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Conserved domains on  [gi|1485525032|ref|NP_001353314|]
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caspase recruitment domain-containing protein 14 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
19-104 2.13e-48

Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD14, also known as BIMP2 or CARMA2 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 2). CARD14 has been identified as a novel member of the MAGUK (membrane-associated guanylate kinase) family that functions as upstream activators of BCL10 (B-cell lymphoma 10) and NF-kB signaling. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260068  Cd Length: 86  Bit Score: 166.20  E-value: 2.13e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   19 LWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPD 98
Cdd:cd08806      1 LWELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPT 80

                   ....*.
gi 1485525032   99 VYTLVT 104
Cdd:cd08806     81 LYTQVT 86
PDZ_CARD11_CARD14-like cd06736
PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related ...
571-645 1.71e-34

PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CARD11, CARD14, and related domains. CARD11 (also known as CARD-containing MAGUK protein 1, CARMA1, Bimp3) and CARD14 (also known as CARD-containing MAGUK protein 2, CARMA2, Bimp2) belong to the CARD-containing membrane-associated guanylate kinase (MAGUK) protein family. They play several crucial biological functions, including regulation of immune response and inflammation. The CARD11-Bcl10-MALT1 (CBM) complex bridges T cell receptor signaling to the canonical IkappaB kinase (IKK)/NF-kappaB pathway. CARD14 can form an analogous biochemical complex to activate NF-kappaB during specialized immunity. The CBM complex of CARD14/CARMA2 may bind with TRAF6 and get involved in IL-17 pathways in keratinocytes. The preponderance of protein interactions occurs through the N-terminal half of CARD11 that includes the CARD, LATCH, and coiled-coil domains; the C-terminal PDZ-SH3-MAGUK region binds the adhesion and degranulation-promoting adapter protein (ADAP) and aryl hydrocarbon receptor interacting protein (AIP). 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 CARD11 and CARD14-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: 467218 [Multi-domain]  Cd Length: 75  Bit Score: 126.22  E-value: 1.71e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  571 MLAFQGDALLEQISVIGGNLTGIFIHRVTPGSAADQMALRPGTQIVMVDYEASEPLFKAVLEDTTLEEAVGLLRR 645
Cdd:cd06736      1 TITFQGDSLLSQITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGCIRGERQSVSLEDCTKEEAHWTLQR 75
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
135-409 8.09e-14

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 8.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  135 LQEELnqEKGQKEVLLRRCQQLQEHLGLAETRAEglhQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNALQEKEL 214
Cdd:COG1196    218 LKEEL--KELEAELLLLKLRELEAELEELEAELE---ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  215 AASRCRSLQEELYLLKQELQRANM-VSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEkdiLEQSLDE 293
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEErLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  294 ARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQR 373
Cdd:COG1196    370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1485525032  374 EISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:COG1196    450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
680-742 1.15e-10

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


The actual alignment was detected with superfamily member cd11859:

Pssm-ID: 473055  Cd Length: 62  Bit Score: 58.07  E-value: 1.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485525032  680 YIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQG-CGCWHAHRV--NSYTMkdtaAHGTIPNYSRAQ 742
Cdd:cd11859      1 YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGtVGSWQAVRVgrNHQEL----ERGVIPNKSRAE 62
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
858-961 7.36e-07

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member smart00072:

Pssm-ID: 450170 [Multi-domain]  Cd Length: 174  Bit Score: 50.37  E-value: 7.36e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   858 YLSQEEYEAWSQRGDIIQEGEVSGGRCWVTRHAVESLMEKNTHALLDVQLDSVCTLHRMDIFPIVIhvSVNEKMAKKLKK 937
Cdd:smart00072   43 FVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVAEKGKHCLLDIDPQGVKQLRKAQLYPIVI--FIAPPSSEELER 120
                            90       100
                    ....*....|....*....|....*...
gi 1485525032   938 GL-QRLGTSEEQL---LEAARQEEGDLD 961
Cdd:smart00072  121 RLrQRGTETSERIqkrLAAAQKEAQEYH 148
 
Name Accession Description Interval E-value
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
19-104 2.13e-48

Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD14, also known as BIMP2 or CARMA2 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 2). CARD14 has been identified as a novel member of the MAGUK (membrane-associated guanylate kinase) family that functions as upstream activators of BCL10 (B-cell lymphoma 10) and NF-kB signaling. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260068  Cd Length: 86  Bit Score: 166.20  E-value: 2.13e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   19 LWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPD 98
Cdd:cd08806      1 LWELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPT 80

                   ....*.
gi 1485525032   99 VYTLVT 104
Cdd:cd08806     81 LYTQVT 86
PDZ_CARD11_CARD14-like cd06736
PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related ...
571-645 1.71e-34

PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CARD11, CARD14, and related domains. CARD11 (also known as CARD-containing MAGUK protein 1, CARMA1, Bimp3) and CARD14 (also known as CARD-containing MAGUK protein 2, CARMA2, Bimp2) belong to the CARD-containing membrane-associated guanylate kinase (MAGUK) protein family. They play several crucial biological functions, including regulation of immune response and inflammation. The CARD11-Bcl10-MALT1 (CBM) complex bridges T cell receptor signaling to the canonical IkappaB kinase (IKK)/NF-kappaB pathway. CARD14 can form an analogous biochemical complex to activate NF-kappaB during specialized immunity. The CBM complex of CARD14/CARMA2 may bind with TRAF6 and get involved in IL-17 pathways in keratinocytes. The preponderance of protein interactions occurs through the N-terminal half of CARD11 that includes the CARD, LATCH, and coiled-coil domains; the C-terminal PDZ-SH3-MAGUK region binds the adhesion and degranulation-promoting adapter protein (ADAP) and aryl hydrocarbon receptor interacting protein (AIP). 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 CARD11 and CARD14-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: 467218 [Multi-domain]  Cd Length: 75  Bit Score: 126.22  E-value: 1.71e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  571 MLAFQGDALLEQISVIGGNLTGIFIHRVTPGSAADQMALRPGTQIVMVDYEASEPLFKAVLEDTTLEEAVGLLRR 645
Cdd:cd06736      1 TITFQGDSLLSQITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGCIRGERQSVSLEDCTKEEAHWTLQR 75
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
20-106 1.02e-16

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 76.06  E-value: 1.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   20 WEMMESHRHRIVRCI-CPSRLTPYLRQAKVLCQLDEEEVLHsprLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPD 98
Cdd:pfam00619    1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKA---NPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                   ....*...
gi 1485525032   99 VYTLVTGL 106
Cdd:pfam00619   78 LASDLEGL 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
135-409 8.09e-14

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 8.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  135 LQEELnqEKGQKEVLLRRCQQLQEHLGLAETRAEglhQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNALQEKEL 214
Cdd:COG1196    218 LKEEL--KELEAELLLLKLRELEAELEELEAELE---ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  215 AASRCRSLQEELYLLKQELQRANM-VSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEkdiLEQSLDE 293
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEErLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  294 ARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQR 373
Cdd:COG1196    370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1485525032  374 EISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:COG1196    450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-409 6.84e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.17  E-value: 6.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  120 ETSKLTECLAGaigsLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEglhQLEADHSRMKREVSAHFHEVLRLKDEML 199
Cdd:TIGR02168  678 EIEELEEKIEE----LEEKIAELEKALAELRKELEELEEELEQLRKELE---ELSRQISALRKDLARLEAEVEQLEERIA 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  200 SLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRAnmvsscELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTF 279
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  280 SLAEkdiLEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQtllqfqkskmacqlyrekvnaLQAQVCELQK 359
Cdd:TIGR02168  825 RLES---LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE---------------------LESELEALLN 880
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1485525032  360 ERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
680-742 1.15e-10

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


Pssm-ID: 212793  Cd Length: 62  Bit Score: 58.07  E-value: 1.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485525032  680 YIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQG-CGCWHAHRV--NSYTMkdtaAHGTIPNYSRAQ 742
Cdd:cd11859      1 YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGtVGSWQAVRVgrNHQEL----ERGVIPNKSRAE 62
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
583-655 2.77e-07

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: 49.30  E-value: 2.77e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032   583 ISVIGG--NLTGIFIHRVTPGSAADQMALRPGTQIVMVDyeaseplfKAVLEDTTLEEAVGLLRRVDGFCCLSVK 655
Cdd:smart00228   16 FSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVN--------GTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
858-961 7.36e-07

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


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 50.37  E-value: 7.36e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   858 YLSQEEYEAWSQRGDIIQEGEVSGGRCWVTRHAVESLMEKNTHALLDVQLDSVCTLHRMDIFPIVIhvSVNEKMAKKLKK 937
Cdd:smart00072   43 FVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVAEKGKHCLLDIDPQGVKQLRKAQLYPIVI--FIAPPSSEELER 120
                            90       100
                    ....*....|....*....|....*...
gi 1485525032   938 GL-QRLGTSEEQL---LEAARQEEGDLD 961
Cdd:smart00072  121 RLrQRGTETSERIqkrLAAAQKEAQEYH 148
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
136-388 2.67e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  136 QEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSahfHEVLRLKDEmlslslhysnalqEKELA 215
Cdd:pfam17380  298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERE---RELERIRQE-------------ERKRE 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  216 ASRCRslQEELYLlkqELQRANMVSSCELELQEQSLRTASDQESGDEElnRLKEEnEKLRSLTFSLAEKDILEQSLDEAR 295
Cdd:pfam17380  362 LERIR--QEEIAM---EISRMRELERLQMERQQKNERVRQELEAARKV--KILEE-ERQRKIQQQKVEMEQIRAEQEEAR 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  296 gsrQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQK---ERDQAYSARDSAQ 372
Cdd:pfam17380  434 ---QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilEKELEERKQAMIE 510
                          250
                   ....*....|....*.
gi 1485525032  373 REISQSLVEKDSLRRQ 388
Cdd:pfam17380  511 EERKRKLLEKEMEERQ 526
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
128-408 3.28e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 3.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  128 LAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSAHFhevlrlkdemlslslhysn 207
Cdd:PRK02224   211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETE------------------- 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  208 alQEKELAASRCRSLQEELYLLKQElqRANMVSSCELElqeqslrtASDQESGDEELNRLKEENEKLRsltfslaekdil 287
Cdd:PRK02224   272 --REREELAEEVRDLRERLEELEEE--RDDLLAEAGLD--------DADAEAVEARREELEDRDEELR------------ 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  288 eQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSA 367
Cdd:PRK02224   328 -DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1485525032  368 RDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQA 408
Cdd:PRK02224   407 LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
222-353 2.47e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 2.47e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   222 LQEELYLLKQELQR----ANMVSSCELELQE---------QSLRTASD--QESGDEELNRLKEENEK-LRSLTFSLAEKD 285
Cdd:smart00787  149 LDENLEGLKEDYKLlmkeLELLNSIKPKLRDrkdaleeelRQLKQLEDelEDCDPTELDRAKEKLKKlLQEIMIKVKKLE 228
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   286 ILEQSLDEARGSRQELVERIHSLRERAVAAERQREQ--YWEEKEQTLLQfqkskmacqlyrEKVNALQAQ 353
Cdd:smart00787  229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQcrGFTFKEIEKLK------------EQLKLLQSL 286
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
583-644 2.52e-03

