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Conserved domains on  [gi|119625804|gb|EAX05399|]
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moesin, isoform CRA_b [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 ...
 189-285 1.92e-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: 228.70  E-value: 1.92e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 189 MYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 268
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 119625804 269 ILALCMGNHELYMRRRK 285
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1-195 4.67e-57

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: 189.81  E-value: 4.67e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804     1 MDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQD-TKGFSTWLKLNKKVTAQDVRKEsPLLFKFRAKFYPEDV 78
Cdd:smart00295   7 LDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKFYPPDP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804    79 sEELIQDITQ-RLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVH-KSGYLAGDKLLPQRVLEQhkLNKDQ 156
Cdd:smart00295  86 -NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS--RKLKE 162

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 119625804   157 WEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 195
Cdd:smart00295 163 WRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 491-566 6.67e-35

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: 125.78  E-value: 6.67e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804  491 DRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM 566
Cdd:pfam00769   2 LEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 336-445 3.73e-21

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: 88.82  E-value: 3.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 415
Cdd:pfam20492  11 LEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQE 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 119625804  416 RISQLEMARQKKESEAVEWQQKAQMVQEDL 445
Cdd:pfam20492  91 EIARLEEEVERKEEEARRLQEELEEAREEE 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 ...
 189-285 1.92e-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: 228.70  E-value: 1.92e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 189 MYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 268
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 119625804 269 ILALCMGNHELYMRRRK 285
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1-195 4.67e-57

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: 189.81  E-value: 4.67e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804     1 MDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQD-TKGFSTWLKLNKKVTAQDVRKEsPLLFKFRAKFYPEDV 78
Cdd:smart00295   7 LDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKFYPPDP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804    79 sEELIQDITQ-RLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVH-KSGYLAGDKLLPQRVLEQhkLNKDQ 156
Cdd:smart00295  86 -NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS--RKLKE 162

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 119625804   157 WEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 195
Cdd:smart00295 163 WRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 1-76 2.37e-50

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: 168.03  E-value: 2.37e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   1 MDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPE 76
Cdd:cd17187    8 MDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKFYPE 83
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 491-566 6.67e-35

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: 125.78  E-value: 6.67e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804  491 DRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM 566
Cdd:pfam00769   2 LEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 77-195 1.26e-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: 126.61  E-value: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   77 DVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVleQHKLNKDQ 156
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQL--LRKMKSKE 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 119625804  157 WEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 195
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
199-284 2.15e-32

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 119.28  E-value: 2.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  199 NKKGSELWLGVDALGLNIYEQNDRLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILALCMGNH 277
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 119625804  278 ELYMRRR 284
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 336-445 3.73e-21

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: 88.82  E-value: 3.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 415
Cdd:pfam20492  11 LEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQE 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 119625804  416 RISQLEMARQKKESEAVEWQQKAQMVQEDL 445
Cdd:pfam20492  91 EIARLEEEVERKEEEARRLQEELEEAREEE 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-523 9.05e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 9.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 369
Cdd:COG1196  261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 370 RAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 449
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119625804 450 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARD 523
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-505 1.85e-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: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 369
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 370 RAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 449
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804 450 AELKTAMSTpHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNE 505
Cdd:COG1196  449 EEEAELEEE-EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 336-565 1.51e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 1.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 415
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   416 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMStphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEE 495
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRERLESLERRIAAT 836

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119625804   496 ERTTE--AEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFES 565
Cdd:TIGR02168  837 ERRLEdlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
PTZ00121 PTZ00121
MAEBL; Provisional
 338-562 3.40e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKAqqeleEQTRRALELE---QERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLAlEMAELT 414
Cdd:PTZ00121 1299 EEKKKADEAKKKA-----EEAKKADEAKkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA-EAAEKK 1372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  415 ARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQ---DENGAEASADLRADAMAKD 491
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAEEAKKADEAKKK 1452

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119625804  492 RSEEERTTEAEKNERVQKHLKALTSELANAR--DESKKTANDM-IHAENMRLGRDKYKTLRQIRQGNTKQRIDE 562
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAkKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 338-536 3.01e-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: 3.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRD-------QKKTQEQLALEM 410
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkqiLRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   411 AELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADaMAK 490
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IAS 397

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 119625804   491 DRSEEERtTEAEKnERVQKHLKALTSELANARDESKKTANDMIHAE 536
Cdd:TIGR02168  398 LNNEIER-LEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 292-490 1.68e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 53.66  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 292 QQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKA---QQELEEQtrRALELEQER 368
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAalkQKQAEEA--AAKAAAAAK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 369 KRAQSEAEKLAKERQEAEEAKEALLQAsrDQKKTQEQLALEMAELTARISQLEMARQKKESEAvewqqKAQMVQEDLEKT 448
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEA--EAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA-----KKKAAAEAKKKA 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119625804 449 RAELKTAmstphvAEPAENEQDEQDENGAEASADLRADAMAK 490
Cdd:PRK09510 220 AAEAKAA------AAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 332-531 9.80e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 39.05  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  332 EKEEL-MERLKQIEEqTKKAQQELEEQTRRALELEQERKRA--QSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLAL 408
Cdd:NF012221 1570 DRQRLeQEKQQQLAA-ISGSQSQLESTDQNALETNGQAQRDaiLEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRN 1648

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  409 EMAE-LTARI-SQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAmstphVAEPAENEQD-EQDENGAEASADLR- 484
Cdd:NF012221 1649 PFAGgLLDRVqEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAG-----VAQGEQNQANaEQDIDDAKADAEKRk 1723

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 119625804  485 ADAMAKDRSEEERTTEAekNERVQKHLKALTSELANARDESKKTAND 531
Cdd:NF012221 1724 DDALAKQNEAQQAESDA--NAAANDAQSRGEQDASAAENKANQAQAD 1768
 
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 ...
 189-285 1.92e-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: 228.70  E-value: 1.92e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 189 MYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 268
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 119625804 269 ILALCMGNHELYMRRRK 285
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1-195 4.67e-57

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: 189.81  E-value: 4.67e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804     1 MDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQD-TKGFSTWLKLNKKVTAQDVRKEsPLLFKFRAKFYPEDV 78
Cdd:smart00295   7 LDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKFYPPDP 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804    79 sEELIQDITQ-RLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVH-KSGYLAGDKLLPQRVLEQhkLNKDQ 156
Cdd:smart00295  86 -NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS--RKLKE 162

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 119625804   157 WEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 195
Cdd:smart00295 163 WRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 1-76 2.37e-50

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: 168.03  E-value: 2.37e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   1 MDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPE 76
Cdd:cd17187    8 MDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKFYPE 83
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 1-76 1.96e-44

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: 152.21  E-value: 1.96e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   1 MDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPE 76
Cdd:cd17237    9 MDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPE 84
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 1-76 1.89e-43

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: 149.37  E-value: 1.89e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   1 MDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPE 76
Cdd:cd17239   10 MDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPE 85
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 1-76 8.30e-41

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: 142.18  E-value: 8.30e-41
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   1 MDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPE 76
Cdd:cd17238    8 MDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPE 83
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 1-76 2.56e-36

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: 130.09  E-value: 2.56e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   1 MDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPE 76
Cdd:cd17097    8 MDAELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVAWLKPDKKVLTQDVSKNNTLKFFFLVKFYPE 83
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 491-566 6.67e-35

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: 125.78  E-value: 6.67e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804  491 DRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM 566
Cdd:pfam00769   2 LEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 77-195 1.26e-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: 126.61  E-value: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   77 DVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVleQHKLNKDQ 156
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQL--LRKMKSKE 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 119625804  157 WEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 195
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 1-76 1.63e-33

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: 122.49  E-value: 1.63e-33
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   1 MDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPE 76
Cdd:cd17186   10 MDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDSKGTVAWLKMDKKVLDQDVPKEEPVTFHFLAKFYPE 85
FERM_C pfam09380
FERM C-terminal PH-like domain;
199-284 2.15e-32

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 119.28  E-value: 2.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  199 NKKGSELWLGVDALGLNIYEQNDRLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILALCMGNH 277
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 119625804  278 ELYMRRR 284
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 ...
 87-187 3.06e-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: 111.18  E-value: 3.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  87 TQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLnkDQWEERIQVWHE 166
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKP--EEWEKRIVELHK 78

                         90       100
                 ....*....|....*....|.
gi 119625804 167 EHRGMLREDAVLEYLKIAQDL 187
Cdd:cd14473   79 KLRGLSPAEAKLKYLKIARKL 99
RA_FERM_F0_F1_like cd01768
Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 ...
 2-71 2.81e-26

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: 103.40  E-value: 2.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLR-----------EVWFFGLQYQDTK-------------GFSTWLKLNKKVTAQ 57
Cdd:cd01768   13 ANYKSVLATARSTARELVAEALERYGLAgspgggpgessCVDAFALCDALGRpaaagvgsgewraEHLRVLGDSERPLLV 92

                         90
                 ....*....|....*...
gi 119625804  58 ----DVRKESPLLFKFRA 71
Cdd:cd01768   93 qelwRARPGWARRFELRG 110
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 336-445 3.73e-21

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: 88.82  E-value: 3.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 415
Cdd:pfam20492  11 LEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQE 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 119625804  416 RISQLEMARQKKESEAVEWQQKAQMVQEDL 445
Cdd:pfam20492  91 EIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 191-281 2.36e-19

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: 82.81  E-value: 2.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 191 GVNYFSIKNK--KGSELWLGVDALGLNIYEQNDRlTPKIGFPWSEIRNISFN-DKKFVIKPIDKKAPDFVFYAPRLRINK 267
Cdd:cd00836    1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEDKQSKLLFQTPSRQAK 79

