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Conserved domains on  [gi|119568032|gb|EAW47647|]
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villin 2 (ezrin), isoform CRA_a [Homo sapiens]

Protein Classification

ezrin/radixin/moesin family protein( domain architecture ID 12200736)

ezrin/radixin/moesin (ERM) family protein links the actin cytoskeleton and the plasma membrane to govern membrane structure and organization

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 200-296 1.69e-73

FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain of ERM is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270015  Cd Length: 97  Bit Score: 229.47  E-value: 1.69e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 200 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 279
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 119568032 280 ILQLCMGNHELYMRRRK 296
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 7-206 3.37e-58

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 193.28  E-value: 3.37e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032     7 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVD-NKGFPTWLKLDKKVSAQEVRKEnPLQFKFRAKF 84
Cdd:smart00295   2 LKVYLLDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032    85 YPEDVaEELIQDITQ-KLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVH-KSGYLSSERLIPQRVMDQhk 162
Cdd:smart00295  81 YPPDP-NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS-- 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 119568032   163 LTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 206
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 510-586 3.05e-34

Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM family of proteins which consists of three closely-related proteins, ezrin, radixin and moesin. These proteins link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain (pfam00373), a common membrane binding module. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). This entry represents the C-terminal actin-binding tail domain. This entry also includes Ermin proteins, oligodendrocyte-specific proteins associated with the cytoskeleton whose C-terminal domain is similar to that in ERM family.


:

Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 124.23  E-value: 3.05e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119568032  510 DDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL 586
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 337-456 1.40e-28

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


:

Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 110.01  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  337 KEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQ 416
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119568032  417 LAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDL 456
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
 
Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 200-296 1.69e-73

FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain of ERM is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270015  Cd Length: 97  Bit Score: 229.47  E-value: 1.69e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 200 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 279
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 119568032 280 ILQLCMGNHELYMRRRK 296
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 7-206 3.37e-58

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 193.28  E-value: 3.37e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032     7 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVD-NKGFPTWLKLDKKVSAQEVRKEnPLQFKFRAKF 84
Cdd:smart00295   2 LKVYLLDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032    85 YPEDVaEELIQDITQ-KLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVH-KSGYLSSERLIPQRVMDQhk 162
Cdd:smart00295  81 YPPDP-NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS-- 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 119568032   163 LTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 206
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 3-87 1.66e-56

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and similar proteins; Ezrin, also termed cytovillin, or villin-2, or p81, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Ezrin is a tyrosine kinase substrate that functions as a cross-linker between actin cytoskeleton and plasma membrane. It has been implicated in the regulation of the proliferation, apoptosis, adhesion, invasion, metastasis and angiogenesis of cancer cells.


Pssm-ID: 340759  Cd Length: 85  Bit Score: 184.81  E-value: 1.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   3 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 82
Cdd:cd17239    1 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 80


                 ....*
gi 119568032  83 KFYPE 87
Cdd:cd17239   81 KFYPE 85
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 510-586 3.05e-34

Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM family of proteins which consists of three closely-related proteins, ezrin, radixin and moesin. These proteins link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain (pfam00373), a common membrane binding module. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). This entry represents the C-terminal actin-binding tail domain. This entry also includes Ermin proteins, oligodendrocyte-specific proteins associated with the cytoskeleton whose C-terminal domain is similar to that in ERM family.


Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 124.23  E-value: 3.05e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119568032  510 DDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL 586
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 88-206 5.65e-34

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 125.07  E-value: 5.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   88 DVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLtrDQ 167
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKS--KE 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 119568032  168 WEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 206
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
210-295 6.23e-33

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 120.82  E-value: 6.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  210 NKKGTDLWLGVDALGLNIYEKDDKLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILQLCMGNH 288
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 119568032  289 ELYMRRR 295
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 337-456 1.40e-28

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 110.01  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  337 KEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQ 416
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119568032  417 LAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDL 456
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 301-547 1.83e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 1.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 381 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 460
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 461 EELHLVMTAPPpppppvyepvsyHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQ 540
Cdd:COG1196  393 RAAAELAAQLE------------ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460


                 ....*..
gi 119568032 541 ARDENKR 547
Cdd:COG1196  461 LLELLAE 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 301-465 2.08e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 381 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 460
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490


                 ....*
gi 119568032 461 EELHL 465
Cdd:COG1196  491 ARLLL 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-583 1.91e-10

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: 63.92  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   307 AQAREEKHQKQLERQQ-LETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEE 385
Cdd:TIGR02168  662 TGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   386 AERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHL 465
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   466 VMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNER--VQRQLLTLSSELSQARD 543
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERasLEEALALLRSELEELSE 901

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 119568032   544 ENKRthndiiHNENMRQGRDKYKTLRQI------RQGNTKQRIDEF 583
Cdd:TIGR02168  902 ELRE------LESKRSELRRELEELREKlaqlelRLEGLEVRIDNL 941
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 303-444 3.53e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.05  E-value: 3.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 303 QQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQmmrEKEELmLRLQDYEEKTKKAERELSEQIQ----RALQLEEE 378
Cdd:PRK09510  70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQL---EKERL-AAQEQKKQAEEAAKQAALKQKQaeeaAAKAAAAA 145

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119568032 379 RKRAQEEAERLEAdrmAALRAKEELERQA-VDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEE 444
Cdd:PRK09510 146 KAKAEAEAKRAAA---AAKKAAAEAKKKAeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 301-464 5.56e-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: 59.30  E-value: 5.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   301 EVQQMKAQAREEKHQKQLERQQLETE----KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLE 376
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   377 EERKRAQEEAERLEAdrmaalrakeELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKED---EVEEWQHRAKEAQ 453
Cdd:TIGR02168  845 EQIEELSEDIESLAA----------EIEELEELIEELESELEALLNERASLEEALALLRSELEElseELRELESKRSELR 914

                          170
                   ....*....|.
gi 119568032   454 DDLVKTKEELH 464
Cdd:TIGR02168  915 RELEELREKLA 925
PTZ00121 PTZ00121
MAEBL; Provisional
 294-547 3.76e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 3.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  294 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRREtvEREKEQMMREKEElmlRLQDYEEKTKKAErELSEQIQRAL 373
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE--EAKKADEAKKKAE---EAKKADEAKKKAE-EAKKKADEAK 1503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  374 QLEEERKRAqEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAElaeytaKIALLEEARRRKEDEVEEWQHRAKEAQ 453
Cdd:PTZ00121 1504 KAAEAKKKA-DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD------ELKKAEELKKAEEKKKAEEAKKAEEDK 1576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  454 DDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDE-----GAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQ 528
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656

                         250
                  ....*....|....*....
gi 119568032  529 RQLLTLSSELSQARDENKR 547
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKK 1675
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 327-423 6.83e-06

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 45.89  E-value: 6.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 327 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA-----LQLEEERKRAQEEAERLEAdrmaalRAKE 401
Cdd:cd06503   29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEArkeaeKIKEEILAEAKEEAERILE------QAKA 102

                         90       100
                 ....*....|....*....|....*.
gi 119568032 402 ELER---QAVDQIKSQ-EQLAAELAE 423
Cdd:cd06503  103 EIEQekeKALAELRKEvADLAVEAAE 128
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 319-418 5.04e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.00  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 319 ERQQLETEKKRRETVEREKEQMMREK--------EELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAE--R 388
Cdd:NF033838 303 EKKVAEAEKKVEEAKKKAKDQKEEDRrnyptntyKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVEskK 382

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 119568032 389 LEADRMAAL-----RAKEELERQAVDQIKSQEQLA 418
Cdd:NF033838 383 AEATRLEKIktdrkKAEEEAKRKAAEEDKVKEKPA 417
 
Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 200-296 1.69e-73

FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain of ERM is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270015  Cd Length: 97  Bit Score: 229.47  E-value: 1.69e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 200 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 279
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 119568032 280 ILQLCMGNHELYMRRRK 296
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 7-206 3.37e-58

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 193.28  E-value: 3.37e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032     7 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVD-NKGFPTWLKLDKKVSAQEVRKEnPLQFKFRAKF 84
Cdd:smart00295   2 LKVYLLDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032    85 YPEDVaEELIQDITQ-KLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVH-KSGYLSSERLIPQRVMDQhk 162
Cdd:smart00295  81 YPPDP-NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS-- 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 119568032   163 LTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 206
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 3-87 1.66e-56

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and similar proteins; Ezrin, also termed cytovillin, or villin-2, or p81, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Ezrin is a tyrosine kinase substrate that functions as a cross-linker between actin cytoskeleton and plasma membrane. It has been implicated in the regulation of the proliferation, apoptosis, adhesion, invasion, metastasis and angiogenesis of cancer cells.


Pssm-ID: 340759  Cd Length: 85  Bit Score: 184.81  E-value: 1.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   3 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 82
Cdd:cd17239    1 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 80


                 ....*
gi 119568032  83 KFYPE 87
Cdd:cd17239   81 KFYPE 85
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 5-87 8.98e-56

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins, Ezrin, Radixin, and Moesin; The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340707 [Multi-domain]  Cd Length: 83  Bit Score: 182.67  E-value: 8.98e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKF 84
Cdd:cd17187    1 VNVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKF 80


                 ...
gi 119568032  85 YPE 87
Cdd:cd17187   81 YPE 83
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 5-87 1.25e-44

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and similar proteins; Radixin is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Radixin plays important roles in cell polarity, cell motility, invasion and tumor progression. It mediates the binding of F-actin to the plasma membrane after a conformational activation through Akt2-dependent phosphorylation at Thr564. It is also involved in reversal learning and short-term memory by regulating synaptic GABAA receptor density.


Pssm-ID: 340758 [Multi-domain]  Cd Length: 83  Bit Score: 152.97  E-value: 1.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKF 84
Cdd:cd17238    1 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKF 80


                 ...
gi 119568032  85 YPE 87
Cdd:cd17238   81 FPE 83
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 5-87 1.19e-42

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins; The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that play an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Merlin, which is highly related to the members of the ezrin, radixin, and moesin (ERM) protein family that are directly attached to and functionally linked with NHE1, is included in this family.


Pssm-ID: 340617  Cd Length: 83  Bit Score: 147.43  E-value: 1.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKF 84
Cdd:cd17097    1 INVRVTTMDAELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVAWLKPDKKVLTQDVSKNNTLKFFFLVKF 80


                 ...
gi 119568032  85 YPE 87
Cdd:cd17097   81 YPE 83
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 5-87 2.20e-42

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and similar proteins; Moesin, also termed membrane-organizing extension spike protein, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Moesin is involved in mitotic spindle function through stabilizing cell shape and microtubules at the cell cortex. It is required for the formation of F-actin networks that mediate endosome biogenesis or maturation and transport through the degradative pathway.


Pssm-ID: 340757  Cd Length: 84  Bit Score: 146.81  E-value: 2.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKF 84
Cdd:cd17237    2 ISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKF 81


                 ...
gi 119568032  85 YPE 87
Cdd:cd17237   82 YPE 84
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 3-87 2.89e-38

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and similar proteins; Merlin, also termed moesin-ezrin-radixin-like protein, or neurofibromin-2 (NF2), or Schwannomerlin, or Schwannomin, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif, merlin however lacks the typical actin-binding motif in the C-tail. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Merlin plays vital roles in controlling proper development of organ sizes by specifically binding to a large number of target proteins localized both in cytoplasm and nuclei. Merlin may function as a tumor suppressor that functions upstream of the core Hippo pathway kinases Lats1/2 (Wts in Drosophila) and Mst1/2 (Hpo in Drosophila), as well as the nuclear E3 ubiquitin ligase DDB1-and-Cullin 4-associated Factor 1 (DCAF1)-associated cullin 4-Roc1 ligase, CRL4(DCAF1). Merlin may also has a tumor suppressor function in melanoma cells, the inhibition of the proto-oncogenic Na(+)/H(+) exchanger isoform 1 (NHE1) activity.


Pssm-ID: 340706  Cd Length: 85  Bit Score: 135.59  E-value: 2.89e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   3 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 82
Cdd:cd17186    1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDSKGTVAWLKMDKKVLDQDVPKEEPVTFHFLA 80


                 ....*
gi 119568032  83 KFYPE 87
Cdd:cd17186   81 KFYPE 85
RA_FERM_F0_F1_like cd01768
Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 ...
 6-82 1.22e-36

Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 sub-domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting, directly or indirectly, with Ras proteins and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras protein is a small GTPase that is involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon. The FERM domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, also known as the N-terminal Ubl-like structural domain of the FERM domain (FERM_N), which is structurally similar to Ub. Some FERM domain-containing proteins contain an N-terminal region, which also has the beta-grasp Ub-like fold, precedes the FERM domain and has been referred to as the F0 domain.


Pssm-ID: 340467  Cd Length: 110  Bit Score: 132.29  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   6 NVRVTTM-----DAELEFAIQPNTTGKQLFDQVVKTIGLR-----------EVWYFGLHYVDNK-------------GFP 56
Cdd:cd01768    1 VLKIFGAglasgANYKSVLATARSTARELVAEALERYGLAgspgggpgessCVDAFALCDALGRpaaagvgsgewraEHL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 119568032  57 TWLKLDKKVSAQ----EVRKENPLQFKFRA 82
Cdd:cd01768   81 RVLGDSERPLLVqelwRARPGWARRFELRG 110
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 510-586 3.05e-34

Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM family of proteins which consists of three closely-related proteins, ezrin, radixin and moesin. These proteins link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain (pfam00373), a common membrane binding module. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). This entry represents the C-terminal actin-binding tail domain. This entry also includes Ermin proteins, oligodendrocyte-specific proteins associated with the cytoskeleton whose C-terminal domain is similar to that in ERM family.


Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 124.23  E-value: 3.05e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119568032  510 DDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL 586
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 88-206 5.65e-34

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 125.07  E-value: 5.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   88 DVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLtrDQ 167
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKS--KE 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 119568032  168 WEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 206
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
210-295 6.23e-33

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 120.82  E-value: 6.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  210 NKKGTDLWLGVDALGLNIYEKDDKLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILQLCMGNH 288
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 119568032  289 ELYMRRR 295
Cdd:pfam09380  79 TFFRLRR 85
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 98-198 1.64e-29

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 111.95  E-value: 1.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  98 TQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLtrDQWEDRIQVWHA 177
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKP--EEWEKRIVELHK 78

                         90       100
                 ....*....|....*....|.
gi 119568032 178 EHRGMLKDNAMLEYLKIAQDL 198
Cdd:cd14473   79 KLRGLSPAEAKLKYLKIARKL 99
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 337-456 1.40e-28

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 110.01  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  337 KEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQ 416
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119568032  417 LAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDL 456
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 5-84 1.94e-21

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 88.41  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 83
Cdd:cd01765    1 ISCRVRLLDgTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKHWLDLDKKISKQ-LKRSGPYQFYFRVK 79


                 .
gi 119568032  84 F 84
Cdd:cd01765   80 F 80
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 202-292 1.08e-18

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 81.27  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 202 GINYFEIKNK--KGTDLWLGVDALGLNIYEKDDKlTPKIGFPWSEIRNISFN-DKKFVIKPIDKKAPDFVFYAPRLRINK 278
Cdd:cd00836    1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEDKQSKLLFQTPSRQAK 79

                         90
                 ....*....|....
gi 119568032 279 RILQLCMGNHELYM 292
Cdd:cd00836   80 EIWKLIVGYHRFLL 93
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 9-68 5.37e-17

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 75.32  E-value: 5.37e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119568032    9 VTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQ 68
Cdd:pfam09379   1 VRLLDGtVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNGEHRWLDLSKRLSKQ 61
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 5-88 6.87e-16

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and pleckstrin domain-containing protein 1 (FARP1) and similar proteins; This family includes the F1 sub-domain of FERM, RhoGEF and pleckstrin domain-containing proteins FARP1, FARP2, and FERM domain-containing protein 7 (FRMD7). FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340618  Cd Length: 85  Bit Score: 73.02  E-value: 6.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 83
Cdd:cd17098    1 LHVKVQMLDdTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKCWLDPEKPILRQ-VKRPKDVVFKFVVK 79


                 ....*
gi 119568032  84 FYPED 88
Cdd:cd17098   80 FYTPD 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 301-547 1.83e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 1.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 381 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 460
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 461 EELHLVMTAPPpppppvyepvsyHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQ 540
Cdd:COG1196  393 RAAAELAAQLE------------ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460


                 ....*..
gi 119568032 541 ARDENKR 547
Cdd:COG1196  461 LLELLAE 467
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 202-296 1.51e-13

FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part of the Par-3/FRMD4A/cytohesin-1 complex that activates Arf6, a central player in actin cytoskeleton dynamics and membrane trafficking, during junctional remodeling and epithelial polarization. The Par-3/Par-6/aPKC/Cdc42 complex regulates the conversion of primordial adherens junctions (AJs) into belt-like AJs and the formation of linear actin cables. When primordial AJs are formed, Par-3 recruits scaffolding protein FRMD4A which connects Par-3 and the Arf6 guanine-nucleotide exchange factor (GEF), cytohesin-1. FRMD4B (also called GRP1-binding protein, GRSP1) is a novel member of GRP1 signaling complexes that are recruited to plasma membrane ruffles in response to insulin receptor signaling. The GRSP1/FRMD4B protein contains a FERM protein domain as well as two coiled coil domains and may function as a scaffolding protein. GRP1 and GRSP1 interact through the coiled coil domains in the two proteins. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270012  Cd Length: 113  Bit Score: 66.99  E-value: 1.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 202 GINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPID-KKAPD-------------F 267
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDpRRNSHrsrrtfqsssvsvH 80

                         90       100
                 ....*....|....*....|....*....
gi 119568032 268 VFYAPRLRINKRILQLCMGNHELYMRRRK 296
Cdd:cd13191   81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQ 109
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 301-465 2.08e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 381 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 460
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490


                 ....*
gi 119568032 461 EELHL 465
Cdd:COG1196  491 ARLLL 495
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 206-297 8.35e-12

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many functions of PTPN13 (also called PTPL1, PTP-BAS, hPTP1E, FAP1, or PTPL1). Mice lacking PTPN13 activity have abnormal regulation of signal transducer and activator of transcription signaling in their T cells, mild impairment of motor nerve repair, and a significant reduction in the growth of retinal glia cultures. It also plays a role in adipocyte differentiation. PTPN13 contains a kinase non-catalytic C-lobe domain (KIND), a FERM domain with two potential phosphatidylinositol 4,5-biphosphate [PtdIns(4,5)P2]-binding motifs, 5 PDZ domains, and a carboxy-terminal catalytic domain. There is an nteraction between the FERM domain of PTPL1 and PtdIns(4,5)P2 which is thought to regulate the membrane localization of PTPN13. PDZ are protein/protein interaction domains so there is the potential for numerous partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated PTPL1 substrates. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270008  Cd Length: 103  Bit Score: 61.96  E-value: 8.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 206 FEIKNKKGTDLWLGVDALGLNIYE-KDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLC 284
Cdd:cd13187    8 YREKKSSTLSLWLGICSRGIIIYEeKNGARTPVLRFPWRETQKISFDKKKFTIESRGGSGIKHTFYTDSYKKSQYLLQLC 87

                         90
                 ....*....|....*
gi 119568032 285 MGNHE--LYMRRRKP 297
Cdd:cd13187   88 SAQHKfhIQMRSRQS 102
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 209-293 1.80e-11

FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and hEx/human expanded) is localized throughout the cytoplasm or along the plasma membrane. The Drosophilla protein Ex is a regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and is tumor suppression by restricting proliferation and promoting apoptosis. Surprisingly, hEx is thought to function independently of the Hippo pathway. Instead it is hypothesized that hEx inhibits progression through the S phase of the cell cycle by upregulating p21(Cip1) and downregulating Cyclin A. It is also implicated in the progression of Alzheimer disease. Not much is known about FRMD1 to date. Both FRMD1 and FRMD6 contains a single FERM domain which has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe is a member of the PH superfamily. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270006  Cd Length: 107  Bit Score: 61.17  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 209 KNKKGTD--LWLGVDALGLNIY-EKDDKLTPKIGFPWSEIRNISFNDKKFVIKPiDKKAPDFVFYAPRLRINKRILQLCM 285
Cdd:cd13185   12 KSKKETPgsVLLGITAKGIQIYqESDGEQQLLRTFPWSNIGKLSFDRKKFEIRP-EGSLRKLTYYTSSDEKSKYLLALCR 90


                 ....*...
gi 119568032 286 GNHELYMR 293
Cdd:cd13185   91 ETHQFSMA 98
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 15-85 3.86e-11

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 3 (FRMD3) and similar proteins; FRMD3, also termed band 4.1-like protein 4O, or ovary type protein 4.1 (4.1O), belongs to the 4.1 protein superfamily, which share the highly conserved membrane-association FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMD3 is involved in maintaining cell shape and integrity. It also functions as a tumour suppressor in non-small cell lung carcinoma (NSCLC). Some single nucleotide polymorphisms (SNPs) located in FRMD3 have been associated with diabetic kidney disease (DKD) in different ethnicities.


Pssm-ID: 340622  Cd Length: 82  Bit Score: 59.18  E-value: 3.86e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119568032  15 ELEFaiQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAKFY 85
Cdd:cd17102   15 CCEF--KKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQRHWLDPNKSIYKQ-LKGVPPYVLCFRVKFY 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 286-463 9.76e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 9.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 286 GNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAEREL 365
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 366 SEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQavdqiksQEQLAAELAEYTAKIALLEEARRRKEDEVEEW 445
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                        170
                 ....*....|....*...
gi 119568032 446 QHRAKEAQDDLVKTKEEL 463
Cdd:COG1196  455 EEEEEALLELLAELLEEA 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-583 1.91e-10

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: 63.92  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   307 AQAREEKHQKQLERQQ-LETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEE 385
Cdd:TIGR02168  662 TGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   386 AERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHL 465
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   466 VMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNER--VQRQLLTLSSELSQARD 543
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERasLEEALALLRSELEELSE 901

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 119568032   544 ENKRthndiiHNENMRQGRDKYKTLRQI------RQGNTKQRIDEF 583
Cdd:TIGR02168  902 ELRE------LESKRSELRRELEELREKlaqlelRLEGLEVRIDNL 941
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 13-89 2.58e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4B (FRMD4B); FRMD4B, also termed GRP1-binding protein GRSP1, interacts with the coil-coil domain of ARF exchange factor GRP1 to form the Grsp1-Grp1 complex that co-localizes with cortical actin rich regions in response to stimulation of CHO-T cells with insulin or epidermal growth factor (EGF). FRMD4B contains a FERM protein interaction domain as well as two coiled coil domains and may therefore function as a scaffolding protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340720  Cd Length: 89  Bit Score: 57.21  E-value: 2.58e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119568032  13 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEV-RKENPLQFKFRAKFYPEDV 89
Cdd:cd17200   12 DRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNWLQLDHRVLDHDLpKKSGPVTLYFAVRFYIESI 89
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 13-89 8.21e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing proteins FRMD4A, FRMD4B, and similar proteins; This family includes FERM domain-containing proteins FRMD4A and FRMD4B, both of which contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMD4A is a cytohesin adaptor involved in cell structure, transport and signaling. It promotes the growth of cancer cells in tongue, head and neck squamous cell carcinomas. FRMD4B, also termed GRP1-binding protein GRSP1, interacts with the coil-coil domain of ARF exchange factor GRP1 to form the Grsp1-Grp1 complex that co-localizes with cortical actin rich regions in response to stimulation of CHO-T cells with insulin or epidermal growth factor (EGF).


Pssm-ID: 340623  Cd Length: 91  Bit Score: 55.75  E-value: 8.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  13 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKEN---PLQFKFRAKFYPEDV 89
Cdd:cd17103   12 DRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDETGHYNWLQLDKRVLDHEFPKKWssgPLVLHFAVKFYVESI 91
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 13-85 9.61e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ubiquitin-protein ligase MYLIP and similar proteins; MYLIP, also termed inducible degrader of the LDL-receptor (Idol), or myosin regulatory light chain interacting protein (MIR), is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family, including UBE2D1, UBE2D2, UBE2D3, and UBE2D4. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains a FERM-domain and a C-terminal C3HC4-type RING-HC finger. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340624  Cd Length: 81  Bit Score: 55.35  E-value: 9.61e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119568032  13 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAKFY 85
Cdd:cd17104   10 SVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERLWLNLRNRISRQ-LPGPPPYRLRLRVKFF 81
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 5-85 1.27e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5) and similar proteins; This family includes FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins, EPB41L5 and EPB41L4B. EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer. Both EPB41L5 and EPB41L4B contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340628  Cd Length: 81  Bit Score: 55.05  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 83
Cdd:cd17108    1 IQCKVILLDgTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQHWLDPTKKIKKQ-VKIGPPYTLRFRVK 79


                 ..
gi 119568032  84 FY 85
Cdd:cd17108   80 FY 81
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 303-444 3.53e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.05  E-value: 3.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 303 QQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQmmrEKEELmLRLQDYEEKTKKAERELSEQIQ----RALQLEEE 378
Cdd:PRK09510  70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQL---EKERL-AAQEQKKQAEEAAKQAALKQKQaeeaAAKAAAAA 145

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119568032 379 RKRAQEEAERLEAdrmAALRAKEELERQA-VDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEE 444
Cdd:PRK09510 146 KAKAEAEAKRAAA---AAKKAAAEAKKKAeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 194-258 3.88e-09

FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FRMD7(FERM domain containing 7). FARP1 and FARP2 are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. These members are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. Other members in this family do not contain the DH domains such as the Human FERM domain containing protein 7 and Caenorhabditis elegans CFRM3, both of which have unknown functions. They contain an N-terminal FERM domain, a PH domain, followed by a FA (FERM adjacent) domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270014  Cd Length: 122  Bit Score: 54.66  E-value: 3.88e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119568032 194 IAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTpkiGFPWSEIRNISFNDKKFVIK 258
Cdd:cd13193    2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 8-88 5.07e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 1 (EPB41L1) and similar proteins; EPB41L1, also termed neuronal protein 4.1 (4.1N), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. It is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. It suppresses hypoxia-induced epithelial-mesenchymal transition in epithelial ovarian cancer (EOC) cells. The down-regulation of EPB41L1 expression is a critical step for non-small cell lung cancer (NSCLC) development. Moreover, EPB41L1 functions as a linker protein between inositol 1,4,5-trisphosphate receptor type1 (IP3R1) and actin filaments in neurons. EPB41L1 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340721  Cd Length: 84  Bit Score: 53.35  E-value: 5.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   8 RVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFYP 86
Cdd:cd17201    5 KVTLLDGsEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKNWLDPSKEIKKQ--IRSGPWHFAFTVKFYP 82


                 ..
gi 119568032  87 ED 88
Cdd:cd17201   83 PD 84
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 301-464 5.56e-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: 59.30  E-value: 5.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   301 EVQQMKAQAREEKHQKQLERQQLETE----KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLE 376
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   377 EERKRAQEEAERLEAdrmaalrakeELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKED---EVEEWQHRAKEAQ 453
Cdd:TIGR02168  845 EQIEELSEDIESLAA----------EIEELEELIEELESELEALLNERASLEEALALLRSELEElseELRELESKRSELR 914

                          170
                   ....*....|.
gi 119568032   454 DDLVKTKEELH 464
Cdd:TIGR02168  915 RELEELREKLA 925
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 7-85 8.04e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins; This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation.