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 37.65  E-value: 2.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  583 ISVIGGN---LTGIFIHRVTPGSAADQMALRPGTQIVMVDYEAseplfkavLEDTTLEEAVGLLR 644
Cdd:pfam00595   14 FSLKGGSdqgDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQD--------VENMTHEEAVLALK 70
Guanylate_kin pfam00625
Guanylate kinase;
858-956 6.22e-03

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 38.90  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  858 YLSQEEYEAWSQRGDIIQEGEVSGGRCWVTRHAVESLMEKNTHALLDVQLDSVCTLHRMDIFPIVIHVSVNEKmaKKLKK 937
Cdd:pfam00625   53 FVSKEEMERDISANEFLEYAQFSGNMYGTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSL--KVLQR 130
                           90       100
                   ....*....|....*....|...
gi 1485525032  938 GLQRLGTSEEQLL----EAARQE 956
Cdd:pfam00625  131 RLKGRGKEQEEKInkrmAAAEQE 153
 
Name Accession Description Interval E-value
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
19-104 2.13e-48

Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD14, also known as BIMP2 or CARMA2 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 2). CARD14 has been identified as a novel member of the MAGUK (membrane-associated guanylate kinase) family that functions as upstream activators of BCL10 (B-cell lymphoma 10) and NF-kB signaling. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260068  Cd Length: 86  Bit Score: 166.20  E-value: 2.13e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   19 LWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPD 98
Cdd:cd08806      1 LWELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPT 80

                   ....*.
gi 1485525032   99 VYTLVT 104
Cdd:cd08806     81 LYTQVT 86
CARD_CARD9-like cd08785
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ...
19-104 1.67e-39

Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation and recruitment domain (CARD) found in CARD9, CARD14 (CARMA2), CARD10 (CARMA3), CARD11 (CARMA1) and BCL10. BCL10 (B-cell lymphoma 10), together with Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), are integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells), and with CARD11 to form L-CBM (CBM complex in lymphoid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. BCL10/Malt1 also associates with CARD10, which is more widely expressed and is not restricted to hematopoietic cells, to play a role in GPCR-induced NF-kB activation. CARD14 has also been shown to associate with BCL10. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260055  Cd Length: 84  Bit Score: 140.97  E-value: 1.67e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   19 LWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTnsAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPD 98
Cdd:cd08785      1 LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLP--RNRAGYLLDILKTRGKNGYDAFLESLEFYYPE 78

                   ....*.
gi 1485525032   99 VYTLVT 104
Cdd:cd08785     79 LFTKVT 84
PDZ_CARD11_CARD14-like cd06736
PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related ...
571-645 1.71e-34

PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CARD11, CARD14, and related domains. CARD11 (also known as CARD-containing MAGUK protein 1, CARMA1, Bimp3) and CARD14 (also known as CARD-containing MAGUK protein 2, CARMA2, Bimp2) belong to the CARD-containing membrane-associated guanylate kinase (MAGUK) protein family. They play several crucial biological functions, including regulation of immune response and inflammation. The CARD11-Bcl10-MALT1 (CBM) complex bridges T cell receptor signaling to the canonical IkappaB kinase (IKK)/NF-kappaB pathway. CARD14 can form an analogous biochemical complex to activate NF-kappaB during specialized immunity. The CBM complex of CARD14/CARMA2 may bind with TRAF6 and get involved in IL-17 pathways in keratinocytes. The preponderance of protein interactions occurs through the N-terminal half of CARD11 that includes the CARD, LATCH, and coiled-coil domains; the C-terminal PDZ-SH3-MAGUK region binds the adhesion and degranulation-promoting adapter protein (ADAP) and aryl hydrocarbon receptor interacting protein (AIP). 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 CARD11 and CARD14-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: 467218 [Multi-domain]  Cd Length: 75  Bit Score: 126.22  E-value: 1.71e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  571 MLAFQGDALLEQISVIGGNLTGIFIHRVTPGSAADQMALRPGTQIVMVDYEASEPLFKAVLEDTTLEEAVGLLRR 645
Cdd:cd06736      1 TITFQGDSLLSQITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGCIRGERQSVSLEDCTKEEAHWTLQR 75
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
19-104 8.26e-28

Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD11, also known as caspase recruitment domain-containing membrane-associated guanylate kinase protein 1 (CARMA1). CARMA1, together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), form the L-CBM signalosome (CBM complex in lymphoid immune cells) which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARMA1 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260070  Cd Length: 86  Bit Score: 107.79  E-value: 8.26e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   19 LWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPD 98
Cdd:cd08808      1 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 80

                   ....*.
gi 1485525032   99 VYTLVT 104
Cdd:cd08808     81 LYKLVT 86
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
19-104 1.40e-25

Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD10, also known as CARMA3 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 3) or BIMP1. The CARMA3-BCL10-MALT1 signalosome plays a role in the GPCR-induced NF-kB activation. CARMA3 is more widely expressed than CARMA1, which is found only in hematopoietic cells. In endothelial and smooth muscle cells, CARMA3-mediated NF-kB activation induces pro-inflammatory signals within the vasculature and is a key factor in atherogenesis. In bronchial epithelial cells, CARMA3-mediated NF-kB signaling is important for the development of allergic airway inflammation. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260069  Cd Length: 86  Bit Score: 101.14  E-value: 1.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   19 LWEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPD 98
Cdd:cd08807      1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80

                   ....*.
gi 1485525032   99 VYTLVT 104
Cdd:cd08807     81 HFTLLT 86
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
20-104 9.83e-21

Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD9. CARD9 is a central regulator of innate immunity and is highly expressed in dendritic cells and macrophages. Together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), it forms the M-CBM signalosome (the CBM complex in myeloid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARD9 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260071  Cd Length: 86  Bit Score: 87.28  E-value: 9.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   20 WEMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPDV 99
Cdd:cd08809      2 WNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQL 81

                   ....*
gi 1485525032  100 YTLVT 104
Cdd:cd08809     82 YKKIT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
20-106 1.02e-16

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 76.06  E-value: 1.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   20 WEMMESHRHRIVRCI-CPSRLTPYLRQAKVLCQLDEEEVLHsprLTNSAMRAGHLLDLLKTRGKNGAIAFLESLKFHNPD 98
Cdd:pfam00619    1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKA---NPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                   ....*...
gi 1485525032   99 VYTLVTGL 106
Cdd:pfam00619   78 LASDLEGL 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
135-409 8.09e-14

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 8.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  135 LQEELnqEKGQKEVLLRRCQQLQEHLGLAETRAEglhQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNALQEKEL 214
Cdd:COG1196    218 LKEEL--KELEAELLLLKLRELEAELEELEAELE---ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  215 AASRCRSLQEELYLLKQELQRANM-VSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEkdiLEQSLDE 293
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEErLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE---AEEALLE 369
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  294 ARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQR 373
Cdd:COG1196    370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1485525032  374 EISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:COG1196    450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
120-409 6.84e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 73.17  E-value: 6.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  120 ETSKLTECLAGaigsLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEglhQLEADHSRMKREVSAHFHEVLRLKDEML 199
Cdd:TIGR02168  678 EIEELEEKIEE----LEEKIAELEKALAELRKELEELEEELEQLRKELE---ELSRQISALRKDLARLEAEVEQLEERIA 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  200 SLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRAnmvsscELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTF 279
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  280 SLAEkdiLEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQtllqfqkskmacqlyrekvnaLQAQVCELQK 359
Cdd:TIGR02168  825 RLES---LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE---------------------LESELEALLN 880
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1485525032  360 ERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
680-742 1.15e-10

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


Pssm-ID: 212793  Cd Length: 62  Bit Score: 58.07  E-value: 1.15e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485525032  680 YIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQG-CGCWHAHRV--NSYTMkdtaAHGTIPNYSRAQ 742
Cdd:cd11859      1 YIRTHFDYEKPAKGELSFKKGEVFHVVDTLYQGtVGSWQAVRVgrNHQEL----ERGVIPNKSRAE 62
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
583-645 3.57e-10

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


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 57.17  E-value: 3.57e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485525032  583 ISVIGGN--LTGIFIHRVTPGSAADQ-MALRPGTQIVMVDYEAseplfkavLEDTTLEEAVGLLRR 645
Cdd:cd00136     14 FSIRGGKdgGGGIFVSRVEPGGPAARdGRLRVGDRILEVNGVS--------LEGLTHEEAVELLKS 71
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
190-422 2.16e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 2.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  190 EVLRLKDEMLSLsLHYSNALQEKELAASRCRSLQEELYLLKQELQRANMvsscELELQEQSLRTASDQ--ESGDEELNRL 267
Cdd:COG1196    220 EELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEA----ELEELRLELEELELEleEAQAEEYELL 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  268 KEENEKLRSLTFSLAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSkmacqlyREKV 347
Cdd:COG1196    295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA-------EEAL 367
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  348 NALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAEPPGVLKQEARTRE 422
Cdd:COG1196    368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
24-102 5.52e-09