                         90
                 ....*....|....
gi 119625804 268 RILALCMGNHELYM 281
Cdd:cd00836   80 EIWKLIVGYHRFLL 93
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 2-73 3.45e-18

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: 79.17  E-value: 3.45e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKF 73
Cdd:cd01765   10 GTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKHWLDLDKKISKQ-LKRSGPYQFYFRVKF 80
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 2-59 3.72e-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: 75.70  E-value: 3.72e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 119625804    2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDV 59
Cdd:pfam09379   6 GTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNGEHRWLDLSKRLSKQAP 63
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 2-77 5.29e-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: 5.29e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFYPED 77
Cdd:cd17098   10 DTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKCWLDPEKPILRQ-VKRPKDVVFKFVVKFYTPD 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-523 9.05e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 9.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 369
Cdd:COG1196  261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 370 RAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 449
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119625804 450 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARD 523
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 287-536 6.04e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.97  E-value: 6.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 287 DTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQ 366
Cdd:COG1196  223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 367 ERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLE 446
Cdd:COG1196  303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 447 KTRAELKTAMstphvAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESK 526
Cdd:COG1196  383 ELAEELLEAL-----RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        250
                 ....*....|
gi 119625804 527 KTANDMIHAE 536
Cdd:COG1196  458 EEALLELLAE 467
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 191-285 1.54e-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: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 191 GVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPID-KKAPD-------------F 256
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDpRRNSHrsrrtfqsssvsvH 80

                         90       100
                 ....*....|....*....|....*....
gi 119625804 257 VFYAPRLRINKRILALCMGNHELYMRRRK 285
Cdd:cd13191   81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQ 109
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 195-286 5.75e-13

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: 65.04  E-value: 5.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 195 FSIKNKKGSELWLGVDALGLNIYE-QNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALC 273
Cdd:cd13187    8 YREKKSSTLSLWLGICSRGIIIYEeKNGARTPVLRFPWRETQKISFDKKKFTIESRGGSGIKHTFYTDSYKKSQYLLQLC 87

                         90
                 ....*....|....*
gi 119625804 274 MGNHE--LYMRRRKP 286
Cdd:cd13187   88 SAQHKfhIQMRSRQS 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-505 1.85e-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: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 369
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 370 RAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 449
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804 450 AELKTAMSTpHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNE 505
Cdd:COG1196  449 EEEAELEEE-EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 282-519 1.47e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 282 RRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRA 361
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 362 LELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMV 441
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119625804 442 QEDLEKTRAELKTAmstphvaepAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELA 519
Cdd:COG1196  462 LELLAELLEEAALL---------EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 4-74 4.79e-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: 58.79  E-value: 4.79e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625804   4 ELEFaiQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFY 74
Cdd:cd17102   15 CCEF--KKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQRHWLDPNKSIYKQ-LKGVPPYVLCFRVKFY 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 297-536 4.88e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 4.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 297 QAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEqtkkaqqELEEQTRRALELEQERKRAQSEAE 376
Cdd:COG1196  219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELELEEAQAEEY 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 377 KLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAM 456
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 457 STPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAE 536
Cdd:COG1196  372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 295-519 8.92e-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: 8.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 295 KAQAREEKHQKQMERAmLENEKKKREMAEKEKEKIERekeeLMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSE 374
Cdd:COG1196  285 EAQAEEYELLAELARL-EQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 375 AEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKT 454
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119625804 455 AmstphvaepAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELA 519
Cdd:COG1196  440 E---------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 198-282 2.28e-10

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: 57.70  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 198 KNKK--GSELWLGVDALGLNIYEQNDRLTPKIG-FPWSEIRNISFNDKKFVIKPiDKKAPDFVFYAPRLRINKRILALCM 274
Cdd:cd13185   12 KSKKetPGSVLLGITAKGIQIYQESDGEQQLLRtFPWSNIGKLSFDRKKFEIRP-EGSLRKLTYYTSSDEKSKYLLALCR 90


                 ....*...
gi 119625804 275 GNHELYMR 282
Cdd:cd13185   91 ETHQFSMA 98
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 176-253 2.78e-10

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: 57.40  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 176 AVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTpkiGFPWSEIRNISFNDKKF---VIKPIDKK 252
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFilhVMQKEEKK 77


                 .
gi 119625804 253 A 253
Cdd:cd13192   78 H 78
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 2-74 3.79e-10

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: 56.20  E-value: 3.79e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFY 74
Cdd:cd17108   10 GTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQHWLDPTKKIKKQ-VKIGPPYTLRFRVKFY 81
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 2-78 4.02e-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: 56.43  E-value: 4.02e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKES-PLLFKFRAKFYPEDV 78
Cdd:cd17200   12 DRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNWLQLDHRVLDHDLPKKSgPVTLYFAVRFYIESI 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 336-565 1.51e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 1.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 415
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   416 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMStphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEE 495
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRERLESLERRIAAT 836

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119625804   496 ERTTE--AEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFES 565
Cdd:TIGR02168  837 ERRLEdlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 2-74 2.56e-09

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: 54.20  E-value: 2.56e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFY 74
Cdd:cd17104   10 SVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERLWLNLRNRISRQ-LPGPPPYRLRLRVKFF 81
PTZ00121 PTZ00121
MAEBL; Provisional
 338-562 3.40e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKAqqeleEQTRRALELE---QERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLAlEMAELT 414
Cdd:PTZ00121 1299 EEKKKADEAKKKA-----EEAKKADEAKkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA-EAAEKK 1372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  415 ARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQ---DENGAEASADLRADAMAKD 491
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAEEAKKADEAKKK 1452

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119625804  492 RSEEERTTEAEKNERVQKHLKALTSELANAR--DESKKTANDM-IHAENMRLGRDKYKTLRQIRQGNTKQRIDE 562
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAkKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 183-247 6.05e-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: 54.27  E-value: 6.05e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119625804 183 IAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTpkiGFPWSEIRNISFNDKKFVIK 247
Cdd:cd13193    2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 4-76 7.41e-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: 53.33  E-value: 7.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   4 ELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFsTWLKLNKKVT----------AQDVRKESPLLFK--FRA 71
Cdd:cd17101   13 RLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAVLKDGEY-FFLDPDTKLSkyapkgwkseAKKGLKGGKPVFTlyFRV 91


                 ....*
gi 119625804  72 KFYPE 76
Cdd:cd17101   92 KFYVD 96
PTZ00121 PTZ00121
MAEBL; Provisional
 295-562 9.66e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 9.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  295 KAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSE 374
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  375 AEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAvewQQKAQMVQEDLEKTRAELKT 454
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---KIKAEELKKAEEEKKKVEQL 1638

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  455 AMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKnERVQKHLKALTSELANARDESKKTANDMIH 534
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-KKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717

                         250       260
                  ....*....|....*....|....*...
gi 119625804  535 AENMRlgrdKYKTLRQIRQGNTKQRIDE 562
Cdd:PTZ00121 1718 AEELK----KAEEENKIKAEEAKKEAEE 1741
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 2-78 1.10e-08

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: 52.67  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRK---ESPLLFKFRAKFYPEDV 78
Cdd:cd17103   12 DRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDETGHYNWLQLDKRVLDHEFPKkwsSGPLVLHFAVKFYVESI 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 290-542 1.15e-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: 58.14  E-value: 1.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   290 EVQQMKAQAREekhqKQMERAMLENEKKK-REMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQER 368
Cdd:TIGR02168  685 KIEELEEKIAE----LEKALAELRKELEElEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   369 KRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLAL----------EMAELTARISQLEMARQKKESEAVEWQQKA 438
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdelraELTLLNEEAANLRERLESLERRIAATERRL 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   439 QMVQEDLEKTRAELktamstphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSEL 518
Cdd:TIGR02168  841 EDLEEQIEELSEDI----------ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250       260
                   ....*....|....*....|....
gi 119625804   519 ANARDESKKtANDMIHAENMRLGR 542
Cdd:TIGR02168  911 SELRRELEE-LREKLAQLELRLEG 933
PTZ00121 PTZ00121
MAEBL; Provisional
 295-536 1.67e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  295 KAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQ--ELEEQTRRALELE---QERK 369
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakKKAEEAKKADEAKkkaEEAK 1496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  370 RAQSEAEKLAKERQEAEEAKEAllqasRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 449
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKA-----EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK 1571

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  450 AELKTAMST--PHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELAnardESKK 527
Cdd:PTZ00121 1572 AEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA----EEKK 1647


                  ....*....
gi 119625804  528 TANDMIHAE 536
Cdd:PTZ00121 1648 KAEELKKAE 1656
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 2-78 2.93e-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: 51.50  E-value: 2.93e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKES-PLLFKFRAKFYPEDV 78
Cdd:cd17199   12 DRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHDFPKKSgPVVLYFCVRFYIESI 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 338-536 3.01e-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: 3.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRD-------QKKTQEQLALEM 410
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkqiLRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   411 AELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADaMAK 490
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IAS 397

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 119625804   491 DRSEEERtTEAEKnERVQKHLKALTSELANARDESKKTANDMIHAE 536
Cdd:TIGR02168  398 LNNEIER-LEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 189-246 3.60e-08

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: 51.16  E-value: 3.60e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119625804 189 MYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPkigFPWSEIRNISFNDKKFVI 246
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINT---FPWSKIVKISFKRKQFFI 55
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 3-77 4.53e-08

