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Conserved domains on  [gi|967505830|ref|XP_014983069|]
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moesin isoform X1 [Macaca mulatta]

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 ...
 207-303 2.91e-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: 2.91e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 207 MYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 286
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 967505830 287 ILALCMGNHELYMRRRK 303
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 14-213 2.25e-59

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: 196.36  E-value: 2.25e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830    14 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQD-TKGFSTWLKLNKKVTAQDVRKEsPLLFKFRAKF 91
Cdd:smart00295   2 LKVYLLDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830    92 YPEDVsEELIQDITQ-RLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVH-KSGYLAGDKLLPQRVLEQhk 169
Cdd:smart00295  81 YPPDP-NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS-- 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 967505830   170 LNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 213
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 509-584 2.83e-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: 127.32  E-value: 2.83e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830  509 DRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM 584
Cdd:pfam00769   2 LEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 354-463 3.41e-22

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: 91.90  E-value: 3.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 433
Cdd:pfam20492  11 LEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQE 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 967505830  434 RISQLEMARQKKESEAVEWQQKAQMVQEDL 463
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 ...
 207-303 2.91e-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: 2.91e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 207 MYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 286
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 967505830 287 ILALCMGNHELYMRRRK 303
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 14-213 2.25e-59

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: 196.36  E-value: 2.25e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830    14 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQD-TKGFSTWLKLNKKVTAQDVRKEsPLLFKFRAKF 91
Cdd:smart00295   2 LKVYLLDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830    92 YPEDVsEELIQDITQ-RLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVH-KSGYLAGDKLLPQRVLEQhk 169
Cdd:smart00295  81 YPPDP-NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS-- 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 967505830   170 LNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 213
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 12-94 3.97e-55

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: 180.74  E-value: 3.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKF 91
Cdd:cd17187    1 VNVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKF 80


                 ...
gi 967505830  92 YPE 94
Cdd:cd17187   81 YPE 83
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 509-584 2.83e-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: 127.32  E-value: 2.83e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830  509 DRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM 584
Cdd:pfam00769   2 LEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 95-213 8.02e-35

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 127.39  E-value: 8.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   95 DVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVleQHKLNKDQ 174
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQL--LRKMKSKE 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 967505830  175 WEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 213
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
217-302 3.39e-32

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 118.90  E-value: 3.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  217 NKKGSELWLGVDALGLNIYEQNDRLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILALCMGNH 295
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 967505830  296 ELYMRRR 302
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 354-463 3.41e-22

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: 91.90  E-value: 3.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 433
Cdd:pfam20492  11 LEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQE 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 967505830  434 RISQLEMARQKKESEAVEWQQKAQMVQEDL 463
Cdd:pfam20492  91 EIARLEEEVERKEEEARRLQEELEEAREEE 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-541 6.26e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 6.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 387
Cdd:COG1196  261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 388 RAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 467
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505830 468 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARD 541
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-523 1.33e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.74  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 387
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 388 RAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 467
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830 468 AELKTAMSTpHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNE 523
Cdd:COG1196  449 EEEAELEEE-EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 354-583 9.20e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.61  E-value: 9.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 433
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   434 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMStphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEE 513
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRERLESLERRIAAT 836

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505830   514 ERTTE--AEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFES 583
Cdd:TIGR02168  837 ERRLEdlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
PTZ00121 PTZ00121
MAEBL; Provisional
 356-580 1.29e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKAqqeleEQTRRALELE---QERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLAlEMAELT 432
Cdd:PTZ00121 1299 EEKKKADEAKKKA-----EEAKKADEAKkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA-EAAEKK 1372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  433 ARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQ---DENGAEASADLRADAMAKD 509
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAEEAKKADEAKKK 1452

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505830  510 RSEEERTTEAEKNERVQKHLKALTSELANAR--DESKKTANDM-IHAENMRLGRDKYKTLRQIRQGNTKQRIDE 580
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAkKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 356-554 1.61e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRD-------QKKTQEQLALEM 428
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkqiLRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   429 AELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADaMAK 508
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IAS 397

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 967505830   509 DRSEEERtTEAEKnERVQKHLKALTSELANARDESKKTANDMIHAE 554
Cdd:TIGR02168  398 LNNEIER-LEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 310-508 5.66e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 55.20  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 310 QQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKA---QQELEEQtrRALELEQER 386
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAalkQKQAEEA--AAKAAAAAK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 387 KRAQSEAEKLAKERQEAEEAKEALLQAsrDQKKTQEQLALEMAELTARISQLEMARQKKESEAvewqqKAQMVQEDLEKT 466
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEA--EAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA-----KKKAAAEAKKKA 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 967505830 467 RAELKTAmstphvAEPAENEQDEQDENGAEASADLRADAMAK 508
Cdd:PRK09510 220 AAEAKAA------AAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
 
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 ...
 207-303 2.91e-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: 2.91e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 207 MYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 286
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 967505830 287 ILALCMGNHELYMRRRK 303
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 14-213 2.25e-59

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: 196.36  E-value: 2.25e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830    14 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQD-TKGFSTWLKLNKKVTAQDVRKEsPLLFKFRAKF 91
Cdd:smart00295   2 LKVYLLDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830    92 YPEDVsEELIQDITQ-RLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVH-KSGYLAGDKLLPQRVLEQhk 169
Cdd:smart00295  81 YPPDP-NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS-- 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 967505830   170 LNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 213
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 12-94 3.97e-55

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: 180.74  E-value: 3.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKF 91
Cdd:cd17187    1 VNVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKF 80


                 ...
gi 967505830  92 YPE 94
Cdd:cd17187   81 YPE 83
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 12-94 7.88e-49

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: 164.15  E-value: 7.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKF 91
Cdd:cd17237    2 ISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKF 81


                 ...
gi 967505830  92 YPE 94
Cdd:cd17237   82 YPE 84
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 12-94 8.40e-48

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: 161.31  E-value: 8.40e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKF 91
Cdd:cd17239    3 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKF 82


                 ...
gi 967505830  92 YPE 94
Cdd:cd17239   83 YPE 85
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 12-94 8.97e-45

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: 153.35  E-value: 8.97e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKF 91
Cdd:cd17238    1 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKF 80


                 ...
gi 967505830  92 YPE 94
Cdd:cd17238   81 FPE 83
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 12-94 1.60e-40

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: 141.65  E-value: 1.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKF 91
Cdd:cd17097    1 INVRVTTMDAELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVAWLKPDKKVLTQDVSKNNTLKFFFLVKF 80


                 ...
gi 967505830  92 YPE 94
Cdd:cd17097   81 YPE 83
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 14-94 3.07e-37