Pssm-ID: 340619  Cd Length: 85  Bit Score: 52.62  E-value: 8.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   7 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFY 85
Cdd:cd17099    6 VRIQLLDNTvLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQLDKHAHEPLLYFGVMFY 85
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 312-547 9.45e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 9.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 312 EKHQKQLERQQlETEKKRRETVEREKEqmmREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERkrAQEEAErLEA 391
Cdd:COG1196  199 ERQLEPLERQA-EKAERYRELKEELKE---LEAELLLLKLRELEAELEELEAELEELEAELEELEAEL--AELEAE-LEE 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 392 DRMAALRAKEELER---QAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMT 468
Cdd:COG1196  272 LRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032 469 APPPPPPPVYEpvsyhVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKR 547
Cdd:COG1196  352 ELEEAEAELAE-----AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 15-87 9.53e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 13 (PTPN13) and similar proteins; This family includes tyrosine-protein phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and FERM domain-containing proteins FRMD1 and FRMD6. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340621  Cd Length: 97  Bit Score: 52.95  E-value: 9.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  15 ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFpTWLKLDKKVSAQ------EVRKENPLQFK------FRA 82
Cdd:cd17101   13 RLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAVLKDGEY-FFLDPDTKLSKYapkgwkSEAKKGLKGGKpvftlyFRV 91


                 ....*
gi 119568032  83 KFYPE 87
Cdd:cd17101   92 KFYVD 96
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 13-89 1.12e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4A (FRMD4A); FRMD4A is a cytohesin adaptor involved in cell structure, transport and signaling. It promotes the growth of cancer cells in tongue, head and neck squamous cell carcinomas. It also regulates tau secretion by activating cytohesin-Arf6 signaling through connecting cytohesin family Arf6-specific guanine-nucleotide exchange factors (GEFs) and Par-3 at primordial adherens junctions during epithelial polarization. As a genetic risk factor for late-onset Alzheimer's disease (AD), FRMD4A may play a role in amyloidogenic and tau-related pathways in AD. FRMD4A contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340719  Cd Length: 89  Bit Score: 52.66  E-value: 1.12e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119568032  13 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEV-RKENPLQFKFRAKFYPEDV 89
Cdd:cd17199   12 DRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHDFpKKSGPVVLYFCVRFYIESI 89
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 310-452 1.31e-08

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 57.65  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  310 REEKHQKQLERQQLETEKKRRETVEREKEqmmREKEELMLRLQDYEEKTKKAERELSEQI-------QRALQLEEE---- 378
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQ---RRFEEIRLRKQRLEEERQRQEEEERKQRlqlqaaqERARQQQEEfrrk 431

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032  379 -----RKRAQEEAERLEADRMaalRAKEELERQAVDQIKSQEQLAAELAEYTAKialLEEARRRKEDEVEEWQHRAKEA 452
Cdd:pfam15709 432 lqelqRKKQQEEAERAEAEKQ---RQKELEMQLAEEQKRLMEMAEEERLEYQRQ---KQEAEEKARLEAEERRQKEEEA 504
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 293-460 1.33e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.12  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 293 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERElseqiqrA 372
Cdd:PRK09510  81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAE-------A 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 373 LQLEEERKRAQEEAERL---EADRMAALRAKEELERQAVDQIKSQEQLAAE-LAEYTAKIALLEEARRRKEDEVEEWQHR 448
Cdd:PRK09510 154 KRAAAAAKKAAAEAKKKaeaEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEaEAKKKAAAEAKKKAAAEAKAAAAKAAAE 233

                        170
                 ....*....|..
gi 119568032 449 AKEAQDDLVKTK 460
Cdd:PRK09510 234 AKAAAEKAAAAK 245
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 187-264 1.49e-08

FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called Band 4.1-like protein 4O/4.1O though it is not a true member of that family) is a novel putative tumor suppressor gene that is implicated in the origin and progression of lung cancer. In humans there are 5 isoforms that are produced by alternative splicing. Less is known about FRMD5, though there are 2 isoforms of the human protein are produced by alternative splicing. Both FRMD3 and FRMD5 contain a N-terminal FERM domain, followed by a FERM adjacent (FA) domain, and 4.1 protein C-terminal domain (CTD). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270013  Cd Length: 105  Bit Score: 52.78  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 187 AMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTpkiGFPWSEIRNISFNDKKF---VIKPIDKK 263
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFilhVMQKEEKK 77


                 .
gi 119568032 264 A 264
Cdd:cd13192   78 H 78
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 290-453 1.99e-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: 57.44  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  290 LYMRRRKPDTIEVQQMKAQAR----EEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLqdyeEKTKKAEREL 365
Cdd:pfam17380 383 LQMERQQKNERVRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM----ERVRLEEQER 458

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  366 SEQIQRALQLEEERKRAQEEAERLEADRMAAlrakEELERQAVDQiksqeqlaaELAEytAKIALLEEARRRK--EDEVE 443
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKRDRKRA----EEQRRKILEK---------ELEE--RKQAMIEEERKRKllEKEME 523

                         170
                  ....*....|
gi 119568032  444 EWQHRAKEAQ 453
Cdd:pfam17380 524 ERQKAIYEEE 533
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 301-465 2.62e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 2.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   301 EVQQMKAQAREEKHQKQ----LERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLE 376
Cdd:TIGR02168  709 ELEEELEQLRKELEELSrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   377 EERKRAQEEAE--------------RLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEV 442
Cdd:TIGR02168  789 AQIEQLKEELKalrealdelraeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868

                          170       180
                   ....*....|....*....|...
gi 119568032   443 EEWQHRAKEAQDDLVKTKEELHL 465
Cdd:TIGR02168  869 EELESELEALLNERASLEEALAL 891
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
301-462 3.21e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 3.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEEL--MLRLQDYEEKTKKAERELSEQIQRALQLE-- 376
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEer 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 377 -EERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQ-EQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQD 454
Cdd:COG4717  155 lEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234


                 ....*...
gi 119568032 455 DLVKTKEE 462
Cdd:COG4717  235 ELEAAALE 242
PTZ00121 PTZ00121
MAEBL; Provisional
 294-547 3.76e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 3.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  294 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRREtvEREKEQMMREKEElmlRLQDYEEKTKKAErELSEQIQRAL 373
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE--EAKKADEAKKKAE---EAKKADEAKKKAE-EAKKKADEAK 1503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  374 QLEEERKRAqEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAElaeytaKIALLEEARRRKEDEVEEWQHRAKEAQ 453
Cdd:PTZ00121 1504 KAAEAKKKA-DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD------ELKKAEELKKAEEKKKAEEAKKAEEDK 1576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  454 DDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDE-----GAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQ 528
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656

                         250
                  ....*....|....*....
gi 119568032  529 RQLLTLSSELSQARDENKR 547
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKK 1675
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 294-544 3.86e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 3.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   294 RRKPDTIEVQQMKAQ------AREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEK---TKKAERE 364
Cdd:TIGR02168  199 ERQLKSLERQAEKAErykelkAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   365 LSEQI------------------QRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTA 426
Cdd:TIGR02168  279 LEEEIeelqkelyalaneisrleQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   427 KIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSE 506
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 119568032   507 GIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDE 544
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 24-88 6.87e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4A (EPB41L4A) and similar proteins; EPB41L4A, also termed protein NBL4, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4A is an important component of the beta-catenin/Tcf pathway. It may be related to determination of cell polarity or proliferation.


Pssm-ID: 340627  Cd Length: 91  Bit Score: 50.42  E-value: 6.87e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119568032  24 TTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPED 88
Cdd:cd17107   27 SKGSVVLDVVFQHLNLLETDYFGLRYIDRQHQTHWLDPAKTLSEQLKLIGPPYTLYFGVKFYAED 91
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 294-585 1.11e-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: 55.07  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   294 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKK------RRETVERE-------KEQMMREKEELMLRLQDYEEKTKK 360
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEgyellkeKEALERQKEAIERQLASLEEELEK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   361 AERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAK--------EELERQAVDQIKSQEQLAAELAEYTAKIALLE 432
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLL 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   433 EARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQ------------ESLQDEGAEPTGYS 500
Cdd:TIGR02169  336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyrekleklkreiNELKRELDRLQEEL 415

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   501 AELSSEGiRDDRNEEKRItEAEKNErVQRQLLTLSSELSQARDENKRTHNDIIHNEnmRQGRDKYKTLRQI--RQGNTKQ 578
Cdd:TIGR02169  416 QRLSEEL-ADLNAAIAGI-EAKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYE--QELYDLKEEYDRVekELSKLQR 490


                   ....*..
gi 119568032   579 RIDEFEA 585
Cdd:TIGR02169  491 ELAEAEA 497
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 7-88 1.35e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins; The family includes erythrocyte membrane protein band 4.1-like proteins EPB41L1/4.1N, EPB41L2/4.1G, and EPB41L3/4.1B. They belong to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L1 is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. EPB41L2 is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 also acts as a tumor suppressor implicated in a variety of meningiomas and carcinomas. Members in this family contain a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340626  Cd Length: 84  Bit Score: 49.36  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   7 VRVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFY 85
Cdd:cd17106    4 CKVLLLDGtEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQKNWLDPAKEIKKQ--IRSGPWLFSFNVKFY 81


                 ...
gi 119568032  86 PED 88
Cdd:cd17106   82 PPD 84
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 301-562 1.36e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   381 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQ---DDLV 457
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrlEDLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   458 KTKEELHLVMTAPPpppppvyepvsyHVQESLQDEGAEptgYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSE 537
Cdd:TIGR02168  845 EQIEELSEDIESLA------------AEIEELEELIEE---LESELEALLNERASLEEALALLRSELEELSEELRELESK 909

                          250       260
                   ....*....|....*....|....*
gi 119568032   538 LSQARDENKRThNDIIHNENMRQGR 562
Cdd:TIGR02168  910 RSELRRELEEL-REKLAQLELRLEG 933
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
303-464 1.41e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  303 QQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRA 382
Cdd:COG4913   242 EALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  383 QEEAERLEADRMAA-LRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKE 461
Cdd:COG4913   322 REELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                  ...
gi 119568032  462 ELH 464
Cdd:COG4913   402 ALE 404
PTZ00121 PTZ00121
MAEBL; Provisional
 292-566 1.45e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  292 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKK----RRETVEREKEQMMREKEELML--RLQDYEEKTKKAEREL 365
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKadeaKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKADEAKK 1541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  366 SEQIQRALQLEE-------ERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRK 438
Cdd:PTZ00121 1542 AEEKKKADELKKaeelkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  439 EDEVEEWQHRAKEAQDDLVKTKEElhlVMTAPPPPPPPVYEPVSyhvQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRI 518
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIK---AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 119568032  519 TEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYK 566
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 13-88 1.59e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 7 (FRMD7); FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. It interacts with the Rho GTPase regulator, RhoGDIalpha, and activates the Rho subfamily member Rac1, which regulates reorganization of actin filaments and controls neuronal outgrowth. Mutations in the FRMD7 gene are responsible for the X-linked idiopathic congenital nystagmus (ICN), a disease which affects ocular motor control. FRMD7 contains a FERM domain, and a pleckstrin homology (PH) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340708  Cd Length: 86  Bit Score: 49.04  E-value: 1.59e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119568032  13 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAKFYPED 88
Cdd:cd17188   11 DSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNVWLELLKPITKQ-IKNPKELIFKFTVKFFPVD 85
PTZ00121 PTZ00121
MAEBL; Provisional
 292-467 1.81e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  292 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLEtEKKRRETVEREKEQMMREKEELMlrlQDYEEKTKKAErELSEQIQR 371
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-EKKKAEELKKAEEENKIKAAEEA---KKAEEDKKKAE-EAKKAEED 1686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  372 ALQLEEERKRAQEEAERLEAdrmaaLRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLE----EARRRKEDEVEEWQH 447
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEE-----LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDkkkaEEAKKDEEEKKKIAH 1761

                         170       180
                  ....*....|....*....|
gi 119568032  448 RAKEAQDDLVKTKEELHLVM 467
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVI 1781
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
306-456 2.00e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  306 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEEL---MLRLQDYEEKTKKAERELSEQI-----QRALQLEE 377
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLeaeLERLEARLDALREELDELEAQIrgnggDRLEQLER 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  378 ERKRAQEEAERLEADRMAALRAKEELERQAVDQIKS----QEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQ 453
Cdd:COG4913   346 EIERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425