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: 50.65  E-value: 4.53e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119625804   3 AELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAKFYPED 77
Cdd:cd17201   12 SEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKNWLDPSKEIKKQ--IRSGPWHFAFTVKFYPPD 84
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 2-77 5.90e-08

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: 50.18  E-value: 5.90e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFYPED 77
Cdd:cd17190   10 NTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWIWLEPMKLIVKQ-VRRPKNTKLRLAVKFFPPD 84
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 5-74 7.84e-08

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: 49.92  E-value: 7.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119625804   5 LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQ-DVRKESPLLFkFRAKFY 74
Cdd:cd17099   16 LECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQlDKHAHEPLLY-FGVMFY 85
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 2-74 1.22e-07

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: 49.23  E-value: 1.22e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFST---WLKLNKKVTAQdVRKESPLLFKFRAKFY 74
Cdd:cd17100   11 DTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPATDsmrWLDPLKPIRKQ-IKGGPPYYLNFRVKFY 85
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 9-77 1.39e-07

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: 49.20  E-value: 1.39e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119625804   9 IQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAKFYPED 77
Cdd:cd17202   18 LEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSANQKNWLDSTKEIKRQ--IRRLPWLFTFNVKFYPPD 84
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 2-77 1.55e-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: 1.55e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFYPED 77
Cdd:cd17188   11 DSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNVWLELLKPITKQ-IKNPKELIFKFTVKFFPVD 85
PTZ00121 PTZ00121
MAEBL; Provisional
 283-546 1.56e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  283 RRKPDTIEVQQMKAQAREEKHQKQMERA-MLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRA 361
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  362 LELEQERKRAQSEAEKLAKERQEAEEAK----------EALLQASRDQKKTQE--------QLALEMAELTARISQLEMA 423
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKkkaeekkkadEAKKKAEEDKKKADElkkaaaakKKADEAKKKAEEKKKADEA 1436

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  424 RQKKES--EAVEWQQKAQMVQ--EDLEKTRAELKTAMSTPHVAEPAE--NEQDEQDENGAEASADLRADAMAKDRSEEER 497
Cdd:PTZ00121 1437 KKKAEEakKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 119625804  498 TT-EAEKNERVQKHLKALTSELANARDESKKtANDMIHAENMRLGRDKYK 546
Cdd:PTZ00121 1517 KAeEAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKAEELKKAEEKKK 1565
PTZ00121 PTZ00121
MAEBL; Provisional
 290-539 1.61e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQiEEQTKKAQQELEEQTRRALELEQ-ER 368
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKADELKKAEEKKKADEAKKaEE 1300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  369 KRAQSEAEKLAKERQEAEEAKeallQASRDQKKTQEQL--ALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLE 446
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAK----KKAEEAKKKADAAkkKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  447 KTRAE-LKTAMSTPHVAEPAENEQDEQDENGAEasadLRADAMAKDRSEEERTTEAEKNERVQKHLKAltsELANARDES 525
Cdd:PTZ00121 1377 KKKADaAKKKAEEKKKADEAKKKAEEDKKKADE----LKKAAAAKKKADEAKKKAEEKKKADEAKKKA---EEAKKADEA 1449

                         250
                  ....*....|....
gi 119625804  526 KKTANDMIHAENMR 539
Cdd:PTZ00121 1450 KKKAEEAKKAEEAK 1463
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 292-490 1.68e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 53.66  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 292 QQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKA---QQELEEQtrRALELEQER 368
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAalkQKQAEEA--AAKAAAAAK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 369 KRAQSEAEKLAKERQEAEEAKEALLQAsrDQKKTQEQLALEMAELTARISQLEMARQKKESEAvewqqKAQMVQEDLEKT 448
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEA--EAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA-----KKKAAAEAKKKA 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119625804 449 RAELKTAmstphvAEPAENEQDEQDENGAEASADLRADAMAK 490
Cdd:PRK09510 220 AAEAKAA------AAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
PTZ00121 PTZ00121
MAEBL; Provisional
 338-557 1.83e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKAQQ---ELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEmAELT 414
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQlkkKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-AEEA 1701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  415 ARISQLemarQKKESEAVewqQKAQMVQEDLEKTRAElktamstphvAEPAENEQDEQDENGAEAsadlRADAMAKDRSE 494
Cdd:PTZ00121 1702 KKAEEL----KKKEAEEK---KKAEELKKAEEENKIK----------AEEAKKEAEEDKKKAEEA----KKDEEEKKKIA 1760

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119625804  495 EERTTEAEKNERVQKHLKALTSELANARDESKKTANDmihaenmRLGRDKYKTLRQIRQGNTK 557
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-------KKIKDIFDNFANIIEGGKE 1816
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 2-77 2.77e-07

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: 48.26  E-value: 2.77e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFYPED 77
Cdd:cd17189   10 DTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMVWLDLLKPIVKQ-IRRPKHVVLRFVVKFFPPD 84
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 338-525 3.14e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.89  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQS------EAEKLAKERQ-EAEEAKEALLQASR---DQKKTQEQLA 407
Cdd:PRK09510  80 QRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEqkkqaeEAAKQAALKQkQAEEAAAKAAAAAKakaEAEAKRAAAA 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 408 LEMAELTARISQLEMARQKKESEAvewqqKAQMVQEDLEKTRAELKtamstphvaEPAENEQDEQdengAEASADLRADA 487
Cdd:PRK09510 160 AKKAAAEAKKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAK---------KKAEAEAKKK----AAAEAKKKAAA 221

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119625804 488 MAKDRSEEErttEAEKNERVQKHLKALTSELANARDES 525
Cdd:PRK09510 222 EAKAAAAKA---AAEAKAAAEKAAAAKAAEKAAAAKAA 256
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 13-77 3.87e-07

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: 48.11  E-value: 3.87e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119625804  13 TTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPED 77
Cdd:cd17107   27 SKGSVVLDVVFQHLNLLETDYFGLRYIDRQHQTHWLDPAKTLSEQLKLIGPPYTLYFGVKFYAED 91
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-524 4.43e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKAQQELEEQTRRALELE--QERKRAQSEAEKLAKERQEAEEAKEALLQASRDqkktqeqlaleMAELTA 415
Cdd:COG4913   624 EELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSDD-----------LAALEE 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  416 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAmstphvaepaeneQDEQDENGAEASADLRADAMAKDRSEE 495
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL-------------QDRLEAAEDLARLELRALLEERFAAAL 759

                         170       180
                  ....*....|....*....|....*....
gi 119625804  496 ERTTEAEKNERVQKHLKALTSELANARDE 524
Cdd:COG4913   760 GDAVERELRENLEERIDALRARLNRAEEE 788
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 283-486 4.45e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 4.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   283 RRKPDTIEVQQMKAQAREEKHQKQMERAMLE--NEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRR 360
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKEltELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   361 ALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQM 440
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 119625804   441 VQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRAD 486
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
PTZ00121 PTZ00121
MAEBL; Provisional
 290-562 5.06e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 369
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  370 RAQSEAEKlAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 449
Cdd:PTZ00121 1278 RKADELKK-AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  450 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEE--RTTEAEKNERVQKHLKALTSELANAR--DES 525
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkKADELKKAAAAKKKADEAKKKAEEKKkaDEA 1436

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 119625804  526 KKTANDMIHAENM-RLGRDKYKTLRQIRQGNTKQRIDE 562
Cdd:PTZ00121 1437 KKKAEEAKKADEAkKKAEEAKKAEEAKKKAEEAKKADE 1474
PTZ00121 PTZ00121
MAEBL; Provisional
 290-564 5.10e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 5.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQEL---EEQTRRALELEQ 366
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkaAAAKKKADEAKK 1425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  367 --ERKRAQSEAEKLAKERQEAEEAKeallqasrdqKKTQEQLALEMAEltarisqlEMARQKKESEAVEWQQKAQMVQED 444
Cdd:PTZ00121 1426 kaEEKKKADEAKKKAEEAKKADEAK----------KKAEEAKKAEEAK--------KKAEEAKKADEAKKKAEEAKKADE 1487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  445 LEKTRAELKTAMSTPHVAEPAENEQDEqdengAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDE 524
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADE-----AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 119625804  525 SKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFE 564
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 12-74 5.15e-07

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: 47.51  E-value: 5.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119625804  12 NTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFY 74
Cdd:cd17204   20 HAKGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAHWLDHTKPIKKQ-IKIGPPYTLHFRIKYY 81
PTZ00121 PTZ00121
MAEBL; Provisional
 283-536 6.21e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  283 RRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIER-EKEELMERLKQIEEQTKKAQQEL---EEQT 358
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAkkaAEAK 1509

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  359 RRALELEQERKRAQSEAEKLAKERQEAEEAKEAllqasRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKA 438
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKA-----EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  439 QMVQedLEKTRAELKTAMSTPHVAEPAENEQDEQDENGA----EASADLRADAMAKDRSEEERTTEAEKNERVQKHLKAL 514
Cdd:PTZ00121 1585 EAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662

                         250       260
                  ....*....|....*....|..
gi 119625804  515 TSELANARDESKKTANDMIHAE 536
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAE 1684
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 337-526 7.76e-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: 7.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   337 MERLKQIEEQTKKAQQELEEQTRRALELeQERKRAQSEAEK--LAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELT 414
Cdd:TIGR02168  188 LDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   415 ARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELktamstphvaEPAENEQDEQDENGAEASADLRADAMAKDRSE 494
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK----------QILRERLANLERQLEELEAQLEELESKLDELA 336