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: 132.89  E-value: 3.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  14 VRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYP 93
Cdd:cd17186    5 VRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDSKGTVAWLKMDKKVLDQDVPKEEPVTFHFLAKFYP 84


                 .
gi 967505830  94 E 94
Cdd:cd17186   85 E 85
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 509-584 2.83e-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: 127.32  E-value: 2.83e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830  509 DRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM 584
Cdd:pfam00769   2 LEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 95-213 8.02e-35

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 127.39  E-value: 8.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   95 DVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVleQHKLNKDQ 174
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQL--LRKMKSKE 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 967505830  175 WEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYF 213
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
217-302 3.39e-32

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 118.90  E-value: 3.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  217 NKKGSELWLGVDALGLNIYEQNDRLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILALCMGNH 295
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 967505830  296 ELYMRRR 302
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 ...
 105-205 2.12e-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: 111.57  E-value: 2.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 105 TQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLnkDQWEERIQVWHE 184
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKP--EEWEKRIVELHK 78

                         90       100
                 ....*....|....*....|.
gi 967505830 185 EHRGMLREDAVLEYLKIAQDL 205
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 ...
 13-89 2.92e-28

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: 109.17  E-value: 2.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  13 SVRVTTM-----DAELEFAIQPNTTGKQLFDQVVKTIGLR-----------EVWFFGLQYQDTK-------------GFS 63
Cdd:cd01768    1 VLKIFGAglasgANYKSVLATARSTARELVAEALERYGLAgspgggpgessCVDAFALCDALGRpaaagvgsgewraEHL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 967505830  64 TWLKLNKKVTAQ----DVRKESPLLFKFRA 89
Cdd:cd01768   81 RVLGDSERPLLVqelwRARPGWARRFELRG 110
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 354-463 3.41e-22

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: 91.90  E-value: 3.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 433
Cdd:pfam20492  11 LEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQE 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 967505830  434 RISQLEMARQKKESEAVEWQQKAQMVQEDL 463
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 ...
 209-299 2.45e-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: 2.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 209 GVNYFSIKNK--KGSELWLGVDALGLNIYEQNDRlTPKIGFPWSEIRNISFN-DKKFVIKPIDKKAPDFVFYAPRLRINK 285
Cdd:cd00836    1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEDKQSKLLFQTPSRQAK 79

                         90
                 ....*....|....
gi 967505830 286 RILALCMGNHELYM 299
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 ...
 12-91 3.80e-19

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: 81.87  E-value: 3.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAK 90
Cdd:cd01765    1 ISCRVRLLDgTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKHWLDLDKKISKQ-LKRSGPYQFYFRVK 79


                 .
gi 967505830  91 F 91
Cdd:cd01765   80 F 80
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 16-77 4.41e-18

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: 78.40  E-value: 4.41e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505830   16 VTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDV 77
Cdd:pfam09379   1 VRLLDGtVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNGEHRWLDLSKRLSKQAP 63
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 12-95 4.77e-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: 73.40  E-value: 4.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAK 90
Cdd:cd17098    1 LHVKVQMLDdTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKCWLDPEKPILRQ-VKRPKDVVFKFVVK 79


                 ....*
gi 967505830  91 FYPED 95
Cdd:cd17098   80 FYTPD 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-541 6.26e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 6.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 387
Cdd:COG1196  261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 388 RAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 467
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505830 468 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARD 541
Cdd:COG1196  421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 305-554 4.46e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.74  E-value: 4.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 305 DTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQ 384
Cdd:COG1196  223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 385 ERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLE 464
Cdd:COG1196  303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 465 KTRAELKTAMstphvAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESK 544
Cdd:COG1196  383 ELAEELLEAL-----RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        250
                 ....*....|
gi 967505830 545 KTANDMIHAE 554
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 ...
 209-303 1.56e-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: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 209 GVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPID-KKAPD-------------F 274
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDpRRNSHrsrrtfqsssvsvH 80

                         90       100
                 ....*....|....*....|....*....
gi 967505830 275 VFYAPRLRINKRILALCMGNHELYMRRRK 303
Cdd:cd13191   81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQ 109
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 213-304 7.03e-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: 7.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 213 FSIKNKKGSELWLGVDALGLNIYE-QNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALC 291
Cdd:cd13187    8 YREKKSSTLSLWLGICSRGIIIYEeKNGARTPVLRFPWRETQKISFDKKKFTIESRGGSGIKHTFYTDSYKKSQYLLQLC 87

                         90
                 ....*....|....*
gi 967505830 292 MGNHE--LYMRRRKP 304
Cdd:cd13187   88 SAQHKfhIQMRSRQS 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 308-523 1.33e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.74  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 387
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 388 RAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 467
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830 468 AELKTAMSTpHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNE 523
Cdd:COG1196  449 EEEAELEEE-EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 300-537 1.15e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.65  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 300 RRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRA 379
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 380 LELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMV 459
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967505830 460 QEDLEKTRAELKTAmstphvaepAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELA 537
Cdd:COG1196  462 LELLAELLEEAALL---------EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 22-92 4.32e-11

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


Pssm-ID: 340622  Cd Length: 82  Bit Score: 59.18  E-value: 4.32e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967505830  22 ELEFaiQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFY 92
Cdd:cd17102   15 CCEF--KKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQRHWLDPNKSIYKQ-LKGVPPYVLCFRVKFY 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 313-537 5.84e-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: 5.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 313 KAQAREEKHQKQMERAmLENEKKKREMAEKEKEKIERekeeLMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSE 392
Cdd:COG1196  285 EAQAEEYELLAELARL-EQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 393 AEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKT 472
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505830 473 AmstphvaepAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELA 537
Cdd:COG1196  440 E---------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 12-92 7.81e-11

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: 58.52  E-value: 7.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAK 90
Cdd:cd17108    1 IQCKVILLDgTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQHWLDPTKKIKKQ-VKIGPPYTLRFRVK 79


                 ..
gi 967505830  91 FY 92
Cdd:cd17108   80 FY 81
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 216-300 2.50e-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: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 216 KNKK--GSELWLGVDALGLNIYEQNDRLTPKIG-FPWSEIRNISFNDKKFVIKPiDKKAPDFVFYAPRLRINKRILALCM 292
Cdd:cd13185   12 KSKKetPGSVLLGITAKGIQIYQESDGEQQLLRtFPWSNIGKLSFDRKKFEIRP-EGSLRKLTYYTSSDEKSKYLLALCR 90


                 ....*...
gi 967505830 293 GNHELYMR 300
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 ...
 194-271 2.88e-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: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 194 AVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTpkiGFPWSEIRNISFNDKKF---VIKPIDKK 270
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFilhVMQKEEKK 77


