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Conserved domains on  [gi|1023301064|ref|NP_001311210|]
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caspase recruitment domain-containing protein 11 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
22-107 6.22e-55

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: 185.21  E-value: 6.22e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   22 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 101
Cdd:cd08808      1 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 80

                   ....*.
gi 1023301064  102 LYKLVT 107
Cdd:cd08808     81 LYKLVT 86
PDZ_CARD11_CARD14-like cd06736
PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related ...
668-742 1.01e-41

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: 147.02  E-value: 1.01e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023301064  668 HTTLNGDSLTSQLTLLGGNARGSFVHSVKPGSLAEKAGLREGHQLLLLEGCIRGERQSVPLDTCTKEEAHWTIQR 742
Cdd:cd06736      1 TITFQGDSLLSQITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGCIRGERQSVSLEDCTKEEAHWTLQR 75
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
205-438 1.66e-11

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: 68.81  E-value: 1.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  205 AMRYAQLSEEK-----NMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIEnrpkkEQVLELERENEMLKTK 279
Cdd:COG1196    212 AERYRELKEELkeleaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE-----ELRLELEELELELEEA 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  280 NQELQSIIQAgkrslpdsdkaiLDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCE 359
Cdd:COG1196    287 QAEEYELLAE------------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1023301064  360 MYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRL 438
Cdd:COG1196    355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
777-839 3.74e-05

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: 42.66  E-value: 3.74e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1023301064  777 YIRLNLNISSQLDAcTMSLKCDDVVHVRDTMYQDR-HEWLCARVDPfTDHDLDMGTIPSYSRAQ 839
Cdd:cd11859      1 YIRTHFDYEKPAKG-ELSFKKGEVFHVVDTLYQGTvGSWQAVRVGR-NHQELERGVIPNKSRAE 62
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
1009-1143 4.71e-03

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: 39.20  E-value: 4.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  1009 VTRDEFLRRQKTETIIYSREKNpNAFECIAPANIEAVAAKNKHCLLEAGIGCTRDLIKSNIYPIVLFIRVceKNIKRFRK 1088
Cdd:smart00072   44 VSKEEFEDDIKSGLFLEWGEYE-GNYYGTSKETIRQVAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAP--PSSEELER 120
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1023301064  1089 LLPRPETEEEFLRVCRLK--EKELEALPCLYATVEPDmwgSVEELLRVVKDKIGEEQ 1143
Cdd:smart00072  121 RLRQRGTETSERIQKRLAaaQKEAQEYHLFDYVIVND---DLEDAYEELKEILEAEQ 174
 
Name Accession Description Interval E-value
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
22-107 6.22e-55

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: 185.21  E-value: 6.22e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   22 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 101
Cdd:cd08808      1 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 80

                   ....*.
gi 1023301064  102 LYKLVT 107
Cdd:cd08808     81 LYKLVT 86
PDZ_CARD11_CARD14-like cd06736
PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related ...
668-742 1.01e-41

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: 147.02  E-value: 1.01e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023301064  668 HTTLNGDSLTSQLTLLGGNARGSFVHSVKPGSLAEKAGLREGHQLLLLEGCIRGERQSVPLDTCTKEEAHWTIQR 742
Cdd:cd06736      1 TITFQGDSLLSQITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGCIRGERQSVSLEDCTKEEAHWTLQR 75
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
23-109 7.59e-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: 73.75  E-value: 7.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   23 WENVECNRHMLSRYI-NPAKLTPYLRQCKVIDEQDEDEVLNapmLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 101
Cdd:pfam00619    1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKA---NPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                   ....*...
gi 1023301064  102 LYKLVTGK 109
Cdd:pfam00619   78 LASDLEGL 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
205-438 1.66e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  205 AMRYAQLSEEK-----NMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIEnrpkkEQVLELERENEMLKTK 279
Cdd:COG1196    212 AERYRELKEELkeleaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE-----ELRLELEELELELEEA 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  280 NQELQSIIQAgkrslpdsdkaiLDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCE 359
Cdd:COG1196    287 QAEEYELLAE------------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1023301064  360 MYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRL 438
Cdd:COG1196    355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
169-449 7.16e-09

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: 60.46  E-value: 7.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  169 TRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERN 248
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  249 QSLKLKNDIENRpkKEQVLELERENEMLKTKNQELQSIIQAGKRSLpDSDKAILDILEHDRKEALEDRQELVNRIYNLQE 328
Cdd:TIGR02168  755 ELTELEAEIEEL--EERLEEAEEELAEAEAEIEELEAQIEQLKEEL-KALREALDELRAELTLLNEEAANLRERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  329 EARQAEELRDKYLEEKEDLElkcstlgKDCEMYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIR 408
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELS-------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1023301064  409 ELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSL 449
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
PTZ00121 PTZ00121
MAEBL; Provisional
133-446 2.52e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  133 NEVIKLQQQMKAKDLQRCELLAR---LRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDElvkvkddnyNLAMRYA 209
Cdd:PTZ00121  1513 DEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK---------NMALRKA 1583
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  210 ----QLSEEKNMAVMRsrdLQLEIDQLKHRLNKMEEEcklERNQSLKLKNDIENRPKKEQVLELEREN----EMLKtKNQ 281
Cdd:PTZ00121  1584 eeakKAEEARIEEVMK---LYEEEKKMKAEEAKKAEE---AKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaEELK-KAE 1656
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  282 ELQSI--IQAGKRSLPDSDKAildilEHDRKEAlEDRQELVNRIYNLQEEARQAEELRDKYLEEKEdlelKCSTLGKDCE 359
Cdd:PTZ00121  1657 EENKIkaAEEAKKAEEDKKKA-----EEAKKAE-EDEKKAAEALKKEAEEAKKAEELKKKEAEEKK----KAEELKKAEE 1726
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  360 MYKhrmntvmLQLEEVERERDQAFHSRDEAQTQYSqcliEKDKYRKQIRELEEKNDEMRIEmvrREACI---VNLESKLR 436
Cdd:PTZ00121  1727 ENK-------IKAEEAKKEAEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKE---KEAVIeeeLDEEDEKR 1792
                          330
                   ....*....|
gi 1023301064  437 RLSKDSNNLD 446
Cdd:PTZ00121  1793 RMEVDKKIKD 1802
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
177-441 3.10e-08

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: 57.83  E-value: 3.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  177 QERYYKMKEERdsyndeLVKVKDDNYNLAMRYAQLsEEKNMAVMRSRDLQLEIDQLKHRLnKMEEECKLERNQSLKLKND 256
Cdd:pfam17380  290 QEKFEKMEQER------LRQEKEEKAREVERRRKL-EEAEKARQAEMDRQAAIYAEQERM-AMERERELERIRQEERKRE 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  257 IENRPKKEQVLELERENEMLK------TKNQELQSIIQAGKRslpdsdkaiLDILEHDRKEALEDRQELVNRIYNLQEEA 330
Cdd:pfam17380  362 LERIRQEEIAMEISRMRELERlqmerqQKNERVRQELEAARK---------VKILEEERQRKIQQQKVEMEQIRAEQEEA 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  331 RQAEELRdkyLEEKEDLELKcstlgkdcemykhrmntvMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKyRKQIREL 410
Cdd:pfam17380  433 RQREVRR---LEEERAREME------------------RVRLEEQERQQQVERLRQQEEERKRKKLELEKEK-RDRKRAE 490
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1023301064  411 EEKNDEMRIEMVRREACIVNLESKLRRLSKD 441
Cdd:pfam17380  491 EQRRKILEKELEERKQAMIEEERKRKLLEKE 521
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
680-749 2.08e-05

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: 43.91  E-value: 2.08e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1023301064   680 LTLLGG--NARGSFVHSVKPGSLAEKAGLREGHQLLLLEGcirgerqsVPLDTCTKEEAHWTIQRCSGPVTL 749
Cdd:smart00228   16 FSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNG--------TSVEGLTHLEAVDLLKKAGGKVTL 79
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
777-839 3.74e-05

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: 42.66  E-value: 3.74e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1023301064  777 YIRLNLNISSQLDAcTMSLKCDDVVHVRDTMYQDR-HEWLCARVDPfTDHDLDMGTIPSYSRAQ 839
Cdd:cd11859      1 YIRTHFDYEKPAKG-ELSFKKGEVFHVVDTLYQGTvGSWQAVRVGR-NHQELERGVIPNKSRAE 62
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
173-257 4.57e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 43.08  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  173 LLTFQERYYKMKEERDSYNDELVKvkddnyNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRL-NKMEEECKLERNQSL 251
Cdd:cd07649     91 LLNFRENFKKDMKKLDHHIADLRK------QLASRYAAVEKARKALLERQKDLEGKTQQLEIKLsNKTEEDIKKARRKST 164

                   ....*.
gi 1023301064  252 KLKNDI 257
Cdd:cd07649    165 QAGDDL 170
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
684-749 4.57e-03

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 37.26  E-value: 4.57e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1023301064  684 GGNARGSFVHSVKPGSLAEKAGLREGHQLLLLEGcirgerqsVPLDTCTKEEAHWTIQRCSGPVTL 749
Cdd:pfam00595   21 DQGDPGIFVSEVLPGGAAEAGGLKVGDRILSING--------QDVENMTHEEAVLALKGSGGKVTL 78
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
1009-1143 4.71e-03

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: 39.20  E-value: 4.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  1009 VTRDEFLRRQKTETIIYSREKNpNAFECIAPANIEAVAAKNKHCLLEAGIGCTRDLIKSNIYPIVLFIRVceKNIKRFRK 1088
Cdd:smart00072   44 VSKEEFEDDIKSGLFLEWGEYE-GNYYGTSKETIRQVAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAP--PSSEELER 120
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1023301064  1089 LLPRPETEEEFLRVCRLK--EKELEALPCLYATVEPDmwgSVEELLRVVKDKIGEEQ 1143
Cdd:smart00072  121 RLRQRGTETSERIQKRLAaaQKEAQEYHLFDYVIVND---DLEDAYEELKEILEAEQ 174
 
