901
Cdd:pfam08687  156 VQEVCKPNELEKYRMFIGDLEKVVSLLLSLSGRLARVENALSSLDSDADAEERQSLLEKRRLLLRQLEDAKELKENLDRR 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 300669666  1902 ERVVLGILANYLSEEQLQDYQHFVKMKSTLLIEQRKLDDKIKLGQEQVKCLLESL 1956
Cdd:pfam08687  236 ERVVSGILARYLTAEQLQDYRHFVKMKAALLIEQRELDEKIKLGEEQLKALKESL 290
ASD1 pfam08688
Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which ...
884-1066 3.45e-67

Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure. ASD1 has been implicated directly in F-actin binding.


:

Pssm-ID: 462562 [Multi-domain]  Cd Length: 179  Bit Score: 224.91  E-value: 3.45e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   884 RLLRSQSTFQLSSEPEREPEWRDRPGSPESPLLDAPFSRAYRNSIKDAQSRVLGATSFRRRDLELGAPVASRSW--RPRP 961
Cdd:pfam08688    1 LLQRSKSTFQLEGEDEAEWSWRRPRGDEPMSDADGSFNRAYREKLKDAQSRVLRATSFRRRDLQPSVPPVPWHLssRPRP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   962 SSAHVGLRSPEASASASPHTPRERHSVTPAEGDlaRPVPPAARRGARRRLTPEQKKRSYSEPEKMNEVGIVEEAEPAPLG 1041
Cdd:pfam08688   81 ASAHLRSPEAPISASPSPHTPRERHSVTPGDRL--AGPPAVRRIGGRKRLTAEQKKRSYSEPEKMNEVGVSPEPEPAPAP 158
                          170       180
                   ....*....|....*....|....*
gi 300669666  1042 PqrngMRFPESSVADRRRLFERDGK 1066
Cdd:pfam08688  159 H----FMFPEGSVADRRKFFERRGK 179
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
27-108 2.75e-46

PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). 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 shroom2,3,4-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: 467232 [Multi-domain]  Cd Length: 82  Bit Score: 160.97  E-value: 2.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   27 YLEAFLEGGAPWGFTLKGGLEHGEPLIISKVEEGGKADTlSSKLQAGDEVVHINEVTLSSSRKEAVSLVKGSYKTLRLVV 106
Cdd:cd06750     2 LIEVQLQGGAPWGFTLKGGLEHGEPLVISKIEEGGKAAS-VGKLQVGDEVVNINGVPLSGSRQEAIQLVKGSHKTLKLVV 80

                  ..
gi 300669666  107 RR 108
Cdd:cd06750    81 RR 82
PHA03247 super family cl33720
large tegument protein UL36; Provisional
959-1521 3.13e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  959 PRPSSAHVGLRSPEASASASPHTPRerhsvTPAE--GDLARPVPPAARRGARRRLTPEQKKRSysepEKMNEVGiveEAE 1036
Cdd:PHA03247 2575 PRPSEPAVTSRARRPDAPPQSARPR-----APVDdrGDPRGPAPPSPLPPDTHAPDPPPPSPS----PAANEPD---PHP 2642
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1037 PAPLGPQRNGMRFPESSVADRRRLFERDGKACSTLS-LSGPelkqfqqsaladyiqRKTGKRPTSAAGCSLQEPGPlrer 1115
Cdd:PHA03247 2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSpPQRP---------------RRRAARPTVGSLTSLADPPP---- 2703
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1116 aQSAYLQPGPAALEGSGLASASSLSSLREPSLQPRREATLLPATVAETQQAPRDRSSSFAGGRRLGERRRGDLLSGAngg 1195
Cdd:PHA03247 2704 -PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP--- 2779
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1196 trgtqrgdeTPREPSSWGARAgkSMSAEDLLERSDVLAGPVHVRSRSSPATADKRQDVLLGqdsgfglvkdPCYLAGPGS 1275
Cdd:PHA03247 2780 ---------PRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP----------PPTSAQPTA 2838
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1276 RSLSCSErgQEEMLPLFHHLTPrwgGSGCKAIGDSSVPSECPGTLDHQ--RQASRTPCPRPPLAGTQGLVTDTRAAPLTP 1353
Cdd:PHA03247 2839 PPPPPGP--PPPSLPLGGSVAP---GGDVRRRPPSRSPAAKPAAPARPpvRRLARPAVSRSTESFALPPDQPERPPQPQA 2913
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1354 IGTPLPSAIPSGYCSQDGQTGRQPLPPYTPAMMHRSNGHTLTQPPGPRGCEGdGPEHGVEEGTRKRVSLPQWPPPSRAKW 1433
Cdd:PHA03247 2914 PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLG-ALVPGRVAVPRFRVPQPAPSREAPASS 2992
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1434 AHAAREDSLP-----------EESSAPDFANLKhyqkqQSLPSLCSTSDPDTPLGAPSTPGRISLrisESVLRDSPPPHE 1502
Cdd:PHA03247 2993 TPPLTGHSLSrvsswasslalHEETDPPPVSLK-----QTLWPPDDTEDSDADSLFDSDSERSDL---EALDPLPPEPHD 3064
                         570
                  ....*....|....*....
gi 300669666 1503 DYEDEVFVRDPHPKATSSP 1521
Cdd:PHA03247 3065 PFAHEPDPATPEAGARESP 3083
 
Name Accession Description Interval E-value
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
1670-1956 5.32e-146

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 453.64  E-value: 5.32e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  1670 ALAKEIVHQDKSLADILDPDSRLKTTMDLMEGLFPRDVNLLKENSVKRKAIQRTVsssgcEGKRNEDKEAVSMLVNCPAY 1749
Cdd:pfam08687    1 ELVKELVPKDKSLADILDPKPSRKTTMDLMEGLFPEDTLRAMKPDLGEAYKKAPS-----EEGSEEEASGTSSLSSCSAY 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  1750 YSVSAPKAELLNKIKEM--------PAEVNEEEEQADVNEKKAELIGSLTHKLETLQEAKGSLLTDIKLNNALGEEVEAL 1821
Cdd:pfam08687   76 YTTSAPKAELLTKMKDLttlpspdqPEEQGEEELDNDLQQKKVELIESLQRKLQVLREEQEALQEEIQANAALGAEVEAL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  1822 ISELCKPNEFDKYRMFIGDLDKVVNLLLSLSGRLARVENVLSGLGEDASNEERSSLYEKRKILAGQHEDARELKENLDRR 1901
Cdd:pfam08687  156 VQEVCKPNELEKYRMFIGDLEKVVSLLLSLSGRLARVENALSSLDSDADAEERQSLLEKRRLLLRQLEDAKELKENLDRR 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 300669666  1902 ERVVLGILANYLSEEQLQDYQHFVKMKSTLLIEQRKLDDKIKLGQEQVKCLLESL 1956
Cdd:pfam08687  236 ERVVSGILARYLTAEQLQDYRHFVKMKAALLIEQRELDEKIKLGEEQLKALKESL 290
ASD1 pfam08688
Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which ...
884-1066 3.45e-67

Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure. ASD1 has been implicated directly in F-actin binding.