                          170       180       190
                   ....*....|....*....|....*....|..
gi 119625804   495 EERTTEAEKNERVQKHLKALTSELANARDESK 526
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELE 368
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 283-513 8.07e-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: 51.88  E-value: 8.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  283 RRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQE---LEEQTR 359
Cdd:pfam15709 296 RSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEqleRAEKMR 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  360 RALELEQERKraqSEAEKLAKERQEAEEAKeallqasRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQ 439
Cdd:pfam15709 376 EELELEQQRR---FEEIRLRKQRLEEERQR-------QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAE 445

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119625804  440 MVQEDLEKTRA-ELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKA 513
Cdd:pfam15709 446 RAEAEKQRQKElEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
PTZ00121 PTZ00121
MAEBL; Provisional
 338-562 1.00e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKA---QQELEEQTRRALELEQERKRAQSEAEKlAKERQEAEEAK--EALLQASRDQKKTQEQLALEMAE 412
Cdd:PTZ00121 1319 EAKKKAEEAKKKAdaaKKKAEEAKKAAEAAKAEAEAAADEAEA-AEEKAEAAEKKkeEAKKKADAAKKKAEEKKKADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  413 LTARisqlemaRQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEpaenEQDEQDENGAEASADLRADAMAKDR 492
Cdd:PTZ00121 1398 KKAE-------EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE----EAKKADEAKKKAEEAKKAEEAKKKA 1466

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119625804  493 SEEERTTEAEKN---ERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTlRQIRQGNTKQRIDE 562
Cdd:PTZ00121 1467 EEAKKADEAKKKaeeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA-DEAKKAEEAKKADE 1538
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 190-282 1.32e-06

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: 46.51  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 190 YGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKigFPWSEIRNISFNDKKFVIKPIDKKAPdFVFYAPRLRINKRI 269
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVF--FRWEDIKNVINHKRTFSIECQNSEET-VQFQFEDAETAKYV 77

                         90
                 ....*....|...
gi 119625804 270 LALCMGNHELYMR 282
Cdd:cd13188   78 WKLCVLQHKFYRQ 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-504 1.37e-06

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: 51.60  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   276 NHELYMRRRKPDTIEVQQMKAQAREEKHQKQMER--AMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQE 353
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEEleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   354 LEEQTRRALELEQERKRAQSEAEKLakERQEAEEAKEalLQASRDQKktqEQLALEMAELTARISQLEMARQKKESEAVE 433
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQL--ELQIASLNNE--IERLEARL---ERLEDRRERLQQEIEELLKKLEEAELKELQ 439

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119625804   434 WQ-QKAQMVQEDLEKTRAELKTAMSTPHvAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKN 504
Cdd:TIGR02168  440 AElEELEEELEELQEELERLEEALEELR-EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 4-77 1.42e-06

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: 46.28  E-value: 1.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119625804   4 ELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAKFYPED 77
Cdd:cd17106   13 EYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQKNWLDPAKEIKKQ--IRSGPWLFSFNVKFYPPD 84
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 190-277 1.99e-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: 46.16  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 190 YGVNYFSIKNKKGSELWLGVDALGLNIYEqnDRLtpKIG-FPWSEIRNISFNDKKFVIK----PIDKKAPDFVFYAPRLR 264
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYR--DRL--RINrFAWPKVLKISYKRNNFYIKirpgEFEQYETTIGFKLPNHR 76

                         90
                 ....*....|...
gi 119625804 265 INKRILALCMGNH 277
Cdd:cd13184   77 AAKRLWKVCVEHH 89
PTZ00121 PTZ00121
MAEBL; Provisional
 283-552 2.52e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  283 RRKPDTIEVQQMKAQAREEKHQKQMERAmlENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRAL 362
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  363 E----LEQERKRAQSEAEKLAKERQEAEEAKEAllQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKA 438
Cdd:PTZ00121 1623 EelkkAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  439 QMVQEDLEKTRAELKtamstphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNeRVQKHLKALTSEL 518
Cdd:PTZ00121 1701 AKKAEELKKKEAEEK---------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKEEEKKA 1770

                         250       260       270
                  ....*....|....*....|....*....|....
gi 119625804  519 ANARDESKKTANDMIHAENMRLGRDKYKTLRQIR 552
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 336-530 2.64e-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: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKE----RQEAEEAKEALLQASRDQKKTQEQL-ALEM 410
Cdd:COG3883   28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARALYRSGGSVsYLDV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 411 -------AELTARISQLE---------MARQKKESEAVEWQQ-KAQMVQEDLEKTRAELKTAMSTphvaepAENEQDEQD 473
Cdd:COG3883  108 llgsesfSDFLDRLSALSkiadadadlLEELKADKAELEAKKaELEAKLAELEALKAELEAAKAE------LEAQQAEQE 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119625804 474 ENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTAN 530
Cdd:COG3883  182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 336-481 2.72e-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: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 415
Cdd:COG3883  117 FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804 416 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASA 481
Cdd:COG3883  197 QLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 290-536 3.30e-06

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: 50.06  E-value: 3.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQtrraLELEQERK 369
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL----EAELEELE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   370 RAQSEAEKLAkerqeaEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKEseavewQQKAQMVQEDLEKTR 449
Cdd:TIGR02168  365 AELEELESRL------EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE------RLQQEIEELLKKLEE 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   450 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRAdamAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTA 529
Cdd:TIGR02168  433 AELKELQAELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509


                   ....*..
gi 119625804   530 NDMIHAE 536
Cdd:TIGR02168  510 ALLKNQS 516
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 9-77 4.19e-06

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: 44.93  E-value: 4.19e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119625804   9 IQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAKFYPED 77
Cdd:cd17203   18 VEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQKNWLDPAKEIKKQ--IRSGAWQFSFNVKFYPPD 84
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 2-77 4.83e-06

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: 44.80  E-value: 4.83e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAKFYPED 77
Cdd:cd17105   10 DTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKTWLDPAKEIKKQ--VHGGPWEFTFNVKFYPPD 83
PTZ00121 PTZ00121
MAEBL; Provisional
 338-562 5.24e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQK--------KTQEQLALE 409
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEernneeirKFEEARMAH 1264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  410 MAELTARIsQLEMARQKKESEAVEWQQKAQMVQEDLEKTRA-ELKTAMSTPHVAEPAENEQDEQDENGAEA---SADLRA 485
Cdd:PTZ00121 1265 FARRQAAI-KAEEARKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAkkkAEEAKK 1343

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119625804  486 DAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENM--RLGRDKYKTLRQIRQGNTKQRIDE 562
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkKAEEDKKKADELKKAAAAKKKADE 1422
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 15-77 5.79e-06

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: 44.65  E-value: 5.79e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119625804  15 GKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFYPED 77
Cdd:cd17205   25 GQELFEQIMYHLDLIEKDYFGLRFMDSAQVAHWLDVTKSIKKQ-VKIGPPYCLHLRVKFYSSE 86
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 304-539 7.77e-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: 48.97  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  304 QKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLkQIEEQTK--KAQQELEEQTRRALELEQERKRAQSEAEKLAKE 381
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISRMRELERL-QMERQQKneRVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  382 RQEAEEAKEallqasRDQKKTQEQLALEMAeltaRISQLEMARQK-----KESEAVEWQQKAQMVQEDLEKTRAELKTAM 456
Cdd:pfam17380 426 RAEQEEARQ------REVRRLEEERAREME----RVRLEEQERQQqverlRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  457 STPHVAEPAENE--QDEQDENGAEASADLRADAMAKD----RSEEERTTEAEKNER--VQKHLKALTSELA--NARDESK 526
Cdd:pfam17380 496 ILEKELEERKQAmiEEERKRKLLEKEMEERQKAIYEEerrrEAEEERRKQQEMEERrrIQEQMRKATEERSrlEAMERER 575

                         250
                  ....*....|...
gi 119625804  527 KTANDMIHAENMR 539
Cdd:pfam17380 576 EMMRQIVESEKAR 588
PTZ00121 PTZ00121
MAEBL; Provisional
 285-565 9.05e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  285 KPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALEL 364
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  365 EQERKRAQSEAEKLAKERQEAEEAKEAllqasRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQED 444
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKA-----EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  445 LEKT-RAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKdRSEEERTTEAEKNERVQK--HLKALTSELANA 521
Cdd:PTZ00121 1239 AEEAkKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKadEAKKKAEEAKKA 1317

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 119625804  522 RDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFES 565
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
340-522 9.12e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 9.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 340 LKQIEEQtKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEmAELTARISQ 419
Cdd:COG4717   70 LKELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPER 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 420 LEMARQKKEsEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTT 499
Cdd:COG4717  148 LEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226

                        170       180
                 ....*....|....*....|...
gi 119625804 500 EAEKNERVQKHLKALTSELANAR 522
Cdd:COG4717  227 EELEQLENELEAAALEERLKEAR 249
PTZ00121 PTZ00121
MAEBL; Provisional
 278-559 9.53e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  278 ELYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEkierekeelmERLKQIEEQTKKAQQ--ELE 355
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA----------DELKKAAAAKKKADEakKKA 1427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  356 EQTRRALELEQ--ERKRAQSEAEKLAKERQEAEEAK---EALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESE 430
Cdd:PTZ00121 1428 EEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  431 AvewQQKAQMVQEDLEKTRA-ELKTAMSTPHVAEPAENEQDEQDENGAEAS----ADLRADAMAKDRSEEERTTEAEKNE 505
Cdd:PTZ00121 1508 A---KKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKADELKKAEelkkAEEKKKAEEAKKAEEDKNMALRKAE 1584