Name Accession Description Interval E-value
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
22-107 6.22e-55

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: 185.21  E-value: 6.22e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   22 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 101
Cdd:cd08808      1 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 80

                   ....*.
gi 1023301064  102 LYKLVT 107
Cdd:cd08808     81 LYKLVT 86
PDZ_CARD11_CARD14-like cd06736
PDZ domain of caspase recruitment domain-containing protein 11 (CARD11), CARD14, and related ...
668-742 1.01e-41

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: 147.02  E-value: 1.01e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023301064  668 HTTLNGDSLTSQLTLLGGNARGSFVHSVKPGSLAEKAGLREGHQLLLLEGCIRGERQSVPLDTCTKEEAHWTIQR 742
Cdd:cd06736      1 TITFQGDSLLSQITIIGGNRTGIFIHSVQPGSAAEKAGLREGTQLLLLEGCIRGERQSVSLEDCTKEEAHWTLQR 75
CARD_CARD9-like cd08785
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ...
22-107 1.55e-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: 1.55e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   22 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPskINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 101
Cdd:cd08785      1 LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLP--RNRAGYLLDILKTRGKNGYDAFLESLEFYYPE 78

                   ....*.
gi 1023301064  102 LYKLVT 107
Cdd:cd08785     79 LFTKVT 84
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
22-107 3.94e-37

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: 134.27  E-value: 3.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   22 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 101
Cdd:cd08807      1 LWERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPE 80

                   ....*.
gi 1023301064  102 LYKLVT 107
Cdd:cd08807     81 HFTLLT 86
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
23-107 1.00e-26

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: 104.62  E-value: 1.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   23 WENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPEL 102
Cdd:cd08809      2 WNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQL 81

                   ....*
gi 1023301064  103 YKLVT 107
Cdd:cd08809     82 YKKIT 86
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
22-107 7.25e-25

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: 99.56  E-value: 7.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   22 LWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 101
Cdd:cd08806      1 LWELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPT 80

                   ....*.
gi 1023301064  102 LYKLVT 107
Cdd:cd08806     81 LYTQVT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
23-109 7.59e-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: 73.75  E-value: 7.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   23 WENVECNRHMLSRYI-NPAKLTPYLRQCKVIDEQDEDEVLNapmLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPE 101
Cdd:pfam00619    1 RKLLKKNRVALVERLgTLDGLLDYLLEKNVLTEEEEEKIKA---NPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77

                   ....*...
gi 1023301064  102 LYKLVTGK 109
Cdd:pfam00619   78 LASDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
29-105 3.10e-12

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: 63.30  E-value: 3.10e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023301064   29 NRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNapmLPSKINRAGRLLDILHTKGQRGYVVFLESL-EFYYPELYKL 105
Cdd:cd01671      4 NRVELVEDLDVEDILDHLIQKGVLTEEDKEEILS---EKTRQDKARKLLDILPRRGPKAFEVFCEALrETGQPHLAEL 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
205-438 1.66e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 1.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  205 AMRYAQLSEEK-----NMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIEnrpkkEQVLELERENEMLKTK 279
Cdd:COG1196    212 AERYRELKEELkeleaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE-----ELRLELEELELELEEA 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  280 NQELQSIIQAgkrslpdsdkaiLDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCE 359
Cdd:COG1196    287 QAEEYELLAE------------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1023301064  360 MYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRL 438
Cdd:COG1196    355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
169-449 7.16e-09

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: 60.46  E-value: 7.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  169 TRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERN 248
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  249 QSLKLKNDIENRpkKEQVLELERENEMLKTKNQELQSIIQAGKRSLpDSDKAILDILEHDRKEALEDRQELVNRIYNLQE 328
Cdd:TIGR02168  755 ELTELEAEIEEL--EERLEEAEEELAEAEAEIEELEAQIEQLKEEL-KALREALDELRAELTLLNEEAANLRERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  329 EARQAEELRDKYLEEKEDLElkcstlgKDCEMYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIR 408
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELS-------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1023301064  409 ELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSL 449
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
133-437 9.63e-09

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: 59.69  E-value: 9.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  133 NEVIKLQQQMKAKDLQRCELLARLRQL----EDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRY 208
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  209 AQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKndIENRPKKEQVLELERENEMLKTKNQELQSIIq 288
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESLERRIAATERRLEDLEEQI- 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  289 agkrslpdsdkaildilehdrKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLgkdcemyKHRMNTV 368
Cdd:TIGR02168  848 ---------------------EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL-------RSELEEL 899
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1023301064  369 MLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEK-NDEMRIEM---VRREACIVNLESKLRR 437
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLeeaEALENKIEDDEEEARR 972
PTZ00121 PTZ00121
MAEBL; Provisional
133-446 2.52e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  133 NEVIKLQQQMKAKDLQRCELLAR---LRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDElvkvkddnyNLAMRYA 209
Cdd:PTZ00121  1513 DEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK---------NMALRKA 1583
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  210 ----QLSEEKNMAVMRsrdLQLEIDQLKHRLNKMEEEcklERNQSLKLKNDIENRPKKEQVLELEREN----EMLKtKNQ 281
Cdd:PTZ00121  1584 eeakKAEEARIEEVMK---LYEEEKKMKAEEAKKAEE---AKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaEELK-KAE 1656
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  282 ELQSI--IQAGKRSLPDSDKAildilEHDRKEAlEDRQELVNRIYNLQEEARQAEELRDKYLEEKEdlelKCSTLGKDCE 359
Cdd:PTZ00121  1657 EENKIkaAEEAKKAEEDKKKA-----EEAKKAE-EDEKKAAEALKKEAEEAKKAEELKKKEAEEKK----KAEELKKAEE 1726
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  360 MYKhrmntvmLQLEEVERERDQAFHSRDEAQTQYSqcliEKDKYRKQIRELEEKNDEMRIEmvrREACI---VNLESKLR 436
Cdd:PTZ00121  1727 ENK-------IKAEEAKKEAEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKE---KEAVIeeeLDEEDEKR 1792
                          330
                   ....*....|
gi 1023301064  437 RLSKDSNNLD 446
Cdd:PTZ00121  1793 RMEVDKKIKD 1802
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
177-441 3.10e-08

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: 57.83  E-value: 3.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  177 QERYYKMKEERdsyndeLVKVKDDNYNLAMRYAQLsEEKNMAVMRSRDLQLEIDQLKHRLnKMEEECKLERNQSLKLKND 256
Cdd:pfam17380  290 QEKFEKMEQER------LRQEKEEKAREVERRRKL-EEAEKARQAEMDRQAAIYAEQERM-AMERERELERIRQEERKRE 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  257 IENRPKKEQVLELERENEMLK------TKNQELQSIIQAGKRslpdsdkaiLDILEHDRKEALEDRQELVNRIYNLQEEA 330
Cdd:pfam17380  362 LERIRQEEIAMEISRMRELERlqmerqQKNERVRQELEAARK---------VKILEEERQRKIQQQKVEMEQIRAEQEEA 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  331 RQAEELRdkyLEEKEDLELKcstlgkdcemykhrmntvMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKyRKQIREL 410
Cdd:pfam17380  433 RQREVRR---LEEERAREME------------------RVRLEEQERQQQVERLRQQEEERKRKKLELEKEK-RDRKRAE 490
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1023301064  411 EEKNDEMRIEMVRREACIVNLESKLRRLSKD 441
Cdd:pfam17380  491 EQRRKILEKELEERKQAMIEEERKRKLLEKE 521
Rabaptin pfam03528
Rabaptin;
138-534 3.62e-08

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 57.42  E-value: 3.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  138 LQQQMKAKDLQRCELLARLRQLEDEKKQmtltrvELLTFQERYYKMKEERDSYNDELVKVKDD----NYNLAMRYAQLSE 213
Cdd:pfam03528    6 LQQRVAELEKENAEFYRLKQQLEAEFNQ------KRAKFKELYLAKEEDLKRQNAVLQEAQVEldalQNQLALARAEMEN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  214 EKNMAVMRSRDLQLEIDQLKHRLNK--------MEEE-CKLERNQSLKLKndiENRPKKEQVLE-LERENEMLK---TKN 280
Cdd:pfam03528   80 IKAVATVSENTKQEAIDEVKSQWQEevaslqaiMKETvREYEVQFHRRLE---QERAQWNQYREsAEREIADLRrrlSEG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  281 QELQSIIQAGKRSLPDSDK--AILDILEHDRKEALEDRQELVNRIYNLqeEARQAEELrDKYLEEKE----DLEL----- 349
Cdd:pfam03528  157 QEEENLEDEMKKAQEDAEKlrSVVMPMEKEIAALKAKLTEAEDKIKEL--EASKMKEL-NHYLEAEKscrtDLEMyvavl 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  350 --KCSTLGKDCEMYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQY--SQCLIEKDKYR-------KQIRELEE--KNDE 416
Cdd:pfam03528  234 ntQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFleSQRLLMRDMQRmesvltsEQLRQVEEikKKDQ 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  417 MRIEMVRreacivnlesklRRLSKDSNNLDQSLPRNLPVTIISQDFGDASPRTNGQEADDSSTSEESPEDSKYFLPYH-P 495
Cdd:pfam03528  314 EEHKRAR------------THKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDVVLGAGdS 381
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1023301064  496 PQRRMNLKGIQLQRAKSPISLKRTSDFQAK--GHEEEGTDA 534
Cdd:pfam03528  382 FNKQEDPFKEGLRRAQSTDSLGSSSSLQHKflGHNQKAKSA 422
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
155-439 5.65e-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: 57.37  E-value: 5.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  155 RLRQLEDEKK--QMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDdnyNLAMRYAQLSE---EKNMAVMRSRDLQLEI 229
Cdd:TIGR02168  214 RYKELKAELRelELALLVLRLEELREELEELQEELKEAEEELEELTA---ELQELEEKLEElrlEVSELEEEIEELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  230 DQLKHRLNKMEEECKLERNQSLKLKNDIENrpKKEQVLELERENEMLKTKNQELQSIIQagkrslpdSDKAILDILEHDR 309
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEE--LEAQLEELESKLDELAEELAELEEKLE--------ELKEELESLEAEL 360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  310 KEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVMLQLEEVERERDQAfhSRDEA 389
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKEL 438
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1023301064  390 QTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLS 439
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
149-441 7.03e-08