                  ...
gi 119568032  454 DDL 456
Cdd:COG4913   426 AEI 428
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 5-88 3.05e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5); EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. It is normally induced during epithelial-mesenchymal transition (EMT) by an EMT-related transcriptional factor, ZEB1, which drives ARF6-based invasion, metastasis and drug resistance. EPB41L5 also binds to paxillin to enhance integrin/paxillin association, and thus promotes focal adhesion dynamics. Moreover, EPB41L5 acts as a substrate for the E3 ubiquitin ligase Mind bomb 1 (Mib1), which is essential for activation of Notch signaling. EPB41L5 is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340725  Cd Length: 86  Bit Score: 48.50  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 83
Cdd:cd17205    3 ITCRVSLLDGtDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAHWLDVTKSIKKQ-VKIGPPYCLHLRVK 81


                 ....*
gi 119568032  84 FYPED 88
Cdd:cd17205   82 FYSSE 86
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 301-462 3.54e-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: 53.53  E-value: 3.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:TIGR02169  834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   381 RAQEEAERLEADRMAALRAKEELERQA------VDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQD 454
Cdd:TIGR02169  914 KKRKRLSELKAKLEALEEELSEIEDPKgedeeiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993


                   ....*...
gi 119568032   455 DLVKTKEE 462
Cdd:TIGR02169  994 KRAKLEEE 1001
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 200-257 3.55e-07

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and PTPN3); PTPN4 (also called PTPMEG, protein tyrosine phosphatase, megakaryocyte) is a cytoplasmic protein-tyrosine phosphatase (PTP) thought to play a role in cerebellar function. PTPMEG-knockout mice have impaired memory formation and cerebellar long-term depression. PTPN3/PTPH1 is a membrane-associated PTP that is implicated in regulating tyrosine phosphorylation of growth factor receptors, p97 VCP (valosin-containing protein, or Cdc48 in Saccharomyces cerevisiae), and HBV (Hepatitis B Virus) gene expression; it is mutated in a subset of colon cancers. PTPMEG and PTPN3/PTPH1 contains a N-terminal FERM domain, a middle PDZ domain, and a C-terminal phosphatase domain. PTP1/Tyrosine-protein phosphatase 1 from nematodes and a FERM_C repeat 1 from Tetraodon nigroviridis are also included in this cd. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270010  Cd Length: 95  Bit Score: 48.46  E-value: 3.55e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119568032 200 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPkigFPWSEIRNISFNDKKFVI 257
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINT---FPWSKIVKISFKRKQFFI 55
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 293-452 3.84e-07

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: 52.46  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 293 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKE-QMMREKEELML-----------RLQDYEEKTKK 360
Cdd:COG4942   67 LARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlYRLGRQPPLALllspedfldavRRLQYLKYLAP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 361 AERELSEQIQRALQ-LEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKE 439
Cdd:COG4942  147 ARREQAEELRADLAeLAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                        170
                 ....*....|...
gi 119568032 440 DEVEEWQHRAKEA 452
Cdd:COG4942  227 ALIARLEAEAAAA 239
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 8-88 3.96e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 3 (EPB41L3) and similar proteins; EPB41L3, also termed 4.1B, or differentially expressed in adenocarcinoma of the lung protein 1 (DAL-1), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 is a tumor suppressor that has been implicated in a variety of meningiomas and carcinomas. EPB41L3 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340723  Cd Length: 84  Bit Score: 48.01  E-value: 3.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   8 RVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFYP 86
Cdd:cd17203    5 KVTLLDgSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQKNWLDPAKEIKKQ--IRSGAWQFSFNVKFYP 82


                 ..
gi 119568032  87 ED 88
Cdd:cd17203   83 PD 84
PRK12704 PRK12704
phosphodiesterase; Provisional
 301-427 4.45e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 4.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETE--------KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRa 372
Cdd:PRK12704  65 EIHKLRNEFEKELRERRNELQKLEKRllqkeenlDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE- 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119568032 373 lqLEEERKRAQEEAERLEADRMaalraKEELERQAVDQIKSQEQLAAELAEYTAK 427
Cdd:PRK12704 144 --LERISGLTAEEAKEILLEKV-----EEEARHEAAVLIKEIEEEAKEEADKKAK 191
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 301-467 5.10e-07

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 52.65  E-value: 5.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  301 EVQQMKAQAREEKHQKQ--LERQQLETEKKRRETVEREKEqmmREKEELMLRLQDYEEKTKKAERELSEQiQRALQLEEE 378
Cdd:pfam15709 344 EMRRLEVERKRREQEEQrrLQQEQLERAEKMREELELEQQ---RRFEEIRLRKQRLEEERQRQEEEERKQ-RLQLQAAQE 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  379 RKRAQEEAERLEADRMAALRAKEELERQAVDQiKSQEQLAAELAEYTAKIALLEEARR----RKEDEVEEwqHRAKEAQD 454
Cdd:pfam15709 420 RARQQQEEFRRKLQELQRKKQQEEAERAEAEK-QRQKELEMQLAEEQKRLMEMAEEERleyqRQKQEAEE--KARLEAEE 496

                         170
                  ....*....|...
gi 119568032  455 DLVKTKEELHLVM 467
Cdd:pfam15709 497 RRQKEEEAARLAL 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 300-456 6.02e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 6.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   300 IEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAL----QL 375
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarleRL 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   376 EEERKRAQEEAERL-----EADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAK 450
Cdd:TIGR02168  413 EDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492


                   ....*.
gi 119568032   451 EAQDDL 456
Cdd:TIGR02168  493 SLERLQ 498
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
304-585 6.90e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.35  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 304 QMKAQArEEKHQKQLERQQLETEKKRRET------VEREKEQMMREKEELMLRLQDYEEK---------------TKKAE 362
Cdd:PRK02224 191 QLKAQI-EEKEEKDLHERLNGLESELAELdeeierYEEQREQARETRDEADEVLEEHEERreeletleaeiedlrETIAE 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 363 ---------RELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELE------RQAVDQIKSQEQLAAELAE-YTA 426
Cdd:PRK02224 270 terereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEdrdeelRDRLEECRVAAQAHNEEAEsLRE 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 427 KIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPV------YEPVSYHvQESLQDEGAEPTGYS 500
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFgdapvdLGNAEDF-LEELREERDELRERE 428

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 501 AELSS--EGIRDDRNEEKRITEA----------EKNERVQR------QLLTLSSELSQARDENKRTHNDIIHNENMRQGR 562
Cdd:PRK02224 429 AELEAtlRTARERVEEAEALLEAgkcpecgqpvEGSPHVETieedreRVEELEAELEDLEEEVEEVEERLERAEDLVEAE 508

                        330       340
                 ....*....|....*....|...
gi 119568032 563 DKYKTLRQIRQgNTKQRIDEFEA 585
Cdd:PRK02224 509 DRIERLEERRE-DLEELIAERRE 530
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 8-88 7.74e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1 (EPB41) and similar proteins; EPB41, also termed protein 4.1 (P4.1), or 4.1R, or Band 4.1, or EPB4.1, belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41 is a widely expressed cytoskeletal phosphoprotein that stabilizes the spectrin-actin cytoskeleton and anchors the cytoskeleton to the cell membrane. EPB41 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340625  Cd Length: 83  Bit Score: 47.11  E-value: 7.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   8 RVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFYP 86
Cdd:cd17105    4 KVSLLDdTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKTWLDPAKEIKKQ--VHGGPWEFTFNVKFYP 81


                 ..
gi 119568032  87 ED 88
Cdd:cd17105   82 PD 83
PTZ00121 PTZ00121
MAEBL; Provisional
 294-582 8.39e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 8.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  294 RRKPDTIEVQQMKAQAREEKhQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA- 372
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAe 1367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  373 ---LQLEEERKRAQEEAERLEADRMAalrakEELERQAVDQIKSQEQL-AAELAEYTAKIALLEEARRRKEDEVEEWQHR 448
Cdd:PTZ00121 1368 aaeKKKEEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELkKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  449 AKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQ 528
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119568032  529 RqlltlSSELSQArdENKRTHNDIIHNENMRQGrDKYKTLRQIRQGNTKQRIDE 582
Cdd:PTZ00121 1523 K-----ADEAKKA--EEAKKADEAKKAEEKKKA-DELKKAEELKKAEEKKKAEE 1568
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 287-464 8.48e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 8.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   287 NHELYMRRRKPDTIEVQQMKAQAREEKHQKQLER--QQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAE-- 362
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEEleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEae 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   363 --------RELSEQIQRA----LQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQE-----QLAAELAEYT 425
Cdd:TIGR02168  367 leelesrlEELEEQLETLrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkELQAELEELE 446

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 119568032   426 AKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELH 464
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 7-81 9.88e-07

Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.


Pssm-ID: 340450  Cd Length: 68  Bit Score: 46.16  E-value: 9.88e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119568032   7 VRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREvWYFGLHYVDnkgfpTWLKLDKKVSaqEVRKENPLQFKFR 81
Cdd:cd00196    1 VKVETPSlKKIVVAVPPSTTLRQVLEKVAKRIGLPP-DVIRLLFNG-----QVLDDLMTAK--QVGLEPGEELHFV 68
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 299-467 1.02e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 299 TIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEE 378
Cdd:COG1196  650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 379 RKRAQEEAERLEADRMAALrakEELERQAVDQIKSQEQLAAELAEYTAKIALL--------EEArrrkeDEVEEwQHRAK 450
Cdd:COG1196  730 LEAEREELLEELLEEEELL---EEEALEELPEPPDLEELERELERLEREIEALgpvnllaiEEY-----EELEE-RYDFL 800

                        170
                 ....*....|....*...
gi 119568032 451 EAQ-DDLVKTKEELHLVM 467
Cdd:COG1196  801 SEQrEDLEEARETLEEAI 818
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 319-586 1.03e-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: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   319 ERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADrmaalr 398
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED------ 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   399 aKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEewQHRAKEAQDDLVKTKEElHLVMTAPPPPPPPVY 478
Cdd:TIGR02169  746 -LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEE-VSRIEARLREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   479 EPVSYHvQESLQDEGAEPTGYSAELSS-EGIRDDRNEEKRITEAEKNERV---QRQLLTLSSELSQARDENKRTHNDIih 554
Cdd:TIGR02169  822 NRLTLE-KEYLEKEIQELQEQRIDLKEqIKSIEKEIENLNGKKEELEEELeelEAALRDLESRLGDLKKERDELEAQL-- 898

                          250       260       270
                   ....*....|....*....|....*....|..
gi 119568032   555 nENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL 586
Cdd:TIGR02169  899 -RELERKIEELEAQIEKKRKRLSELKAKLEAL 929
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 8-88 1.27e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 2 (EPB41L2) and similar proteins; EPB41L2, also termed generally expressed protein 4.1 (4.1G), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L2 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340722  Cd Length: 84  Bit Score: 46.50  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   8 RVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFYP 86
Cdd:cd17202    5 KVTLLDGtEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSANQKNWLDSTKEIKRQ--IRRLPWLFTFNVKFYP 82


                 ..
gi 119568032  87 ED 88
Cdd:cd17202   83 PD 84
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 315-560 1.32e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  315 QKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRA------------ 382
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKiqqqkvemeqir 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  383 --QEEAERLEADRMAALRAKeELERQAVDQIKSQEQLaaelaeytAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 460
Cdd:pfam17380 427 aeQEEARQREVRRLEEERAR-EMERVRLEEQERQQQV--------ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL 497

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  461 EElhlvmTAPPPPPPPVYEPVSYHVQESLQDEGAeptgySAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELS- 539
Cdd:pfam17380 498 EK-----ELEERKQAMIEEERKRKLLEKEMEERQ-----KAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSr 567

                         250       260
                  ....*....|....*....|..
gi 119568032  540 -QARDENKRTHNDIIHNENMRQ 560
Cdd:pfam17380 568 lEAMEREREMMRQIVESEKARA 589
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
273-448 1.44e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  273 RLRINKRILQLCMGNHELYMRRRKpdtieVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELML-RL 351
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQRR-----LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  352 QDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAErLEADRMAALRAKEELERQAVDQIksQEQLAAELAEYTAKIALL 431
Cdd:COG4913   341 EQLEREIERLERELEERERRRARLEALLAALGLPLP-ASAEEFAALRAEAAALLEALEEE--LEALEEALAEAEAALRDL 417

                         170
                  ....*....|....*..
gi 119568032  432 EEARRRKEDEVEEWQHR 448
Cdd:COG4913   418 RRELRELEAEIASLERR 434
PTZ00121 PTZ00121
MAEBL; Provisional
 292-455 1.61e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  292 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELmlrlQDYEEKTKKAERELSEQIQR 371
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA----KKAEEDEKKAAEALKKEAEE 1700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  372 ALQLEEERKRAQEEAERLEADRMAALRAK---EELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHR 448
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKikaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780


                  ....*..
gi 119568032  449 AKEAQDD 455
Cdd:PTZ00121 1781 IEEELDE 1787
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 5-88 1.95e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF and pleckstrin domain-containing protein 2 (FARP2) and similar proteins; FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FARP2 contains a FERM domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340710  Cd Length: 85  Bit Score: 45.94  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLqFKFRAK 83
Cdd:cd17190    1 LQLRVKLLDnTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWIWLEPMKLIVKQVRRPKNTK-LRLAVK 79


                 ....*
gi 119568032  84 FYPED 88
Cdd:cd17190   80 FFPPD 84
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 297-462 2.08e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 50.23  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  297 PDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEElmlrlqdyeEKTKKAErelseqiQRALQLE 376
Cdd:TIGR02794  52 ANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE---------KAAKQAE-------QAAKQAE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  377 EERKRAQEEAERLEADRMAAL------RAKEELERQAVDQIKSQEQLAAELAEytakiallEEARRRKEDEVEEWQHRAK 450
Cdd:TIGR02794 116 EKQKQAEEAKAKQAAEAKAKAeaeaerKAKEEAAKQAEEEAKAKAAAEAKKKA--------EEAKKKAEAEAKAKAEAEA 187

                         170
                  ....*....|..
gi 119568032  451 EAQDDLVKTKEE 462
Cdd:TIGR02794 188 KAKAEEAKAKAE 199
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 4-88 2.37e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF and pleckstrin domain-containing protein 1 (FARP1); FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. As a novel downstream signaling partner of Rif, FARP1 is involved in the regulation of semaphorin signaling in neurons. FARP1 contains a FERM domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340709  Cd Length: 85  Bit Score: 45.95  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   4 PINVRVTTmDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 83
Cdd:cd17189    2 PIKVQMLD-DTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMVWLDLLKPIVKQ-IRRPKHVVLRFVVK 79


                 ....*
gi 119568032  84 FYPED 88
Cdd:cd17189   80 FFPPD 84
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 303-441 2.78e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 49.84  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  303 QQMKAQAREEKHQKQLERQQLETEKKRRETvEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAL--QLEEERK 380
Cdd:TIGR02794  79 EAEKQRAAEQARQKELEQRAAAEKAAKQAE-QAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAakQAEEEAK 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032  381 R-----AQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAEL---AEYTAKIALLEEARRRKEDE 441
Cdd:TIGR02794 158 AkaaaeAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAkaaAEAAAKAEAEAAAAAAAEAE 226
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 5-85 2.85e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4B (EPB41L4B); EPB41L4B, also termed FERM-containing protein CG1, or expressed in high metastatic cells (Ehm2), or Lulu2, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer.