Pssm-ID: 462562 [Multi-domain]  Cd Length: 179  Bit Score: 224.91  E-value: 3.45e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   884 RLLRSQSTFQLSSEPEREPEWRDRPGSPESPLLDAPFSRAYRNSIKDAQSRVLGATSFRRRDLELGAPVASRSW--RPRP 961
Cdd:pfam08688    1 LLQRSKSTFQLEGEDEAEWSWRRPRGDEPMSDADGSFNRAYREKLKDAQSRVLRATSFRRRDLQPSVPPVPWHLssRPRP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   962 SSAHVGLRSPEASASASPHTPRERHSVTPAEGDlaRPVPPAARRGARRRLTPEQKKRSYSEPEKMNEVGIVEEAEPAPLG 1041
Cdd:pfam08688   81 ASAHLRSPEAPISASPSPHTPRERHSVTPGDRL--AGPPAVRRIGGRKRLTAEQKKRSYSEPEKMNEVGVSPEPEPAPAP 158
                          170       180
                   ....*....|....*....|....*
gi 300669666  1042 PqrngMRFPESSVADRRRLFERDGK 1066
Cdd:pfam08688  159 H----FMFPEGSVADRRKFFERRGK 179
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
27-108 2.75e-46

PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). 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 shroom2,3,4-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: 467232 [Multi-domain]  Cd Length: 82  Bit Score: 160.97  E-value: 2.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   27 YLEAFLEGGAPWGFTLKGGLEHGEPLIISKVEEGGKADTlSSKLQAGDEVVHINEVTLSSSRKEAVSLVKGSYKTLRLVV 106
Cdd:cd06750     2 LIEVQLQGGAPWGFTLKGGLEHGEPLVISKIEEGGKAAS-VGKLQVGDEVVNINGVPLSGSRQEAIQLVKGSHKTLKLVV 80

                  ..
gi 300669666  107 RR 108
Cdd:cd06750    81 RR 82
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
34-109 5.19e-12

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: 63.55  E-value: 5.19e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669666     34 GGAPWGFTLKGGLEHGEPLIISKVEEGGKADTlsSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVVRRD 109
Cdd:smart00228   10 GGGGLGFSLVGGKDEGGGVVVSSVVPGSPAAK--AGLRVGDVILEVNGTSVEGlTHLEAVDLLKKAGGKVTLTVLRG 84
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
31-107 4.31e-09

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 54.98  E-value: 4.31e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300669666    31 FLEGGAPWGFTLKGGLEHGE-PLIISKVEEGGKADTlsSKLQAGDEVVHINEVTLSSSRKE-AVSLVKGSYKTLRLVVR 107
Cdd:pfam00595    5 EKDGRGGLGFSLKGGSDQGDpGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEeAVLALKGSGGKVTLTIL 81
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1756-1942 5.68e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 5.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1756 KAELLNKIKEMPAEVNE-EEEQADVN------EKKAELIGSLTHKLETLQEAKGSLLTDIKLNNALGEEVEALISEL--- 1825
Cdd:PRK03918  202 LEEVLREINEISSELPElREELEKLEkevkelEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeek 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1826 ------CKPNEfDKYRMFIGDLDKVVNLLLSLSGRLARVENVLSGLGE---DASN---------EERSSLYEKRKILAGQ 1887
Cdd:PRK03918  282 vkelkeLKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEErikELEEkeerleelkKKLKELEKRLEELEER 360
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 300669666 1888 H---EDARELKENLDR-RERvvlgiLANYLSEEQLQDYQHFVKMKSTLLIEQRKLDDKI 1942
Cdd:PRK03918  361 HelyEEAKAKKEELERlKKR-----LTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
PHA03247 PHA03247
large tegument protein UL36; Provisional
959-1521 3.13e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  959 PRPSSAHVGLRSPEASASASPHTPRerhsvTPAE--GDLARPVPPAARRGARRRLTPEQKKRSysepEKMNEVGiveEAE 1036
Cdd:PHA03247 2575 PRPSEPAVTSRARRPDAPPQSARPR-----APVDdrGDPRGPAPPSPLPPDTHAPDPPPPSPS----PAANEPD---PHP 2642
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1037 PAPLGPQRNGMRFPESSVADRRRLFERDGKACSTLS-LSGPelkqfqqsaladyiqRKTGKRPTSAAGCSLQEPGPlrer 1115
Cdd:PHA03247 2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSpPQRP---------------RRRAARPTVGSLTSLADPPP---- 2703
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1116 aQSAYLQPGPAALEGSGLASASSLSSLREPSLQPRREATLLPATVAETQQAPRDRSSSFAGGRRLGERRRGDLLSGAngg 1195
Cdd:PHA03247 2704 -PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP--- 2779
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1196 trgtqrgdeTPREPSSWGARAgkSMSAEDLLERSDVLAGPVHVRSRSSPATADKRQDVLLGqdsgfglvkdPCYLAGPGS 1275
Cdd:PHA03247 2780 ---------PRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP----------PPTSAQPTA 2838
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1276 RSLSCSErgQEEMLPLFHHLTPrwgGSGCKAIGDSSVPSECPGTLDHQ--RQASRTPCPRPPLAGTQGLVTDTRAAPLTP 1353
Cdd:PHA03247 2839 PPPPPGP--PPPSLPLGGSVAP---GGDVRRRPPSRSPAAKPAAPARPpvRRLARPAVSRSTESFALPPDQPERPPQPQA 2913
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1354 IGTPLPSAIPSGYCSQDGQTGRQPLPPYTPAMMHRSNGHTLTQPPGPRGCEGdGPEHGVEEGTRKRVSLPQWPPPSRAKW 1433
Cdd:PHA03247 2914 PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLG-ALVPGRVAVPRFRVPQPAPSREAPASS 2992
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1434 AHAAREDSLP-----------EESSAPDFANLKhyqkqQSLPSLCSTSDPDTPLGAPSTPGRISLrisESVLRDSPPPHE 1502
Cdd:PHA03247 2993 TPPLTGHSLSrvsswasslalHEETDPPPVSLK-----QTLWPPDDTEDSDADSLFDSDSERSDL---EALDPLPPEPHD 3064
                         570
                  ....*....|....*....
gi 300669666 1503 DYEDEVFVRDPHPKATSSP 1521
Cdd:PHA03247 3065 PFAHEPDPATPEAGARESP 3083
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1748-1903 6.58e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1748 AYYSVSAPKAEL-LNKIKEMPAEVNEEEEQADVNEKKAELIGSLTHKLETLQEAKGSLLTDI-KLNNALG--------EE 1817
Cdd:COG4717    57 ELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELeKLEKLLQllplyqelEA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1818 VEALISELckPNEFDKYRMFIGDLDKVVNLLLSLSGRLARVENVLSGLGEDASNEERSSLYEKRKILAGQHEDARELKEN 1897
Cdd:COG4717   137 LEAELAEL--PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214