                 .
gi 967505830 271 A 271
Cdd:cd13192   78 H 78
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 20-96 4.15e-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: 4.15e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967505830  20 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKES-PLLFKFRAKFYPEDV 96
Cdd:cd17200   12 DRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNWLQLDHRVLDHDLPKKSgPVTLYFAVRFYIESI 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 354-583 9.20e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.61  E-value: 9.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 433
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   434 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMStphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEE 513
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELRAELTLLNEEAANLRERLESLERRIAAT 836

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505830   514 ERTTE--AEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFES 583
Cdd:TIGR02168  837 ERRLEdlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
PTZ00121 PTZ00121
MAEBL; Provisional
 356-580 1.29e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKAqqeleEQTRRALELE---QERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLAlEMAELT 432
Cdd:PTZ00121 1299 EEKKKADEAKKKA-----EEAKKADEAKkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA-EAAEKK 1372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  433 ARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQ---DENGAEASADLRADAMAKD 509
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAEEAKKADEAKKK 1452

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505830  510 RSEEERTTEAEKNERVQKHLKALTSELANAR--DESKKTANDM-IHAENMRLGRDKYKTLRQIRQGNTKQRIDE 580
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAkKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 15-95 1.66e-09

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


Pssm-ID: 340721  Cd Length: 84  Bit Score: 54.89  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  15 RVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAKFYP 93
Cdd:cd17201    5 KVTLLDGsEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKNWLDPSKEIKKQ--IRSGPWHFAFTVKFYP 82


                 ..
gi 967505830  94 ED 95
Cdd:cd17201   83 PD 84
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 20-92 2.64e-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: 2.64e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505830  20 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFY 92
Cdd:cd17104   10 SVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERLWLNLRNRISRQ-LPGPPPYRLRLRVKFF 81
PTZ00121 PTZ00121
MAEBL; Provisional
 313-580 4.80e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  313 KAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSE 392
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  393 AEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAvewQQKAQMVQEDLEKTRAELKT 472
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---KIKAEELKKAEEEKKKVEQL 1638

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  473 AMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKnERVQKHLKALTSELANARDESKKTANDMIH 552
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-KKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717

                         250       260
                  ....*....|....*....|....*...
gi 967505830  553 AENMRlgrdKYKTLRQIRQGNTKQRIDE 580
Cdd:PTZ00121 1718 AEELK----KAEEENKIKAEEAKKEAEE 1741
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 201-265 6.27e-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: 6.27e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505830 201 IAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTpkiGFPWSEIRNISFNDKKFVIK 265
Cdd:cd13193    2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 308-560 6.34e-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: 58.91  E-value: 6.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   308 EVQQMKAQAREekhqKQMERAMLENEKKK-REMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQER 386
Cdd:TIGR02168  685 KIEELEEKIAE----LEKALAELRKELEElEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   387 KRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLAL----------EMAELTARISQLEMARQKKESEAVEWQQKA 456
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdelraELTLLNEEAANLRERLESLERRIAATERRL 840

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   457 QMVQEDLEKTRAELktamstphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSEL 536
Cdd:TIGR02168  841 EDLEEQIEELSEDI----------ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250       260
                   ....*....|....*....|....
gi 967505830   537 ANARDESKKtANDMIHAENMRLGR 560
Cdd:TIGR02168  911 SELRRELEE-LREKLAQLELRLEG 933
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 11-94 6.82e-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: 6.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  11 KISVRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFsTWLKLNKKVT----------AQDVRK 79
Cdd:cd17101    1 RRYVNVVLLNGQrLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAVLKDGEY-FFLDPDTKLSkyapkgwkseAKKGLK 79

                         90
                 ....*....|....*..
gi 967505830  80 ESPLLFK--FRAKFYPE 94
Cdd:cd17101   80 GGKPVFTlyFRVKFYVD 96
PTZ00121 PTZ00121
MAEBL; Provisional
 313-554 8.09e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 8.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  313 KAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQ--ELEEQTRRALELE---QERK 387
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEakKKAEEAKKADEAKkkaEEAK 1496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  388 RAQSEAEKLAKERQEAEEAKEAllqasRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 467
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKA-----EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK 1571

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  468 AELKTAMST--PHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELAnardESKK 545
Cdd:PTZ00121 1572 AEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA----EEKK 1647


                  ....*....
gi 967505830  546 TANDMIHAE 554
Cdd:PTZ00121 1648 KAEELKKAE 1656
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 20-96 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 967505830  20 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRK---ESPLLFKFRAKFYPEDV 96
Cdd:cd17103   12 DRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDETGHYNWLQLDKRVLDHEFPKkwsSGPLVLHFAVKFYVESI 91
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 14-92 1.57e-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: 51.85  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  14 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQ-DVRKESPLLFkFRAKF 91
Cdd:cd17099    6 VRIQLLDNTvLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQlDKHAHEPLLY-FGVMF 84


                 .
gi 967505830  92 Y 92
Cdd:cd17099   85 Y 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 356-554 1.61e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRD-------QKKTQEQLALEM 428
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqqkqiLRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   429 AELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADaMAK 508
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IAS 397

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 967505830   509 DRSEEERtTEAEKnERVQKHLKALTSELANARDESKKTANDMIHAE 554
Cdd:TIGR02168  398 LNNEIER-LEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 12-95 2.23e-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: 51.72  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAK 90
Cdd:cd17190    1 LQLRVKLLDnTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWIWLEPMKLIVKQ-VRRPKNTKLRLAVK 79


                 ....*
gi 967505830  91 FYPED 95
Cdd:cd17190   80 FFPPD 84
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 12-95 2.41e-08

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: 51.51  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAK 90
Cdd:cd17202    2 VLCKVTLLDGtEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSANQKNWLDSTKEIKRQ--IRRLPWLFTFNVK 79


                 ....*
gi 967505830  91 FYPED 95
Cdd:cd17202   80 FYPPD 84
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 20-96 2.80e-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: 2.80e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 967505830  20 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKES-PLLFKFRAKFYPEDV 96
Cdd:cd17199   12 DRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHDFPKKSgPVVLYFCVRFYIESI 89
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 207-264 3.72e-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: 3.72e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 967505830 207 MYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPkigFPWSEIRNISFNDKKFVI 264
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINT---FPWSKIVKISFKRKQFFI 55
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 13-95 3.96e-08

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: 50.90  E-value: 3.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  13 SVRVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAKF 91
Cdd:cd17106    3 QCKVLLLDGtEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQKNWLDPAKEIKKQ--IRSGPWLFSFNVKF 80