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119625804  506 --------RVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQR 559
Cdd:PTZ00121 1585 eakkaeeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 279-443 9.97e-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: 48.58  E-value: 9.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  279 LYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQT 358
Cdd:pfam17380 383 LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  359 RRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQA---SRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQ 435
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeleERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER 542


                  ....*...
gi 119625804  436 QKAQMVQE 443
Cdd:pfam17380 543 RKQQEMEE 550
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 267-468 1.28e-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: 48.14  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   267 KRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQ 346
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   347 TKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQK 426
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 119625804   427 KESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENE 468
Cdd:TIGR02169  467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 281-430 2.04e-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: 47.43  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  281 MRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELM-----ERLKQIEEQTKKA-QQEL 354
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLElekekRDRKRAEEQRRKIlEKEL 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  355 EEQTRRALELEQERKRAQSEAEKLAK------ERQEAEEAKEALlQASRDQKKTQEQLAL---EMAELTARISQLEMARQ 425
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEERQKaiyeeeRRREAEEERRKQ-QEMEERRRIQEQMRKateERSRLEAMEREREMMRQ 580


                  ....*
gi 119625804  426 KKESE 430
Cdd:pfam17380 581 IVESE 585
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 194-273 2.08e-05

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: 43.16  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 194 YFSIKNKKGSELWLGVDALGLNIYEQNDRlTPKIGFPWSEIRNISFND-----KKFVIKPIDkKAPDFVFYAPRLRINKR 268
Cdd:cd00900    7 RVYREPTKRVEGTLYITSDRLILRDKNDG-GLELSIPISDIVNVNVSPqgpssRYLVLVLKD-RGEFVGFSFPKEEDAIE 84


                 ....*
gi 119625804 269 ILALC 273
Cdd:cd00900   85 ISDAL 89
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 338-482 2.45e-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: 46.76  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQtKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAkEALLQASRDQKKTQEQLALEMAELTARI 417
Cdd:TIGR02794  89 ARQKELEQR-AAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA-EAERKAKEEAAKQAEEEAKAKAAAEAKK 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119625804  418 SQLEmARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASAD 482
Cdd:TIGR02794 167 KAEE-AKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKAD 230
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
338-509 2.83e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.79  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 338 ERLKQIEEQTKKAQQELEE-QTRRALELEqERKRAQSEAE---KLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAEL 413
Cdd:COG2268  207 EAERETEIAIAQANREAEEaELEQEREIE-TARIAEAEAElakKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEI 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 414 TARISQLEMARQKKEsEAVEWQQKAQMVQEDLEKTRAELKtamstphvaepAENEQDEQDENG-AEASA-DLRADAMAKD 491
Cdd:COG2268  286 AEREREIELQEKEAE-REEAELEADVRKPAEAEKQAAEAE-----------AEAEAEAIRAKGlAEAEGkRALAEAWNKL 353

                        170
                 ....*....|....*...
gi 119625804 492 RSEEERTTEAEKNERVQK 509
Cdd:COG2268  354 GDAAILLMLIEKLPEIAE 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 348-565 3.02e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 348 KKAQQELEEqTRRAL--------ELEQERKRAQSEAEKLAKERQEAEEAKEALLQAS----RDQKKTQEQLALEMAELTA 415
Cdd:COG1196  175 EEAERKLEA-TEENLerledilgELERQLEPLERQAEKAERYRELKEELKELEAELLllklRELEAELEELEAELEELEA 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 416 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTphvAEPAENEQDEQDENGAEASADLRADAMAKDRSEE 495
Cdd:COG1196  254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEE 330

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 496 ERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFES 565
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 7-74 4.46e-05

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: 42.21  E-value: 4.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119625804   7 FAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFST-WLKLNKKVTAQdVRKESPLLFKFRAKFY 74
Cdd:cd17194   16 FKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDSTDNPrWLDPNKPIRKQ-LKRGSPHNLNFRVKFF 83
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
353-523 4.82e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 353 ELEEQTRRALELEQERKRAQSEAE------KLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAE-LTARISQLEMARQ 425
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGlddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAEsLREDADDLEERAE 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 426 KKESEAVEWQQKAQMVQEDLEKTRAELKtamstphvaepaenEQDEQDENGAEASADLRADamaKDRSEEERTTEAEKNE 505
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIE--------------ELEEEIEELRERFGDAPVD---LGNAEDFLEELREERD 422

                        170
                 ....*....|....*...
gi 119625804 506 RVQKHLKALTSELANARD 523
Cdd:PRK02224 423 ELREREAELEATLRTARE 440
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 290-519 5.55e-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: 46.21  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   290 EVQQMkaQAREEKHQKQMERAM--LENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQE 367
Cdd:TIGR02169  675 ELQRL--RERLEGLKRELSSLQseLRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   368 RKRAQSEAEKLAKERQEAEEAKEALLQA-------------------SRDQKKTQEQLALEMAELTARIS-------QLE 421
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEAlndlearlshsripeiqaeLSKLEEEVSRIEARLREIEQKLNrltlekeYLE 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   422 MARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEA 501
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912

                          250
                   ....*....|....*...
gi 119625804   502 EKNERVQKHLKALTSELA 519
Cdd:TIGR02169  913 EKKRKRLSELKAKLEALE 930
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 338-497 6.92e-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: 45.22  E-value: 6.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKA--QQELEEQTRRALELEQERKRAQSEAEKLAKERQEAE-EAKEALLQASRDQKKTQEQLALEMAELT 414
Cdd:TIGR02794  68 ERQKKLEQQAEEAekQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQkQAEEAKAKQAAEAKAKAEAEAERKAKEE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  415 ARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDengAEASADLRADAMAKDRSE 494
Cdd:TIGR02794 148 AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAA---AEAAAKAEAEAAAAAAAE 224


                  ...
gi 119625804  495 EER 497
Cdd:TIGR02794 225 AER 227
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 352-463 7.61e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.84  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 352 QELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQlalEMAELTARISQLEMARQKKESEA 431
Cdd:COG0542  411 EELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWE---AEKELIEEIQELKEELEQRYGKI 487

                         90       100       110
                 ....*....|....*....|....*....|..
gi 119625804 432 VEWQQKAQMVQEDLEKTRAELKTAMSTPHVAE 463
Cdd:COG0542  488 PELEKELAELEEELAELAPLLREEVTEEDIAE 519
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 341-452 7.96e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 45.82  E-value: 7.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  341 KQIEEQTKKAQQELEEQTRralELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRD-QKKTQEQLALEMAELTARisQ 419
Cdd:PRK10929  105 DALEQEILQVSSQLLEKSR---QAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRlQTLGTPNTPLAQAQLTAL--Q 179

                          90       100       110
                  ....*....|....*....|....*....|...
gi 119625804  420 LEMARQKKESEAVEWQQKAQMVQEDLEKTRAEL 452
Cdd:PRK10929  180 AESAALKALVDELELAQLSANNRQELARLRSEL 212
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 342-531 1.00e-04

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: 44.84  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  342 QIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEAllQASRDQKKTQEQLALEMAeltarisqle 421
Cdd:TIGR02794  58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQA--EQAAKQAEEKQKQAEEAK---------- 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  422 mARQKKESEAVEWQQKAQMVQEDLEKTRAELKtamstphVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEErtTEA 501
Cdd:TIGR02794 126 -AKQAAEAKAKAEAEAERKAKEEAAKQAEEEA-------KAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE--EAK 195

                         170       180       190
                  ....*....|....*....|....*....|
gi 119625804  502 EKNERVQKHLKALTSELANARDESKKTAND 531
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
336-565 1.12e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEallqasrDQKKTQEQLALEMAELTA 415
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE-------DRREEIEELEEEIEELRE 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 416 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTphvaePAENEQDEQDENGAEASADLradamaKDRSEE 495
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER-----VEEAEALLEAGKCPECGQPV------EGSPHV 467

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 496 ERTTEAEknERVQKhlkaLTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQgNTKQRIDEFES 565
Cdd:PRK02224 468 ETIEEDR--ERVEE----LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE-DLEELIAERRE 530
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-456 1.13e-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: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 307 MERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAE 386
Cdd:COG1196  627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 387 EAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAM 456
Cdd:COG1196  707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 345-531 1.26e-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: 44.37  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 345 EQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMAR 424
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 425 QKKESEAVEWQQKAQMVQEdlektRAELKTAMSTPHVAEPAENEQDEQDENGA--EASADLRADAMAKDRSEEERTTEAE 502
Cdd:COG4942  100 EAQKEELAELLRALYRLGR-----QPPLALLLSPEDFLDAVRRLQYLKYLAPArrEQAEELRADLAELAALRAELEAERA 174

                        170       180
                 ....*....|....*....|....*....
gi 119625804 503 KNERVQKHLKALTSELANARDESKKTAND 531
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLAR 203
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 344-531 1.40e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.41  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 344 EEQTKKAQQELEEQTRRaleleQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQlalemaeltariSQLEMA 423
Cdd:PRK09510  67 QQQQQKSAKRAEEQRKK-----KEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEA------------AKQAAL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 424 RQKKESEAVEWQQKAQMVQEDLEKTRAELKTAmstpHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEK 503
Cdd:PRK09510 130 KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAK----KAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205

                        170       180
                 ....*....|....*....|....*...
gi 119625804 504 NERVQKHLKALTSELANARDESKKTAND 531
Cdd:PRK09510 206 EAKKKAAAEAKKKAAAEAKAAAAKAAAE 233
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-453 1.63e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEA-EKLAKERQEAEEAKEALLQASRDQKKTQEQLALEM------ 410
Cdd:COG4913   302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLpasaee 381