                  ....*.
gi 300669666 1898 LDRRER 1903
Cdd:COG4717   215 LEEAQE 220
 
Name Accession Description Interval E-value
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
1670-1956 5.32e-146

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 453.64  E-value: 5.32e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  1670 ALAKEIVHQDKSLADILDPDSRLKTTMDLMEGLFPRDVNLLKENSVKRKAIQRTVsssgcEGKRNEDKEAVSMLVNCPAY 1749
Cdd:pfam08687    1 ELVKELVPKDKSLADILDPKPSRKTTMDLMEGLFPEDTLRAMKPDLGEAYKKAPS-----EEGSEEEASGTSSLSSCSAY 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  1750 YSVSAPKAELLNKIKEM--------PAEVNEEEEQADVNEKKAELIGSLTHKLETLQEAKGSLLTDIKLNNALGEEVEAL 1821
Cdd:pfam08687   76 YTTSAPKAELLTKMKDLttlpspdqPEEQGEEELDNDLQQKKVELIESLQRKLQVLREEQEALQEEIQANAALGAEVEAL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  1822 ISELCKPNEFDKYRMFIGDLDKVVNLLLSLSGRLARVENVLSGLGEDASNEERSSLYEKRKILAGQHEDARELKENLDRR 1901
Cdd:pfam08687  156 VQEVCKPNELEKYRMFIGDLEKVVSLLLSLSGRLARVENALSSLDSDADAEERQSLLEKRRLLLRQLEDAKELKENLDRR 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 300669666  1902 ERVVLGILANYLSEEQLQDYQHFVKMKSTLLIEQRKLDDKIKLGQEQVKCLLESL 1956
Cdd:pfam08687  236 ERVVSGILARYLTAEQLQDYRHFVKMKAALLIEQRELDEKIKLGEEQLKALKESL 290
ASD1 pfam08688
Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which ...
884-1066 3.45e-67

Apx/Shroom domain ASD1; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure. ASD1 has been implicated directly in F-actin binding.


Pssm-ID: 462562 [Multi-domain]  Cd Length: 179  Bit Score: 224.91  E-value: 3.45e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   884 RLLRSQSTFQLSSEPEREPEWRDRPGSPESPLLDAPFSRAYRNSIKDAQSRVLGATSFRRRDLELGAPVASRSW--RPRP 961
Cdd:pfam08688    1 LLQRSKSTFQLEGEDEAEWSWRRPRGDEPMSDADGSFNRAYREKLKDAQSRVLRATSFRRRDLQPSVPPVPWHLssRPRP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   962 SSAHVGLRSPEASASASPHTPRERHSVTPAEGDlaRPVPPAARRGARRRLTPEQKKRSYSEPEKMNEVGIVEEAEPAPLG 1041
Cdd:pfam08688   81 ASAHLRSPEAPISASPSPHTPRERHSVTPGDRL--AGPPAVRRIGGRKRLTAEQKKRSYSEPEKMNEVGVSPEPEPAPAP 158
                          170       180
                   ....*....|....*....|....*
gi 300669666  1042 PqrngMRFPESSVADRRRLFERDGK 1066
Cdd:pfam08688  159 H----FMFPEGSVADRRKFFERRGK 179
PDZ_shroom2_3_4-like cd06750
PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic ...
27-108 2.75e-46

PDZ domain of shroom2, shroom3, shroom4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of shroom2, shroom3, shroom4, and related domains. Shroom family proteins shroom2 (also known as apical-like protein; protein APXL), shroom3 (also known as shroom-related protein), and shroom4 (also known as second homolog of apical protein) are essential regulators of cell morphology during animal development; they regulate cell architecture by directing the subcellular distribution and activation of Rho kinase (ROCK), which results in the localized activation of non-muscle myosin. The interaction between shroom and ROCK is mediated by the shroom domain 2 (SD2). 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 shroom2,3,4-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: 467232 [Multi-domain]  Cd Length: 82  Bit Score: 160.97  E-value: 2.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   27 YLEAFLEGGAPWGFTLKGGLEHGEPLIISKVEEGGKADTlSSKLQAGDEVVHINEVTLSSSRKEAVSLVKGSYKTLRLVV 106
Cdd:cd06750     2 LIEVQLQGGAPWGFTLKGGLEHGEPLVISKIEEGGKAAS-VGKLQVGDEVVNINGVPLSGSRQEAIQLVKGSHKTLKLVV 80

                  ..
gi 300669666  107 RR 108
Cdd:cd06750    81 RR 82
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
32-108 3.73e-16

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). 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 PDLIM-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: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 74.87  E-value: 3.73e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300669666   32 LEGGAPWGFTLKGGLEHGEPLIISKVEEGGKADTlsSKLQAGDEVVHIN-EVTLSSSRKEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06753     4 LSGPAPWGFRLQGGKDFNQPLTISRVTPGGKAAQ--ANLRPGDVILAINgESTEGMTHLEAQNKIKAATGSLSLTLER 79
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
33-107 4.03e-16

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: 74.89  E-value: 4.03e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300669666   33 EGGAPWGFTLKGGLEHGEPLIISKVEEGGKADtLSSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVVR 107
Cdd:cd00136     7 DPGGGLGFSIRGGKDGGGGIFVSRVEPGGPAA-RDGRLRVGDRILEVNGVSLEGlTHEEAVELLKSAGGEVTLTVR 81
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
32-106 1.19e-13

PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. 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 SYNPO2-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: 467264 [Multi-domain]  Cd Length: 78  Bit Score: 67.72  E-value: 1.19e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300669666   32 LEGGAPWGFTLKGGLEHGEPLIISKVEEGGKADTlsSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVV 106
Cdd:cd10820     4 LTGGAPWGFRLQGGSEQKKPLQVAKIRKKSKAAL--AGLCEGDELLSINGKPCADlSHSEAMDLIDSSGDTLQLLI 77
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
34-108 6.17e-13

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: 66.13  E-value: 6.17e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300669666   34 GGAPWGFTLKGGLEHGEPLIISKVEEGGKADTlsSKLQAGDEVVHINEVTLSSS-RKEAVSLVKgSYKTLRLVVRR 108
Cdd:cd06737    11 GPESLGFSVRGGLEHGCGLFVSHVSPGSQADN--KGLRVGDEIVRINGYSISQCtHEEVINLIK-TKKTVSLKVRH 83
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
34-109 5.19e-12

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: 63.55  E-value: 5.19e-12
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669666     34 GGAPWGFTLKGGLEHGEPLIISKVEEGGKADTlsSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVVRRD 109
Cdd:smart00228   10 GGGGLGFSLVGGKDEGGGVVVSSVVPGSPAAK--AGLRVGDVILEVNGTSVEGlTHLEAVDLLKKAGGKVTLTVLRG 84
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
37-108 1.30e-11

PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. 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 Zasp52-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: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 62.16  E-value: 1.30e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300669666   37 PWGFTLKGGLEHGEPLIISKVEEGGKADTlsSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVVRR 108
Cdd:cd23068    12 PWGFRLQGGADFGQPLSIQKVNPGSPADK--AGLRRGDVILRINGTDTSNlTHKQAQDLIKRAGNDLQLTVQR 82
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
39-108 1.35e-10

PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the first PDZ domain of the canonical isoform of PDZD7- isoform 1. 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 PDZD7-like 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: 467269 [Multi-domain]  Cd Length: 84  Bit Score: 59.37  E-value: 1.35e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300669666   39 GFTLKGGLEHGEPLIISKVEEGGKADtlSSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSyKTLRLVVRR 108
Cdd:cd10833    15 GFSVRGGSEHGLGIFVSKVEEGSAAE--RAGLCVGDKITEVNGVSLENiTMSSAVKVLTGS-NRLRMVVRR 82
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
34-108 1.28e-09

PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. 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 MAGI family PDZ5 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: 467217 [Multi-domain]  Cd Length: 84  Bit Score: 56.43  E-value: 1.28e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669666   34 GGAPWGFTLKGGLEHGE-PLIISKVEEGGKADtLSSKLQAGDEVVHIN-EVTLSSSRKEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06735     9 GPKGFGFSIRGGREYNNmPLYVLRLAEDGPAQ-RDGRLRVGDQILEINgESTQGMTHAQAIELIRSGGSVVRLLLRR 84
PDZ2_Scribble-like cd06703
PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
39-108 3.76e-09

PDZ domain 2 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. 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 Scribble-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: 467187 [Multi-domain]  Cd Length: 92  Bit Score: 55.34  E-value: 3.76e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669666   39 GFTLKGGLEH-----GEPLI-ISKVEEGGKADtLSSKLQAGDEVVHINEVTLSSSR-KEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06703    15 GFSIAGGKGStpfrdGDEGIfISRITEGGAAD-RDGKLQVGDRVLSINGVDVTEARhDQAVALLTSSSPTITLVVER 90
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
31-107 4.31e-09

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 54.98  E-value: 4.31e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300669666    31 FLEGGAPWGFTLKGGLEHGE-PLIISKVEEGGKADTlsSKLQAGDEVVHINEVTLSSSRKE-AVSLVKGSYKTLRLVVR 107
Cdd:pfam00595    5 EKDGRGGLGFSLKGGSDQGDpGIFVSEVLPGGAAEA--GGLKVGDRILSINGQDVENMTHEeAVLALKGSGGKVTLTIL 81
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
39-107 9.25e-09

PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. 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 syntrophin-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: 467262 [Multi-domain]  Cd Length: 83  Bit Score: 54.12  E-value: 9.25e-09
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gi 300669666   39 GFTLKGGLEHGEPLIISKVEEGGKADtLSSKLQAGDEVVHINEVTL-SSSRKEAVSLVKGSYKTLRLVVR 107
Cdd:cd06801    14 GISIKGGAEHKMPILISKIFKGQAAD-QTGQLFVGDAILSVNGENLeDATHDEAVQALKNAGDEVTLTVK 82
PDZ_PTPN3-4-like cd06706
PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein ...
39-107 1.99e-08

PDZ domain of tyrosine-protein phosphatase non-receptor type 3 (PTPN3), tyrosine-protein phosphatase non-receptor type 4 (PTNP4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PTPN3, PTPN4 and related domains. PTPN3 (also known as protein-tyrosine phosphatase H1, PTP-H1) has a tumor-suppressive or a tumor-promoting role in many cancers. It serves as a specific phosphatase for the MAP kinase p38gamma; the two interact via their PDZ domains and cooperate to promote Ras-induced oncogenesis. Interaction partners of the PTPN3 PDZ domain include p38gamma and human papillomavirus E6 oncoprotein. PTPN4 (also known as protein-tyrosine phosphatase MEG1) plays a role in immunity, learning, synaptic plasticity or cell homeostasis. p38gamma is also an interaction partner of the PTPN4 PDZ domain: PTPN4 regulates neuronal cell homeostasis by protecting neurons against apoptosis; binding of the C terminus of p38gamma to the PDZ domain of PTPN4, antagonizes the catalytic autoinhibition of PTPN4, leading to cell apoptosis. Other interaction partners of the PTPN4 PDZ domain include glutamate receptor subunit GluN2A, and RABV strain G protein, among others. 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 PTPN3-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: 467190 [Multi-domain]  Cd Length: 90  Bit Score: 53.47  E-value: 1.99e-08
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300669666   39 GFTLKGGLEHGEPLIISKVEEGGKADTLSSKLQAGDEVVHINEVTLSSSRKE-AVSLVKGS----YKTLRLVVR 107
Cdd:cd06706    17 GFNVKGGVDQKMPVIVSRVAPGTPADLCIPRLNEGDQVLLINGRDISEHTHDqVVMFIKASrerhSGELVLLVR 90
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
38-107 2.51e-07

PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. 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 whirlin 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: 467222 [Multi-domain]  Cd Length: 82  Bit Score: 50.05  E-value: 2.51e-07
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300669666   38 WGFTLKGGLEHGEPLIISKVEEGGKADtlSSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSyKTLRLVVR 107
Cdd:cd06740    15 LGFSIRGGAEHGVGIYVSLVEPGSLAE--KEGLRVGDQILRVNDVSFEKvTHAEAVKILRVS-KKLVLSVR 82
PDZ_Lin-7-like cd06796
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
24-107 6.27e-07

PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. 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 Lin-7-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: 467258 [Multi-domain]  Cd Length: 86  Bit Score: 48.97  E-value: 6.27e-07
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gi 300669666   24 RYIYLEAFLEGgapWGFTLKGGLEHGEPLIISKVEEGGKADTlSSKLQAGDEVVHINEVTLSSSRKE-AVSLVKGSYKTL 102
Cdd:cd06796     3 RVVELPKTEEG---LGFNVMGGKEQNSPIYISRIIPGGVADR-HGGLKRGDQLLSVNGVSVEGEHHEkAVELLKAAQGSV 78

                  ....*
gi 300669666  103 RLVVR 107
Cdd:cd06796    79 KLVVR 83
PDZ_GOPC-like cd06800
PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and ...
39-94 1.83e-06

PDZ domain of Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of GOPC and related domains. GOPC, also known as PIST (PDZ domain protein interacting specifically with TC10), FIG (fused in glioblastoma), and CAL (CFTR-associated ligand), regulates the trafficking of a wide array of proteins, including small GTPases, receptors, and cell surface molecules such as cadherin 23 and CFTR. It may regulate CFTR chloride currents and acid-sensing ASIC3 currents by modulating cell surface expression of both channels, and may play a role in autophagy. Interaction partners of the GOPC PDZ domains include: FZD5, FZD8, ASIC3, CFTR, MUC3, ARFRP1, Ggamma13, neuroligin, and Stargazin. 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 GOPC-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: 467261 [Multi-domain]  Cd Length: 83  Bit Score: 47.75  E-value: 1.83e-06
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gi 300669666   39 GFTLKGGLEHGEPLIISKVEEGGKADTlSSKLQAGDEVVHINEVTL-SSSRKEAVSL 94
Cdd:cd06800    14 GISITGGKEHGVPILISEIHEGQPADR-CGGLYVGDAILSVNGIDLrDAKHKEAVTI 69
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
34-107 2.50e-06

PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZD11, and related domains. PDZD11 (also known as ATPase-interacting PDZ protein, plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PISP) is involved in the dynamic assembly of apical junctions (AJs). It is recruited by PLEKHA7 to AJs to promote the efficient junctional recruitment and stabilization of nectins, and the efficient early phases of assembly of AJs in epithelial cells. The PDZD11 PDZ domain binds nectin-1 and nectin-3. PDZD11 also binds to a PDZ binding motif located in the C-terminal tail of the human sodium-dependent multivitamin transporter, to the cytoplasmic tail of the Menkes copper ATPase ATP7A, and to the cytoplasmic tail of all plasma membrane Ca2+-ATPase b-splice variants. 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 PDZD11-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: 467234 [Multi-domain]  Cd Length: 83  Bit Score: 47.31  E-value: 2.50e-06
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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300669666   34 GGAPWGFTLKGGLEHGEPLIISKVEEGGKADTLSskLQAGDEVVHINEVTLSS-SRKEAVSLVKGSyKTLRLVVR 107
Cdd:cd06752     9 PGEQLGFNIRGGKASGLGIFISKVIPDSDAHRLG--LKEGDQILSVNGVDFEDiEHSEAVKVLKTA-REIQMRVR 80
PDZ2_FL-whirlin cd06741
PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
32-108 3.47e-06

PDZ domain 2 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the full-length isoform of whirlin and related domains. Whirlin is an essential protein for developmental pathways in photoreceptor cells of the retina and hair cells of the inner ear. The full-length whirlin isoform has two harmonin N-like domains, three PDZ domains, a proline-rich region, and a PDZ-binding motif. Whirlin isoforms may form different complexes at the periciliary membrane complex (PMC) in photoreceptors, and the stereociliary tip and base in inner ear hair cells. It interacts with ADGRV1 and usherin at the PMC; with SANS and RpgrORF15 at the connecting cilium in photoreceptors; with EPS8, MYO15A, p55, and CASK proteins at the stereociliary tip of inner ear hair cells; and with ADGRV1, usherin, and PDZD7 at the stereociliary base in inner ear hair cells. Mutations in the gene encoding whirlin (WHRN; also known as USH2D and DFNB31), have been found to cause either USH2 subtype (USH2D) or autosomal recessive non-syndromic deafness type 31 (DFNB31). Whirlin is the key protein in the USH2 complex (whirlin, usherin and GPR98) which recruits other USH2 causative proteins at the periciliary membrane in photoreceptors and the ankle link of the stereocilia in hair cells. Whirlin's interaction with espin, another stereociliary protein, may be important for the architecture of the USH2 complex. 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 whirlin 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: 467223 [Multi-domain]  Cd Length: 84  Bit Score: 46.87  E-value: 3.47e-06
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gi 300669666   32 LEGGAPWGFTLKGGLEHGEPLIISKVEEGGKADTlsSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSyKTLRLVVRR 108
Cdd:cd06741     8 VEDGQSLGLMIRGGAEYGLGIYVTGVDPGSVAEN--AGLKVGDQILEVNGRSFLDiTHDEAVKILKSS-KHLIMTVKD 82
PDZ3_Dlg1-2-4-like cd06795
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
39-106 3.47e-06

PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. 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 Dlg-like family PDZ3 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: 467257 [Multi-domain]  Cd Length: 91  Bit Score: 46.96  E-value: 3.47e-06
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gi 300669666   39 GFTLKGGlEHGEPLIISKVEEGGKADtLSSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVV 106
Cdd:cd06795    15 GFNIVGG-EDGEGIFISFILAGGPAD-LSGELRRGDQILSVNGVDLRNaTHEQAAAALKNAGQTVTIIA 81
PDZ2_PDZD7-like cd10834
PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
38-107 1.39e-05

PDZ domain 2 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the second PDZ domain of the canonical isoform of PDZD7- isoform 1. 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 PDZD7-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: 467270 [Multi-domain]  Cd Length: 85  Bit Score: 45.07  E-value: 1.39e-05
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gi 300669666   38 WGFTLKGGLEHGEPLIISKVEEGGKADtlSSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSyKTLRLVVR 107
Cdd:cd10834    15 LGFNIRGGSEYGLGIYVSKVDPGGLAE--QNGIKVGDQILAVNGVSFEDiTHSKAVEVLKSQ-THLMLTIK 82
PDZ7_PDZD2-PDZ4_hPro-IL-16-like cd06763
PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 ...
34-96 1.41e-05