                 ....
gi 967505830  92 YPED 95
Cdd:cd17106   81 YPPD 84
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 12-95 4.79e-08

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: 50.57  E-value: 4.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMDAELE-FAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAK 90
Cdd:cd17189    1 VPIKVQMLDDTQEvFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMVWLDLLKPIVKQ-IRRPKHVVLRFVVK 79


                 ....*
gi 967505830  91 FYPED 95
Cdd:cd17189   80 FFPPD 84
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 310-508 5.66e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 55.20  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 310 QQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKA---QQELEEQtrRALELEQER 386
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAalkQKQAEEA--AAKAAAAAK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 387 KRAQSEAEKLAKERQEAEEAKEALLQAsrDQKKTQEQLALEMAELTARISQLEMARQKKESEAvewqqKAQMVQEDLEKT 466
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEA--EAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA-----KKKAAAEAKKKA 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 967505830 467 RAELKTAmstphvAEPAENEQDEQDENGAEASADLRADAMAK 508
Cdd:PRK09510 220 AAEAKAA------AAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
PTZ00121 PTZ00121
MAEBL; Provisional
 356-575 6.18e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKAQQ---ELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEmAELT 432
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQlkkKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-AEEA 1701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  433 ARISQLemarQKKESEAVewqQKAQMVQEDLEKTRAElktamstphvAEPAENEQDEQDENGAEAsadlRADAMAKDRSE 512
Cdd:PTZ00121 1702 KKAEEL----KKKEAEEK---KKAEELKKAEEENKIK----------AEEAKKEAEEDKKKAEEA----KKDEEEKKKIA 1760

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505830  513 EERTTEAEKNERVQKHLKALTSELANARDESKKTANDmihaenmRLGRDKYKTLRQIRQGNTK 575
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-------KKIKDIFDNFANIIEGGKE 1816
PTZ00121 PTZ00121
MAEBL; Provisional
 301-564 6.45e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  301 RRKPDTIEVQQMKAQAREEKHQKQMERA-MLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRA 379
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  380 LELEQERKRAQSEAEKLAKERQEAEEAK----------EALLQASRDQKKTQE--------QLALEMAELTARISQLEMA 441
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKkkaeekkkadEAKKKAEEDKKKADElkkaaaakKKADEAKKKAEEKKKADEA 1436

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  442 RQKKES--EAVEWQQKAQMVQ--EDLEKTRAELKTAMSTPHVAEPAE--NEQDEQDENGAEASADLRADAMAKDRSEEER 515
Cdd:PTZ00121 1437 KKKAEEakKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 967505830  516 TT-EAEKNERVQKHLKALTSELANARDESKKtANDMIHAENMRLGRDKYK 564
Cdd:PTZ00121 1517 KAeEAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKAEELKKAEEKKK 1565
PTZ00121 PTZ00121
MAEBL; Provisional
 308-557 6.51e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 6.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQiEEQTKKAQQELEEQTRRALELEQ-ER 386
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKADELKKAEEKKKADEAKKaEE 1300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  387 KRAQSEAEKLAKERQEAEEAKeallQASRDQKKTQEQL--ALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLE 464
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAK----KKAEEAKKKADAAkkKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  465 KTRAE-LKTAMSTPHVAEPAENEQDEQDENGAEasadLRADAMAKDRSEEERTTEAEKNERVQKHLKAltsELANARDES 543
Cdd:PTZ00121 1377 KKKADaAKKKAEEKKKADEAKKKAEEDKKKADE----LKKAAAAKKKADEAKKKAEEKKKADEAKKKA---EEAKKADEA 1449

                         250
                  ....*....|....
gi 967505830  544 KKTANDMIHAENMR 557
Cdd:PTZ00121 1450 KKKAEEAKKAEEAK 1463
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 356-543 7.50e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 54.81  E-value: 7.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQS------EAEKLAKERQ-EAEEAKEALLQASR---DQKKTQEQLA 425
Cdd:PRK09510  80 QRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEqkkqaeEAAKQAALKQkQAEEAAAKAAAAAKakaEAEAKRAAAA 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 426 LEMAELTARISQLEMARQKKESEAvewqqKAQMVQEDLEKTRAELKtamstphvaEPAENEQDEQdengAEASADLRADA 505
Cdd:PRK09510 160 AKKAAAEAKKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAK---------KKAEAEAKKK----AAAEAKKKAAA 221

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 967505830 506 MAKDRSEEErttEAEKNERVQKHLKALTSELANARDES 543
Cdd:PRK09510 222 EAKAAAAKA---AAEAKAAAEKAAAAKAAEKAAAAKAA 256
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 12-92 1.22e-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: 49.43  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAK 90
Cdd:cd17204    1 LTCRVLLLDgTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAHWLDHTKPIKKQ-IKIGPPYTLHFRIK 79


                 ..
gi 967505830  91 FY 92
Cdd:cd17204   80 YY 81
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 20-92 1.23e-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: 49.61  E-value: 1.23e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830  20 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFST---WLKLNKKVTAQdVRKESPLLFKFRAKFY 92
Cdd:cd17100   11 DTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPATDsmrWLDPLKPIRKQ-IKGGPPYYLNFRVKFY 85
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 20-95 1.63e-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: 1.63e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830  20 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAKFYPED 95
Cdd:cd17188   11 DSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNVWLELLKPITKQ-IKNPKELIFKFTVKFFPVD 85
PTZ00121 PTZ00121
MAEBL; Provisional
 308-582 2.57e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQEL---EEQTRRALELEQ 384
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkaAAAKKKADEAKK 1425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  385 --ERKRAQSEAEKLAKERQEAEEAKeallqasrdqKKTQEQLALEMAEltarisqlEMARQKKESEAVEWQQKAQMVQED 462
Cdd:PTZ00121 1426 kaEEKKKADEAKKKAEEAKKADEAK----------KKAEEAKKAEEAK--------KKAEEAKKADEAKKKAEEAKKADE 1487

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  463 LEKTRAELKTAMSTPHVAEPAENEQDEqdengAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDE 542
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADE-----AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 967505830  543 SKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFE 582
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 301-531 2.89e-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: 53.42  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  301 RRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQE---LEEQTR 377
Cdd:pfam15709 296 RSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEqleRAEKMR 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  378 RALELEQERKraqSEAEKLAKERQEAEEAKeallqasRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQ 457
Cdd:pfam15709 376 EELELEQQRR---FEEIRLRKQRLEEERQR-------QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAE 445