Pssm-ID: 340724  Cd Length: 84  Bit Score: 45.58  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   5 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 83
Cdd:cd17204    1 LTCRVLLLDgTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAHWLDHTKPIKKQ-IKIGPPYTLHFRIK 79


                 ..
gi 119568032  84 FY 85
Cdd:cd17204   80 YY 81
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
343-452 2.94e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 48.28  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 343 EKEELMLR--LQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRA-KEELERQAVDQIKSQEQLAA 419
Cdd:COG1842   22 EDPEKMLDqaIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERKAELEAQAE 101

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 119568032 420 EL----AEYTAKIALLEEARRRKEDEVEEWQHRAKEA 452
Cdd:COG1842  102 ALeaqlAQLEEQVEKLKEALRQLESKLEELKAKKDTL 138
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-507 3.20e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 307 AQAREEKHQKQLERQQLETEKkrrETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEE- 385
Cdd:COG3883   12 AFADPQIQAKQKELSELQAEL---EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEl 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 386 AERLEA------------------------DRMAALRAKEELERQAVDQIKS-QEQLAAELAEYTAKIALLEEARRRKED 440
Cdd:COG3883   89 GERARAlyrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKAdKAELEAKKAELEAKLAELEALKAELEA 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119568032 441 EVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEG 507
Cdd:COG3883  169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 305-463 5.33e-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: 49.68  E-value: 5.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   305 MKAQAREEKHQKQLER------QQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEE 378
Cdd:TIGR02169  694 QSELRRIENRLDELSQelsdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   379 RKRAQEEAERLEAD----RMAALRAK-EELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKE-- 451
Cdd:TIGR02169  774 LHKLEEALNDLEARlshsRIPEIQAElSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSie 853

                          170
                   ....*....|...
gi 119568032   452 -AQDDLVKTKEEL 463
Cdd:TIGR02169  854 kEIENLNGKKEEL 866
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 307-544 5.56e-06

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: 48.99  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 307 AQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQE 384
Cdd:COG4942   18 QADAAAEAEAELEqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 385 EAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELH 464
Cdd:COG4942   98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 465 LVMTAPPPPpppvyepvsyhvQESLQDEGAEPTGYSAELSsegiRDDRNEEKRITEAEKNE-RVQRQLLTLSSELSQARD 543
Cdd:COG4942  178 ALLAELEEE------------RAALEALKAERQKLLARLE----KELAELAAELAELQQEAeELEALIARLEAEAAAAAE 241


                 .
gi 119568032 544 E 544
Cdd:COG4942  242 R 242
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 293-437 5.92e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 293 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA 372
Cdd:COG1196  676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 373 LQLEEERKRAQEEAERLEAdRMAAL-----RAKEELERqavdqiksqeqLAAELAEYTAKIALLEEARRR 437
Cdd:COG1196  756 LPEPPDLEELERELERLER-EIEALgpvnlLAIEEYEE-----------LEERYDFLSEQREDLEEARET 813
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 327-423 6.83e-06

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 45.89  E-value: 6.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 327 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA-----LQLEEERKRAQEEAERLEAdrmaalRAKE 401
Cdd:cd06503   29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEArkeaeKIKEEILAEAKEEAERILE------QAKA 102

                         90       100
                 ....*....|....*....|....*.
gi 119568032 402 ELER---QAVDQIKSQ-EQLAAELAE 423
Cdd:cd06503  103 EIEQekeKALAELRKEvADLAVEAAE 128
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 201-288 7.50e-06

FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined members: erythroid protein 4.1 (4.1R), the best known and characterized member, 4.1G (general), 4.1N (neuronal), and 4.1 B (brain). The less well understood 4.1O/FRMD3 is not a true member of this family and is not included in this hierarchy. Besides three highly conserved domains, FERM, SAB (spectrin and actin binding domain) and CTD (C-terminal domain), the proteins from this family contain several unique domains: U1, U2 and U3. FERM domains like other members of the FERM domain superfamily have a cloverleaf architecture with three distinct lobes: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The brain is a particularly rich source of protein 4.1 isoforms. The various 4.1R, 4.1G, 4.1N, and 4.1B mRNAs are all expressed in distinct patterns within the brain. It is likely that 4.1 proteins play important functional roles in the brain including motor coordination and spatial learning, postmitotic differentiation, and synaptic architecture and function. In addition they are found in nonerythroid, nonneuronal cells where they may play a general structural role in nuclear architecture and/or may interact with splicing factors. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270005  Cd Length: 94  Bit Score: 44.62  E-value: 7.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 201 YGINYFEIKNKKGTDLWLGVDALGLNIYEkdDKLtpKIG-FPWSEIRNISFNDKKFVIK----PIDKKAPDFVFYAPRLR 275
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYR--DRL--RINrFAWPKVLKISYKRNNFYIKirpgEFEQYETTIGFKLPNHR 76

                         90
                 ....*....|...
gi 119568032 276 INKRILQLCMGNH 288
Cdd:cd13184   77 AAKRLWKVCVEHH 89
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-85 7.80e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 4 (PTPN4); PTPN4, also termed protein-tyrosine phosphatase MEG1 (MEG) or PTPase-MEG1, belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN4 protects cells against apoptosis. It associates with the mitogen-activated protein kinase p38gamma (also known as MAPK12) to form a PTPN4-p38gamma complex that promotes cellular signaling, preventing cell death induction. It also inhibits tyrosine phosphorylation and subsequent cytoplasm translocation of TRIF-related adaptor molecule (TRAM, also known as TICAM2), resulting in the disturbance of TRAM-TRIF interaction. Moreover, PTPN4 negatively regulates cell proliferation and motility through dephosphorylation of CrkI.


Pssm-ID: 340714  Cd Length: 84  Bit Score: 44.14  E-value: 7.80e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032  18 FAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNK-GFPTWLKLDKKVSAQeVRKENPLQFKFRAKFY 85
Cdd:cd17194   16 FKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDStDNPRWLDPNKPIRKQ-LKRGSPHNLNFRVKFF 83
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 301-462 1.04e-05

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: 47.84  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 381 RAQEE-AERLEA-------------------------------------DRMAALRA-KEELERQAVDQIKSQEQLAAEL 421
Cdd:COG4942  101 AQKEElAELLRAlyrlgrqpplalllspedfldavrrlqylkylaparrEQAEELRAdLAELAALRAELEAERAELEALL 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 119568032 422 AEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEE 462
Cdd:COG4942  181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 201-293 1.29e-05

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270009  Cd Length: 91  Bit Score: 43.82  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 201 YGINYFEIKNKKGTDLWLGVDALGlnIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPdFVFYAPRLRINKRI 280
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEG--IFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEET-VQFQFEDAETAKYV 77

                         90
                 ....*....|...
gi 119568032 281 LQLCMGNHELYMR 293
Cdd:cd13188   78 WKLCVLQHKFYRQ 90
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 327-423 1.55e-05

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 45.16  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 327 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAL-QLEEERKRAQEEAERlEADRMAAlRAKEELER 405
Cdd:COG0711   30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARkEAEAIAEEAKAEAEA-EAERIIA-QAEAEIEQ 107

                         90       100
                 ....*....|....*....|..
gi 119568032 406 ---QAVDQIKSQ-EQLAAELAE 423
Cdd:COG0711  108 eraKALAELRAEvADLAVAIAE 129
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 298-444 1.65e-05

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: 46.46  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 298 DTIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKA---------ERELS 366
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIE 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119568032 367 EQIQRALQLEEERKRAQEEAERLEAdrmAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEE 444
Cdd:COG1579  100 SLKRRISDLEDEILELMERIEELEE---ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
PTZ00121 PTZ00121
MAEBL; Provisional
 292-585 2.11e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  292 MRRRKPDTIEVQ--QMKAQAREEKHQkqlERQQLETEKKRRETVEREKEqmmREKEELMLRLQDYEEKTKKAERELSEQI 369
Cdd:PTZ00121 1069 DEGLKPSYKDFDfdAKEDNRADEATE---EAFGKAEEAKKTETGKAEEA---RKAEEAKKKAEDARKAEEARKAEDARKA 1142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  370 QRALQLEEERK----RAQEEAERLE-------ADRMAALRAKEELeRQAVDQIKSQEQLAAELAEYTAKIALLEEARRRK 438
Cdd:PTZ00121 1143 EEARKAEDAKRveiaRKAEDARKAEearkaedAKKAEAARKAEEV-RKAEELRKAEDARKAEAARKAEEERKAEEARKAE 1221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  439 EDEVEEWQHRAKEAQddlvKTKEElhlvmtAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKR- 517
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAK----KDAEE------AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKk 1291

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  518 ITEAEKNERVQR--QLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEA 585
Cdd:PTZ00121 1292 ADEAKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 13-85 2.34e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and similar proteins; This family includes two tyrosine-protein phosphatase non-receptors, PTPN3 and PTPN4, both of which belong to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340620  Cd Length: 86  Bit Score: 43.06  E-value: 2.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119568032  13 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGF---PTWLKLDKKVSAQeVRKENPLQFKFRAKFY 85
Cdd:cd17100   11 DTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPAtdsMRWLDPLKPIRKQ-IKGGPPYYLNFRVKFY 85
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 332-463 3.37e-05

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: 45.69  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 332 TVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAErleadrmaALRAKEELERQAVDQI 411
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE--------EVEARIKKYEEQLGNV 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119568032 412 KSQEQLAA---ELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEEL 463
Cdd:COG1579   86 RNNKEYEAlqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 313-582 3.52e-05

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: 46.66  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  313 KHQKQL-ERQQLET-EKKRRETVEREKEQMMREKE--------------ELMLRLQDYEEKTKKA---ERELSEQIQRAL 373
Cdd:pfam17380 279 QHQKAVsERQQQEKfEKMEQERLRQEKEEKAREVErrrkleeaekarqaEMDRQAAIYAEQERMAmerERELERIRQEER 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  374 QLEEERKRAQEEAerLEADRMaalrakEELERQAVDQIKSQEQLAAELaEYTAKIALLEEARRRKEDEVEEWQHRAKEAQ 453
Cdd:pfam17380 359 KRELERIRQEEIA--MEISRM------RELERLQMERQQKNERVRQEL-EAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  454 DDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKR--ITEAEKNERvQRQL 531
Cdd:pfam17380 430 EEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkILEKELEER-KQAM 508

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 119568032  532 LTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQgntKQRIDE 582
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE---RRRIQE 556
PRK12704 PRK12704
phosphodiesterase; Provisional
 306-462 4.66e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 306 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELmlrlqdyEEKTKKAERELSEQIQRALQLEEERKRAQEE 385
Cdd:PRK12704  32 KIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-------EKELRERRNELQKLEKRLLQKEENLDRKLEL 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032 386 AERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALL--EEARRRKEDEVEEwqhRAKEAQDDLVKTKEE 462
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLtaEEAKEILLEKVEE---EARHEAAVLIKEIEE 180
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 294-437 4.97e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 4.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  294 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRREtVEREKEQMMRE---KEELMLRLQDYEEKTKKAERELSEQIQ 370
Cdd:TIGR02794  83 QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ-AEEAKAKQAAEakaKAEAEAERKAKEEAAKQAEEEAKAKAA 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119568032  371 RALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRR 437
Cdd:TIGR02794 162 AEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERK 228
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
294-565 5.00e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  294 RRKPDTIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVER------------EKEQMMREKEELMLRLQDYEEKTK 359
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRlaeyswdeidvaSAEREIAELEAELERLDASSDDLA 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  360 KAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVD-QIKSQEQLAAELAEYtakiaLLEEARRRK 438
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEER-----FAAALGDAV 763