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: 57.05  E-value: 7.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  149 RCELLARLRQLEDE----KKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDnynLAMRYAQLSEEK--------- 215
Cdd:pfam15921  330 RSELREAKRMYEDKieelEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAD---LHKREKELSLEKeqnkrlwdr 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  216 ----NMAVMRSR----DLQLEIDQLKHRLNKMEEECK--LERnQSLKLKNDIENRPKKEQVL-ELERENEMLKTKNQELQ 284
Cdd:pfam15921  407 dtgnSITIDHLRreldDRNMEVQRLEALLKAMKSECQgqMER-QMAAIQGKNESLEKVSSLTaQLESTKEMLRKVVEELT 485
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  285 siiqAGKRSLPDSDKAILDI----------LEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYlEEKEDLELKCSTL 354
Cdd:pfam15921  486 ----AKKMTLESSERTVSDLtaslqekeraIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ-TECEALKLQMAEK 560
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  355 GKDCEMYKHRMNTVM------------LQLEEVERERDQafhsrDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMV 422
Cdd:pfam15921  561 DKVIEILRQQIENMTqlvgqhgrtagaMQVEKAQLEKEI-----NDRRLELQEFKILKDKKDAKIRELEARVSDLELEKV 635
                          330
                   ....*....|....*....
gi 1023301064  423 RreacIVNLESKLRRLSKD 441
Cdd:pfam15921  636 K----LVNAGSERLRAVKD 650
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
182-447 1.91e-07

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: 55.41  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  182 KMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNmavmrsrDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRP 261
Cdd:TIGR04523  374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ-------QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  262 KKEQVLELEREN-----EMLKTKNQELQSIIQAGKRSLPDSDKAiLDILEHDRKEALEDRQELVNRIYNLQEEARQAEEL 336
Cdd:TIGR04523  447 NQDSVKELIIKNldntrESLETQLKVLSRSINKIKQNLEQKQKE-LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  337 RDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVmlQLEEVERERDQAFhsrDEAQTQYSQCLIEKDKYRKQIRELEEKNDE 416
Cdd:TIGR04523  526 IEKLESEKKEKESKISDLEDELNKDDFELKKE--NLEKEIDEKNKEI---EELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1023301064  417 MRIEMVRREACIVNLESKLRRLSKDSNNLDQ 447
Cdd:TIGR04523  601 LIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
106-447 2.12e-07

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: 55.50  E-value: 2.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  106 VTGKEPTRRFSTIVVEEGHEGLTHflMNEVIKLQQQMKAKDLQRCELLARlrQLEDEKKQMTLTRVELLTFQE------- 178
Cdd:pfam05483  249 ITEKENKMKDLTFLLEESRDKANQ--LEEKTKLQDENLKELIEKKDHLTK--ELEDIKMSLQRSMSTQKALEEdlqiatk 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  179 RYYKMKEERDSYNDELVKVKDDNYNLAMRYAQ--------LSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQS 250
Cdd:pfam05483  325 TICQLTEEKEAQMEELNKAKAAHSFVVTEFEAttcsleelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  251 LKLKNDIENRPKKEQVL----ELERENEMLKTKNQELQSIIQAGKRSLPDSD---KAILDILEHDRKEALEDRQELVNRI 323
Cdd:pfam05483  405 VELEELKKILAEDEKLLdekkQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqlTAIKTSEEHYLKEVEDLKTELEKEK 484
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  324 YNLQEEARQAEEL---RDKYLEEKEDLELKCSTLGKD---CEMYKHRMNTVMLQLEEVERE-RDQAFHSRDEAQTQYSQC 396
Cdd:pfam05483  485 LKNIELTAHCDKLlleNKELTQEASDMTLELKKHQEDiinCKKQEERMLKQIENLEEKEMNlRDELESVREEFIQKGDEV 564
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1023301064  397 LIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQ 447
Cdd:pfam05483  565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
131-449 3.18e-07

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: 54.64  E-value: 3.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQQMKAKDLQRCELLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQ 210
Cdd:TIGR04523  178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  211 LSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIE---NRPKKEQVLELERENEMLKTKNQELQSII 287
Cdd:TIGR04523  258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwNKELKSELKNQEKKLEEIQNQISQNNKII 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  288 QAGKRSLPDsdkaildiLEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLgkdcemykhrmNT 367
Cdd:TIGR04523  338 SQLNEQISQ--------LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL-----------ES 398
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  368 VMLQLEEVERERDQAFHS----RDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSN 443
Cdd:TIGR04523  399 KIQNQEKLNQQKDEQIKKlqqeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN 478

                   ....*.
gi 1023301064  444 NLDQSL 449
Cdd:TIGR04523  479 KIKQNL 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
133-446 3.45e-07

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: 54.69  E-value: 3.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  133 NEVIKLQQQMKAKDLQRCELLARLRQLEDEKKQmtltrvelltfQERYYKMKEErdsyndelvKVKDDNYNLAMRYAQLS 212
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREK-----------AERYQALLKE---------KREYEGYELLKEKEALE 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  213 EEKNMAVMRSRDLQLEIDQLKHRLNKMEEECklerNQSLKLKNDIENRPKKEQvlelERENEMLKTKNQELQSIIQAGKR 292
Cdd:TIGR02169  237 RQKEAIERQLASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLG----EEEQLRVKEKIGELEAEIASLER 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  293 SLpdsdkaildilehdrkEALEDRQElvnriyNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMY-------KHRM 365
Cdd:TIGR02169  309 SI----------------AEKERELE------DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeyaelKEEL 366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  366 NTVMLQLEEVERERDQAFHSRDEAQTqysqcliEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNL 445
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYRE-------KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439

                   .
gi 1023301064  446 D 446
Cdd:TIGR02169  440 E 440
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
30-96 3.78e-07

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: 48.88  E-value: 3.78e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1023301064   30 RHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNApmlPSKINRAGRLLDILHTKGQRGYVVFLESLE 96
Cdd:cd08810      9 RHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCR---TTRKKRVDKLLDILAREGPDGLDALIESIR 72
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
680-749 9.84e-07

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: 47.54  E-value: 9.84e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1023301064  680 LTLLGGNARGS--FVHSVKPGSLAEKAG-LREGHQLLLLEGcirgerqsVPLDTCTKEEAHWTIQRCSGPVTL 749
Cdd:cd00136     14 FSIRGGKDGGGgiFVSRVEPGGPAARDGrLRVGDRILEVNG--------VSLEGLTHEEAVELLKSAGGEVTL 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
304-449 9.85e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 9.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  304 ILEHD--RKEA-------------LED-RQELVNRIYNLQEEARQAEelrdKYLEEKEDLELKcstlgkDCEMYKHRMNT 367
Cdd:COG1196    167 ISKYKerKEEAerkleateenlerLEDiLGELERQLEPLERQAEKAE----RYRELKEELKEL------EAELLLLKLRE 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  368 VMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQ 447
Cdd:COG1196    237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                   ..
gi 1023301064  448 SL 449
Cdd:COG1196    317 RL 318
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
151-445 1.07e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.12  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  151 ELLARLRQLEDEkkqMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDLQLEID 230
Cdd:PRK02224   360 ELREEAAELESE---LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  231 QLKHRLNKMEEecKLERNQSLKLKNDIENRP-------KKEQVLELERENEMLKTKNQELQSIIQAGK---------RSL 294
Cdd:PRK02224   437 TARERVEEAEA--LLEAGKCPECGQPVEGSPhvetieeDRERVEELEAELEDLEEEVEEVEERLERAEdlveaedriERL 514
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  295 PDSDKAILDILEHDRKEALEDR---QELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHR---MNTV 368
Cdd:PRK02224   515 EERREDLEELIAERRETIEEKReraEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERiesLERI 594
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  369 MLQLEEVERERDQAFHSRD------EAQTQYSQCLIEKdkyRKQIRELEEKNDEMRIEMVRR-----EACIVNLESKLRR 437
Cdd:PRK02224   595 RTLLAAIADAEDEIERLREkrealaELNDERRERLAEK---RERKRELEAEFDEARIEEAREdkeraEEYLEQVEEKLDE 671

                   ....*...
gi 1023301064  438 LSKDSNNL 445
Cdd:PRK02224   672 LREERDDL 679
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
137-435 1.26e-06