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 53.67  E-value: 5.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   24 ESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLHSPRltnSAMRAGHLLDLLKTRGKNGAIAFLESLK-FHNPDVYTL 102
Cdd:cd01671      2 RKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKT---RQDKARKLLDILPRRGPKAFEVFCEALReTGQPHLAEL 78
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
168-427 3.28e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 3.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  168 EGLHQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLKQEL-QRANMVSSCELEL 246
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLeELEEDLSSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  247 Q--EQSLRT-ASDQESGDEELNRLKEENEKL-RSLTFSlaEKDILEQSLDEARGSRQELVERIHSLrERAVAAERQREQY 322
Cdd:TIGR02169  754 EnvKSELKElEARIEELEEDLHKLEEALNDLeARLSHS--RIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  323 WEEKEQTLLQFQ-----KSKMACQ---LYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTD 394
Cdd:TIGR02169  831 LEKEIQELQEQRidlkeQIKSIEKeieNLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1485525032  395 QVCELRTQLRQLQAEpPGVLKQEARTREPCPRE 427
Cdd:TIGR02169  911 QIEKKRKRLSELKAK-LEALEEELSEIEDPKGE 942
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
207-430 9.17e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 9.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  207 NALQEKELAASRCRSLQEEL-----YLLKQELQRANMvsscELE-LQEQSLRTASDQESGDEELNRLKEENEKLRSLTFS 280
Cdd:TIGR02168  203 KSLERQAEKAERYKELKAELrelelALLVLRLEELRE----ELEeLQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  281 LAEK-DILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTL-----LQFQKSKMACQL--YREKVNALQA 352
Cdd:TIGR02168  279 LEEEiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEskldeLAEELAELEEKLeeLKEELESLEA 358
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485525032  353 QVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAEpPGVLKQEARTREPCPREKQR 430
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR-RERLQQEIEELLKKLEEAEL 435
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
583-655 2.77e-07

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: 49.30  E-value: 2.77e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032   583 ISVIGG--NLTGIFIHRVTPGSAADQMALRPGTQIVMVDyeaseplfKAVLEDTTLEEAVGLLRRVDGFCCLSVK 655
Cdd:smart00228   16 FSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVN--------GTSVEGLTHLEAVDLLKKAGGKVTLTVL 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
131-337 3.12e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  131 AIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLH----QLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYS 206
Cdd:COG1196    282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEeelaELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  207 NALQEKELAASRCRSLQEELYLLKQELQRANMVsscELELQEQSLRTASDQESGDEELNRLKEENEKLRS-LTFSLAEKD 285
Cdd:COG1196    362 EAEEALLEAEAELAEAEEELEELAEELLEALRA---AAELAAQLEELEEAEEALLERLERLEEELEELEEaLAELEEEEE 438
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1485525032  286 ILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSK 337
Cdd:COG1196    439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
858-961 7.36e-07

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


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 50.37  E-value: 7.36e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   858 YLSQEEYEAWSQRGDIIQEGEVSGGRCWVTRHAVESLMEKNTHALLDVQLDSVCTLHRMDIFPIVIhvSVNEKMAKKLKK 937
Cdd:smart00072   43 FVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVAEKGKHCLLDIDPQGVKQLRKAQLYPIVI--FIAPPSSEELER 120
                            90       100
                    ....*....|....*....|....*...
gi 1485525032   938 GL-QRLGTSEEQL---LEAARQEEGDLD 961
Cdd:smart00072  121 RLrQRGTETSERIqkrLAAAQKEAQEYH 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
126-334 7.51e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 7.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  126 ECLAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEglhQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHY 205
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE---ELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  206 SNALQEKELAASRCRSLQEELYLLKQELQRAN-MVSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLtfsLAEK 284
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEELEELIEELESELEALLNERASLEEALALL---RSEL 896
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1485525032  285 DILEQSLDEARGSRQELVERIHSLRERAVAAERQreqyWEEKEQTLLQFQ 334
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELR----LEGLEVRIDNLQ 942
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
254-409 9.94e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 9.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  254 ASDQESGDEELNRLKEENEKLRS-LTFSLAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQ 332
Cdd:COG4372     30 SEQLRKALFELDKLQEELEQLREeLEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1485525032  333 FQKskmacqlYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:COG4372    110 AEE-------LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
163-405 1.26e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  163 AETRAEGLHQLEADHSRMKREVSAhfhevLRLKDEMLSLSLHYsNALQEKELAASRCRSLQEELYLLKQELQRAnmvsSC 242
Cdd:COG4913    247 AREQIELLEPIRELAERYAAARER-----LAELEYLRAALRLW-FAQRRLELLEAELEELRAELARLEAELERL----EA 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  243 ELELQEQSLRTASDQ--ESGDEELNRLKEENEKLrsltfslaekdilEQSLDEARGSRQELVERIHSLRERAVAAErqrE 320
Cdd:COG4913    317 RLDALREELDELEAQirGNGGDRLEQLEREIERL-------------ERELEERERRRARLEALLAALGLPLPASA---E 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  321 QYWEEKEQTllqfqkskmacqlyREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELR 400
Cdd:COG4913    381 EFAALRAEA--------------AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR 446

                   ....*
gi 1485525032  401 TQLRQ 405
Cdd:COG4913    447 DALAE 451
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
136-388 2.67e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  136 QEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSahfHEVLRLKDEmlslslhysnalqEKELA 215
Cdd:pfam17380  298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERE---RELERIRQE-------------ERKRE 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  216 ASRCRslQEELYLlkqELQRANMVSSCELELQEQSLRTASDQESGDEElnRLKEEnEKLRSLTFSLAEKDILEQSLDEAR 295
Cdd:pfam17380  362 LERIR--QEEIAM---EISRMRELERLQMERQQKNERVRQELEAARKV--KILEE-ERQRKIQQQKVEMEQIRAEQEEAR 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  296 gsrQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQK---ERDQAYSARDSAQ 372
Cdd:pfam17380  434 ---QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilEKELEERKQAMIE 510
                          250
                   ....*....|....*.
gi 1485525032  373 REISQSLVEKDSLRRQ 388
Cdd:pfam17380  511 EERKRKLLEKEMEERQ 526
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
182-409 3.27e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 3.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  182 REVSAHFHEVLRLKDEMLSLSLHYsNALQEKELAASRCRSLQEELYLLKQELQRAnmvsscELELQEQSLRTASDQ-ESG 260
Cdd:COG4913    228 DALVEHFDDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLRAAL------RLWFAQRRLELLEAElEEL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  261 DEELNRLKEENEKLRsltfslAEKDILEQSLDEARGSRQEL-VERIHSLRERAVAAERQREqyweEKEQTLLQFQKskmA 339
Cdd:COG4913    301 RAELARLEAELERLE------ARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELE----ERERRRARLEA---L 367
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  340 CQLYREKVNALQAqvcELQKERDQAYSARDSAQREisqslveKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:COG4913    368 LAALGLPLPASAE---EFAALRAEAAALLEALEEE-------LEALEEALAEAEAALRDLRRELRELEAE 427
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
128-408 3.28e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 3.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  128 LAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSAHFhevlrlkdemlslslhysn 207
Cdd:PRK02224   211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETE------------------- 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  208 alQEKELAASRCRSLQEELYLLKQElqRANMVSSCELElqeqslrtASDQESGDEELNRLKEENEKLRsltfslaekdil 287
Cdd:PRK02224   272 --REREELAEEVRDLRERLEELEEE--RDDLLAEAGLD--------DADAEAVEARREELEDRDEELR------------ 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  288 eQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSA 367
Cdd:PRK02224   328 -DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1485525032  368 RDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQA 408
Cdd:PRK02224   407 LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
SH3_DLG5 cd11860
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ...
680-743 4.61e-06

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


Pssm-ID: 212794  Cd Length: 63  Bit Score: 45.02  E-value: 4.61e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  680 YIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQGC-GCWHAHRVNSYTMKDTaaHGTIPNYSRAQQ 743
Cdd:cd11860      1 YVRALFDRSAENEDELSFKKDDILYVDNTMFNGVfGQWRAWLVDEEGRKRK--CGIIPSKYKVEE 63
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
126-440 4.67e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 50.74  E-value: 4.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  126 ECLAGAIGSLQEELNQEK------GQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREvsahfhevLRLKDEML 199
Cdd:TIGR00618  222 QVLEKELKHLREALQQTQqshaylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQER--------INRARKAA 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  200 SLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRANMVSSCELELQEQslRTASDQESGDEELNRLKEENEKLRsltf 279
Cdd:TIGR00618  294 PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ--RRLLQTLHSQEIHIRDAHEVATSI---- 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  280 slaeKDILEQSLdeargsrqELVERIHSLRERAVAAERQREQYWEEKEQtlLQFQKSKMACQLYREkvNALQAQV----- 354
Cdd:TIGR00618  368 ----REISCQQH--------TLTQHIHTLQQQKTTLTQKLQSLCKELDI--LQREQATIDTRTSAF--RDLQGQLahakk 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  355 -CELQKERD-----------QAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCE---LRTQLRQLQAEPPGVLKQeaR 419
Cdd:TIGR00618  432 qQELQQRYAelcaaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRkkaVVLARLLELQEEPCPLCG--S 509
                          330       340
                   ....*....|....*....|.
gi 1485525032  420 TREPCPrEKQRLVRMHAICPR 440
Cdd:TIGR00618  510 CIHPNP-ARQDIDNPGPLTRR 529
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
583-643 4.67e-06