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  439 EDEVEEW-QHRAKEAQDDLVKTKEELHLVMTAPPPPpppvYEPVSYHVQESLQDEGAeptgYSAELSSegIRDDR--NEE 515
Cdd:COG4913   764 ERELRENlEERIDALRARLNRAEEELERAMRAFNRE----WPAETADLDADLESLPE----YLALLDR--LEEDGlpEYE 833

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119568032  516 KRITEAeKNERVQRQLLTLSSELSQARDENKRTHNDIihNENMRQ---GRDKY 565
Cdd:COG4913   834 ERFKEL-LNENSIEFVADLLSKLRRAIREIKERIDPL--NDSLKRipfGPGRY 883
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 292-427 5.90e-05

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: 46.27  E-value: 5.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  292 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMM-REKEELMLRLQDYEEKTKKAERELSEQiQ 370
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILeKELEERKQAMIEEERKRKLLEKEMEER-Q 526

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119568032  371 RALQLEEERKRAQEEAERL------------------EADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAK 427
Cdd:pfam17380 527 KAIYEEERRREAEEERRKQqemeerrriqeqmrkateERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 298-417 6.20e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.97  E-value: 6.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 298 DTIEVQQMKAqaREEKHQKQLERQQLETEKKRRET------VEREKEQMMREKEELMLRL-QDYEEKTKKAERELSEQIQ 370
Cdd:PRK00409 514 DKEKLNELIA--SLEELERELEQKAEEAEALLKEAeklkeeLEEKKEKLQEEEDKLLEEAeKEAQQAIKEAKKEADEIIK 591

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 119568032 371 RALQLEEERKRAQEEAERLEADRmaALR-AKEELERQAVDQIKSQEQL 417
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARK--RLNkANEKKEKKKKKQKEKQEEL 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 295-462 8.65e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 8.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   295 RKPDTIEVQQMKAQAREEKhqkqlERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSE------- 367
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEK-----LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlsh 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   368 ----QIQRALQ-LEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEV 442
Cdd:TIGR02169  791 sripEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                          170       180
                   ....*....|....*....|
gi 119568032   443 EEWQHRAKEAQDDLVKTKEE 462
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKE 890
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 316-444 8.72e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 8.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   316 KQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELseqiqraLQLEEERKRAQEEAERLEADRMA 395
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-------RDLESRLGDLKKERDELEAQLRE 900

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 119568032   396 ALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEE 444
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 306-410 9.64e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 45.71  E-value: 9.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  306 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEqiqraLQLEEERKRAQEE 385
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQ-----LQEKAAETSQERK 215

                          90       100
                  ....*....|....*....|....*..
gi 119568032  386 AERLEADRMAA--LRAKEELERQAVDQ 410
Cdd:PRK11448  216 QKRKEITDQAAkrLELSEEETRILIDQ 242
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 298-446 9.91e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 9.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 298 DTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREK--------------EELMLRLQDYEEKTKKAER 363
Cdd:COG3883   54 NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGsvsyldvllgsesfSDFLDRLSALSKIADADAD 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 364 ELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVE 443
Cdd:COG3883  134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213


                 ...
gi 119568032 444 EWQ 446
Cdd:COG3883  214 AAA 216
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 301-444 1.11e-04

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 44.36  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  301 EVQQMKAQAREEKHQKQLERQQLETEKKRREtverekEQMMREKEELMLRLQDYEEkTKKAERELSEQIQRAL-QLEEER 379
Cdd:pfam09787  51 ELRQERDLLREEIQKLRGQIQQLRTELQELE------AQQQEEAESSREQLQELEE-QLATERSARREAEAELeRLQEEL 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119568032  380 KRAQEEAERLEADRMAALRAKE-ELERQAvDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEE 444
Cdd:pfam09787 124 RYLEEELRRSKATLQSRIKDREaEIEKLR-NQLTSKSQSSSSQSELENRLHQLTETLIQKQTMLEA 188
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-456 1.15e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 307 AQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEA 386
Cdd:COG1196  630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 387 ERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARrrkEDEVEEWQHRAKEAQDDL 456
Cdd:COG1196  710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE---PPDLEELERELERLEREI 776
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 296-462 1.16e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 296 KPDTIEVQQMKAQAREEKHQKQLER--QQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQ----- 368
Cdd:COG3883   24 ELSELQAELEAAQAELDALQAELEElnEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvs 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 369 --------------IQRALQLE-------EERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAK 427
Cdd:COG3883  104 yldvllgsesfsdfLDRLSALSkiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 119568032 428 IALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEE 462
Cdd:COG3883  184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 351-453 1.38e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 43.51  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  351 LQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAAL-RAKEELERQAVDQIKSQEQLAAEL-------- 421
Cdd:pfam04012  31 IRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALtKGNEELAREALAEKKSLEKQAEALetqlaqqr 110

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 119568032  422 ---AEYTAKIALLEEARRRKEDEVEEWQHRAKEAQ 453
Cdd:pfam04012 111 savEQLRKQLAALETKIQQLKAKKNLLKARLKAAK 145
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 310-391 1.77e-04

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 43.76  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  310 REEKHQKQLERQQLETEKKRRETVEREKEQMM--REKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAE 387
Cdd:pfam15991  20 RERERKKQEQEAKMEEERLRREREEREKEDRMtlEETKEQILKLEKKLADLKEEKHQLFLQLKKVLHEDETRKRQLKEQS 99


                  ....
gi 119568032  388 RLEA 391
Cdd:pfam15991 100 ELFA 103
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 306-434 1.78e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 44.36  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  306 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLqdyEEKTKKAERELSEQIQRALQ---------LE 376
Cdd:pfam09731 291 HAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARL---EEVRAADEAQLRLEFEREREeiresyeekLR 367

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119568032  377 EERKRAQEEAErlEADRMAALRAKEELERQAVDQIKS-----QEQLAAELAEYTAKIALLEEA 434
Cdd:pfam09731 368 TELERQAEAHE--EHLKDVLVEQEIELQREFLQDIKEkveeeRAGRLLKLNELLANLKGLEKA 428
PTZ00121 PTZ00121
MAEBL; Provisional
 300-582 1.83e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  300 IEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAlqleEER 379
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA----EEK 1289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  380 KRAQEEAERLEADRMAALRAKEELERQAvDQIKSQEQLAAELAEYTAKIAllEEARrrKEDEVEewQHRAKEAQDDLVKT 459
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKKKA--EEAK--KAAEAA--KAEAEAAADEAEAA 1362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  460 KEELHLVMTAPPPPPPPVyEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELS 539
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKA-DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 119568032  540 QAR--DENKRTHNDIIHNENM-RQGRDKYKTLRQIRQGNTKQRIDE 582
Cdd:PTZ00121 1442 EAKkaDEAKKKAEEAKKAEEAkKKAEEAKKADEAKKKAEEAKKADE 1487
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 313-461 1.96e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.40  E-value: 1.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   313 KHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQ-------DYEEKTKKAERELSEQIQRALQLEEERKRAQ 383
Cdd:pfam01576  549 RLQRELEalTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsNLEKKQKKFDQMLAEEKAISARYAEERDRAE 628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   384 EEAERLEADRMA-------ALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDL 456
Cdd:pfam01576  629 AEAREKETRALSlaraleeALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL 708


                   ....*
gi 119568032   457 VKTKE 461
Cdd:pfam01576  709 QATED 713
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 301-407 2.17e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.95  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDyEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:pfam05672  30 EEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAE-EEAEEREQREQEEQERLQKQKEEAEA 108

                          90       100
                  ....*....|....*....|....*..
gi 119568032  381 RAQEEAERLEADRmAALRAKEELERQA 407
Cdd:pfam05672 109 KAREEAERQRQER-EKIMQQEEQERLE 134
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 381-548 2.37e-04

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 43.57  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  381 RAQEEAERLEADRMAALRAKEELERqavdQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 460
Cdd:pfam00529  55 DYQAALDSAEAQLAKAQAQVARLQA----ELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRR 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  461 eelhlvmtapppppppVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNER--------VQRQLL 532
Cdd:pfam00529 131 ----------------VLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAevrselsgAQLQIA 194

                         170
                  ....*....|....*.
gi 119568032  533 TLSSELSQARDENKRT 548
Cdd:pfam00529 195 EAEAELKLAKLDLERT 210
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 8-68 2.58e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and similar proteins; PTPN21, also termed protein-tyrosine phosphatase D1 (PTPD1), is a cytosolic non-receptor protein-tyrosine phosphatase (PTP) that belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation. It also associates with and activates Src tyrosine kinase, and directs epidermal growth factor (EGF)/Src signaling to the nucleus through activating ERK1/2- and Elk1-dependent gene transcription. PTPD1-Src complex interacts a protein kinase A-anchoring protein AKAP121 to forms a PTPD1-Src-AKAP121 complex, which is required for efficient maintenance of mitochondrial membrane potential and ATP oxidative synthesis. As a novel component of the endocytic pathway, PTPN21 supports EGF receptor stability and mitogenic signaling in bladder cancer cells. Moreover, PTPD1 regulates focal adhesion kinase (FAK) autophosphorylation and cell migration through modulating Src-FAK signaling at adhesion sites.


Pssm-ID: 340712  Cd Length: 87  Bit Score: 40.01  E-value: 2.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119568032   8 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQ 68
Cdd:cd17192    7 RIQLLNNEfVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQ 68
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 289-406 2.64e-04

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 42.77  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  289 ELYMRRRKPDTIEVQQMKA-----QAREEKHQKQLERQQLETEKKRRETVEREK------EQMMREKEELmlRLQDYEEK 357
Cdd:pfam13904  38 LTYARKLEGLKLERQPLEAyenwlAAKQRQRQKELQAQKEEREKEEQEAELRKRlakekyQEWLQRKARQ--QTKKREES 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119568032  358 TKKAERELS-------------EQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQ 406
Cdd:pfam13904 116 HKQKAAESAskslakperkvsqEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQERK 177
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 334-542 2.76e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 334 EREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAA----LRAKEELERQAVD 409
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeiEERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 410 QIKSQEQL--------AAELAEYTAKIALLE---EARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPpppvy 478
Cdd:COG3883   95 LYRSGGSVsyldvllgSESFSDFLDRLSALSkiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----- 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119568032 479 epvsyhvQESLQDEGAEPTGYSAELSSEgiRDDRNEEKRITEAEKNERVQRQLLTLSSELSQAR 542
Cdd:COG3883  170 -------KAELEAQQAEQEALLAQLSAE--EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 299-456 2.79e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 299 TIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAEREL----SEQIQRA 372
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAelEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKEYEA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 373 LQLEEER-KRAQEEAERLEADRMAALRAKEELERQAvdqiksQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKE 451
Cdd:COG1579   94 LQKEIESlKRRISDLEDEILELMERIEELEEELAEL------EAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167


                 ....*
gi 119568032 452 AQDDL 456
Cdd:COG1579  168 LAAKI 172
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 310-427 3.88e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.57  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  310 REEKHQKQLERQQLEteKKRRETVEREKEQmmrekeelmlrlqdyeektkKAERELSEQIQRALQLEEERKRAQEEAERL 389
Cdd:PTZ00266  442 KENAHRKALEMKILE--KKRIERLEREERE--------------------RLERERMERIERERLERERLERERLERDRL 499

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 119568032  390 EADRMaalrakEELERQAVDQIKSQEQLAAELAEYTAK 427
Cdd:PTZ00266  500 ERDRL------DRLERERVDRLERDRLEKARRNSYFLK 531
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 357-444 4.75e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 42.75  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 357 KTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAAlrAKE--ELERQAVDqiksQEQLAAELAEYTAKIALLEEA 434
Cdd:PRK05431  15 KEALAKRGFPLDVDELLELDEERRELQTELEELQAERNAL--SKEigQAKRKGED----AEALIAEVKELKEEIKALEAE 88

                         90
                 ....*....|
gi 119568032 435 RRRKEDEVEE 444
Cdd:PRK05431  89 LDELEAELEE 98
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
295-460 6.12e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 295 RKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQ 374
Cdd:COG4372   19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 375 LEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQD 454
Cdd:COG4372   99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178


                 ....*.
gi 119568032 455 DLVKTK 460
Cdd:COG4372  179 AEAEQA 184
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 298-400 6.18e-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: 42.44  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 298 DTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAlqlee 377
Cdd:COG4942  158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL----- 232

                         90       100
                 ....*....|....*....|...
gi 119568032 378 eRKRAQEEAERLEADRMAALRAK 400
Cdd:COG4942  233 -EAEAAAAAERTPAAGFAALKGK 254
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
288-422 8.42e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 288 HELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTK-KAERELS 366
Cdd:COG4717  116 EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQ 195

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119568032 367 EQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQiKSQEQLAAELA 422
Cdd:COG4717  196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARL 250
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
293-463 8.48e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 8.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 293 RRRKPDTIEVQQMKAQAREEKHQKQLER--------QQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERE 364
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERaedlveaeDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 365 LSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQA--VDQIKSQEQLAAELAEYTAKIALLEEARRRK---- 438
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRtlLAAIADAEDEIERLREKREALAELNDERRERlaek 632