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: 52.87  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  137 KLQQQMKakDLQR---------CELLARLRqlEDEKKQMTLtRVELLTFQE------RYYKMKE-ERDSYNDELVK---- 196
Cdd:pfam01576  802 KLQAQMK--DLQReleearasrDEILAQSK--ESEKKLKNL-EAELLQLQEdlaaseRARRQAQqERDELADEIASgasg 876
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  197 ---VKDDNYNLAMRYAQLSEE-----KNMAVM--RSRDLQLEIDQLKHRLNKmeeecklERNQSLKLKNdienrpKKEQv 266
Cdd:pfam01576  877 ksaLQDEKRRLEARIAQLEEEleeeqSNTELLndRLRKSTLQVEQLTTELAA-------ERSTSQKSES------ARQQ- 942
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  267 leLERENEMLKTKNQELQSIIQAGKRSLPDSDKAILDILEHDRKEALEDRQ---ELVNR--------IYNLQEEARQAEE 335
Cdd:pfam01576  943 --LERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanKLVRRtekklkevLLQVEDERRHADQ 1020
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  336 LRDKYleEKEDLelkcstlgkdcemykhRMNTVMLQLEEVERERDQAFHSRdeaqtqysqcliekdkyRKQIRELEEKND 415
Cdd:pfam01576 1021 YKDQA--EKGNS----------------RMKQLKRQLEEAEEEASRANAAR-----------------RKLQRELDDATE 1065
                          330       340
                   ....*....|....*....|
gi 1023301064  416 EMriEMVRREacIVNLESKL 435
Cdd:pfam01576 1066 SN--ESMNRE--VSTLKSKL 1081
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
138-449 1.28e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 52.90  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  138 LQQQMKAKDLQRCELLARLRQLEDEKKQMTLTRVelltfqeryYKMKE------ERDSYNDELvKVKDDNYNLAMRYAQL 211
Cdd:pfam10174  201 LDQKEKENIHLREELHRRNQLQPDPAKTKALQTV---------IEMKDtkisslERNIRDLED-EVQMLKTNGLLHTEDR 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  212 SEE-KNMAVMRSRD--LQLEIDQLKHRLNKMEEE-----CKLE--RNQSLKLKNDI----ENRPKKEQVLE-LERENEML 276
Cdd:pfam10174  271 EEEiKQMEVYKSHSkfMKNKIDQLKQELSKKESEllalqTKLEtlTNQNSDCKQHIevlkESLTAKEQRAAiLQTEVDAL 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  277 KTKNQELQSIIQAGKRSLPD--SDKAILDILEHDRKEALEDRQELVN----RIYNLQEEARQaeelRDKYLEEKEDlelK 350
Cdd:pfam10174  351 RLRLEEKESFLNKKTKQLQDltEEKSTLAGEIRDLKDMLDVKERKINvlqkKIENLQEQLRD----KDKQLAGLKE---R 423
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  351 CSTLGKDCEMYKHRMNTVMLQLEEVER--ERDQAFHSRDEAQTqysqcLIEKDKYRKQIRELEEKNDEMRIEMVRREACI 428
Cdd:pfam10174  424 VKSLQTDSSNTDTALTTLEEALSEKERiiERLKEQREREDRER-----LEELESLKKENKDLKEKVSALQPELTEKESSL 498
                          330       340
                   ....*....|....*....|.
gi 1023301064  429 VNLESKLRRLSKDSNNLDQSL 449
Cdd:pfam10174  499 IDLKEHASSLASSGLKKDSKL 519
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
172-455 2.75e-06

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: 51.99  E-value: 2.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  172 ELLTFQERYYKMKEERDSYNDELVKVKDdnynlamRYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSL 251
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIEN-------RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  252 KLKNDIENrpKKEQVLELERENEMLKTKNQELQSIIQAGKRSLPDSD----KAILDILEHDRKEALEDRQELVNRIYNLQ 327
Cdd:TIGR02169  748 SLEQEIEN--VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEEVSRIEARLREIEQKLNRLT 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  328 EEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKhrmntvmLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQI 407
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN-------GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1023301064  408 RELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSLPRNLPV 455
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
127-451 8.19e-06

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 50.43  E-value: 8.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  127 LTHFLMNEVIKLQQQMKAKDLQRCELLARLRQLEDEKKqmTLTRVELLTFQE--RYYKMKEERDSYNDELVKVKDDNYN- 203
Cdd:TIGR00606  495 LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT--TRTQMEMLTKDKmdKDEQIRKIKSRHSDELTSLLGYFPNk 572
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  204 --LAMRYAQLSEEKNMAVMRSRDLQLEI---DQLKHRLNKMEEE-----------------CKLERNQSLKLKNDIENRP 261
Cdd:TIGR00606  573 kqLEDWLHSKSKEINQTRDRLAKLNKELaslEQNKNHINNELESkeeqlssyedklfdvcgSQDEESDLERLKEEIEKSS 652
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  262 KKEQVL------------ELERENE--------MLKTKN--QELQSIIQAGKRSLPDSDKAI---LDILEHDRKEAL--- 313
Cdd:TIGR00606  653 KQRAMLagatavysqfitQLTDENQsccpvcqrVFQTEAelQEFISDLQSKLRLAPDKLKSTeseLKKKEKRRDEMLgla 732
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  314 EDRQELVNRIYNLQEEARQA-EELRDKYLEEKEDLELKCSTLG---------KDCEMYKHRMNTVMLQLEEVERERDQAF 383
Cdd:TIGR00606  733 PGRQSIIDLKEKEIPELRNKlQKVNRDIQRLKNDIEEQETLLGtimpeeesaKVCLTDVTIMERFQMELKDVERKIAQQA 812
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  384 HSRD--EAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSLPR 451
Cdd:TIGR00606  813 AKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR 882
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
134-339 9.03e-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: 50.12  E-value: 9.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  134 EVIKLQQQMKAKDLQRCELLARL---RQLEDEK--KQMTLTRVELLTFQERYYKMKEERDsyndELVKVKDDNYNLAMRY 208
Cdd:pfam17380  361 ELERIRQEEIAMEISRMRELERLqmeRQQKNERvrQELEAARKVKILEEERQRKIQQQKV----EMEQIRAEQEEARQRE 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  209 AQ-LSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECK-----LERNQSLKLKNDIENRPKKEQVLElERENEMLKTKNQE 282
Cdd:pfam17380  437 VRrLEEERAREMERVRLEEQERQQQVERLRQQEEERKrkkleLEKEKRDRKRAEEQRRKILEKELE-ERKQAMIEEERKR 515
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  283 lqsiiQAGKRSLPDSDKAILDilEHDRKEALEDR---QELVNRiYNLQEEARQAEELRDK 339
Cdd:pfam17380  516 -----KLLEKEMEERQKAIYE--EERRREAEEERrkqQEMEER-RRIQEQMRKATEERSR 567
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
137-426 1.65e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  137 KLQQQMKAKDLQRCELLARLRQLEDEKKQMTLT----RVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLS 212
Cdd:COG1196    243 ELEAELEELEAELEELEAELAELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  213 EEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENrpKKEQVLELERENEMLKTKNQELQSIIQAGKR 292
Cdd:COG1196    323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE--AEAELAEAEEELEELAEELLEALRAAAELAA 400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  293 SLPDSDKAILDILEHD--RKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELkcstlgkdcemykhrmnTVML 370
Cdd:COG1196    401 QLEELEEAEEALLERLerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE-----------------ALLE 463
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1023301064  371 QLEEVERERDQAFHSRDEAQTQysqclIEKDKYRKQIRELEEKNDEMRIEMVRREA 426
Cdd:COG1196    464 LLAELLEEAALLEAALAELLEE-----LAEAAARLLLLLEAEADYEGFLEGVKAAL 514
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
131-350 1.73e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQQMKAKDLQRCELLARLRQLEDEKKQMTLTRVELltfqeryykmKEERDSYNDELVKVKDDNYNLAMRYAQ 210
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----------EEELEELEEELEEAEEELEEAEAELAE 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  211 LSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRpkkeqvleLERENEMLKTKNQELQSIIQAg 290
Cdd:COG1196    363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL--------LERLERLEEELEELEEALAEL- 433
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  291 kRSLPDSDKAILDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELK 350
Cdd:COG1196    434 -EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
680-749 2.08e-05

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: 43.91  E-value: 2.08e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1023301064   680 LTLLGG--NARGSFVHSVKPGSLAEKAGLREGHQLLLLEGcirgerqsVPLDTCTKEEAHWTIQRCSGPVTL 749
Cdd:smart00228   16 FSLVGGkdEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNG--------TSVEGLTHLEAVDLLKKAGGKVTL 79
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
139-440 2.31e-05

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: 48.63  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  139 QQQMKAKDLQRCELLARlrQLEDEkkqmtlTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNMA 218
Cdd:pfam01576  318 QQELRSKREQEVTELKK--ALEEE------TRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  219 VMRSRDLQLEIDQLKHRLNKME---EECKLERNQSLKLKNDIENRPKKEQvLELERENEMLktkNQELQSIIQAGKrslp 295
Cdd:pfam01576  390 QAELRTLQQAKQDSEHKRKKLEgqlQELQARLSESERQRAELAEKLSKLQ-SELESVSSLL---NEAEGKNIKLSK---- 461
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  296 dsDKAILDILEHDRKEAL--EDRQELVN--RIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVMLQ 371
Cdd:pfam01576  462 --DVSSLESQLQDTQELLqeETRQKLNLstRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1023301064  372 LEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSK 440
Cdd:pfam01576  540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQ 608
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
131-426 2.39e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.60  E-value: 2.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQQMKAKDLQRCELLARLRQLEDEKKQMtltRVELLTFQERYYKMKEERDSYNDELvkvkddnynlamryAQ 210
Cdd:COG1340     13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDEL---NAQVKELREEAQELREKRDELNEKV--------------KE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  211 LSEEKNMAVMRSRDLQLEIDQLKhrlnKMEEECKLERNQSLKLKNDIENRPKKEQ--VLELERENEMLKtKNQELQSIIQ 288
Cdd:COG1340     76 LKEERDELNEKLNELREELDELR----KELAELNKAGGSIDKLRKEIERLEWRQQteVLSPEEEKELVE-KIKELEKELE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  289 AgkrslpdsdkaildilehdRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEekedlelkcstLGKDCEMYKHRMNTV 368
Cdd:COG1340    151 K-------------------AKKALEKNEKLKELRAELKELRKEAEEIHKKIKE-----------LAEEAQELHEEMIEL 200
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023301064  369 MLQLEEVERERDQAFHSRDEAQ-------TQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREA 426
Cdd:COG1340    201 YKEADELRKEADELHKEIVEAQekadelhEEIIELQKELRELRKELKKLRKKQRALKREKEKEEL 265
SH3_ZO cd11859
Src homology 3 domain of the Tight junction proteins, Zonula occludens (ZO) proteins; ZO ...
777-839 3.74e-05