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505830  458 MVQEDLEKTRA-ELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKA 531
Cdd:pfam15709 446 RAEAEKQRQKElEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
PTZ00121 PTZ00121
MAEBL; Provisional
 308-580 2.90e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 387
Cdd:PTZ00121 1198 DARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  388 RAQSEAEKlAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 467
Cdd:PTZ00121 1278 RKADELKK-AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  468 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEE--RTTEAEKNERVQKHLKALTSELANAR--DES 543
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkKADELKKAAAAKKKADEAKKKAEEKKkaDEA 1436

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 967505830  544 KKTANDMIHAENM-RLGRDKYKTLRQIRQGNTKQRIDE 580
Cdd:PTZ00121 1437 KKKAEEAKKADEAkKKAEEAKKAEEAKKKAEEAKKADE 1474
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
356-542 3.06e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKAQQELEEQTRRALELE--QERKRAQSEAEKLAKERQEAEEAKEALLQASRDqkktqeqlaleMAELTA 433
Cdd:COG4913   624 EELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSDD-----------LAALEE 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  434 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAmstphvaepaeneQDEQDENGAEASADLRADAMAKDRSEE 513
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL-------------QDRLEAAEDLARLELRALLEERFAAAL 759

                         170       180
                  ....*....|....*....|....*....
gi 967505830  514 ERTTEAEKNERVQKHLKALTSELANARDE 542
Cdd:COG4913   760 GDAVERELRENLEERIDALRARLNRAEEE 788
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 301-504 3.10e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 3.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   301 RRKPDTIEVQQMKAQAREEKHQKQMERAMLE--NEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRR 378
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKEltELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   379 ALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQM 458
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 967505830   459 VQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRAD 504
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 10-95 3.14e-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: 48.49  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  10 HKISVRVTTMD-AELEFAIQPN----TTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLL 84
Cdd:cd17107    1 EEFYCEIVLLDeSELILTIQQDgiksSKGSVVLDVVFQHLNLLETDYFGLRYIDRQHQTHWLDPAKTLSEQLKLIGPPYT 80

                         90
                 ....*....|.
gi 967505830  85 FKFRAKFYPED 95
Cdd:cd17107   81 LYFGVKFYAED 91
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 12-95 3.25e-07

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


Pssm-ID: 340725  Cd Length: 86  Bit Score: 48.50  E-value: 3.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  12 ISVRVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdVRKESPLLFKFRAK 90
Cdd:cd17205    3 ITCRVSLLDGtDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAHWLDVTKSIKKQ-VKIGPPYCLHLRVK 81


                 ....*
gi 967505830  91 FYPED 95
Cdd:cd17205   82 FYSSE 86
PTZ00121 PTZ00121
MAEBL; Provisional
 301-554 3.32e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  301 RRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIER-EKEELMERLKQIEEQTKKAQQEL---EEQT 376
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAkkaAEAK 1509

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  377 RRALELEQERKRAQSEAEKLAKERQEAEEAKEAllqasRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKA 456
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKA-----EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  457 QMVQedLEKTRAELKTAMSTPHVAEPAENEQDEQDENG----AEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKAL 532
Cdd:PTZ00121 1585 EAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662

                         250       260
                  ....*....|....*....|..
gi 967505830  533 TSELANARDESKKTANDMIHAE 554
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAE 1684
PTZ00121 PTZ00121
MAEBL; Provisional
 356-580 4.01e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 4.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKA---QQELEEQTRRALELEQERKRAQSEAEKlAKERQEAEEAK--EALLQASRDQKKTQEQLALEMAE 430
Cdd:PTZ00121 1319 EAKKKAEEAKKKAdaaKKKAEEAKKAAEAAKAEAEAAADEAEA-AEEKAEAAEKKkeEAKKKADAAKKKAEEKKKADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  431 LTARisqlemaRQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEpaenEQDEQDENGAEASADLRADAMAKDR 510
Cdd:PTZ00121 1398 KKAE-------EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE----EAKKADEAKKKAEEAKKAEEAKKKA 1466

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505830  511 SEEERTTEAEKN---ERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTlRQIRQGNTKQRIDE 580
Cdd:PTZ00121 1467 EEAKKADEAKKKaeeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA-DEAKKAEEAKKADE 1538
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-544 5.00e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 5.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   355 MERLKQIEEQTKKAQQELEEQTRRALELeQERKRAQSEAEK--LAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELT 432
Cdd:TIGR02168  188 LDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   433 ARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELktamstphvaEPAENEQDEQDENGAEASADLRADAMAKDRSE 512
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK----------QILRERLANLERQLEELEAQLEELESKLDELA 336

                          170       180       190
                   ....*....|....*....|....*....|..
gi 967505830   513 EERTTEAEKNERVQKHLKALTSELANARDESK 544
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELE 368
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 294-522 9.03e-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: 51.98  E-value: 9.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   294 NHELYMRRRKPDTIEVQQMKAQAREEKHQKQMER--AMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQE 371
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEEleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   372 LEEQTRRALELEQERKRAQSEAEKLakERQEAEEAKEalLQASRDQKktqEQLALEMAELTARISQLEMARQKKESEAVE 451
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQL--ELQIASLNNE--IERLEARL---ERLEDRRERLQQEIEELLKKLEEAELKELQ 439

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505830   452 WQ-QKAQMVQEDLEKTRAELKTAMSTPHvAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKN 522
Cdd:TIGR02168  440 AElEELEEELEELQEELERLEEALEELR-EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 354-548 9.39e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.37  E-value: 9.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKE----RQEAEEAKEALLQASRDQKKTQEQL-ALEM 428
Cdd:COG3883   28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERARALYRSGGSVsYLDV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 429 -------AELTARISQLE---------MARQKKESEAVEWQQ-KAQMVQEDLEKTRAELKTAMSTphvaepAENEQDEQD 491
Cdd:COG3883  108 llgsesfSDFLDRLSALSkiadadadlLEELKADKAELEAKKaELEAKLAELEALKAELEAAKAE------LEAQQAEQE 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 967505830 492 ENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTAN 548
Cdd:COG3883  182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 15-95 9.80e-07

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


Pssm-ID: 340723  Cd Length: 84  Bit Score: 46.86  E-value: 9.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  15 RVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAKFYP 93
Cdd:cd17203    5 KVTLLDgSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQKNWLDPAKEIKKQ--IRSGAWQFSFNVKFYP 82


                 ..
gi 967505830  94 ED 95
Cdd:cd17203   83 PD 84
PTZ00121 PTZ00121
MAEBL; Provisional
 301-570 1.17e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  301 RRKPDTIEVQQMKAQAREEKHQKQMERAmlENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRAL 380
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  381 E----LEQERKRAQSEAEKLAKERQEAEEAKEAllQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKA 456
Cdd:PTZ00121 1623 EelkkAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  457 QMVQEDLEKTRAELKtamstphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNeRVQKHLKALTSEL 536
Cdd:PTZ00121 1701 AKKAEELKKKEAEEK---------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKEEEKKA 1770