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 119625804  411 -----AELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELK 453
Cdd:COG4913   382 faalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
336-443 1.71e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQAsrdqKKTQEQLALEMAELTA 415
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL----EKELESLEGSKRKLEE 259

                         90       100
                 ....*....|....*....|....*...
gi 119625804 416 RISQLEMARQKKESEAVEWQQKAQMVQE 443
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKE 287
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 337-518 1.81e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   337 MERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTAR 416
Cdd:TIGR02169  790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   417 ISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLrADAMAKDRSEEE 496
Cdd:TIGR02169  870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPE 948

                          170       180
                   ....*....|....*....|..
gi 119625804   497 RTTEAEKnerVQKHLKALTSEL 518
Cdd:TIGR02169  949 EELSLED---VQAELQRVEEEI 967
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 304-526 1.96e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 304 QKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQ 383
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 384 EAEEAKEALLQASRDQKKTQEQLAL-------EMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAM 456
Cdd:COG4942  101 AQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 457 STphvaepAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESK 526
Cdd:COG4942  181 AE------LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
292-524 2.09e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  292 QQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERkra 371
Cdd:COG4913   249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL--- 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  372 qseaeklakerqeaEEAKEALLQASRDQKktqeqlalemAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAE 451
Cdd:COG4913   326 --------------DELEAQIRGNGGDRL----------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119625804  452 LKTAMST-PHVAEPAENEQDEQDENGAEASADLRADAmakdrsEEERTTEAEKnERVQKHLKALTSELANARDE 524
Cdd:COG4913   382 FAALRAEaAALLEALEEELEALEEALAEAEAALRDLR------RELRELEAEI-ASLERRKSNIPARLLALRDA 448
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 340-513 2.56e-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: 42.74  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  340 LKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEA------EEAKEALLQASRDQK-----KTQEQLAL 408
Cdd:pfam04012  31 IRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAltkgneELAREALAEKKSLEKqaealETQLAQQR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  409 EMAE-LTARISQLEMARQKKESE--AVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRA 485
Cdd:pfam04012 111 SAVEqLRKQLAALETKIQQLKAKknLLKARLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASAV 190

                         170       180
                  ....*....|....*....|....*...
gi 119625804  486 DAMAKDRSEEErttEAEKNERVQKHLKA 513
Cdd:pfam04012 191 DLDAKLEQAGI---QMEVSEDVLARLKA 215
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 292-492 2.75e-04

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: 43.30  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  292 QQMKAQAREEKHQKQMERAmLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQtrralelEQERKRA 371
Cdd:TIGR02794  79 EAEKQRAAEQARQKELEQR-AAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERK-------AKEEAAK 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  372 QSEAEKLAKERQEAE-EAKEALLQASRDQKKTQEqlALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR- 449
Cdd:TIGR02794 151 QAEEEAKAKAAAEAKkKAEEAKKKAEAEAKAKAE--AEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERk 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 119625804  450 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDR 492
Cdd:TIGR02794 229 ADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
PTZ00121 PTZ00121
MAEBL; Provisional
 292-517 3.06e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  292 QQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREkeelmERLKQIEEQTKKAQQELEEQTRRALELEQERKRA 371
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-----EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  372 QSEAEKLAKERQEAEE----AKEALLQASRDQKKTQEQLALEmaELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEK 447
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  448 TRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSE 517
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNE 1859
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 284-506 3.87e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   284 RKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALE 363
Cdd:TIGR02169  786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   364 LEQERKRAQ-------SEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQL--EMARQKKESEAVEW 434
Cdd:TIGR02169  866 LEEELEELEaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALeeELSEIEDPKGEDEE 945

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119625804   435 QQKAQMVQEDLEKTRAELKTAMSTphvAEPAENEQDEQDENGAEASADL---RADAMAKDRSEEERTTEAEKNER 506
Cdd:TIGR02169  946 IPEEELSLEDVQAELQRVEEEIRA---LEPVNMLAIQEYEEVLKRLDELkekRAKLEEERKAILERIEEYEKKKR 1017
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 2-70 4.06e-04

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: 38.84  E-value: 4.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119625804   2 DAELEFAIQPNTTGKQLFDQVVKTIGLREvWFFGLQYQDtkgfsTWLKLNKkvTAQDVRKESPLLFKFR 70
Cdd:cd00196    8 LKKIVVAVPPSTTLRQVLEKVAKRIGLPP-DVIRLLFNG-----QVLDDLM--TAKQVGLEPGEELHFV 68
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
336-433 4.40e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKE----ALLQASRDQKKTQEQLALEMA 411
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelrALLEERFAAALGDAVERELRE 769

                          90       100
                  ....*....|....*....|..
gi 119625804  412 ELTARISQLEMARQKKESEAVE 433
Cdd:COG4913   770 NLEERIDALRARLNRAEEELER 791
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 338-443 4.92e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.89  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKER-QEAEEAKEALLQASRDQKKtQEQLALEMAELTAR 416
Cdd:PRK00409 534 QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAiKEAKKEADEIIKELRQLQK-GGYASVKAHELIEA 612

                         90       100
                 ....*....|....*....|....*..
gi 119625804 417 ISQLEMARQKKESEAVEWQQKAQMVQE 443
Cdd:PRK00409 613 RKRLNKANEKKEKKKKKQKEKQEELKV 639
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
338-537 5.40e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQ---SEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELT 414
Cdd:PRK02224 220 EEIERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 415 A--------------RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTphvAEPAENEQDEQDENGAEAS 480
Cdd:PRK02224 300 AeaglddadaeaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER---AEELREEAAELESELEEAR 376

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119625804 481 ADLRADAMAKDRSEEERTTEAEK-------NERVQKHLKALTSELANARDESKKTANDMIHAEN 537
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELREREAELEATLRTARE 440
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 295-529 5.71e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 42.63  E-value: 5.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 295 KAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQieeqtKKAQQELEEQTRRALELEQERKRAQSE 374
Cdd:PRK05035 450 EAKARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKA-----KKAAATQPIVIKAGARPDNSAVIAARE 524

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 375 AEKLAKeRQEAEEAKEAllqASRDQKKTQEQLALEMAeltarisQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKT 454
Cdd:PRK05035 525 ARKAQA-RARQAEKQAA---AAADPKKAAVAAAIARA-------KAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKK 593

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119625804 455 AMSTPHVAEPAENEQDEQDENGAEASADLRADA--MAKDRSEEERTTEAEKNERVQKhlkaltselANARDESKKTA 529
Cdd:PRK05035 594 AAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAkkAEQQANAEPEEPVDPRKAAVAA---------AIARAKARKAA 661
PRK12704 PRK12704
phosphodiesterase; Provisional
 341-533 5.84e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 5.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 341 KQIEEQTKKAQQELEEQTrraLELEQERKRAQSEAEKLAKERQEAEEAKEALLQasrdQKKtqEQLALEMAELtarisql 420
Cdd:PRK12704  42 RILEEAKKEAEAIKKEAL---LEAKEEIHKLRNEFEKELRERRNELQKLEKRLL----QKE--ENLDRKLELL------- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 421 emarQKKESEAVEWQQKAQMVQEDLEKTRAELKTamstphvaepAENEQDEQDENGAEASADlRADAMAKDRSEEERTTE 500
Cdd:PRK12704 106 ----EKREEELEKKEKELEQKQQELEKKEEELEE----------LIEEQLQELERISGLTAE-EAKEILLEKVEEEARHE 170

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119625804 501 AeknervQKHLKALTSElanARDESKKTANDMI 533
Cdd:PRK12704 171 A------AVLIKEIEEE---AKEEADKKAKEIL 194
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 338-527 7.53e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 7.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLakeRQEAEEAKEALlqasRDQKKTQEQLALEMAELTARI 417
Cdd:TIGR02169  294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL---LAEIEELEREI----EEERKRRDKLTEEYAELKEEL 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   418 SQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELktamstphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEEER 497
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREI----------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436

                          170       180       190
                   ....*....|....*....|....*....|
gi 119625804   498 TTEAEKNERVQKHLKALTSELANARDESKK 527
Cdd:TIGR02169  437 NELEEEKEDKALEIKKQEWKLEQLAADLSK 466
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
336-522 7.86e-04

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 42.27  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 336 LMERL--KQIEEQTKKAQQELE----EQTRRALELEQERKRAQSEAEklAKERQEAEEAKEALLQASRDQKKTQEQLALE 409
Cdd:PRK07735  22 ARKRLvaKHGAEISKLEEENREkekaLPKNDDMTIEEAKRRAAAAAK--AKAAALAKQKREGTEEVTEEEKAKAKAKAAA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 410 MAELTARisqlEMARQKKE-----SEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQD-EQDENGAEASADL 483
Cdd:PRK07735 100 AAKAKAA----ALAKQKREgteevTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDkEKAKAKAAAAAKA 175

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 119625804 484 RADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANAR 522
Cdd:PRK07735 176 KAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAK 214
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
296-452 9.29e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 9.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 296 AQAREEKHQKQMERAMLENEKKKREMAEKEKEKierekeelMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEA 375
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEK--------LLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119625804 376 EKLAKERQEAEEAKEALLQASRDQKKTQEQlalEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAEL 452
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 330-524 9.32e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 9.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   330 EREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQ-KKTQEQLAL 408
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   409 EMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKtamSTPHVAEPAENEQDEQDENGAEASADLRADAM 488
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA---ELKEELEDLRAELEEVDKEFAETRDELKDYRE 392