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: 42.66  E-value: 3.74e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1023301064  777 YIRLNLNISSQLDAcTMSLKCDDVVHVRDTMYQDR-HEWLCARVDPfTDHDLDMGTIPSYSRAQ 839
Cdd:cd11859      1 YIRTHFDYEKPAKG-ELSFKKGEVFHVVDTLYQGTvGSWQAVRVGR-NHQELERGVIPNKSRAE 62
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
142-425 3.82e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 47.81  E-value: 3.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  142 MKAKDLQRCELLARLRQLEDEKKQMTLTR--VELLTFQERYYKMKEER-DSYNDELVKVKDDNYNLAmryAQLSEEKNMA 218
Cdd:pfam05557  192 SKSELARIPELEKELERLREHNKHLNENIenKLLLKEEVEDLKRKLEReEKYREEAATLELEKEKLE---QELQSWVKLA 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  219 VM------RSRDLQLEIDQL-------KHRLNKMEEECKLERNQSLKLKNDIENRPKKeqVLELERENEMLKTKNQELQ- 284
Cdd:pfam05557  269 QDtglnlrSPEDLSRRIEQLqqreivlKEENSSLTSSARQLEKARRELEQELAQYLKK--IEDLNKKLKRHKALVRRLQr 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  285 SIIQAGKRSlpDSDKAILdilehdrkEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHR 364
Cdd:pfam05557  347 RVLLLTKER--DGYRAIL--------ESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQ 416
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023301064  365 MNTVMLQLEEVERERDQAfhSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRRE 425
Cdd:pfam05557  417 AQTLERELQALRQQESLA--DPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRC 475
PDZ3_ZO1-like_domain cd06729
PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs ZO-2 and ZO-3, and related domains; PDZ ...
680-736 3.85e-05

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: 42.94  E-value: 3.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1023301064  680 LTLLGGNARGSFVHSVKPGSLAEKAGLREGHQLLLLEGcirgerqsVPLDTCTKEEA 736
Cdd:cd06729     15 LRLAGGNDVGIFVAGVQEGSPAEKQGLQEGDQILKVNG--------VDFRNLTREEA 63
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
131-449 4.48e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 4.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQQMKAKdlqRCELLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQ 210
Cdd:COG4372     43 LQEELEQLREELEQA---REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  211 LSEEKnmavmrsRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPKKEQVLELERENEMLKTKNQELQSIIQAG 290
Cdd:COG4372    120 LQKER-------QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  291 KRSLPDSDKAILDILEHDrKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCST---------LGKDCEMY 361
Cdd:COG4372    193 NRNAEKEEELAEAEKLIE-SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEvilkeieelELAILVEK 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  362 KHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKD 441
Cdd:COG4372    272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLL 351

                   ....*...
gi 1023301064  442 SNNLDQSL 449
Cdd:COG4372    352 DNDVLELL 359
PLN02939 PLN02939
transferase, transferring glycosyl groups
122-435 4.48e-05

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 47.97  E-value: 4.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  122 EGHEGLTHFLMNEVIKLQQQMKAKDLQRCEllARLRQLEDEKKqmTLTRVELLtfqERYYKMKEERDSYNDELVKVK-DD 200
Cdd:PLN02939   120 KDGEQLSDFQLEDLVGMIQNAEKNILLLNQ--ARLQALEDLEK--ILTEKEAL---QGKINILEMRLSETDARIKLAaQE 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  201 NYNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPKKEQ-VLELERENEMLKTK 279
Cdd:PLN02939   193 KIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEErVFKLEKERSLLDAS 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  280 NQELQSiiqagKRSLPDSDKAILDILEHD-RKEALEDRQELVNRIYNLQEEA----RQAEELRDKYleEKEDLELKCSTL 354
Cdd:PLN02939   273 LRELES-----KFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAalvlDQNQDLRDKV--DKLEASLKEANV 345
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  355 GKDCEMYKHRMNTVMLQLEEVERERDQAFHSR---DEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVN- 430
Cdd:PLN02939   346 SKFSSYKVELLQQKLKLLEERLQASDHEIHSYiqlYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSEFWSRILLLIDg 425

                   ....*..
gi 1023301064  431 --LESKL 435
Cdd:PLN02939   426 wlLEKKI 432
PDZ4_DLG5-like cd06766
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
680-749 7.86e-05

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: 42.38  E-value: 7.86e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023301064  680 LTLLGGNARGSFVHSVKPGSLA-EKAGLREGHQLLllegcirgERQSVPLDTCTKEEAHWTIQRCSGPVTL 749
Cdd:cd06766     16 IQLCGGNLHGIFVEDVEDDSPAkGPDGLVPGDLIL--------EYNSVDMRNKTAEEAYLEMLKPAETVTL 78
PTZ00121 PTZ00121
MAEBL; Provisional
110-443 8.89e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 8.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  110 EPTRRFSTIVVEEGHEGLTHFLMNEVIKLQQQMKAKDLQRCEllaRLRQLEDEKKQMTLTRVELLtfqeryyKMKEERDS 189
Cdd:PTZ00121  1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE---EKKKADEAKKAEEKKKADEA-------KKKAEEAK 1315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  190 YNDELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDlqlEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPKK----EQ 265
Cdd:PTZ00121  1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA---EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKaeekKK 1392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  266 VLELERENEMLKTKNQELQSIIQAGKRS---------LPDSDKAILDILEHDRKEALEDRQELVNRIYNLQ---EEARQA 333
Cdd:PTZ00121  1393 ADEAKKKAEEDKKKADELKKAAAAKKKAdeakkkaeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKkkaEEAKKA 1472
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  334 EELRDKYLEEKEDLELKcstlgKDCEMYKHRMNtvmlQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRK--QIRELE 411
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAK-----KKAEEAKKKAD----EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadEAKKAE 1543
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1023301064  412 E--KNDEMR-IEMVRREACIVNLESKlRRLSKDSN 443
Cdd:PTZ00121  1544 EkkKADELKkAEELKKAEEKKKAEEA-KKAEEDKN 1577
PDZ2_harmonin cd06738
PDZ domain 2 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ...
685-713 9.33e-05

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: 41.92  E-value: 9.33e-05
                           10        20
                   ....*....|....*....|....*....
gi 1023301064  685 GNARGSFVHSVKPGSLAEKAGLREGHQLL 713
Cdd:cd06738     24 TQKPGIFISNVKPGSLAEEVGLEVGDQIV 52
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
148-455 1.10e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 46.27  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  148 QRCELLARLRQLEDEKKQMTLtrvelltfqeryykmkeerdSYNDELVKVKDDNYNLAMRYAQLSEeknmavmRSRDLQL 227
Cdd:pfam05557    3 ELIESKARLSQLQNEKKQMEL--------------------EHKRARIELEKKASALKRQLDRESD-------RNQELQK 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  228 EIDQLKHRLNKMEEECK--LERNQSLKLKNDIENRPKKEQVLELERENEMLKTKNQE---LQSIIQAGKRSLPDSDKAIL 302
Cdd:pfam05557   56 RIRLLEKREAEAEEALReqAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNElseLRRQIQRAELELQSTNSELE 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  303 DILE-HDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDcemykhrMNTVMLQLEEVERERDQ 381
Cdd:pfam05557  136 ELQErLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKN-------SKSELARIPELEKELER 208
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023301064  382 AFHSRDEAQTQYSQCLIEKDkyrkQIRELEEKNDemRIEMVRREACIVNLE-SKLRRLSKDSNNLDQSLPRNLPV 455
Cdd:pfam05557  209 LREHNKHLNENIENKLLLKE----EVEDLKRKLE--REEKYREEAATLELEkEKLEQELQSWVKLAQDTGLNLRS 277
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
153-350 1.21e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  153 LARLRQLEDEKKQMTLTrvelltfQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKN--MAVMRSRDLQLEID 230
Cdd:COG4717     70 LKELKELEEELKEAEEK-------EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELA 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  231 QLKHRLNKMEEecklernqslklkndienrpKKEQVLELERENEMLKTKNQELQSIIQAGKRSLPDSDKAILDILEHDRK 310
Cdd:COG4717    143 ELPERLEELEE--------------------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1023301064  311 EALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELK 350
Cdd:COG4717    203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
131-350 1.27e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQQMKAKDLQRceLLARLR-QLEDEKKQMTLTRVELLTFQERYykmkeerdsyndELVKVKDDNYNLAMRYA 209
Cdd:COG3206    157 LAEAYLEQNLELRREEARK--ALEFLEeQLPELRKELEEAEAALEEFRQKN------------GLVDLSEEAKLLLQQLS 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  210 QLSEEKNmavmrsrDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPKKEQVLELERE-NEMLKTKN------QE 282
Cdd:COG3206    223 ELESQLA-------EARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAElAELSARYTpnhpdvIA 295
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023301064  283 LQSIIQAGKRSLPDSDKAILDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELK 350
Cdd:COG3206    296 LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
680-749 1.58e-04

PDZ domain 3 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 3 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 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: 467248 [Multi-domain]  Cd Length: 82  Bit Score: 41.54  E-value: 1.58e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  680 LTLLGGNARGSFVHSVKPGSLAEKAGLREGHQLLllegcirgERQSVPLDTCTKEEAHWTIQRCSGPVTL 749
Cdd:cd06767     17 ISIVSGENGGIFVSSVTEGSLAHQAGLEYGDQLL--------EVNGINLRNATEQQAALILRQCGDTITM 78
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
263-436 2.02e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  263 KEQVLELERENEMLKTKNQELQSIIQA--GKRSLPDSDKAILDILEHDRKEALEDRQELVNRIynlQEEARQAEELRDky 340
Cdd:PRK02224   219 DEEIERYEEQREQARETRDEADEVLEEheERREELETLEAEIEDLRETIAETEREREELAEEV---RDLRERLEELEE-- 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  341 leEKEDLELKCSTLGKDCEmykhrmnTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIE 420
Cdd:PRK02224   294 --ERDDLLAEAGLDDADAE-------AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE 364
                          170
                   ....*....|....*.
gi 1023301064  421 MVRREACIVNLESKLR 436
Cdd:PRK02224   365 AAELESELEEAREAVE 380
SH3_ZO-3 cd12028
Src homology 3 domain of the Tight junction protein, Zonula occludens protein 3; ZO-3 is a ...
774-839 3.57e-04