                         250       260       270
                  ....*....|....*....|....*....|....
gi 967505830  537 ANARDESKKTANDMIHAENMRLGRDKYKTLRQIR 570
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 208-300 1.21e-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: 46.90  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 208 YGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKigFPWSEIRNISFNDKKFVIKPIDKKAPdFVFYAPRLRINKRI 287
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVF--FRWEDIKNVINHKRTFSIECQNSEET-VQFQFEDAETAKYV 77

                         90
                 ....*....|...
gi 967505830 288 LALCMGNHELYMR 300
Cdd:cd13188   78 WKLCVLQHKFYRQ 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 354-499 1.55e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.60  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 433
Cdd:COG3883  117 FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830 434 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASA 499
Cdd:COG3883  197 QLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 208-295 2.23e-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: 2.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 208 YGVNYFSIKNKKGSELWLGVDALGLNIYEqnDRLtpKIG-FPWSEIRNISFNDKKFVIK----PIDKKAPDFVFYAPRLR 282
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYR--DRL--RINrFAWPKVLKISYKRNNFYIKirpgEFEQYETTIGFKLPNHR 76

                         90
                 ....*....|...
gi 967505830 283 INKRILALCMGNH 295
Cdd:cd13184   77 AAKRLWKVCVEHH 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 308-554 2.26e-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: 50.83  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQtrraLELEQERK 387
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL----EAELEELE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   388 RAQSEAEKLAkerqeaEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKEseavewQQKAQMVQEDLEKTR 467
Cdd:TIGR02168  365 AELEELESRL------EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE------RLQQEIEELLKKLEE 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   468 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRAdamAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTA 547
Cdd:TIGR02168  433 AELKELQAELEELEEELEELQEELERLEEALEELRE---ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509


                   ....*..
gi 967505830   548 NDMIHAE 554
Cdd:TIGR02168  510 ALLKNQS 516
PTZ00121 PTZ00121
MAEBL; Provisional
 356-580 2.34e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQK--------KTQEQLALE 427
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEernneeirKFEEARMAH 1264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  428 MAELTARIsQLEMARQKKESEAVEWQQKAQMVQEDLEKTRA-ELKTAMSTPHVAEPAENEQDEQDENGAEA---SADLRA 503
Cdd:PTZ00121 1265 FARRQAAI-KAEEARKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKKADAAkkkAEEAKK 1343

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967505830  504 DAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENM--RLGRDKYKTLRQIRQGNTKQRIDE 580
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkKAEEDKKKADELKKAAAAKKKADE 1422
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 322-557 3.30e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.12  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  322 QKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLkQIEEQTK--KAQQELEEQTRRALELEQERKRAQSEAEKLAKE 399
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISRMRELERL-QMERQQKneRVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  400 RQEAEEAKEallqasRDQKKTQEQLALEMAeltaRISQLEMARQK-----KESEAVEWQQKAQMVQEDLEKTRAELKTAM 474
Cdd:pfam17380 426 RAEQEEARQ------REVRRLEEERAREME----RVRLEEQERQQqverlRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  475 STPHVAEPAENE--QDEQDENGAEASADLRADAMAKD----RSEEERTTEAEKNER--VQKHLKALTSELA--NARDESK 544
Cdd:pfam17380 496 ILEKELEERKQAmiEEERKRKLLEKEMEERQKAIYEEerrrEAEEERRKQQEMEERrrIQEQMRKATEERSrlEAMERER 575

                         250
                  ....*....|...
gi 967505830  545 KTANDMIHAENMR 557
Cdd:pfam17380 576 EMMRQIVESEKAR 588
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 15-95 3.58e-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: 45.19  E-value: 3.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  15 RVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQdvRKESPLLFKFRAKFYP 93
Cdd:cd17105    4 KVSLLDdTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKTWLDPAKEIKKQ--VHGGPWEFTFNVKFYP 81


                 ..
gi 967505830  94 ED 95
Cdd:cd17105   82 PD 83
PTZ00121 PTZ00121
MAEBL; Provisional
 296-577 3.88e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  296 ELYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEkierekeelmERLKQIEEQTKKAQQ--ELE 373
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA----------DELKKAAAAKKKADEakKKA 1427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  374 EQTRRALELEQ--ERKRAQSEAEKLAKERQEAEEAK---EALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESE 448
Cdd:PTZ00121 1428 EEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  449 AvewQQKAQMVQEDLEKTRA-ELKTAMSTPHVAEPAENEQDEQDENGAEAS----ADLRADAMAKDRSEEERTTEAEKNE 523
Cdd:PTZ00121 1508 A---KKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKADELKKAEelkkAEEKKKAEEAKKAEEDKNMALRKAE 1584

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505830  524 --------RVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQR 577
Cdd:PTZ00121 1585 eakkaeeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
PTZ00121 PTZ00121
MAEBL; Provisional
 303-583 4.88e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  303 KPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALEL 382
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  383 EQERKRAQSEAEKLAKERQEAEEAKEAllqasRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQED 462
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKA-----EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  463 LEKT-RAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKdRSEEERTTEAEKNERVQK--HLKALTSELANA 539
Cdd:PTZ00121 1239 AEEAkKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKadEAKKKAEEAKKA 1317

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 967505830  540 RDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFES 583
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
358-540 5.64e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 5.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 358 LKQIEEQtKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEmAELTARISQ 437
Cdd:COG4717   70 LKELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-AELAELPER 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 438 LEMARQKKEsEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTT 517
Cdd:COG4717  148 LEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226

                        170       180
                 ....*....|....*....|...
gi 967505830 518 EAEKNERVQKHLKALTSELANAR 540
Cdd:COG4717  227 EELEQLENELEAAALEERLKEAR 249
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 297-461 6.56e-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: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  297 LYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQT 376
Cdd:pfam17380 383 LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  377 RRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQA---SRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQ 453
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeleERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER 542


                  ....*...
gi 967505830  454 QKAQMVQE 461
Cdd:pfam17380 543 RKQQEMEE 550
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 356-523 7.85e-06

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 48.30  E-value: 7.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQtKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAkEALLQASRDQKKTQEQLALEMAELTARI 435
Cdd:TIGR02794  89 ARQKELEQR-AAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA-EAERKAKEEAAKQAEEEAKAKAAAEAKK 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  436 SQLEmARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASAD---LRADAMAKDRSE 512
Cdd:TIGR02794 167 KAEE-AKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADeaeLGDIFGLASGSN 245