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 119625804   489 AKDRSEEERTTEAEKNERVQKHLKALTSELANARDE 524
Cdd:TIGR02169  393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 339-433 1.07e-03

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


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 41.95  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  339 RLKQIEEQTKKAQQELEEqtrraleLEQERKRAQSEAEKLAKERQEAEEAKEALLQ------------------ASRDQK 400
Cdd:pfam10168 562 RVKLLKLQKEQQLQELQS-------LEEERKSLSERAEKLAEKYEEIKDKQEKLMRrckkvlqrlnsqlpvlsdAEREMK 634

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 119625804  401 KTQEQLALEMAELTARISQLE--MARQKKESEAVE 433
Cdd:pfam10168 635 KELETINEQLKHLANAIKQAKkkMNYQRYQIAKSQ 669
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 7-74 1.09e-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: 38.30  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119625804   7 FAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFS-TWLKLNKKVTAQdVRKESPLLFKFRAKFY 74
Cdd:cd17193   16 FKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSpRWLEPSKPIRKQ-LKGGFPCSLHFRVRFF 83
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 290-501 1.13e-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: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEelmERLKQIEEQTKKAQQELEEQTRRALELEQERK 369
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 370 RAQSEAEKLAKERQ------------------EAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEA 431
Cdd:COG4942  101 AQKEELAELLRALYrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 432 VEWQQKaqmvQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEA 501
Cdd:COG4942  181 AELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 336-524 1.52e-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: 41.59  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQsEAEKLAKERQEAEEAkeALLQASRDQKKTQEQLALEMAELTA 415
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   416 RISQLEMARQKKESEAVEWQQKAQMVQEDLEK----TRAELKTAMSTPHVA-EPAENEQDEQDENGAEASADLRADAMAK 490
Cdd:TIGR02169  252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEiASLERSIAEKERELEDAEERLAKLEAEI 331

                          170       180       190
                   ....*....|....*....|....*....|....
gi 119625804   491 DRSEEERTTEAEKNERVQKHLKALTSELANARDE 524
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 348-509 1.62e-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: 41.48  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  348 KKAQQELEE--QTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEmarq 425
Cdd:COG3096   495 QTARELLRRyrSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE---- 570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  426 KKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRAdAMAKdRSEEERTTEAEKNE 505
Cdd:COG3096   571 EQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTA-AMQQ-LLEREREATVERDE 648


                  ....
gi 119625804  506 RVQK 509
Cdd:COG3096   649 LAAR 652
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
340-526 1.70e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 340 LKQIEEQTKKAQQELE-----------EQTRRALELEQERKRAQSEAEKLA--KERQEAEEAK----------EALLQAS 396
Cdd:PRK02224 435 LRTARERVEEAEALLEagkcpecgqpvEGSPHVETIEEDRERVEELEAELEdlEEEVEEVEERleraedlveaEDRIERL 514

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 397 RDQKKTQEQLALE----MAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMStphvaEPAENEQDEQ 472
Cdd:PRK02224 515 EERREDLEELIAErretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS-----KLAELKERIE 589

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119625804 473 DENGAEASADLRADAMAK-DRSEEERTTEAEKNERVQKHLKAL---TSELANARDESK 526
Cdd:PRK02224 590 SLERIRTLLAAIADAEDEiERLREKREALAELNDERRERLAEKrerKRELEAEFDEAR 647
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 5-57 1.73e-03

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: 37.69  E-value: 1.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119625804   5 LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQ 57
Cdd:cd17192   16 VEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQ 68
Ermin pfam20491
Ermin; This is a cytoskeletal protein exclusively expressed in oligodendrocytes that plays a ...
 391-566 1.80e-03

Ermin; This is a cytoskeletal protein exclusively expressed in oligodendrocytes that plays a role in cytoskeletal rearrangements during the late wrapping and/or compaction phases of myelinogenesis and in maintenance and stability of myelin sheath in the adult. It may also play an important role in late-stage oligodendroglia maturation, myelin/Ranvier node formation during CNS development, and in the maintenance and plasticity of related structures in the mature CNS. Ermin associates with the myosin phosphatase Rho interacting protein protein (Mprip/p116RIP) and inactivates RhoA, a GTPase that controls cytoskeletal rearrangement in differentiating cells, thus contributing to oligodendrocyte morphogenesis. It has a C-terminal actin-binding domain similar to those of members of the ERM family but lacks the conserved N-terminal FERM domain.


Pssm-ID: 466640 [Multi-domain]  Cd Length: 284  Bit Score: 40.60  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  391 ALLQASRDQKKTQEQLALEMAELTAriSQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELK-TAMSTPHVAEPAENEQ 469
Cdd:pfam20491  98 SLQETSADEMTFREGHQWEKIPLSG--SNQEIRRQKERITEQPLKEEEDEDRKNKGHQAAEIEwLGFRKPSQADMLHSKH 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  470 DEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLK----ALTSELANARDESKKTANDMIHAENMRLGRDKY 545
Cdd:pfam20491 176 DEEQKVWDEEIDDDDDDNCNNDEDEVRVIEFKKKHEEVSQFKEegdaSEDSPLSSASSQAVTPDEQPTLGKKSDISRNAY 255

                         170       180
                  ....*....|....*....|....*.
gi 119625804  546 K-----TLRQIRQGNTKQRIDEFESM 566
Cdd:pfam20491 256 SryntiSYRKIRKGNTKQRIDEFESM 281
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 190-244 1.81e-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: 38.38  E-value: 1.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119625804 190 YGVNYFSIKNKKGSELWLGVDALGLNIYeqNDRLTPKIGFPWSEIRNISFNDKKF 244
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGITIC--NDDFEVIERIPYTAIQMATSSGRVF 53
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 336-504 1.84e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAK---EALLQAS---------------- 396
Cdd:COG3883   49 LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVsylDVLLGSEsfsdfldrlsalskia 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 397 -------RDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQ 469
Cdd:COG3883  129 dadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 119625804 470 DEQDENGAEASADLRADAMAKDRSEEERTTEAEKN 504
Cdd:COG3883  209 EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-456 1.97e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 308 ERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEE 387
Cdd:COG1196  667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119625804 388 AKEALLQASRDQKKTQEQLALEMAELTARISQL---------EMARQKKESEAVEwQQKaqmvqEDLEKTRAELKTAM 456
Cdd:COG1196  747 LLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieEYEELEERYDFLS-EQR-----EDLEEARETLEEAI 818
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 363-467 2.07e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 363 ELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQ 442
Cdd:COG4942  147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                         90       100
                 ....*....|....*....|....*
gi 119625804 443 EDLEKTRAELKTAMSTPHVAEPAEN 467
Cdd:COG4942  227 ALIARLEAEAAAAAERTPAAGFAAL 251
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 340-531 2.11e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.09  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 340 LKQIEEQTKKAqqeleEQTRRALELEQERkraqseaekLAKERQEAEE-AKEAllqASRDQKKTQEQLALEMAELTARIS 418
Cdd:PRK05035 438 IRAIEQEKKKA-----EEAKARFEARQAR---------LEREKAAREArHKKA---AEARAAKDKDAVAAALARVKAKKA 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 419 QLEMARQKKESEAVEwqQKAQMVQEDLEKTRAElktamstphvAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERT 498
Cdd:PRK05035 501 AATQPIVIKAGARPD--NSAVIAAREARKAQAR----------ARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAAN 568

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119625804 499 TEAEKNERVQKHLKALTSELANARDESKKTAND 531
Cdd:PRK05035 569 AEAEEEVDPKKAAVAAAIARAKAKKAAQQAASA 601
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 336-457 2.15e-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: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEakeaLLQASRDQK------KTQEQLALE 409
Cdd:COG1579   29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----QLGNVRNNKeyealqKEIESLKRR 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 119625804 410 MAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMS 457
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
345-517 2.23e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  345 EQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALlqasrdqKKTQEQLALEMAELTARISQLEMAR 424
Cdd:COG4913   664 ASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDEL-------KGEIGRLEKELEQAEEELDELQDRL 736

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  425 QKKESEAVEWQqkaqmvQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRaDAMAKDRSE-----EERTT 499
Cdd:COG4913   737 EAAEDLARLEL------RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE-RAMRAFNREwpaetADLDA 809

                         170
                  ....*....|....*...
gi 119625804  500 EAEKNERVQKHLKALTSE 517
Cdd:COG4913   810 DLESLPEYLALLDRLEED 827
PRK12472 PRK12472
hypothetical protein; Provisional
 371-513 2.55e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 40.62  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 371 AQSEAEKLAKERQEA----EEAKEALLQASRDQKKtqeqlalemaeLTARISQLEmaRQKKESEavewqqkAQMVQEDle 446
Cdd:PRK12472 188 APARAETLAREAEDAaraaDEAKTAAAAAAREAAP-----------LKASLRKLE--RAKARAD-------AELKRAD-- 245

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119625804 447 KTRAELKTAMSTPHvaepAENEQDEQDENGAEASADL---RADAMAKDRS-----EEERTTEAEKNERVQKHLKA 513
Cdd:PRK12472 246 KALAAAKTDEAKAR----AEERQQKAAQQAAEAATQLdtaKADAEAKRAAaaatkEAAKAAAAKKAETAKAATDA 316
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 336-426 3.12e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 415
Cdd:COG4942  162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241