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: 39.85  E-value: 3.57e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023301064  774 DSFYIRLNLNISSQlDACTMSLKCDDVVHVRDTMYQDR-HEWLCARVDpfTD-HDLDMGTIPSYSRAQ 839
Cdd:cd12028      1 DSFYIRTHFDYEPD-PPSGLSFTRGEVFHVLDTMHRGKlGSWLAVRMG--RDlREMEKGIIPNQSRAE 65
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
131-310 3.76e-04

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: 44.67  E-value: 3.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQQMKAKdlqrcellarLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQ 210
Cdd:TIGR02169  355 LTEEYAELKEELEDL----------RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  211 LSEEknMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPKKEQVLELERENEMLKTKNQELQSIIQAG 290
Cdd:TIGR02169  425 LNAA--IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
                          170       180
                   ....*....|....*....|
gi 1023301064  291 KRSLPDSdKAILDILEHDRK 310
Cdd:TIGR02169  503 EERVRGG-RAVEEVLKASIQ 521
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
134-425 4.00e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.14  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  134 EVIKLQQQMKAKDLQRCEllARLRQLEDEKKQMTLTRVElltFQERYYKMKEERDSYNDELVKVKDDnynlAMRYAQLSE 213
Cdd:pfam13868   52 ERERALEEEEEKEEERKE--ERKRYRQELEEQIEEREQK---RQEEYEEKLQEREQMDEIVERIQEE----DQAEAEEKL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  214 EKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQS-LKLKNDIENRpKKEQVLELERENEMLKTKNQELQSIIQAGKR 292
Cdd:pfam13868  123 EKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEyLKEKAEREEE-REAEREEIEEEKEREIARLRAQQEKAQDEKA 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  293 SLpDSDKAILDILEHDRKEALEDRQELvnriynlQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVMLQL 372
Cdd:pfam13868  202 ER-DELRAKLYQEEQERKERQKEREEA-------EKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAED 273
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1023301064  373 EEVERERDQAFHSRDEAQTQYSQCLIE---KDKYRKQIRELEEKNDEMRIEMVRRE 425
Cdd:pfam13868  274 EEIEQEEAEKRRMKRLEHRRELEKQIEereEQRAAEREEELEEGERLREEEAERRE 329
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
173-257 4.57e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 43.08  E-value: 4.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  173 LLTFQERYYKMKEERDSYNDELVKvkddnyNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRL-NKMEEECKLERNQSL 251
Cdd:cd07649     91 LLNFRENFKKDMKKLDHHIADLRK------QLASRYAAVEKARKALLERQKDLEGKTQQLEIKLsNKTEEDIKKARRKST 164

                   ....*.
gi 1023301064  252 KLKNDI 257
Cdd:cd07649    165 QAGDDL 170
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
151-335 4.69e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 4.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  151 ELLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDdnynlamRYAQLSEEKNmavmrsrDLQLEID 230
Cdd:COG4913    665 SAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKG-------EIGRLEKELE-------QAEEELD 730
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  231 QLKHRLNKMEEECKLERNQSLKLKNDIENRPKKEQVL------ELERENEMLKTKNQELQSIIQAGKRSLPDSDK----- 299
Cdd:COG4913    731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELrenleeRIDALRARLNRAEEELERAMRAFNREWPAETAdldad 810
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1023301064  300 --------AILDILEHDRKEALEDR-QELVNR-----IYNLQEEARQAEE 335
Cdd:COG4913    811 leslpeylALLDRLEEDGLPEYEERfKELLNEnsiefVADLLSKLRRAIR 860
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
228-451 5.50e-04

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: 43.60  E-value: 5.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  228 EIDQLKHRLNKMEEECKLERNQSLKLKNDIENrpKKEQVLELERENEMLKTKNQELQSIIQAGKRSLPDSDKAILDIleh 307
Cdd:COG4942     21 AAAEAEAELEQLQQEIAELEKELAALKKEEKA--LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--- 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  308 dRKEALEDRQELVNRIYNLQEEARQAeelRDKYLEEKEDLelkcSTLGKDCEMYKHRMNTVMLQLEEVERERDQAFHSRD 387
Cdd:COG4942     96 -RAELEAQKEELAELLRALYRLGRQP---PLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1023301064  388 EAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSLPR 451
Cdd:COG4942    168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
252-418 5.81e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.33  E-value: 5.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  252 KLKNDIENRPKK----EQVLElerenEMLKTKNQELQSIIQAGKrSLPDSDKAILDilEHDRKEALEDRQELvnriynLQ 327
Cdd:cd16269    153 KLVEKYRQVPRKgvkaEEVLQ-----EFLQSKEAEAEAILQADQ-ALTEKEKEIEA--ERAKAEAAEQERKL------LE 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  328 EEARQAEELrdkyLEEKEdlelkcstlgkdcEMYKHRMNTVMLQLEEvERERDQAFHSRDEAQTQYSQCLIEKDKYRKQI 407
Cdd:cd16269    219 EQQRELEQK----LEDQE-------------RSYEEHLRQLKEKMEE-ERENLLKEQERALESKLKEQEALLEEGFKEQA 280
                          170
                   ....*....|.
gi 1023301064  408 RELEEKNDEMR 418
Cdd:cd16269    281 ELLQEEIRSLK 291
PDZ1_FL-whirlin cd06740
PDZ domain 1 of the full-length isoform of whirlin and related domains; PDZ (PSD-95 ...
689-736 5.82e-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: 5.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1023301064  689 GSFVHSVKPGSLAEKAGLREGHQLLLLEGcirgerqsVPLDTCTKEEA 736
Cdd:cd06740     28 GIYVSLVEPGSLAEKEGLRVGDQILRVND--------VSFEKVTHAEA 67
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
129-438 6.13e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 6.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  129 HFLMNEVIKLQQQM-----KAKDLQRCELLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVK----- 198
Cdd:PRK03918   361 HELYEEAKAKKEELerlkkRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpv 440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  199 -------DDNYNLAMRY----AQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLErnQSLKLKNDIENRPKKEQVL 267
Cdd:PRK03918   441 cgrelteEHRKELLEEYtaelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--ELAEQLKELEEKLKKYNLE 518
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  268 ELEREN---EMLKTKNQELQSIIQAGKRSLPDSD--KAILDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLE 342
Cdd:PRK03918   519 ELEKKAeeyEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE 598
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  343 E--KEDLELKCStlgkdcemyKHRMNTVMLQLEEVERERDQAFHSRDEAQTqysqcliEKDKYRKQIRELEEKNDEMRIE 420
Cdd:PRK03918   599 PfyNEYLELKDA---------EKELEREEKELKKLEEELDKAFEELAETEK-------RLEELRKELEELEKKYSEEEYE 662
                          330
                   ....*....|....*...
gi 1023301064  421 MVRREacIVNLESKLRRL 438
Cdd:PRK03918   663 ELREE--YLELSRELAGL 678
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
210-289 6.64e-04

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 39.57  E-value: 6.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  210 QLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEEcklerNQSLKLKNDienrpkkeqvlELERENEMLKTKNQELQSIIQA 289
Cdd:COG3074      8 ELEAKVQQAVDTIELLQMEVEELKEKNEELEQE-----NEELQSENE-----------ELQSENEQLKTENAEWQERIRS 71
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
150-387 7.79e-04

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: 43.21  E-value: 7.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  150 CELLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDLQLEI 229
Cdd:COG4942     13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  230 DQLKHRLNKMEEE--------CKLERNQSLKLKNDIENrpkkeqVLELERENEMLKTKNQELQSIIQAGKRSLpDSDKAI 301
Cdd:COG4942     93 AELRAELEAQKEElaellralYRLGRQPPLALLLSPED------FLDAVRRLQYLKYLAPARREQAEELRADL-AELAAL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  302 LDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDcemyKHRMNTVMLQLEEVERERDQ 381
Cdd:COG4942    166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE----AEELEALIARLEAEAAAAAE 241

                   ....*.
gi 1023301064  382 AFHSRD 387
Cdd:COG4942    242 RTPAAG 247
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
134-340 8.62e-04

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: 43.52  E-value: 8.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  134 EVIKLQQQMKAKDLQRCELLARLRQLEdekKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSE 213
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELE---REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  214 EKNMAVMRSRDLQLEIDQLKHRLNKMEEEcklernqSLKLKNDIENrpKKEQVLELERENEM----LKTKNQELQSIIQa 289
Cdd:TIGR02169  393 KLEKLKREINELKRELDRLQEELQRLSEE-------LADLNAAIAG--IEAKINELEEEKEDkaleIKKQEWKLEQLAA- 462
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1023301064  290 gkrSLPDSDKAILDILEHDRKeaLEDRQELVNRIYNLQEEARQAEELRDKY 340
Cdd:TIGR02169  463 ---DLSKYEQELYDLKEEYDR--VEKELSKLQRELAEAEAQARASEERVRG 508
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
131-348 9.37e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 9.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQQMK--AKDLQRCELL-ARLRQLEDEKKQMTLTRVELLT-FQERYYKMKEERDSYNDELVKVKDDNYNLAM 206
Cdd:PRK03918   530 LKEKLIKLKGEIKslKKELEKLEELkKKLAELEKKLDELEEELAELLKeLEELGFESVEELEERLKELEPFYNEYLELKD 609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  207 RYAQLSEEKNmavmRSRDLQLEIDQLKHRLNKME---EECKLERNQSLKLKNDIENRPKKEQVLELERENEMLKTKNQEL 283
Cdd:PRK03918   610 AEKELEREEK----ELKKLEEELDKAFEELAETEkrlEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEEL 685
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1023301064  284 QSIIQAGKRSLpdsdkaildileHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLE 348
Cdd:PRK03918   686 EKRREEIKKTL------------EKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
131-347 9.65e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.19  E-value: 9.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQ--------------QMKAKDLQRCELLARLRQ----LEDEKKQMTLTRVELLTFQERYYKMKEERDSYNd 192
Cdd:pfam05557  281 LSRRIEQLQQreivlkeenssltsSARQLEKARRELEQELAQylkkIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYR- 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  193 ELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECK--------LERN-QSLKLKNDIENRP-K 262
Cdd:pfam05557  360 AILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGgykqqaqtLERElQALRQQESLADPSyS 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  263 KEQVLELERENEMLKTKNQELQSII-----QAGKRSLP-DSDKAILDILEHDRKEALEDRQELVNRIYNLQEEARQAEEL 336
Cdd:pfam05557  440 KEEVDSLRRKLETLELERQRLREQKnelemELERRCLQgDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRL 519
                          250
                   ....*....|.
gi 1023301064  337 RDKYLEEKEDL 347
Cdd:pfam05557  520 LKKLEDDLEQV 530
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
154-258 1.15e-03