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 119568032 439 ------------EDEVEEWQHRAKEAQDDLVKTKEEL 463
Cdd:PRK02224 633 rerkreleaefdEARIEEAREDKERAEEYLEQVEEKL 669
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
311-444 8.56e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 8.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 311 EEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAER---ELSEQIQRALQLEEERKRAQEEAE 387
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEErikELEEKEERLEELKKKLKELEKRLE 355

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032 388 RLEADRMAALRAKEELERqavdqiksQEQLAAELAEYTAK--IALLEEARRRKEdEVEE 444
Cdd:PRK03918 356 ELEERHELYEEAKAKKEE--------LERLKKRLTGLTPEklEKELEELEKAKE-EIEE 405
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 327-423 8.68e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 40.14  E-value: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 327 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA-----LQLEEERKRAQEEAERLEAdrmaalRAKE 401
Cdd:PRK05759  34 EERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAkkraaQIIEEAKAEAEAEAARIKA------QAQA 107

                         90       100
                 ....*....|....*....|....*.
gi 119568032 402 ELER---QAVDQIKSQ-EQLAAELAE 423
Cdd:PRK05759 108 EIEQerkRAREELRKQvADLAVAGAE 133
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
301-439 9.34e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 9.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEK------KRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQ 374
Cdd:COG4717   99 ELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE 178

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032 375 LEEERKRAQEEAERLE---ADRMAALRAKEELERQAVDQIKSQ-EQLAAELAEYTAKIALLEEARRRKE 439
Cdd:COG4717  179 LEELLEQLSLATEEELqdlAEELEELQQRLAELEEELEEAQEElEELEEELEQLENELEAAALEERLKE 247
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 313-405 9.47e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 41.64  E-value: 9.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 313 KHQKQLERQQLETEKKRRETVErEKEQMMREKEELMLRLQDYEEKTKKAERELSEqiqralqLEEERKRAQEEAERLEaD 392
Cdd:COG4026  128 PEYNELREELLELKEKIDEIAK-EKEKLTKENEELESELEELREEYKKLREENSI-------LEEEFDNIKSEYSDLK-S 198

                         90
                 ....*....|...
gi 119568032 393 RMAALRAKEELER 405
Cdd:COG4026  199 RFEELLKKRLLEV 211
PLN02316 PLN02316
synthase/transferase
 355-406 9.91e-04

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 42.16  E-value: 9.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119568032  355 EEKTKKAERELSEQIQRALQLEEERKRAQEEAERlEADRMaalRAKEELERQ 406
Cdd:PLN02316  252 EEKRRELEKLAKEEAERERQAEEQRRREEEKAAM-EADRA---QAKAEVEKR 299
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 316-452 1.05e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.75  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  316 KQLERQQLETEKKRRETVEREKEQMmREKEELmlrlqdyeEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMA 395
Cdd:TIGR02794  50 QQANRIQQQKKPAAKKEQERQKKLE-QQAEEA--------EKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119568032  396 AlrakEELERQAvdqikSQEQLAAELAEytAKIALLEEARRRKEDE-----VEEWQHRAKEA 452
Cdd:TIGR02794 121 A----EEAKAKQ-----AAEAKAKAEAE--AERKAKEEAAKQAEEEakakaAAEAKKKAEEA 171
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 301-421 1.13e-03

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: 41.41  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREK-EQMMREKEELMLRLQDYEEKTKKAERELSEQIQR-ALQLEEE 378
Cdd:cd16269  170 EVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKaEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQlKEKMEEE 249

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 119568032 379 RKRAQEEAErleadRMAALRAKEELERQAVDQIKSQEQLAAEL 421
Cdd:cd16269  250 RENLLKEQE-----RALESKLKEQEALLEEGFKEQAELLQEEI 287
mukB PRK04863
chromosome partition protein MukB;
308-449 1.18e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  308 QAREEKHQKQlERQQLE---TEKKRRETVEREKEQMMRE-----------KEELMLRLQDYEEKTKKAERELSEQIQRAL 373
Cdd:PRK04863  504 RLREQRHLAE-QLQQLRmrlSELEQRLRQQQRAERLLAEfckrlgknlddEDELEQLQEELEARLESLSESVSEARERRM 582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  374 QLEEERKRAQEEAERLEADRMAALRAKEELER------------QAVDQIksQEQLAAELAEYTAKIALLEEARRRKEDE 441
Cdd:PRK04863  583 ALRQQLEQLQARIQRLAARAPAWLAAQDALARlreqsgeefedsQDVTEY--MQQLLERERELTVERDELAARKQALDEE 660


                  ....*...
gi 119568032  442 VEEWQHRA 449
Cdd:PRK04863  661 IERLSQPG 668
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 302-399 1.21e-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: 41.29  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 302 VQQMKAQARE-EKHQKQLERQQLETEKKRRETVEREKEQmMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:COG4942  145 APARREQAEElRADLAELAALRAELEAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                         90
                 ....*....|....*....
gi 119568032 381 RAQEEAERLEADRMAALRA 399
Cdd:COG4942  224 ELEALIARLEAEAAAAAER 242
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
306-463 1.47e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 306 KAQAREEKHQKQLERQQLETEKKRRETVEREKE-QMMREKEELMLRLQDYEEKTKKAERELSEQIQRalqLEEERKRAQE 384
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR---LEEEINGIEE 328

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032 385 EAERLEADRmaalRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEEL 463
Cdd:PRK03918 329 RIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEI 403
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 292-392 1.57e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 39.39  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  292 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRET-VEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQ 370
Cdd:pfam15236  48 ERKRQKALEHQNAIKKQLEEKERQKKLEEERRRQEEQEEEErLRREREEEQKQFEEERRKQKEKEEAMTRKTQALLQAMQ 127

                          90       100
                  ....*....|....*....|....*
gi 119568032  371 RALQL---EEERKRAQEEAERLEAD 392
Cdd:pfam15236 128 KAQELaqrLKQEQRIRELAEKGHDT 152
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
315-437 1.58e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 315 QKQLERQQLETEKkRRETVEREKEQMMREKEELMLRLQDYEEKTK--KAERELSEQIQRALQLEEERKRAQEEAERLEAd 392
Cdd:COG3206  163 EQNLELRREEARK-ALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEA- 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119568032 393 RMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRR 437
Cdd:COG3206  241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSAR 285
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 211-284 1.64e-03

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


Pssm-ID: 275390  Cd Length: 89  Bit Score: 37.76  E-value: 1.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032 211 KKGTDLWLGVDALGLnIYEKDDKLTPKIGFPWSEIRNISFND-----KKFVIKPIDkKAPDFVFYAPRLRINKRILQLC 284
Cdd:cd00900   13 TKRVEGTLYITSDRL-ILRDKNDGGLELSIPISDIVNVNVSPqgpssRYLVLVLKD-RGEFVGFSFPKEEDAIEISDAL 89
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 298-441 1.69e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.87  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  298 DTIEVQQMKAQAReekhqkqleRQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELS---EQIQRALQ 374
Cdd:pfam00529  61 DSAEAQLAKAQAQ---------VARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAqaqIDLARRRV 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119568032  375 LEEE---RKRAQEEAERL----EADRMAALRAKEELERQAVDQIK-SQEQLAAELAEYTAKIALLEEARRRKEDE 441
Cdd:pfam00529 132 LAPIggiSRESLVTAGALvaqaQANLLATVAQLDQIYVQITQSAAeNQAEVRSELSGAQLQIAEAEAELKLAKLD 206
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 327-410 1.74e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 38.83  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  327 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA-----LQLEEERKRAQEEAERLEADRMAAL---- 397
Cdd:pfam00430  29 DKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAkkraeKLKEEIVAAAEAEAERIIEQAAAEIeqek 108

                          90
                  ....*....|....
gi 119568032  398 -RAKEELERQAVDQ 410
Cdd:pfam00430 109 dRALAELRQQVVAL 122
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 292-436 1.86e-03

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: 41.21  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   292 MRRRKPDTIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYE-------------- 355
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEEELEELEAALRdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRkrlselkakleale 930

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   356 ------EKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIA 429
Cdd:TIGR02169  931 eelseiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010


                   ....*..
gi 119568032   430 LLEEARR 436
Cdd:TIGR02169 1011 EYEKKKR 1017
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 315-462 1.92e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.36  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   315 QKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQ-----EEAERL 389
Cdd:pfam12128  662 KQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQlallkAAIAAR 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   390 EADRMAALRA-----KEELERQAVDQIKSQeQLAAELAEYTAKIallEEARRRkEDEVEEW----QHRAKEAQDDLVKTK 460
Cdd:pfam12128  742 RSGAKAELKAletwyKRDLASLGVDPDVIA-KLKREIRTLERKI---ERIAVR-RQEVLRYfdwyQETWLQRRPRLATQL 816


                   ..
gi 119568032   461 EE 462
Cdd:pfam12128  817 SN 818
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 321-433 2.00e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 321 QQLETEKKRRETVEREKEQMMREKEELML-RLQDYEEKTKKAERELSEqiqralqleeerKRAQEEAERLEADRMAALra 399
Cdd:COG0542  411 EELDELERRLEQLEIEKEALKKEQDEASFeRLAELRDELAELEEELEA------------LKARWEAEKELIEEIQEL-- 476

                         90       100       110
                 ....*....|....*....|....*....|....
gi 119568032 400 KEELERQAVDQIKSQEQLAAELAEYTAKIALLEE 433
Cdd:COG0542  477 KEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
PTZ00121 PTZ00121
MAEBL; Provisional
 295-410 2.18e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  295 RKPDTIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA 372
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 119568032  373 LQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQ 410
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
PRK12705 PRK12705
hypothetical protein; Provisional
 294-440 2.25e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.85  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 294 RRKPDTIEVQQMKAQAREEKHQKQLERqqletekKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAL 373
Cdd:PRK12705  47 EEKLEAALLEAKELLLRERNQQRQEAR-------REREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSAREL 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119568032 374 QLEEERKRAQEEAERL------EADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKED 440
Cdd:PRK12705 120 ELEELEKQLDNELYRVagltpeQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRIASE 192
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 331-451 2.26e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 331 ETVEREKEQMMREKEELmlrlqdyeektKKAERELSEQiqRALQLEEERKRAQEEAErleadrmaALRAKEELERQAVDQ 410
Cdd:COG0542  414 DELERRLEQLEIEKEAL-----------KKEQDEASFE--RLAELRDELAELEEELE--------ALKARWEAEKELIEE 472

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 119568032 411 IKSqeqLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKE 451
Cdd:COG0542  473 IQE---LKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 372-459 2.28e-03

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 37.80  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  372 ALQLEEERKRAQEEAERLEADRMAALRAKEELERQAvdqiksQEQLAAELAEYTAKIAllEEARRRKEDEVEEWQHRAKE 451
Cdd:pfam16999  18 DQQIEAARKEAEREVEAAEAEAARILREAEAKAKAL------QAEYRQELAAETARIR--EEARARAEAEAQAVRTRAEG 89


                  ....*...
gi 119568032  452 AQDDLVKT 459
Cdd:pfam16999  90 RLQQAVEL 97
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 316-462 2.32e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 316 KQLERQQLETEKKRRETVEREKEQMMREkEELMlrlqdyeektkkaERELSEQiQRALQLEEERKRAQ------EEAERL 389
Cdd:PRK09510  62 EQYNRQQQQQKSAKRAEEQRKKKEQQQA-EELQ-------------QKQAAEQ-ERLKQLEKERLAAQeqkkqaEEAAKQ 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119568032 390 EADR-----MAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEE 462
Cdd:PRK09510 127 AALKqkqaeEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
301-435 2.43e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERqqlETEKKRRETVEREKEQMMREKEELMlrlqdyEEKTKKAERELSEQIQRalqlEEERK 380
Cdd:COG2268  211 ETEIAIAQANREAEEAELEQ---EREIETARIAEAEAELAKKKAEERR------EAETARAEAEAAYEIAE----ANAER 277

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119568032 381 RAQEEAERLEADRMAALRAKEELERQAvdQIKSQEQLAAElAEYTAKIAlLEEAR 435
Cdd:COG2268  278 EVQRQLEIAEREREIELQEKEAEREEA--ELEADVRKPAE-AEKQAAEA-EAEAE 328
PTZ00121 PTZ00121
MAEBL; Provisional
 287-582 2.50e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  287 NHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAErels 366
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE---- 1325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  367 EQIQRAlqlEEERKRAQEEAERLEADRMAALRAKEELErqAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQ 446
Cdd:PTZ00121 1326 EAKKKA---DAAKKKAEEAKKAAEAAKAEAEAAADEAE--AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  447 HRAKEAQDDLVKTKEELHLVMTAPPPPPPPvyepvsYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNER 526
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEK------KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119568032  527 VQRQlltlSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDE 582
Cdd:PTZ00121 1475 AKKK----AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 301-438 2.52e-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: 39.91  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETV--EREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEE 378
Cdd:COG1579   53 ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 379 RKRAQEEAERLEADRMAALrakEELERQAVDQIKSQEQLAAELAEYTakIALLEEARRRK 438
Cdd:COG1579  133 LAELEAELEEKKAELDEEL---AELEAELEELEAEREELAAKIPPEL--LALYERIRKRK 187
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-85 2.70e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3); PTPN3, also termed protein-tyrosine phosphatase H1 (PTP-H1), belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN3 associates with the mitogen-activated protein kinase p38gamma (also known as MAPK12) to form a PTPN3-p38gamma complex that promotes Ras-induced oncogenesis. It may also act as a tumor suppressor in lung cancer through its modulation of epidermal growth factor receptor (EGFR) signaling. Moreover, PTPN3 shows sensitizing effect to anti-estrogens. It dephosphorylates the tyrosine kinase EGFR, disrupts its interaction with the nuclear estrogen receptor, and increases breast cancer sensitivity to small molecule tyrosine kinase inhibitors (TKIs). It also cooperates with vitamin D receptor to stimulate breast cancer growth through their mutual stabilization.