PDZ domain 3 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 3 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 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: 467211 [Multi-domain]  Cd Length: 82  Bit Score: 45.64  E-value: 4.67e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1485525032  583 ISVIGGNLTGIFIHRVTPGSAADQMALRPGTQIVMVDyeasEPLFKAVledtTLEEAVGLL 643
Cdd:cd06729     15 LRLAGGNDVGIFVAGVQEGSPAEKQGLQEGDQILKVN----GVDFRNL----TREEAVLFL 67
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
137-394 7.18e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 7.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  137 EELNQEKGQKEVLLRRCQQL-----------QEHLGLAETRAEGLHQLEADHSRMKREVSAHFHEVLRLKDEMlslslhY 205
Cdd:pfam05483  408 EELKKILAEDEKLLDEKKQFekiaeelkgkeQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL------E 481
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  206 SNALQEKELAASrCRSLQEELYLLKQElqranmVSSCELELQEQSlrtasdqesgdEELNRLKEENEKLRSLTFSLAEKD 285
Cdd:pfam05483  482 KEKLKNIELTAH-CDKLLLENKELTQE------ASDMTLELKKHQ-----------EDIINCKKQEERMLKQIENLEEKE 543
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  286 IleQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKErDQAY 365
Cdd:pfam05483  544 M--NLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKAL 620
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1485525032  366 SARDSAQR--------EISQSLVEKDSLRRQVFELTD 394
Cdd:pfam05483  621 KKKGSAENkqlnayeiKVNKLELELASAKQKFEEIID 657
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
116-421 9.98e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.65  E-value: 9.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  116 SGLMETSKLTECLAGAIGSLQEELNQEKGQKEVLLRRC-QQLQEHLGLA----------ETRAEGLHQ----LEADHSRM 180
Cdd:PRK02224   296 DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrVAAQAHNEEAeslredaddlEERAEELREeaaeLESELEEA 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  181 KREVSAHFHEVLRLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLK--------------------QELQRANMVS 240
Cdd:PRK02224   376 REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRereaeleatlrtarerveeaEALLEAGKCP 455
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  241 SC---------------------ELELQEQSLRTasDQESGDEELNRLKEENEKLRSLTFSLAEKDILEQSLDEARGSRQ 299
Cdd:PRK02224   456 ECgqpvegsphvetieedrerveELEAELEDLEE--EVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIE 533
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  300 ELVERIHSLRERAVAAERQREQyWEEKEQTLLQfqkskmACQLYREKVNALQAQVCELQKERDQ------------AYSA 367
Cdd:PRK02224   534 EKRERAEELRERAAELEAEAEE-KREAAAEAEE------EAEEAREEVAELNSKLAELKERIESlerirtllaaiaDAED 606
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1485525032  368 RDSAQREISQSLVEKDSLRRqvfeltDQVCELRTQLRQLQAEPPGVLKQEARTR 421
Cdd:PRK02224   607 EIERLREKREALAELNDERR------ERLAEKRERKRELEAEFDEARIEEARED 654
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
96-431 1.01e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   96 NPDVYTLVtgLQPDV-DFSNFSGLmETSKLTECLAGaIGSLQEELNQEKGQKEVLLRRCQQLQehLGLAETRAEgLHQLE 174
Cdd:TIGR02169  132 YPEGYNVV--LQGDVtDFISMSPV-ERRKIIDEIAG-VAEFDRKKEKALEELEEVEENIERLD--LIIDEKRQQ-LERLR 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  175 ADhsrmkREVSAHFHEVLRLKDEM-LSLSLHYSNALQ-EKELAASRCRSLQEELYLLKQELQRANMvsscELELQEQSLR 252
Cdd:TIGR02169  205 RE-----REKAERYQALLKEKREYeGYELLKEKEALErQKEAIERQLASLEEELEKLTEEISELEK----RLEEIEQLLE 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  253 TASDQ--ESGDEELNRLKEENEKL----RSLTFSLAEKdilEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEK 326
Cdd:TIGR02169  276 ELNKKikDLGEEEQLRVKEKIGELeaeiASLERSIAEK---ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  327 EQ-------------TLLQ--------FQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSL 385
Cdd:TIGR02169  353 DKlteeyaelkeeleDLRAeleevdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1485525032  386 RRQVFELTDQVCELRTQLRQLQAEppgvLKQEARTREPCPREKQRL 431
Cdd:TIGR02169  433 EAKINELEEEKEDKALEIKKQEWK----LEQLAADLSKYEQELYDL 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
130-360 1.16e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  130 GAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEglhQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHYSNAL 209
Cdd:TIGR02168  288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLE---ELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  210 QEKELAASRCRSLQEELYLLKQELQranmvsscELELQEQSLRtaSDQESGDEELNRLKEENEKLRSLTfSLAEKDILEQ 289
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVA--------QLELQIASLN--NEIERLEARLERLEDRRERLQQEI-EELLKKLEEA 433
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  290 SLDEARGS----RQELVERIHSLRERAVAAERQREQYwEEKEQTLLQFQKSKmacQLYREKVNALQAQVCELQKE 360
Cdd:TIGR02168  434 ELKELQAEleelEEELEELQEELERLEEALEELREEL-EEAEQALDAAEREL---AQLQARLDSLERLQENLEGF 504
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
21-93 1.56e-05

Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and recruitment domain (CARD) similar to that found in BCL10 (B-cell lymphoma 10). BCL10 and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1) are the integral components of CBM signalosomes. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. Both CARMA1 and CARD9 associate with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260072 [Multi-domain]  Cd Length: 85  Bit Score: 44.26  E-value: 1.56e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1485525032   21 EMMESHRHRIVRCICPSRLTPYLRQAKVLCQLDEEEVLhspRLTNSAMRAGHLLDLLKTRGKNGAIAFLESLK 93
Cdd:cd08810      3 EVLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQ---CRTTRKKRVDKLLDILAREGPDGLDALIESIR 72
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
282-433 1.58e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  282 AEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEK-----EQTLLQFQKSKMACQLYREKVNALQAQVCE 356
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaEREIAELEAELERLDASSDDLAALEEQLEE 696
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485525032  357 LQKERDQAYSARDSAQREISQslvekdsLRRQVFELTDQVCELRTQLRQLQAEPPGVLKQ--EARTREPCPREKQRLVR 433
Cdd:COG4913    697 LEAELEELEEELDELKGEIGR-------LEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVERELR 768
SH3_ZO-3 cd12028
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ...
677-742 2.16e-05

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


Pssm-ID: 212961  Cd Length: 65  Bit Score: 43.32  E-value: 2.16e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1485525032  677 DSFYIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQG-CGCWHAHRVNSYTMKdtAAHGTIPNYSRAQ 742
Cdd:cd12028      1 DSFYIRTHFDYEPDPPSGLSFTRGEVFHVLDTMHRGkLGSWLAVRMGRDLRE--MEKGIIPNQSRAE 65
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
583-645 2.18e-05

PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. 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 MUPP1-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: 467253 [Multi-domain]  Cd Length: 89  Bit Score: 43.76  E-value: 2.18e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1485525032  583 ISVIG-------GNLTGIFIHRVTPGSAADQMA-LRPGTQIVMVDYEAseplfkavLEDTTLEEAVGLLRR 645
Cdd:cd06791     16 ITIAGyvgekasGELSGIFVKSIIPGSAADQDGrIQVNDQIIAVDGVN--------LQGFTNQEAVEVLRN 78
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
120-409 2.43e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  120 ETSKLTEcLAGAIGSLQEELNQEKGQ----KEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSA----HFHEV 191
Cdd:TIGR04523  237 KQQEINE-KTTEISNTQTQLNQLKDEqnkiKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkELKSE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  192 LRLKDEMLSLSlhySNALQEKELAASrcrSLQEELYLLKQELQRANmvsSCELELQEQSLRTASDQESGDEELNRLKEEN 271
Cdd:TIGR04523  316 LKNQEKKLEEI---QNQISQNNKIIS---QLNEQISQLKKELTNSE---SENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  272 EKLRSltfslaEKDILEQSLDEARGSRQELVERIHSLreravaaerQREQYWEEKEQTLLQFQKSKMACQLYR--EKVNA 349
Cdd:TIGR04523  387 KNLES------QINDLESKIQNQEKLNQQKDEQIKKL---------QQEKELLEKEIERLKETIIKNNSEIKDltNQDSV 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  350 LQAQVCELQKERDQ----------AYSARDSAQREISQSLVEKDS-----------LRRQVFELTDQVCELRTQLRQLQA 408
Cdd:TIGR04523  452 KELIIKNLDNTRESletqlkvlsrSINKIKQNLEQKQKELKSKEKelkklneekkeLEEKVKDLTKKISSLKEKIEKLES 531

                   .
gi 1485525032  409 E 409
Cdd:TIGR04523  532 E 532
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
139-409 2.61e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.97  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  139 LNQEKGQKEVLLRRCQQLQEHLGlAETRAEglhqlEADHSRMKREVSAHFHEVLRLKDEMLSLSlhysNALQEKELAASR 218
Cdd:pfam07888  141 LTQRVLERETELERMKERAKKAG-AQRKEE-----EAERKQLQAKLQQTEEELRSLSKEFQELR----NSLAQRDTQVLQ 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  219 crsLQEELYLLKQELQRANMvSSCELELQEQSLRTASdqesgdEELNRLKEENEKLRSLTFSLAEkdILEQSLDEARGSR 298
Cdd:pfam07888  211 ---LQDTITTLTQKLTTAHR-KEAENEALLEELRSLQ------ERLNASERKVEGLGEELSSMAA--QRDRTQAELHQAR 278
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  299 QELVERIHSLRERAVAAERQREQYWEEKeQTLLQfqkskmACQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQs 378
Cdd:pfam07888  279 LQAAQLTLQLADASLALREGRARWAQER-ETLQQ------SAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR- 350
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1485525032  379 lvEKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:pfam07888  351 --EKDCNRVQLSESRRELQELKASLRVAQKE 379
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
118-393 4.71e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 4.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  118 LMETSKLTECLAGAIGSL---QEELNQEKGQKEVLLRRCQQLQE-----HLGLAETRAEGLHQLEADHSRM-KREVSAHF 188
Cdd:pfam05483  498 LLENKELTQEASDMTLELkkhQEDIINCKKQEERMLKQIENLEEkemnlRDELESVREEFIQKGDEVKCKLdKSEENARS 577
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  189 --HEVLRLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRAN-MVSSCELELQEQSLRTASDQESGDEELN 265
Cdd:pfam05483  578 ieYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkQLNAYEIKVNKLELELASAKQKFEEIID 657
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  266 RLKEENEKLRsltfsLAEKDILEQ------SLDEARGSRQELVERI-HSLRERAVAAERQREQYWE--EKEQTLLQFQKS 336
Cdd:pfam05483  658 NYQKEIEDKK-----ISEEKLLEEvekakaIADEAVKLQKEIDKRCqHKIAEMVALMEKHKHQYDKiiEERDSELGLYKN 732
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1485525032  337 KMacqlyREKVNALQAQVCELQKERDQAYSARDsaQREISQSlvEKDSLRRQVFELT 393
Cdd:pfam05483  733 KE-----QEQSSAKAALEIELSNIKAELLSLKK--QLEIEKE--EKEKLKMEAKENT 780
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
287-408 4.92e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 4.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  287 LEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKskmacQLYREKVNALQAQVCELQKERDQAYS 366
Cdd:COG3206    166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA-----KLLLQQLSELESQLAEARAELAEAEA 240
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1485525032  367 ARDSAQREISQSLVEKDSLRR--QVFELTDQVCELRTQLRQLQA 408
Cdd:COG3206    241 RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSA 284
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
198-337 5.70e-05