                         170
                  ....*....|.
gi 967505830  513 EERTTEAEKNE 523
Cdd:TIGR02794 246 AEKQGGARGAA 256
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 285-486 9.01e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 9.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   285 KRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQ 364
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   365 TKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQK 444
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 967505830   445 KESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENE 486
Cdd:TIGR02169  467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 299-448 1.12e-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: 48.58  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  299 MRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELM-----ERLKQIEEQTKKA-QQEL 372
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLElekekRDRKRAEEQRRKIlEKEL 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  373 EEQTRRALELEQERKRAQSEAEKLAK------ERQEAEEAKEALlQASRDQKKTQEQLAL---EMAELTARISQLEMARQ 443
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEERQKaiyeeeRRREAEEERRKQ-QEMEERRRIQEQMRKateERSRLEAMEREREMMRQ 580


                  ....*
gi 967505830  444 KKESE 448
Cdd:pfam17380 581 IVESE 585
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 14-88 1.13e-05

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: 43.47  E-value: 1.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830  14 VRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREvWFFGLQYQDtkgfsTWLKLNKkvTAQDVRKESPLLFKFR 88
Cdd:cd00196    1 VKVETPSlKKIVVAVPPSTTLRQVLEKVAKRIGLPP-DVIRLLFNG-----QVLDDLM--TAKQVGLEPGEELHFV 68
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
356-527 1.58e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.56  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 356 ERLKQIEEQTKKAQQELEE-QTRRALELEqERKRAQSEAE---KLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAEL 431
Cdd:COG2268  207 EAERETEIAIAQANREAEEaELEQEREIE-TARIAEAEAElakKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEI 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 432 TARISQLEMARQKKEsEAVEWQQKAQMVQEDLEKTRAELKtamstphvaepAENEQDEQDENG-AEASA-DLRADAMAKD 509
Cdd:COG2268  286 AEREREIELQEKEAE-REEAELEADVRKPAEAEKQAAEAE-----------AEAEAEAIRAKGlAEAEGkRALAEAWNKL 353

                        170
                 ....*....|....*...
gi 967505830 510 RSEEERTTEAEKNERVQK 527
Cdd:COG2268  354 GDAAILLMLIEKLPEIAE 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 366-583 1.87e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 366 KKAQQELEEqTRRAL--------ELEQERKRAQSEAEKLAKERQEAEEAKEALLQAS----RDQKKTQEQLALEMAELTA 433
Cdd:COG1196  175 EEAERKLEA-TEENLerledilgELERQLEPLERQAEKAERYRELKEELKELEAELLllklRELEAELEELEAELEELEA 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 434 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTphvAEPAENEQDEQDENGAEASADLRADAMAKDRSEE 513
Cdd:COG1196  254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEE 330

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 514 ERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFES 583
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 356-515 2.47e-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: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKA--QQELEEQTRRALELEQERKRAQSEAEKLAKERQEAE-EAKEALLQASRDQKKTQEQLALEMAELT 432
Cdd:TIGR02794  68 ERQKKLEQQAEEAekQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQkQAEEAKAKQAAEAKAKAEAEAERKAKEE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  433 ARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDengAEASADLRADAMAKDRSE 512
Cdd:TIGR02794 148 AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAA---AEAAAKAEAEAAAAAAAE 224


                  ...
gi 967505830  513 EER 515
Cdd:TIGR02794 225 AER 227
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 218-291 2.49e-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: 2.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967505830 218 KKGSELWLGVDALGLNIYEQNDRlTPKIGFPWSEIRNISFND-----KKFVIKPIDkKAPDFVFYAPRLRINKRILALC 291
Cdd:cd00900   13 TKRVEGTLYITSDRLILRDKNDG-GLELSIPISDIVNVNVSPqgpssRYLVLVLKD-RGEFVGFSFPKEEDAIEISDAL 89
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 360-549 2.67e-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: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  360 QIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEAllQASRDQKKTQEQLALEmaeltARISQLE 439
Cdd:TIGR02794  58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQA--EQAAKQAEEKQKQAEE-----AKAKQAA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  440 MARQKKESEAvewqqkAQMVQEDLEKTRAELKtamstphVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEErtTEA 519
Cdd:TIGR02794 131 EAKAKAEAEA------ERKAKEEAAKQAEEEA-------KAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE--EAK 195

                         170       180       190
                  ....*....|....*....|....*....|
gi 967505830  520 EKNERVQKHLKALTSELANARDESKKTAND 549
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
371-541 2.70e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 371 ELEEQTRRALELEQERKRAQSEAE------KLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAE-LTARISQLEMARQ 443
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGlddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAEsLREDADDLEERAE 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 444 KKESEAVEWQQKAQMVQEDLEKTRAELKtamstphvaepaenEQDEQDENGAEASADLRADamaKDRSEEERTTEAEKNE 523
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIE--------------ELEEEIEELRERFGDAPVD---LGNAEDFLEELREERD 422

                        170
                 ....*....|....*...
gi 967505830 524 RVQKHLKALTSELANARD 541
Cdd:PRK02224 423 ELREREAELEATLRTARE 440
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 308-537 3.36e-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: 46.98  E-value: 3.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   308 EVQQMkaQAREEKHQKQMERAM--LENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQE 385
Cdd:TIGR02169  675 ELQRL--RERLEGLKRELSSLQseLRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   386 RKRAQSEAEKLAKERQEAEEAKEALLQA-------------------SRDQKKTQEQLALEMAELTARIS-------QLE 439
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEAlndlearlshsripeiqaeLSKLEEEVSRIEARLREIEQKLNrltlekeYLE 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   440 MARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEA 519
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912

                          250
                   ....*....|....*...
gi 967505830   520 EKNERVQKHLKALTSELA 537
Cdd:TIGR02169  913 EKKRKRLSELKAKLEALE 930
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 25-92 4.31e-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: 4.31e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967505830  25 FAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFST-WLKLNKKVTAQdVRKESPLLFKFRAKFY 92
Cdd:cd17194   16 FKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDSTDNPrWLDPNKPIRKQ-LKRGSPHNLNFRVKFF 83
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
354-583 5.44e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 5.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEallqasrDQKKTQEQLALEMAELTA 433
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE-------DRREEIEELEEEIEELRE 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 434 RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTphvaePAENEQDEQDENGAEASADLradamaKDRSEE 513
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER-----VEEAEALLEAGKCPECGQPV------EGSPHV 467