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 39.84  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  154 ARLRQLEdekkqmtltrVELLTFQERYYKMKEERDSYNDELVKVKDDNynlamryaqlsEEKNMAVMRSRDLQLEIDQLK 233
Cdd:pfam12325   19 STIRRLE----------GELASLKEELARLEAQRDEARQEIVKLMKEN-----------EELKELKKELEELEKELKELE 77
                           90       100
                   ....*....|....*....|....*...
gi 1023301064  234 HRLNKMEE---EcKLERNQslKLKNDIE 258
Cdd:pfam12325   78 QRYETTLEllgE-KSEEVE--ELKADVE 102
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
133-335 1.54e-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: 42.44  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  133 NEVIKLQQQMKAKDLQRCELLARLRQLEdekKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMR-YAQL 211
Cdd:COG4942     48 KEEKALLKQLAALERRIAALARRIRALE---QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpPLAL 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  212 ---SEEKNMAVMRSRDLQLEIDQLKHRLNKMEEEckLERNQSLKLKNDIENRPKKEQVLELERENEMLKTKNQELQSIIQ 288
Cdd:COG4942    125 llsPEDFLDAVRRLQYLKYLAPARREQAEELRAD--LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1023301064  289 AGKRSLPDSDKAIldilehdrKEALEDRQELVNRIYNLQEEARQAEE 335
Cdd:COG4942    203 RLEKELAELAAEL--------AELQQEAEELEALIARLEAEAAAAAE 241
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
213-445 1.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  213 EEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENrpKKEQVLELERENEMLKTKNQELQSIIQAgKR 292
Cdd:PRK03918   179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK--LEKEVKELEELKEEIEELEKELESLEGS-KR 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  293 SLPDSDKAILDILEHDRKE--ALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLG----------KDCEM 360
Cdd:PRK03918   256 KLEEKIRELEERIEELKKEieELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEeeingieeriKELEE 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  361 YKHRMNTVMLQLEEVERERdQAFHSRDEAQTQYSQCLIEKDKYRKQ------------IRELEEKNDEMRIEMVRREACI 428
Cdd:PRK03918   336 KEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRltgltpeklekeLEELEKAKEEIEEEISKITARI 414
                          250
                   ....*....|....*..
gi 1023301064  429 VNLESKLRRLSKDSNNL 445
Cdd:PRK03918   415 GELKKEIKELKKAIEEL 431
PDZ1_L-delphilin-like cd06743
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
683-717 1.63e-03

PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family 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: 467225 [Multi-domain]  Cd Length: 76  Bit Score: 38.42  E-value: 1.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1023301064  683 LGGNARgSFVHSVKPGSLAEKAGLREGHQLLLLEG 717
Cdd:cd06743     15 IGGSGP-CYILSVEEGSSAHAAGLQPGDQILELDG 48
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
682-713 1.84e-03

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: 38.40  E-value: 1.84e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1023301064  682 LLGGNARGS--FVHSVKPGSLAEKAGLREGHQLL 713
Cdd:cd06755     18 LLGGSEKGFgiFVSKVEKGSKAAEAGLKRGDQIL 51
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
148-446 2.48e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  148 QRCELLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEE---------------------RDSYNDELVKVKDDNYNLAM 206
Cdd:PRK02224   214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEletleaeiedlretiaetereREELAEEVRDLRERLEELEE 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  207 RYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENrpKKEQVLELERENEMLKTKNQELQSI 286
Cdd:PRK02224   294 ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES--LREDADDLEERAEELREEAAELESE 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  287 IQAGKRSLPDSDKAI--------------------LDILEHDRKEALEDRQELVNRIYNLQEEARQAEELrdkyLEEKED 346
Cdd:PRK02224   372 LEEAREAVEDRREEIeeleeeieelrerfgdapvdLGNAEDFLEELREERDELREREAELEATLRTARER----VEEAEA 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  347 L--ELKCSTLGKDCEMYKH--RMNTVMLQLEEVERERDQAFHSRDEAQTQYSQcLIEKDKYRKQIRELEEKND--EMRIE 420
Cdd:PRK02224   448 LleAGKCPECGQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREdlEELIA 526
                          330       340
                   ....*....|....*....|....*.
gi 1023301064  421 mvRREACIVNLESKLRRLSKDSNNLD 446
Cdd:PRK02224   527 --ERRETIEEKRERAEELRERAAELE 550
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
313-449 2.51e-03

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: 41.97  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  313 LED-RQELVNRIYNLQEEARQAEELRDkYLEEKEDLELKCSTLgkdcemykhrmntvmlQLEEVERERDQAFHSRDEAQT 391
Cdd:TIGR02168  191 LEDiLNELERQLKSLERQAEKAERYKE-LKAELRELELALLVL----------------RLEELREELEELQEELKEAEE 253
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1023301064  392 QYsqcliekDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSL 449
Cdd:TIGR02168  254 EL-------EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
223-426 2.67e-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: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  223 RDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPKKEQVLE-----LERENEMLKTKNQELQSIIQAGKRSLPDS 297
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEqelaaLEAELAELEKEIAELRAELEAQKEELAEL 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  298 DKAILDILEHDRKEAL---EDRQELVNRIYNL----QEEARQAEELRDKyLEEKEDLELKCSTLGKDCEMYKHRMNTVML 370
Cdd:COG4942    110 LRALYRLGRQPPLALLlspEDFLDAVRRLQYLkylaPARREQAEELRAD-LAELAALRAELEAERAELEALLAELEEERA 188
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1023301064  371 QLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREA 426
Cdd:COG4942    189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
233-413 2.94e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  233 KHRLNKMEEECKLERNQSLKLKNDiENRPKKEQVLELERENEMLKTKNQELQSIIQagkrslpdsDKAILDILEHDRKEA 312
Cdd:COG4717     65 KPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELE---------KLEKLLQLLPLYQEL 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  313 LEDRQELVNRIYNLQEEARQAEELRDKyLEEKEDLELKCSTLGKDCEMYKHRMNTVML-QLEEVERERDQAFHSRDEAQT 391
Cdd:COG4717    135 EALEAELAELPERLEELEERLEELREL-EEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEE 213
                          170       180
                   ....*....|....*....|..
gi 1023301064  392 QYSQCLIEKDKYRKQIRELEEK 413
Cdd:COG4717    214 ELEEAQEELEELEEELEQLENE 235
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
688-713 2.99e-03

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


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 37.80  E-value: 2.99e-03
                           10        20
                   ....*....|....*....|....*.
gi 1023301064  688 RGSFVHSVKPGSLAEKAGLREGHQLL 713
Cdd:cd06768     23 PGHFIREVDPGSPAERAGLKDGDRLV 48
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
136-433 3.21e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  136 IKLQQQMKAKDLQRCELLARLRQLEDEKKQMTLTRVELLTFQERyyKMKEERDSYNDELVKVKDdnynLAMRYAQLSEEK 215
Cdd:PRK03918   174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP--ELREELEKLEKEVKELEE----LKEEIEELEKEL 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  216 NMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKndiENRPKKEQVLELERENEMLKTKNQELQsiiqagKRslp 295
Cdd:PRK03918   248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK---ELKEKAEEYIKLSEFYEEYLDELREIE------KR--- 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  296 dsdKAILDILEHDRKEALEDRQELVNRIYNLQEEArqaEELRDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVMLQLEEV 375
Cdd:PRK03918   316 ---LSRLEEEINGIEERIKELEEKEERLEELKKKL---KELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKL 389
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1023301064  376 ERERDQAFHsrdeaqtqysqcliEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLES 433
Cdd:PRK03918   390 EKELEELEK--------------AKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
269-452 3.43e-03