PDZ domain 7 of PDZ domain containing 2 (PDZD2), PDZ domain 4 of human pro-interleukin-16 (isoform 1, 1332 AA), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of PDZD2, also known as KIAA0300, PIN-1, PAPIN, activated in prostate cancer (AIPC) and PDZ domain-containing protein 3 (PDZK3). PDZD2 has seven PDZ domains. PDZD2 is expressed at exceptionally high levels in the pancreas and certain cancer tissues, such as prostate cancer. It promotes the proliferation of insulinoma cells and is upregulated during prostate tumorigenesis. In osteosarcoma (OS), the microRNA miR-363 acts as a tumor suppressor by inhibiting PDZD2. This family include the PDZ domain of the secreted mature form of human interleukin-16 (IL-16); this is the fourth PDZ domain (PDZ4) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16). Precursor IL-16 is cleaved to produce pro-IL-16 and C-terminal mature IL-16. Pro-IL-16 functions as a regulator of T cell growth; mature IL-16 is a CD4 ligand that induces chemotaxis and CD25 expression in CD4+ T cells. IL-16 bioactivity has been closely associated with the progression of several different cancers 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 PDZD2-like family PDZ7 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: 467244 [Multi-domain]  Cd Length: 86  Bit Score: 45.30  E-value: 1.41e-05
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gi 300669666   34 GGAPWGFTLKGGLE--HGE-PLIISKVEEGGKADTlSSKLQAGDEVVHINEVTLSS-SRKEAVSLVK 96
Cdd:cd06763     9 GSAGLGFSLEGGKGspLGDrPLTIKRIFKGGAAEQ-SGVLQVGDEILQINGTSLQGlTRFEAWNIIK 74
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1756-1942 5.68e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 5.68e-05
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gi 300669666 1756 KAELLNKIKEMPAEVNE-EEEQADVN------EKKAELIGSLTHKLETLQEAKGSLLTDIKLNNALGEEVEALISEL--- 1825
Cdd:PRK03918  202 LEEVLREINEISSELPElREELEKLEkevkelEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeek 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1826 ------CKPNEfDKYRMFIGDLDKVVNLLLSLSGRLARVENVLSGLGE---DASN---------EERSSLYEKRKILAGQ 1887
Cdd:PRK03918  282 vkelkeLKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEErikELEEkeerleelkKKLKELEKRLEELEER 360
                         170       180       190       200       210
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gi 300669666 1888 H---EDARELKENLDR-RERvvlgiLANYLSEEQLQDYQHFVKMKSTLLIEQRKLDDKI 1942
Cdd:PRK03918  361 HelyEEAKAKKEELERlKKR-----LTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
PDZ2_GRIP1-2-like cd06681
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
33-109 7.48e-05

PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. 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 GRIP 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: 467169 [Multi-domain]  Cd Length: 89  Bit Score: 43.38  E-value: 7.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   33 EGGAPwGFTLKGGLeHGE-----PLIISKVEEGGKADTlSSKLQAGDEVVHINEVTL-SSSRKEAVSLVKGSYKTLRLVV 106
Cdd:cd06681    10 EGNSF-GFVIRGGA-HEDrnksrPLTVTHVRPGGPADR-EGTIKPGDRLLSVDGISLhGATHAEAMSILKQCGQEATLLI 86

                  ...
gi 300669666  107 RRD 109
Cdd:cd06681    87 EYD 89
PDZ3_MAGI-1_3-like cd06733
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
39-108 1.20e-04

PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. 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 MAGI family PDZ3 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: 467215 [Multi-domain]  Cd Length: 85  Bit Score: 42.60  E-value: 1.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300669666   39 GFTLKGGLEHGEPLIISKVEEGGKADtLSSKLQAGDEVVHINEV-TLSSSRKEAVSLVKGSYKT--LRLVVRR 108
Cdd:cd06733    14 GFRILGGTEEGSQVSIGAIVPGGAAD-LDGRLRTGDELLSVDGVnVVGASHHKVVDLMGNAARNgqVNLTVRR 85
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
36-80 1.34e-04

PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). 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 RapGEF2 and RapGEF6 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: 467237 [Multi-domain]  Cd Length: 83  Bit Score: 42.25  E-value: 1.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 300669666   36 APWGFTLKGGLEHGEPLIISKVEEGGKADTLSskLQAGDEVVHIN 80
Cdd:cd06755    12 SPLHFSLLGGSEKGFGIFVSKVEKGSKAAEAG--LKRGDQILEVN 54
PDZ1_DLG5-like cd06764
PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
39-108 1.92e-04

PDZ domain 1 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. 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 Dlg5-like 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: 467245 [Multi-domain]  Cd Length: 95  Bit Score: 42.39  E-value: 1.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300669666   39 GFTLKGGLE----HGEP-LIISKVEEGGKADtlsSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06764    22 GFDIAGGVNdpqfPGDCsIFVTKVDKGSIAD---GRLRVNDCLLRINDVDLTNkDKKQAIQAVLNGGGVINMVVRR 94
PDZ4_PTPN13-like cd06696
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ...
39-109 1.98e-04

PDZ domain 4 of protein tyrosine 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 4 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)] and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. 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 family PDZ4 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: 467182 [Multi-domain]  Cd Length: 85  Bit Score: 41.91  E-value: 1.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300669666   39 GFTLKGGLEHGEPLIISKVEEGGKADtlsSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVVRRD 109
Cdd:cd06696    17 GFTVTKGKDDNGCYIHDIVQDPAKSD---GRLRPGDRLIMVNGVDVTNmSHTEAVSLLRAAPKEVTLVLGRA 85
PDZ1_ZO1-like cd06727
PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
39-108 2.67e-04

PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of ZO-1, -2, -3 and related domains. Zonula occludens proteins (ZO-1, ZO-2, ZO-3) are multi-PDZ domain proteins involved in the maintenance and biogenesis of multi-protein networks at the cytoplasmic surface of intercellular contacts in epithelial and endothelial cells. They have three N-terminal PDZ domains, PDZ1-3, followed by a Src homology-3 (SH3) domain and a guanylate kinase (GuK)-like domain. Among protein-protein interactions for all ZO proteins is the binding of the first PDZ domain (PDZ1) to the C-termini of claudins, and the homo- and hetero-dimerization of ZO-proteins via their second PDZ domain (PDZ2), which takes place by symmetrical domain swapping of the first two beta-strands of PDZ2. At the cell level, ZO-1 and ZO-2 are involved in polarity maintenance, gene transcription, cell proliferation, and tumor cell metastasis. 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 ZO 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: 467209 [Multi-domain]  Cd Length: 87  Bit Score: 41.49  E-value: 2.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669666   39 GFTLKGGL-----EHGEP-LIISKVEEGGKADtlsSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06727    14 GIAVSGGRdnphfQSGDTsIVISDVLKGGPAE---GKLQENDRVVSVNGVSMENvEHSFAVQILRKCGKTANITVKR 87
PHA03247 PHA03247
large tegument protein UL36; Provisional
959-1521 3.13e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666  959 PRPSSAHVGLRSPEASASASPHTPRerhsvTPAE--GDLARPVPPAARRGARRRLTPEQKKRSysepEKMNEVGiveEAE 1036
Cdd:PHA03247 2575 PRPSEPAVTSRARRPDAPPQSARPR-----APVDdrGDPRGPAPPSPLPPDTHAPDPPPPSPS----PAANEPD---PHP 2642
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1037 PAPLGPQRNGMRFPESSVADRRRLFERDGKACSTLS-LSGPelkqfqqsaladyiqRKTGKRPTSAAGCSLQEPGPlrer 1115
Cdd:PHA03247 2643 PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSpPQRP---------------RRRAARPTVGSLTSLADPPP---- 2703
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1116 aQSAYLQPGPAALEGSGLASASSLSSLREPSLQPRREATLLPATVAETQQAPRDRSSSFAGGRRLGERRRGDLLSGAngg 1195
Cdd:PHA03247 2704 -PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP--- 2779
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1196 trgtqrgdeTPREPSSWGARAgkSMSAEDLLERSDVLAGPVHVRSRSSPATADKRQDVLLGqdsgfglvkdPCYLAGPGS 1275
Cdd:PHA03247 2780 ---------PRRLTRPAVASL--SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP----------PPTSAQPTA 2838
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1276 RSLSCSErgQEEMLPLFHHLTPrwgGSGCKAIGDSSVPSECPGTLDHQ--RQASRTPCPRPPLAGTQGLVTDTRAAPLTP 1353
Cdd:PHA03247 2839 PPPPPGP--PPPSLPLGGSVAP---GGDVRRRPPSRSPAAKPAAPARPpvRRLARPAVSRSTESFALPPDQPERPPQPQA 2913
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1354 IGTPLPSAIPSGYCSQDGQTGRQPLPPYTPAMMHRSNGHTLTQPPGPRGCEGdGPEHGVEEGTRKRVSLPQWPPPSRAKW 1433
Cdd:PHA03247 2914 PPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLG-ALVPGRVAVPRFRVPQPAPSREAPASS 2992
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1434 AHAAREDSLP-----------EESSAPDFANLKhyqkqQSLPSLCSTSDPDTPLGAPSTPGRISLrisESVLRDSPPPHE 1502
Cdd:PHA03247 2993 TPPLTGHSLSrvsswasslalHEETDPPPVSLK-----QTLWPPDDTEDSDADSLFDSDSERSDL---EALDPLPPEPHD 3064
                         570
                  ....*....|....*....
gi 300669666 1503 DYEDEVFVRDPHPKATSSP 1521
Cdd:PHA03247 3065 PFAHEPDPATPEAGARESP 3083
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
35-108 3.27e-04

PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. 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 GRIP family PDZ6 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: 467171 [Multi-domain]  Cd Length: 85  Bit Score: 41.14  E-value: 3.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300669666   35 GAPWGFTLKGGLEHGEPLIISKVEEGGKADTlSSKLQAGDEVVHINEVTLSSSR-KEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06683    12 GGPLGITISGTEEPFDPIVISGLTEGGLAER-TGAIHVGDRILAINGESLRGKPlSEAIHLLQNAGDTVTLKISR 85
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
24-106 3.56e-04

PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. 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 tamalin-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: 467197 [Multi-domain]  Cd Length: 91  Bit Score: 41.45  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   24 RYIYLEAFLEGgaPWGFTLKG-GLEH-GEPLI-----ISKVEEGGKADTlsSKLQAGDEVVHINEV-TLSSSRKEAVSLV 95
Cdd:cd06713     4 RTIILEKQDNE--TFGFEIQTyGLHHkNSNEVemctyVCRVHEDSPAYL--AGLTAGDVILSVNGVsVEGASHQEIVELI 79
                          90
                  ....*....|.
gi 300669666   96 KGSYKTLRLVV 106
Cdd:cd06713    80 RSSGNTLRLET 90
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
39-106 4.57e-04

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: 41.43  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666   39 GFTLKGGLEHGEPL------------IISKVEEGGKADTlsSKLQAGDEVVHIN-EVTLSSSRKEAVSLVKGSYKTLRLV 105
Cdd:cd06746    19 GFVLRGAKAVGPILeftptpafpalqYLESVDPGGVADK--AGLKKGDFLLEINgEDVVKASHEQVVNLIRQSGNTLVLK 96

                  .
gi 300669666  106 V 106
Cdd:cd06746    97 V 97
PDZ2-PTPN13_FRMPD2-like cd06792
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ...
39-108 7.86e-04

PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). 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 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: 467254 [Multi-domain]  Cd Length: 87  Bit Score: 40.27  E-value: 7.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300669666   39 GFTLKGGLEHGEPL---IISKVEEGGKADtLSSKLQAGDEVVHINEVTL-SSSRKEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06792    15 GISVTGGINTSVRHggiYVKSLVPGGAAE-QDGRIQKGDRLLEVNGVSLeGVTHKQAVECLKNAGQVVTLVLER 87
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
39-108 8.86e-04

PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. 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 Scribble-like 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: 467188 [Multi-domain]  Cd Length: 87  Bit Score: 39.95  E-value: 8.86e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669666   39 GFTLKGGL------EHGEPLIISKVEEGGKADtlSSKLQAGDEVVHINEVTL-SSSRKEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06704    13 GISIAGGKgstpykGDDEGIFISRVTEGGPAA--KAGVRVGDKLLEVNGVDLvDADHHEAVEALKNSGNTVTMVVLR 87
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
39-106 1.32e-03

PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). 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 FRMPD1,3,4-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: 467250 [Multi-domain]  Cd Length: 75  Bit Score: 39.15  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300669666   39 GFTLKGGLehgePLIISKVEEGGKADtlsSKLQAGDEVVHINEVTLS-SSRKEAVSLVKGSYKTLRLVV 106
Cdd:cd06769    13 GFVAGSER----PVVVRSVTPGGPSE---GKLLPGDQILKINNEPVEdLPRERVIDLIRECKDSIVLTV 74
PDZ1_MAGI-1_3-like cd06731
PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
39-94 1.44e-03