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 44.22  E-value: 5.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  198 MLSLSLHYSNALQEKELAASRCRSLQEELYLLKQE---LQRANMVSSCELELQEQSLrtasdqesgdEELNRLKEENEKL 274
Cdd:pfam12718    2 MNSLKLEAENAQERAEELEEKVKELEQENLEKEQEiksLTHKNQQLEEEVEKLEEQL----------KEAKEKAEESEKL 71
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485525032  275 RSLTFSLAEK-DILEQSLDEARGSRQELVERihsLR---------ERAVAAERQREQYWEEK-EQTLLQFQKSK 337
Cdd:pfam12718   72 KTNNENLTRKiQLLEEELEESDKRLKETTEK---LRetdvkaehlERKVQALEQERDEWEKKyEELEEKYKEAK 142
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
128-356 6.43e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 6.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  128 LAGAIGSLQEELNQE---KGQKEVLLRRCQQLQEHLG--LAETRAEGLHQLEADHSRMKrEVSAHFHEVLRLKDemlsls 202
Cdd:PRK03918   537 LKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAelLKELEELGFESVEELEERLK-ELEPFYNEYLELKD------ 609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  203 lhysnalqekelAASRCRSLQEELYLLKQELQRAnmvsSCELELQEQSLRTASDQEsgdEELNRL--KEENEKLRSLTFS 280
Cdd:PRK03918   610 ------------AEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKEL---EELEKKysEEEYEELREEYLE 670
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1485525032  281 LA-EKDILEQSLDEARGSRQELVERIHSLRERavaaERQREQYWEEKEqtllQFQKSKMACQLYREKVNALQAQVCE 356
Cdd:PRK03918   671 LSrELAGLRAELEELEKRREEIKKTLEKLKEE----LEEREKAKKELE----KLEKALERVEELREKVKKYKALLKE 739
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
132-405 9.42e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 9.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  132 IGSLQEELNQEKGQKEVLLRRCQQLQEHLGLA------ETRAEGLHQLEADHSRMKREVSAHFHEVLRLKDEMLSLSLHY 205
Cdd:PRK02224   477 VEELEAELEDLEEEVEEVEERLERAEDLVEAEdrierlEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  206 SNALQEKELAASRCR----SLQEELYLLKQELQRANMVSS-------CELELQEQSLRTASDQESGDEELNRLKEENEKl 274
Cdd:PRK02224   557 REAAAEAEEEAEEAReevaELNSKLAELKERIESLERIRTllaaiadAEDEIERLREKREALAELNDERRERLAEKRER- 635
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  275 rsltfslaeKDILEQSLDEARgsrqelVERIHSLRERAVAAERQREQYWEEKeqtllqfqkskmacqlyREKVNALQAQV 354
Cdd:PRK02224   636 ---------KRELEAEFDEAR------IEEAREDKERAEEYLEQVEEKLDEL-----------------REERDDLQAEI 683
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1485525032  355 CELQKERDQAYSARDsaQREISQSLVEK-DSLRRQVFELTDQVCELRTQLRQ 405
Cdd:PRK02224   684 GAVENELEELEELRE--RREALENRVEAlEALYDEAEELESMYGDLRAELRQ 733
SH3_ZO-1 cd12026
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 1; ZO-1 is a ...
677-742 1.46e-04

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


Pssm-ID: 212959  Cd Length: 65  Bit Score: 40.83  E-value: 1.46e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1485525032  677 DSFYIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQG-CGCWHAHRVNSYTMKdtAAHGTIPNYSRAQ 742
Cdd:cd12026      1 DSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGkLGSWLAIRIGKNHKE--VERGIIPNKNRAE 65
SH3_ZO-2 cd12027
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 2; ZO-2 is a ...
676-742 1.59e-04

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


Pssm-ID: 212960  Cd Length: 63  Bit Score: 40.67  E-value: 1.59e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485525032  676 GDSFYIRVNLAMEGRAKGELQVHCNEVLHVTDTMFQG-CGCWHAHRVNSYTMKdtaahGTIPNYSRAQ 742
Cdd:cd12027      1 GDSFFIRTHFEYEKELPQSLAFTRGEIFRVVDTLYDGkLGNWLAVRIGNELEK-----GLIPNKSRAE 63
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
210-375 1.72e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  210 QEKELAASRCRSLQEELYLLKQELQRANMVSSCELELQEQSlRTASDQESGDEELNRLKEENEKLRSLTFSLAEkdiLEQ 289
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS-WDEIDVASAEREIAELEAELERLDASSDDLAA---LEE 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  290 SLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQ-KSKMACQLYREKVNALQAQVC----------ELQ 358
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaAEDLARLELRALLEERFAAALgdaverelreNLE 772
                          170
                   ....*....|....*..
gi 1485525032  359 KERDQAYSARDSAQREI 375
Cdd:COG4913    773 ERIDALRARLNRAEEEL 789
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
132-421 2.01e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.49  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  132 IGSLQEEL---NQEKGQKEVLLR----RCQ-QLQEHLGLAETRAEGLH-------QLEADHSRMKREVSAHFHEVLRLKD 196
Cdd:pfam15921  414 IDHLRRELddrNMEVQRLEALLKamksECQgQMERQMAAIQGKNESLEkvssltaQLESTKEMLRKVVEELTAKKMTLES 493
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  197 EMLSLSlHYSNALQEKELAASRCRSlqeELYLLKqelqranmvSSCELELQE-QSLRTASDQesgdeeLNRLKEENEKLR 275
Cdd:pfam15921  494 SERTVS-DLTASLQEKERAIEATNA---EITKLR---------SRVDLKLQElQHLKNEGDH------LRNVQTECEALK 554
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  276 sltFSLAEKDILEQSLDEARGSRQELVERiHSlrERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVC 355
Cdd:pfam15921  555 ---LQMAEKDKVIEILRQQIENMTQLVGQ-HG--RTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485525032  356 ELQKERDQ---AYSARDSAQREISQslvEKDslrrqvfELTDQVCELRTQLRQLqAEPPGVLKQEARTR 421
Cdd:pfam15921  629 DLELEKVKlvnAGSERLRAVKDIKQ---ERD-------QLLNEVKTSRNELNSL-SEDYEVLKRNFRNK 686
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
212-419 2.91e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.13  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  212 KELAASRcRSLQEELYLLKQELQRANMVSScelELQEQ--SLRTASDQESGD-EELNRLKEENEKLrsltfslaEKDILE 288
Cdd:COG1340     60 QELREKR-DELNEKVKELKEERDELNEKLN---ELREEldELRKELAELNKAgGSIDKLRKEIERL--------EWRQQT 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  289 QSLDEARgsRQELVERIHSLRERAVAAERQREQywEEKEQTLL-QFQKSKMACQLYREKVNAL--QAQVC-----ELQKE 360
Cdd:COG1340    128 EVLSPEE--EKELVEKIKELEKELEKAKKALEK--NEKLKELRaELKELRKEAEEIHKKIKELaeEAQELheemiELYKE 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1485525032  361 RDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAEPPGVLKQEAR 419
Cdd:COG1340    204 ADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
222-418 2.93e-04

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 44.65  E-value: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  222 LQEElYLLKQELQRAnmvsscELELQEQSLRTASDQESgdEELNRLKEENEKLRSLTFSLAEKdileqsLDEARGSRQEL 301
Cdd:pfam10168  544 FREE-YLKKHDLARE------EIQKRVKLLKLQKEQQL--QELQSLEEERKSLSERAEKLAEK------YEEIKDKQEKL 608
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  302 VERIHSLRERAVA-------AERQreqyweekeqtllqfqkskmacqlYREKVNALQAQVCELQKERDQAYSARDSAQRE 374
Cdd:pfam10168  609 MRRCKKVLQRLNSqlpvlsdAERE------------------------MKKELETINEQLKHLANAIKQAKKKMNYQRYQ 664
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1485525032  375 ISQSlveKDSLRRQVFELTDQvcelrtQLRQLQaeppGVLKQEA 418
Cdd:pfam10168  665 IAKS---QSIRKKSSLSLSEK------QRKTIK----EILKQLG 695
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
203-408 3.00e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  203 LHYSNALQEKELAASRcRSLQEELYLLKQELQRAnmvsscELELQE--QSLRTASDQESGDEELNRLKEENEKLRSLTFS 280
Cdd:COG3206    162 LEQNLELRREEARKAL-EFLEEQLPELRKELEEA------EAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  281 LAE----KDILEQSLDEARGSRQELVE--RIHSLRERAVAAERQREQyweekEQTLLQFQKSKMacQLYREKVNALQAQV 354
Cdd:COG3206    235 LAEaearLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAE-----LSARYTPNHPDV--IALRAQIAALRAQL 307
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  355 -CELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQA 408
Cdd:COG3206    308 qQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
PDZ_PDZD11-like cd06752
PDZ domain of PDZ domain-containing protein 11, and related domains; PDZ (PSD-95 (Postsynaptic ...
591-647 3.06e-04

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: 40.37  E-value: 3.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1485525032  591 TGIFIHRVTPGSAADQMALRPGTQIVMVDyeaseplfKAVLEDTTLEEAVGLLRRVD 647
Cdd:cd06752     25 LGIFISKVIPDSDAHRLGLKEGDQILSVN--------GVDFEDIEHSEAVKVLKTAR 73
PDZ10_MUPP1-PDZ8_PATJ-like cd06673
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ...
583-654 3.12e-04

PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. 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 MUPP1-like family PDZ10 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: 467161 [Multi-domain]  Cd Length: 86  Bit Score: 40.35  E-value: 3.12e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485525032  583 ISVIGGN---LTGIFIHRVTP-GSAADQMALRPGTQIVMVDYEAseplfkavLEDTTLEEAVGLLRRVDGFCCLSV 654
Cdd:cd06673     17 LSIVGGSdtlLGAIIIHEVYEdGAAAKDGRLWAGDQILEVNGED--------LRKATHDEAINVLRQTPQKVRLLV 84
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
129-457 4.46e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.44  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  129 AGAIGSLQEELNQekgqKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKRE----VSAHFHEVL-RLKDEMLSLSL 203
Cdd:pfam12128  240 RPEFTKLQQEFNT----LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQllrtLDDQWKEKRdELNGELSAADA 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  204 HYSNALQEKELAASRCRS-LQEELYLLKQELQRANMVSScELELQEQSL-----------------------RTASDQES 259
Cdd:pfam12128  316 AVAKDRSELEALEDQHGAfLDADIETAAADQEQLPSWQS-ELENLEERLkaltgkhqdvtakynrrrskikeQNNRDIAG 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  260 GDEELNRLKEENEKLRSLTFSLAEK------DILEQSLDEARGSRQELVERIHSLRERAVAAerqreQYWEEkeqTLLQF 333
Cdd:pfam12128  395 IKDKLAKIREARDRQLAVAEDDLQAleselrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQA-----TATPE---LLLQL 466
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  334 QKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQSlvekdslRRQVFELTDQVCELRTQLrqlqAEPPGV 413
Cdd:pfam12128  467 ENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQA-------SRRLEERQSALDELELQL----FPQAGT 535
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1485525032  414 LKQEARTREPCPREKQRLVRMHAICPRDDSDCSLVSSTESQLLS 457
Cdd:pfam12128  536 LLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELN 579
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
190-398 4.64e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 4.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  190 EVLRLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRAnmvsscELELQEQSLRTASDQEsgdeELNRLKE 269
Cdd:COG1579     18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKYEE----QLGNVRN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  270 ENEkLRSLTfslAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREqyweEKEQTLlqfqkskmacqlyREKVNA 349
Cdd:COG1579     88 NKE-YEALQ---KEIESLKRRISDLEDEILELMERIEELEEELAELEAELA----ELEAEL-------------EEKKAE 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  350 LQAQVCELQKERDQAYSARDSAQREISQSLVEK-DSLRRQ-----VFELTDQVCE 398
Cdd:COG1579    147 LDEELAELEAELEELEAEREELAAKIPPELLALyERIRKRknglaVVPVEGGACG 201
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
120-330 4.95e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 42.71  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  120 ETSKLTECLAGAIGSLQE-ELNQEKGQKEV--LLRRCQQLQEHLGLAETR-AEGLHQLE-----ADHSRMKREVSahfhE 190
Cdd:pfam00261    9 ELDEAEERLKEAMKKLEEaEKRAEKAEAEVaaLNRRIQLLEEELERTEERlAEALEKLEeaekaADESERGRKVL----E 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  191 VLRLKDE--MLSLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRA--------NMVSSCELELQEQSLRTASDQESG 260
Cdd:pfam00261   85 NRALKDEekMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAeeraelaeSKIVELEEELKVVGNNLKSLEASE 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  261 DEELNRLKEENEKLRSLTFSLAEkdiLEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTL 330
Cdd:pfam00261  165 EKASEREDKYEEQIRFLTEKLKE---AETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTL 231
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
208-395 5.15e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  208 ALQEKELAASRCRSLQEELYLLKQELQRAnmvsscelelqEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEKDIL 287
Cdd:COG4717     79 ELKEAEEKEEEYAELQEELEELEEELEEL-----------EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  288 EQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTllqfqkskmacqlYREKVNALQAQVCELQKERDQAYSA 367
Cdd:COG4717    148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA-------------TEEELQDLAEELEELQQRLAELEEE 214
                          170       180
                   ....*....|....*....|....*...
gi 1485525032  368 RDSAQREISQSLVEKDSLRRQVFELTDQ 395
Cdd:COG4717    215 LEEAQEELEELEEELEQLENELEAAALE 242
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
262-391 5.40e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  262 EELNRLKEENEKLRSLTFSLAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQ 341
Cdd:COG1340    147 KELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1485525032  342 LYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDslRRQVFE 391
Cdd:COG1340    227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK--AEEIFE 274
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
591-644 5.84e-04

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: 39.65  E-value: 5.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1485525032  591 TGIFIHRVTPGSAADQMALRPGTQIVMVDyeaseplfKAVLEDTTLEEAVGLLR 644
Cdd:cd06740     27 VGIYVSLVEPGSLAEKEGLRVGDQILRVN--------DVSFEKVTHAEAVKILR 72
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
120-416 6.37e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  120 ETSKLTECLAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSAHFHEvlrLKDEMl 199
Cdd:pfam01576  205 ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE---LQEDL- 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  200 slslhySNALQEKELAASRCRSLQEELYLLKQELQranmvSSCELELQEQSLRTASDQE------SGDEELNRLKEENEK 273
Cdd:pfam01576  281 ------ESERAARNKAEKQRRDLGEELEALKTELE-----DTLDTTAAQQELRSKREQEvtelkkALEEETRSHEAQLQE 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  274 LRSLTFSLAEK--DILEQ------SLDEARGS----RQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQ 341
Cdd:pfam01576  350 MRQKHTQALEEltEQLEQakrnkaNLEKAKQAleseNAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRA 429
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  342 LYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAEPPGVLKQ 416
Cdd:pfam01576  430 ELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQ 504
PDZ4_PDZD2-PDZ2_hPro-IL-16-like cd06760
PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 of human pro-interleukin-16 ...
563-643 6.52e-04

PDZ domain 4 of PDZ domain containing 2 (PDZD2), PDZ domain 2 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 4 of PDZD2, also known as KIAA0300, PIN-1, 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 also includes the second PDZ domain (PDZ2) of human pro-interleukin-16 (isoform 1, also known as nPro-Il-16; 1332 amino-acid protein). Precursor IL-16 is cleaved to produce pro-IL-16 and mature IL-16 (derived from the C-terminal 121 AA). 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 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: 467241 [Multi-domain]  Cd Length: 90  Bit Score: 39.56  E-value: 6.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  563 RRILSQVTMLAFQGDAL-LEQISV-IGGNLTGIFIHRVTPGSAADQ-MALRPGTQIVMVDyeaseplfKAVLEDTTLEEA 639
Cdd:cd06760      1 DRIIMEVTLNKEPGVGLgIGLCCLpLENDIPGIFIHHLSPGSVAHMdGRLRRGDQILEIN--------GTSLRNVTLNEA 72

                   ....
gi 1485525032  640 VGLL 643
Cdd:cd06760     73 YAIL 76
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
583-615 7.29e-04

PDZ domain 4 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 4 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 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: 467247 [Multi-domain]  Cd Length: 81  Bit Score: 39.30  E-value: 7.29e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1485525032  583 ISVIGGNLTGIFIHRVTPGS-AADQMALRPGTQI 615
Cdd:cd06766     16 IQLCGGNLHGIFVEDVEDDSpAKGPDGLVPGDLI 49
DUF4795 pfam16043
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ...
119-306 7.36e-04

Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.


Pssm-ID: 464990 [Multi-domain]  Cd Length: 181  Bit Score: 41.52  E-value: 7.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  119 METSKLTECLAGAIGSLQEELNQEKGQKEVLLRRCQQLQEHLglaetraEGLHQlEADHSRMKREVSAHFHEVLRLKDem 198
Cdd:pfam16043    3 VEDAELLDQLQALILDLQEELEKLSETTSELSERLQQRQKHL-------EALYQ-QIEKLEKVKADKEVVEEELDEKA-- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  199 lslslhysnalqEKELAASRCRSLQEELYL--LKQELQraNMVSSceLELQEQSLRTASDQESGD-------EELNRLKE 269
Cdd:pfam16043   73 ------------DKEALASKVSRDQFDETLeeLNQMLQ--ELLDK--LEGQEDAWKKALETLSEEldtkldrLELDPLKE 136
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1485525032  270 E-NEKLRSLTFSLAEKDILEQSlDEARGSRQELVERIH 306
Cdd:pfam16043  137 LlERRIKALQKLLQEGSEELDE-AEAAGFRKKLLERFH 173
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
137-315 7.63e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 7.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  137 EELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGL----HQLEADHSRMKREVSAH--FHEVLRLKDEMLSLSLHYSNALQ 210
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEELeaelEELREELEKLEKLLQLLplYQELEALEAELAELPERLEELEE 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  211 EKElaasRCRSLQEELYLLKQELQRANmvSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRS-LTFSLAEKDILEQ 289
Cdd:COG4717    154 RLE----ELRELEEELEELEAELAELQ--EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEeLEEAQEELEELEE 227
                          170       180
                   ....*....|....*....|....*...
gi 1485525032  290 SLD--EARGSRQELVERIHSLRERAVAA 315
Cdd:COG4717    228 ELEqlENELEAAALEERLKEARLLLLIA 255
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
566-657 8.03e-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: 39.17  E-value: 8.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  566 LSQVTMLAFqgdalleqiSVIGGNL--TGIFIHRVTPGSAADQMALRPGTQIVMVDYEAseplfkavLEDTTLEEAVGLL 643
Cdd:cd06755      8 PSRESPLHF---------SLLGGSEkgFGIFVSKVEKGSKAAEAGLKRGDQILEVNGQN--------FENITLKKALEIL 70
                           90
                   ....*....|....
gi 1485525032  644 RRVDGFcCLSVKVN 657
Cdd:cd06755     71 RNNTHL-SITVKTN 83
COG5022 COG5022
Myosin heavy chain [General function prediction only];
145-414 8.67e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.53  E-value: 8.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  145 QKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHS-----RMKREVSAHFHEVLRLKDEMLSLSL--------HYSnALQE 211
Cdd:COG5022    788 DYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKlqktiKREKKLRETEEVEFSLKAEVLIQKFgrslkakkRFS-LLKK 866
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  212 KELA---ASRCRSLQEELYLLKQELQRANMVSSCELELQEQSLRTASDQESgdEELNRLKEENEKLRSLTFSLAEKDILE 288
Cdd:COG5022    867 ETIYlqsAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSS--DLIENLEFKTELIARLKKLLNNIDLEE 944
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  289 QSLDEARgsRQELVERIHS----LRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKV---NALQAQVCELQKER 361
Cdd:COG5022    945 GPSIEYV--KLPELNKLHEveskLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSkqyGALQESTKQLKELP 1022
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1485525032  362 D-----QAYSARDSAQREISQSLVEKDSLRRqvfELTDQVCELRTQLRQLQAEPPGVL 414
Cdd:COG5022   1023 VevaelQSASKIISSESTELSILKPLQKLKG---LLLLENNQLQARYKALKLRRENSL 1077
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
583-619 1.04e-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: 38.84  E-value: 1.04e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1485525032  583 ISVIGG--NLTGIFIHRVTPGSAADQMALRPGTQIVMVD 619
Cdd:cd06738     17 CSISSGptQKPGIFISNVKPGSLAEEVGLEVGDQIVEVN 55
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
120-452 1.06e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.02  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  120 ETSKLTECLAGAIGSLQEELNQEKGQKEVLLRRCQQLqEHLGLAETRAEGLHQLEADHSRMKREVSAHFHEVLRLKDEML 199
Cdd:COG3096    279 ERRELSERALELRRELFGARRQLAEEQYRLVEMAREL-EELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQEDLE 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  200 SLSLHY-------SNALQEKELAASRCRSLQEELYLLKQEL---QRAnmvssceLELQE------QSLRTASDQESGDEE 263
Cdd:COG3096    358 ELTERLeeqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLadyQQA-------LDVQQtraiqyQQAVQALEKARALCG 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  264 LNRLKEENEKLRSLTFSLAEKDI------LEQSLDEARGSRQ------ELVERIHSLRERAVAAERQREQYWEEKEQTLL 331
Cdd:COG3096    431 LPDLTPENAEDYLAAFRAKEQQAteevleLEQKLSVADAARRqfekayELVCKIAGEVERSQAWQTARELLRRYRSQQAL 510
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  332 QFQKSKMACQLYR-----EKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQL 406
Cdd:COG3096    511 AQRLQQLRAQLAEleqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL 590
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1485525032  407 QAEppgvlKQEARTREPCPREKQ-RLVRMhaicpRDDSDCSLVSSTE 452
Cdd:COG3096    591 RAR-----IKELAARAPAWLAAQdALERL-----REQSGEALADSQE 627
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
264-409 1.30e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  264 LNRLKEENEKLRSLTFSLAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQY-----WEEKEQTLLQFQKSKM 338
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLE 149
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485525032  339 ACQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEK-DSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:COG4717    150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEE 221
PDZ1_GgSTXBP4-like cd06692
PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, ...
583-645 1.45e-03