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: 41.58  E-value: 3.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  269 LERENEM--LKTKNQELQSIIQAGKRSLPDSDKAiLDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKED 346
Cdd:TIGR02168  673 LERRREIeeLEEKIEELEEKIAELEKALAELRKE-LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  347 LELKCSTLGKDCEMYKHRMNTVMLQLEEVERERDQAfhsrdeaQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREA 426
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180
                   ....*....|....*....|....*.
gi 1023301064  427 CIVNLESKLRRLSKDSNNLDQSLPRN 452
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEEL 850
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
134-449 3.45e-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: 41.70  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  134 EVIKLQQQMKAKDLQRCELLARLRQLEDEkKQMTLTRVElltfqeryykmkEERDSYNDELVKVKDDNYNLAMRYAQLSE 213
Cdd:pfam01576  216 ESTDLQEQIAELQAQIAELRAQLAKKEEE-LQAALARLE------------EETAQKNNALKKIRELEAQISELQEDLES 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  214 EK---NMAVMRSRDLQLEIDQLKHRL------NKMEEECKLERNQSL-KLKNDIEN------------RPKKEQVLE--- 268
Cdd:pfam01576  283 ERaarNKAEKQRRDLGEELEALKTELedtldtTAAQQELRSKREQEVtELKKALEEetrsheaqlqemRQKHTQALEelt 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  269 ------------LERENEMLKTKNQELQSIIQAGKRSLPDSdkaildilEHDRKEALEDRQELVNRiynLQEEARQAEEL 336
Cdd:pfam01576  363 eqleqakrnkanLEKAKQALESENAELQAELRTLQQAKQDS--------EHKRKKLEGQLQELQAR---LSESERQRAEL 431
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  337 RDKYLEEK----------EDLELKCSTLGKDCEMYKHRMNTVMLQLEEVERER-------DQAFHSRDEAQTQYSQCLIE 399
Cdd:pfam01576  432 AEKLSKLQselesvssllNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEA 511
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1023301064  400 KDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSL 449
Cdd:pfam01576  512 KRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
131-416 4.35e-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: 4.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQQMKAKDLQrceLLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNynlamryAQ 210
Cdd:TIGR00618  533 GEQTYAQLETSEEDVYHQ---LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT-------EK 602
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  211 LSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLkndienrpkkeqvLELERENEMLKTKNQELQSI-IQA 289
Cdd:TIGR00618  603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKL-------------TALHALQLTLTQERVREHALsIRV 669
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  290 GKRSLPDSDKAILDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRdkylEEKEDLELKCSTLGKDCEMYKHRMNTVm 369
Cdd:TIGR00618  670 LPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD----REFNEIENASSSLGSDLAAREDALNQS- 744
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1023301064  370 lqLEEVERERDQAFHSRDEAQTQYSQ----CLIEKDKYRKQIRELEEKNDE 416
Cdd:TIGR00618  745 --LKELMHQARTVLKARTEAHFNNNEevtaALQTGAELSHLAAEIQFFNRL 793
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
131-344 4.46e-03

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: 41.16  E-value: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  131 LMNEVIKLQQQMKAKDLQRCELLARLRQLEDEKKQMTLTRVEL------LTFQERYYKMKEERDSYNDELVKVKDDNYNL 204
Cdd:TIGR04523  501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLedelnkDDFELKKENLEKEIDEKNKEIEELKQTQKSL 580
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  205 amryaqlsEEKNmavmrsrdlqleiDQLKHRLNKMEEECKlernqslKLKNDIENrpKKEQVLELERENEMLKTKNQELQ 284
Cdd:TIGR04523  581 --------KKKQ-------------EEKQELIDQKEKEKK-------DLIKEIEE--KEKKISSLEKELEKAKKENEKLS 630
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1023301064  285 SI---IQAGKRSLPDSDKAILDILehdrKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEK 344
Cdd:TIGR04523  631 SIiknIKSKKNKLKQEVKQIKETI----KEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKEL 689
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
684-749 4.57e-03

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 37.26  E-value: 4.57e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1023301064  684 GGNARGSFVHSVKPGSLAEKAGLREGHQLLLLEGcirgerqsVPLDTCTKEEAHWTIQRCSGPVTL 749
Cdd:pfam00595   21 DQGDPGIFVSEVLPGGAAEAGGLKVGDRILSING--------QDVENMTHEEAVLALKGSGGKVTL 78
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
1009-1143 4.71e-03

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: 39.20  E-value: 4.71e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  1009 VTRDEFLRRQKTETIIYSREKNpNAFECIAPANIEAVAAKNKHCLLEAGIGCTRDLIKSNIYPIVLFIRVceKNIKRFRK 1088
Cdd:smart00072   44 VSKEEFEDDIKSGLFLEWGEYE-GNYYGTSKETIRQVAEKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAP--PSSEELER 120
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1023301064  1089 LLPRPETEEEFLRVCRLK--EKELEALPCLYATVEPDmwgSVEELLRVVKDKIGEEQ 1143
Cdd:smart00072  121 RLRQRGTETSERIQKRLAaaQKEAQEYHLFDYVIVND---DLEDAYEELKEILEAEQ 174
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
224-347 5.85e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.78  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  224 DLQLEIDQLKHRLNKMEEEckLERNQSLKLKNDIENRPKKEQVLELEREN-------EMLKT--KN-QELQSIIQAGKRS 293
Cdd:pfam05667  339 ELQEQLEDLESSIQELEKE--IKKLESSIKQVEEELEELKEQNEELEKQYkvkkktlDLLPDaeENiAKLQALVDASAQR 416
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1023301064  294 L------------PDSD-----KAILDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDL 347
Cdd:pfam05667  417 LvelagqwekhrvPLIEeyralKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERL 487
COG5022 COG5022
Myosin heavy chain [General function prediction only];
134-530 6.34e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.83  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  134 EVIKLQQQMKA-KDLQRcellarlrQLEDEKKQMTLTRVELLtfqeryyKMKEERDSYNDELVKVKDDNYNLAMRYAQLs 212
Cdd:COG5022    955 ELNKLHEVESKlKETSE--------EYEDLLKKSTILVREGN-------KANSELKNFKKELAELSKQYGALQESTKQL- 1018
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  213 EEKNMAVMRsrdLQLEIDQLKHR---LNKMEEECKLERNQSLKLKndiENRPKKEQvLELERENEMLKTKNQELQsiiqa 289
Cdd:COG5022   1019 KELPVEVAE---LQSASKIISSEsteLSILKPLQKLKGLLLLENN---QLQARYKA-LKLRRENSLLDDKQLYQL----- 1086
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  290 gkrslpdsdkAILDILEhdrKEALEDRQELVNRIYNLQEEARQ---AEELRDKYLEEKEDLelkCSTLGKDCEMYKHRMN 366
Cdd:COG5022   1087 ----------ESTENLL---KTINVKDLEVTNRNLVKPANVLQfivAQMIKLNLLQEISKF---LSQLVNTLEPVFQKLS 1150
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  367 TVMLQLEEVERERD-QAFHSRDEAQTQYSQCLIE----KDKYRKQIRELEEKNDEMrIEMVRREACIVNLESKLRRLSKD 441
Cdd:COG5022   1151 VLQLELDGLFWEANlEALPSPPPFAALSEKRLYQsalyDEKSKLSSSEVNDLKNEL-IALFSKIFSGWPRGDKLKKLISE 1229
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  442 SNN---LDQSLPRNLPVTII---SQDFGDASPRTNGQEADDSSTSEEsPEDSKYFLPYHPPQRRMNLKGIQLQRAK-SPI 514
Cdd:COG5022   1230 GWVpteYSTSLKGFNNLNKKfdtPASMSNEKLLSLLNSIDNLLSSYK-LEEEVLPATINSLLQYINVGLFNALRTKaSSL 1308
                          410
                   ....*....|....*.
gi 1023301064  515 SLKRTSDFQAKGHEEE 530
Cdd:COG5022   1309 RWKSATEVNYNSEELD 1324
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
302-453 7.23e-03

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: 39.52  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  302 LDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVML--QLEEVERER 379
Cdd:COG1579     19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEI 98
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1023301064  380 DQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEK----NDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSLPRNL 453
Cdd:COG1579     99 ESLKRRISDLEDEILELMERIEELEEELAELEAElaelEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
134-348 7.72e-03

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: 40.43  E-value: 7.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  134 EVIKLQQQMkAKDLQRCELLARlrQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSE 213
Cdd:TIGR02168  783 EIEELEAQI-EQLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  214 EKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENrpKKEQVLELERENEMLKTKN-------QELQSI 286
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE--LESKRSELRRELEELREKLaqlelrlEGLEVR 937
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1023301064  287 IQAGKRSLPDSDKAILDILEHDRKEALEDRQELVNRIYNLQ--------------EEARQAEELRDKYLEEKEDLE 348
Cdd:TIGR02168  938 IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEnkikelgpvnlaaiEEYEELKERYDFLTAQKEDLT 1013
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
93-468 8.76e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.42  E-value: 8.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064   93 ESLEFYYPELYKLVTGKEPTRRFSTIVVEEGHEGLTHFLMnevIKLQQQMKAKDLQ-RCELLARLRQLEDEKKQMTLTRV 171
Cdd:TIGR00606  169 KALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQME---LKYLKQYKEKACEiRDQITSKEAQLESSREIVKSYEN 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  172 ELLTFQERYYKMKEERDS---YNDELVKVKDDNYNLAMRYAQLsEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERN 248
Cdd:TIGR00606  246 ELDPLKNRLKEIEHNLSKimkLDNEIKALKSRKKQMEKDNSEL-ELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDC 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  249 QSLKLKNDIENRPKKEQVLELERENEMLKTKNQELQSIIQA-GKRSLPDSDKAILDILEHD-------------RKEALE 314
Cdd:TIGR00606  325 QRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArDSLIQSLATRLELDGFERGpfserqiknfhtlVIERQE 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  315 DRQELVNRIY-----NLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHrmntVMLQLEEVERERDQafhsrdea 389
Cdd:TIGR00606  405 DEAKTAAQLCadlqsKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKF----VIKELQQLEGSSDR-------- 472
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  390 qtqysqcLIEKDK-YRKQIRELEEKNDEMRIEMVRREACIV-----NLESKLRRLSKDSNNLDQSLPRNLPVTIISQDFG 463
Cdd:TIGR00606  473 -------ILELDQeLRKAERELSKAEKNSLTETLKKEVKSLqnekaDLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKM 545

                   ....*
gi 1023301064  464 DASPR 468
Cdd:TIGR00606  546 DKDEQ 550
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
229-421 9.91e-03

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: 40.00  E-value: 9.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  229 IDQLKHRLNKMEEECKLERNQSLKLKNDIeNRPKKE-------------QVLELERENEMLKTKNQELQSIIQAGKRSLP 295
Cdd:TIGR04523   98 INKLNSDLSKINSEIKNDKEQKNKLEVEL-NKLEKQkkenkknidkfltEIKKKEKELEKLNNKYNDLKKQKEELENELN 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1023301064  296 DSDKAILDIlEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEekedLELKCSTLGKDCEMYKHRMNTVMLQLEEV 375
Cdd:TIGR04523  177 LLEKEKLNI-QKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNT 251
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1023301064  376 ERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEM 421
Cdd:TIGR04523  252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI 297
 
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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