                         90
                 ....*....|.
gi 119625804 416 RISQLEMARQK 426
Cdd:COG4942  242 RTPAAGFAALK 252
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
338-552 3.15e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARI 417
Cdd:COG4372   52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 418 SQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQ--DEQDENGAEASADLRADAMAKDRSEE 495
Cdd:COG4372  132 KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQalDELLKEANRNAEKEEELAEAEKLIES 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119625804 496 ERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIR 552
Cdd:COG4372  212 LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 338-452 3.23e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 338 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARI 417
Cdd:COG1196  665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 119625804 418 SQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAEL 452
Cdd:COG1196  745 EELLEEEALEELPEPPDLEELERELERLEREIEAL 779
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
336-524 3.28e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  336 LMERLKQIEE---QTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAE 412
Cdd:COG4913   673 LEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  413 ltARISQLemARQKKESEAVEWQQKAQMV-QEDLEKTRAELKTAMStphvaepAENEQDEQDENGAEASADLRADAMAK- 490
Cdd:COG4913   753 --ERFAAA--LGDAVERELRENLEERIDAlRARLNRAEEELERAMR-------AFNREWPAETADLDADLESLPEYLALl 821

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 119625804  491 DRSEEERTTEAE------KNERVQKHLKALTSELANARDE 524
Cdd:COG4913   822 DRLEEDGLPEYEerfkelLNENSIEFVADLLSKLRRAIRE 861
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
372-559 3.54e-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: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  372 QSEAEKLAKERQEAEEAKEALLQASRDqkktQEQLALEMAELTARISQLEMARQKKESEaVEWQQkaqmVQEDLEKTRAE 451
Cdd:COG4913   606 FDNRAKLAALEAELAELEEELAEAEER----LEALEAELDALQERREALQRLAEYSWDE-IDVAS----AEREIAELEAE 676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  452 LKTAMSTPHVAEPAENEQDEQDENGAEASADLradamakDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTAND 531
Cdd:COG4913   677 LERLDASSDDLAALEEQLEELEAELEELEEEL-------DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749

                         170       180
                  ....*....|....*....|....*...
gi 119625804  532 miHAENMRLGRDKYKTLRQIRQGNTKQR 559
Cdd:COG4913   750 --LLEERFAAALGDAVERELRENLEERI 775
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
341-522 3.57e-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: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  341 KQIEEQTKKAQQELEE--QTRRALELEQERKRAQSEAEKLAKERQEAEEAKEAL------LQASRDQKKTQ------EQL 406
Cdd:COG4913   221 PDTFEAADALVEHFDDleRAHEALEDAREQIELLEPIRELAERYAAARERLAELeylraaLRLWFAQRRLElleaelEEL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  407 ALEMAELTARISQLEMARQKKESEAVE---------------WQQKAQMVQEDLEKTRAELKTAMSTPHVAE-PAENEQD 470
Cdd:COG4913   301 RAELARLEAELERLEARLDALREELDEleaqirgnggdrleqLEREIERLERELEERERRRARLEALLAALGlPLPASAE 380

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119625804  471 EQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANAR 522
Cdd:COG4913   381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
mukB PRK04863
chromosome partition protein MukB;
336-455 4.07e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEAL---------LQASRDQKKTQEQL 406
Cdd:PRK04863  990 LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadsgaeERARARRDELHARL 1069

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 119625804  407 alemAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTA 455
Cdd:PRK04863 1070 ----SANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 338-530 4.95e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 39.60  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKAQQELEEQtrralelEQERKRAQSEAEKLAKERQEA-EEAKEALLQASRDQKKTQEQLALEmaeltar 416
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKA-------QQKADFAQDNADKQRDEVRQKqQEAKNLPKPADTSSPKEDKQVAEN------- 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  417 isqlemarQKKESEavEWQQKAQMVQEDLEKtraelktamSTPHVAEPAENEQDEQDEngaeasadlradaMAKDRSEEE 496
Cdd:pfam05262 279 --------QKREIE--KAQIEIKKNDEEALK---------AKDHKAFDLKQESKASEK-------------EAEDKELEA 326

                         170       180       190
                  ....*....|....*....|....*....|....
gi 119625804  497 RTTEAEKNERVQKHLKALTSELANARDESKKTAN 530
Cdd:pfam05262 327 QKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSN 360
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 336-440 5.41e-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: 39.36  E-value: 5.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 336 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 415
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230

                         90       100
                 ....*....|....*....|....*
gi 119625804 416 RISQLEMARQKKESEAVEWQQKAQM 440
Cdd:COG4942  231 RLEAEAAAAAERTPAAGFAALKGKL 255
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 338-527 6.43e-03

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: 39.34  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQieEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLA-----KERQEAEEAKEALLQASRDQKKT-----QEQLA 407
Cdd:pfam17380 294 EKMEQ--ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiyaeQERMAMERERELERIRQEERKRElerirQEEIA 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  408 LEMAELTaRISQLEMARQKKES---EAVEWQQKAQMVQEDLEKTRAELKTAMstphvaEPAENEQDEQDENGAEASADLR 484
Cdd:pfam17380 372 MEISRMR-ELERLQMERQQKNErvrQELEAARKVKILEEERQRKIQQQKVEM------EQIRAEQEEARQREVRRLEEER 444

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 119625804  485 ADAMAKDRSEE-ERTTEAEKNERVQKHLKALTSELANARDESKK 527
Cdd:pfam17380 445 AREMERVRLEEqERQQQVERLRQQEEERKRKKLELEKEKRDRKR 488
mukB PRK04863
chromosome partition protein MukB;
336-436 6.97e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  336 LMERLKQIEEQTKKAQQELEEQ---TRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAE 412
Cdd:PRK04863  511 LAEQLQQLRMRLSELEQRLRQQqraERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590

                          90       100
                  ....*....|....*....|....
gi 119625804  413 LTARISQLemarqkkESEAVEWQQ 436
Cdd:PRK04863  591 LQARIQRL-------AARAPAWLA 607
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 339-532 7.37e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 7.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   339 RLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARIS 418
Cdd:pfam01576  490 RLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804   419 QLEMARQKKESE----AVEWQQKAQMVQeDLEKTRAELKTAMSTphvaEPAENEQDEQDENGAEASADLR-ADAMAKDRS 493
Cdd:pfam01576  570 KLEKTKNRLQQElddlLVDLDHQRQLVS-NLEKKQKKFDQMLAE----EKAISARYAEERDRAEAEAREKeTRALSLARA 644

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 119625804   494 EEERTTEAEKNERVQKHLKALTSELANARDESKKTANDM 532
Cdd:pfam01576  645 LEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHEL 683
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 338-524 7.80e-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: 39.17  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  338 ERLKQIEEQTKKA-------QQELEEQTRRALELEQERkRAQSEAEKLAKERQEAEEAKEALLQASRDQKK--TQEQLAL 408
Cdd:COG3096   382 ARLEAAEEEVDSLksqladyQQALDVQQTRAIQYQQAV-QALEKARALCGLPDLTPENAEDYLAAFRAKEQqaTEEVLEL 460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  409 E--MAELTARISQLEMARQ--KKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHV-AEPAENEQDEQDENGAEASADL 483
Cdd:COG3096   461 EqkLSVADAARRQFEKAYElvCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLrAQLAELEQRLRQQQNAERLLEE 540

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 119625804  484 RADAMAKDRSEEERTTEAEknERVQKHLKALTSELANARDE 524
Cdd:COG3096   541 FCQRIGQQLDAAEELEELL--AELEAQLEELEEQAAEAVEQ 579
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
290-453 8.26e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 290 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELmERLKQIEEQTKKAQQELEEQTRRALELEQERK 369
Cdd:COG4717  348 ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEALD 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804 370 RAQSEaEKLAKERQEAEEAKEALLQASRDQKKTQEQL--ALEMAELTARISQLEMARQKKESEAVEWqQKAQMVQEDLEK 447
Cdd:COG4717  427 EEELE-EELEELEEELEELEEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEW-AALKLALELLEE 504


                 ....*.
gi 119625804 448 TRAELK 453
Cdd:COG4717  505 AREEYR 510
mukB PRK04863
chromosome partition protein MukB;
346-495 9.07e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 9.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  346 QTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQ---EQLALEMAEltARISQLEM 422
Cdd:PRK04863  341 QTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladYQQALDVQQ--TRAIQYQQ 418

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119625804  423 ARQKKEsEAVEWQQKAQMVQEDLEKTRAELKtamstphvaepaeNEQDEQDENGAEASADLRADAMAKDRSEE 495
Cdd:PRK04863  419 AVQALE-RAKQLCGLPDLTADNAEDWLEEFQ-------------AKEQEATEELLSLEQKLSVAQAAHSQFEQ 477
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 332-531 9.80e-03

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 39.05  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  332 EKEEL-MERLKQIEEqTKKAQQELEEQTRRALELEQERKRA--QSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLAL 408
Cdd:NF012221 1570 DRQRLeQEKQQQLAA-ISGSQSQLESTDQNALETNGQAQRDaiLEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRN 1648

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625804  409 EMAE-LTARI-SQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAmstphVAEPAENEQD-EQDENGAEASADLR- 484
Cdd:NF012221 1649 PFAGgLLDRVqEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAG-----VAQGEQNQANaEQDIDDAKADAEKRk 1723

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 119625804  485 ADAMAKDRSEEERTTEAekNERVQKHLKALTSELANARDESKKTAND 531
Cdd:NF012221 1724 DDALAKQNEAQQAESDA--NAAANDAQSRGEQDASAAENKANQAQAD 1768
 
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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