PDZ1 domain of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Gallus gallus uncharacterized syntaxin-binding protein 4 (STXBP4) isoform X1, and related domains. Gallus gallus STXBP4 isoform X1 contains 2 PDZ domains (PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This STXBP4-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: 467179 [Multi-domain]  Cd Length: 88  Bit Score: 38.74  E-value: 1.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  583 ISVIGGNLT------GIFIHRVTPGSAADQMA-LRPGTQIVMVDYEAseplfkavLEDTTLEEAVGLLRR 645
Cdd:cd06692     12 IKIIGGYREntgeefGIFIKRILPGGLAATDGrLKEGDLILEVNGES--------LQGVTNERAVSILRS 73
PDZ1_Scribble-like cd06704
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
583-654 1.46e-03

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: 38.80  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  583 ISVIGG--------NLTGIFIHRVTPGSAADQMALRPGTQIVMVDyeaseplfKAVLEDTTLEEAVGLLRRVDGFCCLSV 654
Cdd:cd06704     14 ISIAGGkgstpykgDDEGIFISRVTEGGPAAKAGVRVGDKLLEVN--------GVDLVDADHHEAVEALKNSGNTVTMVV 85
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
215-409 1.84e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  215 AASRCRSLQEELYLLKQELQRANMvsscELELQEQSLRTASDQ-ESGDEELNRLKEENEKLRS-LTFSLAEKDILEQSLD 292
Cdd:COG4942     18 QADAAAEAEAELEQLQQEIAELEK----ELAALKKEEKALLKQlAALERRIAALARRIRALEQeLAALEAELAELEKEIA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  293 EARgsrQELVERIHSLRERAVAAERQREQYWEE---KEQTLLQFQKSKMACQLY-----------REKVNALQAQVCELQ 358
Cdd:COG4942     94 ELR---AELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLaparreqaeelRADLAELAALRAELE 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1485525032  359 KERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:COG4942    171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
211-377 1.92e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.25  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  211 EKELAASRCRSLQEELYLLKQELQRANMVSSCELELQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAEKDI-LEQ 289
Cdd:COG3096    506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSeLRQ 585
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  290 SLDEARGSRQELVERIHSLRERAVAAERQREQYWEEKE--QTLLQFqkskMACQLYREKvnalqaqvcELQKERDQAYSA 367
Cdd:COG3096    586 QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALAdsQEVTAA----MQQLLERER---------EATVERDELAAR 652
                          170
                   ....*....|
gi 1485525032  368 RDSAQREISQ 377
Cdd:COG3096    653 KQALESQIER 662
PDZ3_PDZD7-like cd06751
PDZ domain 3 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
583-645 2.01e-03

PDZ domain 3 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 3 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of the 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 and can also form homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the third 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 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: 467233 [Multi-domain]  Cd Length: 89  Bit Score: 38.19  E-value: 2.01e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485525032  583 ISVIGG----NLTGIFIHRVTPGSAA-DQMALRPGTQIVMVDYEAseplfkavLEDTTLEEAVGLLRR 645
Cdd:cd06751     15 ISISGGieskVQPVVKIEKIFPGGAAaLSGNLKAGYELVSVDGES--------LQQVTHQQAVDIIRR 74
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
240-409 2.19e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.28  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  240 SSCELELQEQSLRTASDQESgdEELNRLKEENEKLRSltfslAEKDILEQSLDEARGSRQELverihSLRERAVAAERQR 319
Cdd:pfam09787   41 SSTALTLELEELRQERDLLR--EEIQKLRGQIQQLRT-----ELQELEAQQQEEAESSREQL-----QELEEQLATERSA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  320 EQyweEKEQTLLQFQK--SKMACQLYREK---VNALQAQVCELQKERDQAYSArdsaqreiSQSLVEKDSLRRQVFELTD 394
Cdd:pfam09787  109 RR---EAEAELERLQEelRYLEEELRRSKatlQSRIKDREAEIEKLRNQLTSK--------SQSSSSQSELENRLHQLTE 177
                          170
                   ....*....|....*
gi 1485525032  395 QVCELRTQLRQLQAE 409
Cdd:pfam09787  178 TLIQKQTMLEALSTE 192
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
261-409 2.22e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  261 DEELNRLKEENEKLRsltfslAEKDILEQSLDEARGSRQE---LVERIHSLRERAVAAERQREQYWEE----KEQTL-LQ 332
Cdd:PRK02224   219 DEEIERYEEQREQAR------ETRDEADEVLEEHEERREEletLEAEIEDLRETIAETEREREELAEEvrdlRERLEeLE 292
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1485525032  333 FQKSKMA--CQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAE 409
Cdd:PRK02224   293 EERDDLLaeAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
132-374 2.29e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  132 IGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRaegLHQLEADHSRMKREVSahfhevlRLKDEMLSLslhysnalqE 211
Cdd:COG4942     36 IAELEKELAALKKEEKALLKQLAALERRIAALARR---IRALEQELAALEAELA-------ELEKEIAEL---------R 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  212 KELAAsrcrsLQEELYLLKQELQRANMVSSCELEL-QEQSLRTASDQESGDEELNRLKEENEKLRsltfslAEKDILEQS 290
Cdd:COG4942     97 AELEA-----QKEELAELLRALYRLGRQPPLALLLsPEDFLDAVRRLQYLKYLAPARREQAEELR------ADLAELAAL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  291 LDEARGSRQELVERIHSLRERAVAAERQREqyweEKEQTLLQFQKSKmacQLYREKVNALQAQVCELQKERDQAYSARDS 370
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAA 238

                   ....
gi 1485525032  371 AQRE 374
Cdd:COG4942    239 AAER 242
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
201-335 2.31e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.28  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  201 LSLHYSNALQEKELAASRCRSLQEELYLLKQELQR------ANMVSSCEL--ELQEQSLRTASDQESGDEELNRLKEE-- 270
Cdd:pfam09787   45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQEleaqqqEEAESSREQlqELEEQLATERSARREAEAELERLQEElr 124
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485525032  271 ---NEKLRSLTFSLAEKDILEQSLDEARG----------SRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQK 335
Cdd:pfam09787  125 yleEELRRSKATLQSRIKDREAEIEKLRNqltsksqsssSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLER 202
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
222-353 2.47e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 2.47e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   222 LQEELYLLKQELQR----ANMVSSCELELQE---------QSLRTASD--QESGDEELNRLKEENEK-LRSLTFSLAEKD 285
Cdd:smart00787  149 LDENLEGLKEDYKLlmkeLELLNSIKPKLRDrkdaleeelRQLKQLEDelEDCDPTELDRAKEKLKKlLQEIMIKVKKLE 228
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032   286 ILEQSLDEARGSRQELVERIHSLRERAVAAERQREQ--YWEEKEQTLLQfqkskmacqlyrEKVNALQAQ 353
Cdd:smart00787  229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQcrGFTFKEIEKLK------------EQLKLLQSL 286
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
583-644 2.52e-03

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 37.65  E-value: 2.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  583 ISVIGGN---LTGIFIHRVTPGSAADQMALRPGTQIVMVDYEAseplfkavLEDTTLEEAVGLLR 644
Cdd:pfam00595   14 FSLKGGSdqgDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQD--------VENMTHEEAVLALK 70
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
135-318 2.72e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  135 LQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEaDHSRMKREVSAHFHEVLRLKDEMLSLslhysnalqekEL 214
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELEAELERL-----------DA 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  215 AASRCRSLQEELYLLKQELQRANMvsscEL-ELQEQSLRTASDQESGDEELNRLKEENEKL----RSLTFSLAEKDILEQ 289
Cdd:COG4913    683 SSDDLAALEEQLEELEAELEELEE----ELdELKGEIGRLEKELEQAEEELDELQDRLEAAedlaRLELRALLEERFAAA 758
                          170       180       190
                   ....*....|....*....|....*....|
gi 1485525032  290 SLDEARGS-RQELVERIHSLRERAVAAERQ 318
Cdd:COG4913    759 LGDAVERElRENLEERIDALRARLNRAEEE 788
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
220-438 2.89e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.49  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  220 RSLQEELYLLKQELQRANMVSSCELELQEQSLRTASDQESG-DEELNRLKEENEKLRSLTFSLAEKDILEQSLDEARGSR 298
Cdd:TIGR00618  190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHlREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARI 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  299 QEL--VERIHSLRERAVAAERQREQYWEEKEQ------------TLLQFQKSKMA---------------CQLYREKVNA 349
Cdd:TIGR00618  270 EELraQEAVLEETQERINRARKAAPLAAHIKAvtqieqqaqrihTELQSKMRSRAkllmkraahvkqqssIEEQRRLLQT 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  350 LQAQVCELQKERDQAYSARD--SAQREISQSLVekdSLRRQVFELTDQVCELRTQLRQLQAEPPGVLKQEARTREpcprE 427
Cdd:TIGR00618  350 LHSQEIHIRDAHEVATSIREisCQQHTLTQHIH---TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD----L 422
                          250
                   ....*....|.
gi 1485525032  428 KQRLVRMHAIC 438
Cdd:TIGR00618  423 QGQLAHAKKQQ 433
PRK09039 PRK09039
peptidoglycan -binding protein;
261-408 3.43e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  261 DEELNRLkeeNEKLRSLTFSLAekdiLEqsldeaRGSRQELVERIHSLRERAVAAERQREQyweekeqtlLQFQKSKMAc 340
Cdd:PRK09039    52 DSALDRL---NSQIAELADLLS----LE------RQGNQDLQDSVANLRASLSAAEAERSR---------LQALLAELA- 108
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1485525032  341 qlyrEKVNALQAQVCELQKERDqaysardsAQREISQSLvekdslRRQVFELTDQVCELRTQLRQLQA 408
Cdd:PRK09039   109 ----GAGAAAEGRAGELAQELD--------SEKQVSARA------LAQVELLNQQIAALRRQLAALEA 158
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
134-417 4.48e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.83  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  134 SLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREVSAHFHEVLRLKdeMLSLSLH-YSNALQEK 212
Cdd:pfam05622   70 QLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVK--KLEATVEtYKKKLEDL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  213 ELAASRCRSLQEE--LYL-----LKQELQRANMVSScELEL---QEQSLRTASDQESG-----DEELNRLKEENEKL-RS 276
Cdd:pfam05622  148 GDLRRQVKLLEERnaEYMqrtlqLEEELKKANALRG-QLETykrQVQELHGKLSEESKkadklEFEYKKLEEKLEALqKE 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  277 LTFSLAEKDILEQSLDEAR--------GSRQELVERIHSLRERAVAAERQREQYWEEKEQtlLQFQKSKMACQL---YRE 345
Cdd:pfam05622  227 KERLIIERDTLRETNEELRcaqlqqaeLSQADALLSPSSDPGDNLAAEIMPAEIREKLIR--LQHENKMLRLGQegsYRE 304
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485525032  346 KVNALQAQVcelqkerdqaysarDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQL--QAEPPGVLKQE 417
Cdd:pfam05622  305 RLTELQQLL--------------EDANRRKNELETQNRLANQRILELQQQVEELQKALQEQgsKAEDSSLLKQK 364
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
246-405 4.90e-03