Pssm-ID: 340713  Cd Length: 84  Bit Score: 37.14  E-value: 2.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032  18 FAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNK-GFPTWLKLDKKVSAQeVRKENPLQFKFRAKFY 85
Cdd:cd17193   16 FKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSvDSPRWLEPSKPIRKQ-LKGGFPCSLHFRVRFF 83
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
324-462 2.94e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 324 ETEKKRRETVEREKEQMMREKEelmlRLQDYEEKTKKAERELSE--QIQRALQLEEERKRAQEEAERLEADRMAALrAKE 401
Cdd:COG2268  199 RDARIAEAEAERETEIAIAQAN----REAEEAELEQEREIETARiaEAEAELAKKKAEERREAETARAEAEAAYEI-AEA 273

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119568032 402 ELERQAvdqiksqeQLAAELAEYTAKIAlLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEE 462
Cdd:COG2268  274 NAEREV--------QRQLEIAEREREIE-LQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 299-391 3.29e-03

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: 39.87  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 299 TIEVQQMKAQArEEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELmlrlqdyEEKTKKAERELSEQIQRALQLEEE 378
Cdd:cd16269  199 EIEAERAKAEA-AEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKM-------EEERENLLKEQERALESKLKEQEA 270

                         90
                 ....*....|....*
gi 119568032 379 --RKRAQEEAERLEA 391
Cdd:cd16269  271 llEEGFKEQAELLQE 285
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
308-451 3.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 308 QAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAE 387
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119568032 388 RLEADRMAALRAKEELErQAVDQIKSQEQLAAELAEytaKIALLEEARRRKEDEVEEWQHRAKE 451
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEE---KIRELEERIEELKKEIEELEEKVKE 284
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
352-553 3.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  352 QDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRakeeLERQAVDQIKSQeQLAAELAEYTAKIALL 431
Cdd:COG4913   606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR----LAEYSWDEIDVA-SAEREIAELEAELERL 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  432 EEArrrkEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPvyepvsyhvQESLQDEGAEPTGYSAELSSEGIRDD 511
Cdd:COG4913   681 DAS----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE---------LEQAEEELDELQDRLEAAEDLARLEL 747

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 119568032  512 RNE-EKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDII 553
Cdd:COG4913   748 RALlEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 338-426 4.03e-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: 39.75  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 338 EQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAV---DQIKSQ 414
Cdd:COG4942  153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEeleALIARL 232

                         90
                 ....*....|..
gi 119568032 415 EQLAAELAEYTA 426
Cdd:COG4942  233 EAEAAAAAERTP 244
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 316-409 4.12e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 316 KQLERQ--QLETEK----KRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERL 389
Cdd:COG0542  414 DELERRleQLEIEKealkKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493

                         90       100
                 ....*....|....*....|
gi 119568032 390 EADRMAALRAKEELERQAVD 409
Cdd:COG0542  494 LAELEEELAELAPLLREEVT 513
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 289-462 4.30e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.34  E-value: 4.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   289 ELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQ 368
Cdd:pfam02463  209 ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEEL 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   369 IQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHR 448
Cdd:pfam02463  289 KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL 368

                          170
                   ....*....|....
gi 119568032   449 AKEAQDDLVKTKEE 462
Cdd:pfam02463  369 EQLEEELLAKKKLE 382
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 308-406 4.42e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.10  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  308 QAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRalqlEEERKRAQEEAE 387
Cdd:pfam05672  22 QAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEA----EEREQREQEEQE 97

                          90       100
                  ....*....|....*....|
gi 119568032  388 RLEADRMAA-LRAKEELERQ 406
Cdd:pfam05672  98 RLQKQKEEAeAKAREEAERQ 117
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 303-410 4.71e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  303 QQMKAQAREEKHQKQLERQQleteKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRalQLEEERKRA 382
Cdd:pfam15709 418 QERARQQQEEFRRKLQELQR----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ--KQEAEEKAR 491

                          90       100
                  ....*....|....*....|....*...
gi 119568032  383 QEEAERLEADRMAALRAKEELERQAVDQ 410
Cdd:pfam15709 492 LEAEERRQKEEEAARLALEEAMKQAQEQ 519
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 317-452 4.98e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  317 QLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRalqLEEERKRAQEEAERLEADRMAA 396
Cdd:pfam07888  30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE---LKEELRQSREKHEELEEKYKEL 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119568032  397 LRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEA 452
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKA 162
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
301-461 5.03e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEE-----------KTKKAERELsEQI 369
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEakakkeelerlKKRLTGLTP-EKL 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 370 QRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKS-------------QEQLAAELAEYTAKIALLEEARR 436
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgreltEEHRKELLEEYTAELKRIEKELK 469

                        170       180
                 ....*....|....*....|....*
gi 119568032 437 RKEDEVEEWQHRAKEAQDDLVKTKE 461
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESE 494
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 319-418 5.04e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.00  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 319 ERQQLETEKKRRETVEREKEQMMREK--------EELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAE--R 388
Cdd:NF033838 303 EKKVAEAEKKVEEAKKKAKDQKEEDRrnyptntyKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVEskK 382

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 119568032 389 LEADRMAAL-----RAKEELERQAVDQIKSQEQLA 418
Cdd:NF033838 383 AEATRLEKIktdrkKAEEEAKRKAAEEDKVKEKPA 417
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 317-456 5.16e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  317 QLERQQLETEKKRRETVEREKEqMMREKEELMLRLQDYEEKTKKAERELSeQIQRALQLEEERKRAQEE----AERLEAD 392
Cdd:COG3096   289 ELRRELFGARRQLAEEQYRLVE-MARELEELSARESDLEQDYQAASDHLN-LVQTALRQQEKIERYQEDleelTERLEEQ 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  393 RMAALRAKEELER---------QAVDQIKSQeqlaaeLAEY--------TAKIAL------LEEARRRKE------DEVE 443
Cdd:COG3096   367 EEVVEEAAEQLAEaearleaaeEEVDSLKSQ------LADYqqaldvqqTRAIQYqqavqaLEKARALCGlpdltpENAE 440

                         170
                  ....*....|...
gi 119568032  444 EWQHRAKEAQDDL 456
Cdd:COG3096   441 DYLAAFRAKEQQA 453
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
299-453 5.26e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 299 TIEVQQMkAQAREEKHQKQLERQQLETekkRRETVEREKEQMMREKEELML--RLQDYEEKTKKAERELSE--------- 367
Cdd:COG3206  215 KLLLQQL-SELESQLAEARAELAEAEA---RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAElsarytpnh 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 368 -QIQRAL-QLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEW 445
Cdd:COG3206  291 pDVIALRaQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370


                 ....*...
gi 119568032 446 QHRAKEAQ 453
Cdd:COG3206  371 LQRLEEAR 378
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 367-468 5.51e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.68  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 367 EQIQRAL-QLEEERKRAQEEAERLEADRMAALRAKEElerqavdqiKSQEQLAAELAEYTAKIALLEEARRRKEdEVEEW 445
Cdd:COG0542  414 DELERRLeQLEIEKEALKKEQDEASFERLAELRDELA---------ELEEELEALKARWEAEKELIEEIQELKE-ELEQR 483

                         90       100
                 ....*....|....*....|...
gi 119568032 446 QHRAKEAQDDLVKTKEELHLVMT 468
Cdd:COG0542  484 YGKIPELEKELAELEEELAELAP 506
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 201-255 5.84e-03

FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein (MYLIP; also called inducible degrader of the LDL receptor, IDOL); MYLIP/IDOL is a regulator of the LDL receptor (LDLR) pathway via the nuclear receptor liver X receptor (LXR). In response to cellular cholesterol loading, the activation of LXR leads to the induction of MYLIP expression. MYLIP stimulates ubiquitination of the LDLR on its cytoplasmic tail, directing its degradation. The LXR-MYLIP-LDLR pathway provides a complementary pathway to sterol regulatory element-binding proteins for the feedback inhibition of cholesterol uptake. MYLIP has an N-terminal FERM domain and in some cases a C-terminal RING domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270016  Cd Length: 111  Bit Score: 36.84  E-value: 5.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119568032 201 YGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIgfPWSEIRNISFNDKKF 255
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERI--PYTAIQMATSSGRVF 53
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
301-429 5.93e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.47  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 301 EVQQMKAQAREEKHQKQLERQQ---LETEKKRR------ETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQR 371
Cdd:COG2268  245 ELAKKKAEERREAETARAEAEAayeIAEANAERevqrqlEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE 324

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119568032 372 A-LQLEEERKRAQEEAERLEAdrMAAlrAKEELERQAVDQ--IKSQEQLAAELAEYTAKIA 429
Cdd:COG2268  325 AeAEAEAIRAKGLAEAEGKRA--LAE--AWNKLGDAAILLmlIEKLPEIAEAAAKPLEKID 381
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 363-579 7.07e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.44  E-value: 7.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   363 RELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIK-SQEQLAAEL-AEYTAKIALLEEARRRKED 440
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARlDLRRLFDEKqSEKDKKNKALAERKDSANE 682

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032   441 EVEEWQHRAK----EAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSyhVQESLQDEG--AEPTGYSAELSSEGIRDDRNE 514
Cdd:pfam12128  683 RLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALD--AQLALLKAAiaARRSGAKAELKALETWYKRDL 760

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119568032   515 EKRITEAEKNERVQRQLLTLSSELSQ-ARDENKRTHNDIIHNENMRQGRDKYKTlrQIRQGNTKQR 579
Cdd:pfam12128  761 ASLGVDPDVIAKLKREIRTLERKIERiAVRRQEVLRYFDWYQETWLQRRPRLAT--QLSNIERAIS 824
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 308-460 7.16e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 39.16  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 308 QAREEKHQKQLERQQLETEKKRREtverekeqmmREKEElmlRlqdyEEKTKKAERELSEQIQRALQLEEERKRAQEEAE 387
Cdd:PRK05035 440 AIEQEKKKAEEAKARFEARQARLE----------REKAA---R----EARHKKAAEARAAKDKDAVAAALARVKAKKAAA 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 388 RLEADRMA-------ALRAKEELERQAVDQIKSQEQLAAELAEYTAKI-ALLEEARRRKEDEVEEwqHRAKEAQDDLVKT 459
Cdd:PRK05035 503 TQPIVIKAgarpdnsAVIAAREARKAQARARQAEKQAAAAADPKKAAVaAAIARAKAKKAAQQAA--NAEAEEEVDPKKA 580


                 .
gi 119568032 460 K 460
Cdd:PRK05035 581 A 581
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
303-464 7.93e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 303 QQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQmmREKEELMLRLQDYEEKTKKAERELSEQIQRAlQLEEERKRA 382
Cdd:COG4717  361 EELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALDEE-ELEEELEEL 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 383 QEEAERLEADRMAALRAKEELErQAVDQIKSQEQLAAELAEYtakiallEEARRRKEDEVEEWQhRAKEAQDDLVKTKEE 462
Cdd:COG4717  438 EEELEELEEELEELREELAELE-AELEQLEEDGELAELLQEL-------EELKAELRELAEEWA-ALKLALELLEEAREE 508


                 ..
gi 119568032 463 LH 464
Cdd:COG4717  509 YR 510
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
293-405 9.26e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 9.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032 293 RRRKPDTIEVQQMKAQAREEKHQKQLERQ--QLETEKKR-RETVEREKEQMMREKEELMLRLQDYEEKTKKaERELSEQI 369
Cdd:COG2433  393 EEPEAEREKEHEERELTEEEEEIRRLEEQveRLEAEVEElEAELEEKDERIERLERELSEARSEERREIRK-DREISRLD 471

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 119568032 370 QRALQLEEERKRAQEEAERLEA--DRMAALRAKEELER 405
Cdd:COG2433  472 REIERLERELEEERERIEELKRklERLKELWKLEHSGE 509
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 301-439 9.83e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 38.48  E-value: 9.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  301 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 380
Cdd:pfam15558  43 KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRK 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119568032  381 RAQEEaerleadrmaALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKE 439
Cdd:pfam15558 123 QCQEQ----------RLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQE 171
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 289-419 9.97e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 38.78  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  289 ELYMRRRKPDTIEVQQMKAQAREEKHQKQLER-------------QQLETEKKRRETVEREK---EQMMREK-----EEL 347
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELeqqrrfeeirlrkQRLEEERQRQEEEERKQrlqLQAAQERarqqqEEF 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119568032  348 MLRLQDYE-----EKTKKAERELSEQIQRALQLEEERKR---------------AQEEAERLEADRMAALRAKEELERQA 407
Cdd:pfam15709 429 RRKLQELQrkkqqEEAERAEAEKQRQKELEMQLAEEQKRlmemaeeerleyqrqKQEAEEKARLEAEERRQKEEEAARLA 508

                         170
                  ....*....|..
gi 119568032  408 VDQIKSQEQLAA 419
Cdd:pfam15709 509 LEEAMKQAQEQA 520
 
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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