PDZ domain 1 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. 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 MAGI family PDZ1 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: 467213 [Multi-domain]  Cd Length: 85  Bit Score: 39.50  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300669666   39 GFTLKGGLEHGEPLIISKVEEGGKADtLSSKLQAGDEVVHINEV-TLSSSRKEAVSL 94
Cdd:cd06731    14 GFTIIGGDEPDEFLQIKSVVPDGPAA-LDGKLRTGDVLVSVNDTcVLGYTHADVVKL 69
PDZ2_Dlg1-2-4-like cd06724
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ...
39-106 1.79e-03

PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. 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 Dlg-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: 467207 [Multi-domain]  Cd Length: 85  Bit Score: 39.17  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300669666   39 GFTLKGGL--EH--GEPLI-ISKVEEGGKADTlSSKLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVV 106
Cdd:cd06724    12 GFSIAGGVgnQHipGDNGIyVTKIIEGGAAQK-DGRLQVGDKLLAVNDVSLEEvTHEEAVAALKNTSDVVYLKV 84
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
45-114 1.94e-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: 39.00  E-value: 1.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300669666   45 GLEHGEPLIISKVEEGGKADtlSSKLQAGDEVVHIN-EVTLSSSRKEAVSLVKGSYKT-LRLVVRRDVCTDP 114
Cdd:cd06782     9 GKDDDGYLVVVSPIPGGPAE--KAGIKPGDVIVAVDgESVRGMSLDEVVKLLRGPKGTkVKLTIRRGGEGEP 78
PDZ_RGS12-like cd06710
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ...
34-106 2.63e-03

PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. 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 RGS12-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: 467194 [Multi-domain]  Cd Length: 76  Bit Score: 38.38  E-value: 2.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300669666   34 GGAPWGFTLKGGlehgEPLIISKVEEGGKADtlSSKLQAGDEVVHINEVTLS-SSRKEAVSLVKGSYKTLRLVV 106
Cdd:cd06710     8 GRAGYGFTISGQ----APCVLSCVVRGSPAD--VAGLKAGDQILAVNGINVSkASHEDVVKLIGKCTGVLRLVI 75
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
39-108 3.15e-03

PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of densin, erbin, and related domains. Densin (also known as leucine-rich repeat-containing protein 7, LRRC7, densin-180, protein LAP1) and erbin (also known as densin-180-like protein, Erbb2-interacting protein, protein LAP2) belong to the LAP (leucine-rich repeat and PDZ domain) family of scaffolding proteins that play roles in the maintenance of cell shape and apical-basal polarity. Densin and erbin are components of the excitatory postsynaptic compartment and are regulators of dendritic morphology and postsynaptic structure. The densin PDZ domain binds CaV1.3 alpha1 subunit, delta-catenin, and MAGUIN-1. Binding partners of the erbin PDZ domain include ErbB receptor tyrosine kinase ErbB2, HTLV-1 Tax1, Cav1.3 Ca2+channels, and constituents of the cadherin:catenin cell adhesion complex, in particular delta-catenin, p0071 and ARVCF. The erbin PDZ domain binds Smad3, a transductor of the TGFbeta pathway, possibly by a novel interface of binding. Erbin and two other LAP proteins (scribble and lano) redundantly regulate epithelial polarity and apical adhesion complex. 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 densin and erbin-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: 467231 [Multi-domain]  Cd Length: 87  Bit Score: 38.46  E-value: 3.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300669666   39 GFTLKGGLE-HGEP-------LIISKVEEGGKADTLsskLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06749    12 GFSISGGIGsQGNPfrpdddgIFVTKVQPDGPASKL---LQPGDKILEVNGYDFVNiEHGQAVSLLKSFQNTVDLVVER 87
PDZ5_GRIP1-2-like cd06682
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
49-108 4.55e-03

PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. 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 GRIP family domain PDZ5 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: 467170 [Multi-domain]  Cd Length: 85  Bit Score: 38.09  E-value: 4.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300669666   49 GEPLIISKVEEGGKADTLSSkLQAGDEVVHINEVTLSS-SRKEAVSLVKGSYKTLRLVVRR 108
Cdd:cd06682    26 GDPLIISDVKKGSVAHRTGT-LEPGDKLLAIDNIRLDNcSMEDAAQILQQAEDIVKLKIRK 85
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1758-1904 5.16e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1758 ELLNKIKEMPAEVNEE-EEQADVNEKKAELIgsltHKLETLQEAKGSLLTDIKlnnALG----EEVEALISELCKPnefd 1832
Cdd:PRK03918  532 EKLIKLKGEIKSLKKElEKLEELKKKLAELE----KKLDELEEELAELLKELE---ELGfesvEELEERLKELEPF---- 600
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1833 kYRMFIG--------------------DLDKVVNLLLSLSGRLARVENVLSGLGEDASNEERSSLYEKRKILAGQHEDAR 1892
Cdd:PRK03918  601 -YNEYLElkdaekelereekelkkleeELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR 679
                         170
                  ....*....|...
gi 300669666 1893 -ELKENLDRRERV 1904
Cdd:PRK03918  680 aELEELEKRREEI 692
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1748-1903 6.58e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1748 AYYSVSAPKAEL-LNKIKEMPAEVNEEEEQADVNEKKAELIGSLTHKLETLQEAKGSLLTDI-KLNNALG--------EE 1817
Cdd:COG4717    57 ELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELeKLEKLLQllplyqelEA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669666 1818 VEALISELckPNEFDKYRMFIGDLDKVVNLLLSLSGRLARVENVLSGLGEDASNEERSSLYEKRKILAGQHEDARELKEN 1897
Cdd:COG4717   137 LEAELAEL--PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214

                  ....*.
gi 300669666 1898 LDRRER 1903
Cdd:COG4717   215 LEEAQE 220
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
32-107 8.47e-03

PDZ domain 2 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 2 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 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: 467220 [Multi-domain]  Cd Length: 82  Bit Score: 37.30  E-value: 8.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669666   32 LEGGAPWGFTLKGGLEHGEPLIISKVEEGGKADTLSskLQAGDEVVHINEVTLSS-SRKEAVSLVKGSyKTLRLVVR 107
Cdd:cd06738     9 LVGTRGLGCSISSGPTQKPGIFISNVKPGSLAEEVG--LEVGDQIVEVNGTSFTNvDHKEAVMALKSS-RHLTITVR 82
 
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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