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 39.39  E-value: 4.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  246 LQEQSLRTASDQESGDEELNRLKEENEKLRSLTFSLAekdileQSLDEARGSRQELVERIHSLRERAVAAERQREQYW-- 323
Cdd:pfam14662   20 LLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQ------QAVQKEKLLEEELEDLKLIVNSLEEARRSLLAQNKql 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  324 EEKEQTLLQfqkskmacqlyreKVNALQAQVCELQKERDQaysardsAQREISQSLVEKDSLRRQVFELTDQVCELRTQL 403
Cdd:pfam14662   94 EKENQSLLQ-------------EIESLQEENKKNQAERDK-------LQKKKKELLKSKACLKEQLHSCEDLACNRETIL 153

                   ..
gi 1485525032  404 RQ 405
Cdd:pfam14662  154 IE 155
Guanylate_kin pfam00625
Guanylate kinase;
858-956 6.22e-03

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 38.90  E-value: 6.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  858 YLSQEEYEAWSQRGDIIQEGEVSGGRCWVTRHAVESLMEKNTHALLDVQLDSVCTLHRMDIFPIVIHVSVNEKmaKKLKK 937
Cdd:pfam00625   53 FVSKEEMERDISANEFLEYAQFSGNMYGTSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSL--KVLQR 130
                           90       100
                   ....*....|....*....|...
gi 1485525032  938 GLQRLGTSEEQLL----EAARQE 956
Cdd:pfam00625  131 RLKGRGKEQEEKInkrmAAAEQE 153
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
193-412 6.32e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 6.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  193 RLKDEMLSLSLHYSNALQEKELAASRCRSLQEELYLLKQELQRANMvsscELELQEQSLRTASDQESG-DEELNRLKEEN 271
Cdd:COG4942     31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAElRAELEAQKEEL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  272 EKLRSLTFSLAEKDIL------EQSLDEARgsRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKmacqlyRE 345
Cdd:COG4942    107 AELLRALYRLGRQPPLalllspEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL------EA 178
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1485525032  346 KVNALQAQVCELQKERDQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVCELRTQLRQLQAEPPG 412
Cdd:COG4942    179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
243-409 6.84e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  243 ELELQEQSLRTASDQESGDEELNRLKEENEKLRSLtfsLAEKDIleqSLDEARGSRQELVERIHSLRERAVAAERQREQY 322
Cdd:COG4717    341 ELLDRIEELQELLREAEELEEELQLEELEQEIAAL---LAEAGV---EDEEELRAALEQAEEYQELKEELEELEEQLEEL 414
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  323 WEEKEQTLLQFQKSKMacqlyREKVNALQAQVCELQKERDQAYSARDSAQREISQsLVEKDSLRrqvfELTDQVCELRTQ 402
Cdd:COG4717    415 LGELEELLEALDEEEL-----EEELEELEEELEELEEELEELREELAELEAELEQ-LEEDGELA----ELLQELEELKAE 484

                   ....*..
gi 1485525032  403 LRQLQAE 409
Cdd:COG4717    485 LRELAEE 491
PDZ_syntrophin-like cd06801
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ...
583-655 6.96e-03

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: 36.40  E-value: 6.96e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1485525032  583 ISVIGG--NLTGIFIHRVTPGSAADQM-ALRPGTQIVMVDYEAseplfkavLEDTTLEEAVGLLRRVDGFCCLSVK 655
Cdd:cd06801     15 ISIKGGaeHKMPILISKIFKGQAADQTgQLFVGDAILSVNGEN--------LEDATHDEAVQALKNAGDEVTLTVK 82
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
299-405 7.13e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.32  E-value: 7.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  299 QELVERIHSLRERAVAAERQREQYWEEKEQtllQFQKSKMACQL---YREKVNALQAQVCELQKERDQAYSARDSAQREI 375
Cdd:PRK11448   145 HALQQEVLTLKQQLELQAREKAQSQALAEA---QQQELVALEGLaaeLEEKQQELEAQLEQLQEKAAETSQERKQKRKEI 221
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1485525032  376 SQSLVEKdslrrqvFELTDQvcELRT----QLRQ 405
Cdd:PRK11448   222 TDQAAKR-------LELSEE--ETRIlidqQLRK 246
mukB PRK04863
chromosome partition protein MukB;
131-409 7.31e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 7.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  131 AIGSLQEELNQEKGQKEVLLRRCQQLQEHLGLAETRAEGLHQLEADHSRMKREvsahfhevlRLKDEMLSLSLHySNALQ 210
Cdd:PRK04863   852 ALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLD---------EAEEAKRFVQQH-GNALA 921
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  211 EKELAASRCRSLQEELYLLKQELQRAnmvsscelelqEQSLRTASDQesgdeeLNRLKEENEKLRSLTFSLAEKDILEQS 290
Cdd:PRK04863   922 QLEPIVSVLQSDPEQFEQLKQDYQQA-----------QQTQRDAKQQ------AFALTEVVQRRAHFSYEDAAEMLAKNS 984
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  291 ldeargsrqELVERihsLRERAVAAERQREQYWEEKEQTLLQF-------QKSKMACQLYREKVNALQAQVCELQKERDQ 363
Cdd:PRK04863   985 ---------DLNEK---LRQRLEQAEQERTRAREQLRQAQAQLaqynqvlASLKSSYDAKRQMLQELKQELQDLGVPADS 1052
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1485525032  364 AYSARDSAQR-EISQSLVEKDSLRRQVfELTDQVCE--LRTQLRQLQAE 409
Cdd:PRK04863  1053 GAEERARARRdELHARLSANRSRRNQL-EKQLTFCEaeMDNLTKKLRKL 1100
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
211-422 7.38e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 7.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  211 EKELAASRCRSLQEELYLLKQElqraNMVSSCELELQEQSLRTASDQESGDEE----LNRLKEENEKLRS-LTFSLAEKD 285
Cdd:pfam01576  125 EKVTTEAKIKKLEEDILLLEDQ----NSKLSKERKLLEERISEFTSNLAEEEEkaksLSKLKNKHEAMISdLEERLKKEE 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  286 ILEQSLDEAR----GSRQELVERIHSLRERAVAAERQREQYWEEKEQTLLQFQKSKMACQLYREKVNALQAQVCELQKER 361
Cdd:pfam01576  201 KGRQELEKAKrkleGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL 280
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1485525032  362 DQAYSARDSAQREISQSLVEKDSLRRQVFELTDQVC---ELRTQLRQLQAEPPGVLKQEARTRE 422
Cdd:pfam01576  281 ESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAaqqELRSKREQEVTELKKALEEETRSHE 344
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
262-377 7.54e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 7.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  262 EELNRLKEENEKLRsltfslAEKDILEQSLDEARGSRQELVERIHSLRERAVAAERQREQYWEEkeqtllqFQKSKMACQ 341
Cdd:COG1340     15 EKIEELREEIEELK------EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEK-------VKELKEERD 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1485525032  342 LYREKVNALQAQVCELQKERDQAYSAR---DSAQREISQ 377
Cdd:COG1340     82 ELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIER 120
mukB PRK04863
chromosome partition protein MukB;
212-414 7.69e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  212 KELAASRCRSLQEELYLLKQELQRANMVSSCELELQEQslrtasdqesgdEELNRLKEENEKLRSLTFSLAEKdiLEQSL 291
Cdd:PRK04863   495 WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ------------QRAERLLAEFCKRLGKNLDDEDE--LEQLQ 560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  292 DEARGSRQELVERIHSLRERAVAAERQREQYweekEQTLLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSA 371
Cdd:PRK04863   561 EELEARLESLSESVSEARERRMALRQQLEQL----QARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQL 636
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1485525032  372 QREISQSLVEKDSLRRQVFELTDQVCELR-------TQLRQLQAEPPGVL 414
Cdd:PRK04863   637 LERERELTVERDELAARKQALDEEIERLSqpggsedPRLNALAERFGGVL 686
PDZ1_harmonin cd06737
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
591-644 8.05e-03

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


Pssm-ID: 467219 [Multi-domain]  Cd Length: 85  Bit Score: 36.47  E-value: 8.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1485525032  591 TGIFIHRVTPGSAADQMALRPGTQIVMVD-YEaseplfkavLEDTTLEEAVGLLR 644
Cdd:cd06737     27 CGLFVSHVSPGSQADNKGLRVGDEIVRINgYS---------ISQCTHEEVINLIK 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
298-422 9.09e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 9.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485525032  298 RQELVERIHSLRERAVAAERQREqyweekeqtlLQFQKSKMACQLYREKVNALQAQVCELQKERDQAYSARDSAQREISQ 377
Cdd:COG1196    195 LGELERQLEPLERQAEKAERYRE----------LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1485525032  378 SLVEKDSLRRQVFELTDQVCELRTQLRQLQAEPPGVLKQEARTRE 422
Cdd:COG1196    265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
 
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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