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 514 ERTTEAEknERVQKhlkaLTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQgNTKQRIDEFES 583
Cdd:PRK02224 468 ETIEEDR--ERVEE----LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE-DLEELIAERRE 530
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 362-549 5.46e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.57  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 362 EEQTKKAQQELEEQTRRaleleQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQlalemaeltariSQLEMA 441
Cdd:PRK09510  67 QQQQQKSAKRAEEQRKK-----KEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEA------------AKQAAL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 442 RQKKESEAVEWQQKAQMVQEDLEKTRAELKTAmstpHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEK 521
Cdd:PRK09510 130 KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAK----KAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205

                        170       180
                 ....*....|....*....|....*...
gi 967505830 522 NERVQKHLKALTSELANARDESKKTAND 549
Cdd:PRK09510 206 EAKKKAAAEAKKKAAAEAKAAAAKAAAE 233
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 370-481 7.43e-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: 7.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 370 QELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQlalEMAELTARISQLEMARQKKESEA 449
Cdd:COG0542  411 EELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWE---AEKELIEEIQELKEELEQRYGKI 487

                         90       100       110
                 ....*....|....*....|....*....|..
gi 967505830 450 VEWQQKAQMVQEDLEKTRAELKTAMSTPHVAE 481
Cdd:COG0542  488 PELEKELAELEEELAELAPLLREEVTEEDIAE 519
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 325-474 8.31e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 8.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 325 MERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAE 404
Cdd:COG1196  627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 405 EAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAM 474
Cdd:COG1196  707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 363-549 8.60e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 8.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 363 EQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMAR 442
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 443 QKKESEAVEWQQKAQMVQEdlektRAELKTAMSTPHVAEPAENEQDEQDENGA--EASADLRADAMAKDRSEEERTTEAE 520
Cdd:COG4942  100 EAQKEELAELLRALYRLGR-----QPPLALLLSPEDFLDAVRRLQYLKYLAPArrEQAEELRADLAELAALRAELEAERA 174

                        170       180
                 ....*....|....*....|....*....
gi 967505830 521 KNERVQKHLKALTSELANARDESKKTAND 549
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLAR 203
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 359-470 9.22e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 45.43  E-value: 9.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  359 KQIEEQTKKAQQELEEQTRralELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRD-QKKTQEQLALEMAELTARisQ 437
Cdd:PRK10929  105 DALEQEILQVSSQLLEKSR---QAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRlQTLGTPNTPLAQAQLTAL--Q 179

                          90       100       110
                  ....*....|....*....|....*....|...
gi 967505830  438 LEMARQKKESEAVEWQQKAQMVQEDLEKTRAEL 470
Cdd:PRK10929  180 AESAALKALVDELELAQLSANNRQELARLRSEL 212
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 310-510 9.74e-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: 44.84  E-value: 9.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  310 QQMKAQAREEKHQKQMERAmLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQtrralelEQERKRA 389
Cdd:TIGR02794  79 EAEKQRAAEQARQKELEQR-AAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERK-------AKEEAAK 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  390 QSEAEKLAKERQEAE-EAKEALLQASRDQKKTQEqlALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR- 467
Cdd:TIGR02794 151 QAEEEAKAKAAAEAKkKAEEAKKKAEAEAKAKAE--AEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERk 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 967505830  468 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDR 510
Cdd:TIGR02794 229 ADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 358-531 1.03e-04

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 43.90  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  358 LKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEA------EEAKEALLQASRDQK-----KTQEQLAL 426
Cdd:pfam04012  31 IRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAltkgneELAREALAEKKSLEKqaealETQLAQQR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  427 EMAE-LTARISQLEMARQKKESE--AVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRA 503
Cdd:pfam04012 111 SAVEqLRKQLAALETKIQQLKAKknLLKARLKAAKAQEAVQTSLGSLSTSSATDSFERIEEKIEEREARADAAAELASAV 190

                         170       180
                  ....*....|....*....|....*...
gi 967505830  504 DAMAKDRSEEErttEAEKNERVQKHLKA 531
Cdd:pfam04012 191 DLDAKLEQAGI---QMEVSEDVLARLKA 215
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 355-536 1.14e-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: 45.44  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   355 MERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTAR 434
Cdd:TIGR02169  790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   435 ISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLrADAMAKDRSEEE 514
Cdd:TIGR02169  870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPE 948

                          170       180
                   ....*....|....*....|..
gi 967505830   515 RTTEAEKnerVQKHLKALTSEL 536
Cdd:TIGR02169  949 EELSLED---VQAELQRVEEEI 967
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
354-461 1.15e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQAsrdqKKTQEQLALEMAELTA 433
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL----EKELESLEGSKRKLEE 259

                         90       100
                 ....*....|....*....|....*...
gi 967505830 434 RISQLEMARQKKESEAVEWQQKAQMVQE 461
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKE 287
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
356-471 1.21e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEA-EKLAKERQEAEEAKEALLQASRDQKKTQEQLALEM------ 428
Cdd:COG4913   302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLpasaee 381

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 967505830  429 -----AELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELK 471
Cdd:COG4913   382 faalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
310-542 1.42e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  310 QQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERkra 389
Cdd:COG4913   249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL--- 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  390 qseaeklakerqeaEEAKEALLQASRDQKktqeqlalemAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAE 469
Cdd:COG4913   326 --------------DELEAQIRGNGGDRL----------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505830  470 LKTAMST-PHVAEPAENEQDEQDENGAEASADLRADAmakdrsEEERTTEAEKnERVQKHLKALTSELANARDE 542
Cdd:COG4913   382 FAALRAEaAALLEALEEELEALEEALAEAEAALRDLR------RELRELEAEI-ASLERRKSNIPARLLALRDA 448
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 322-544 1.70e-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: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 322 QKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQ 401
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 402 EAEEAKEALLQASRDQKKTQEQLAL-------EMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAM 474
Cdd:COG4942  101 AQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 475 STphvaepAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESK 544
Cdd:COG4942  181 AE------LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
PTZ00121 PTZ00121
MAEBL; Provisional
 310-535 1.84e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  310 QQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREkeelmERLKQIEEQTKKAQQELEEQTRRALELEQERKRA 389
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA-----EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  390 QSEAEKLAKERQEAEE----AKEALLQASRDQKKTQEQLALEmaELTARISQLEMARQKKESEAveWQQKAQMVQEDLEK 465
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKAEEI--RKEKEAVIEEELDE 1787

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505830  466 --TRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSE 535
Cdd:PTZ00121 1788 edEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNE 1859
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 302-524 2.59e-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: 44.29  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   302 RKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALE 381
Cdd:TIGR02169  786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   382 LEQERKRAQ-------SEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQL--EMARQKKESEAVEW 452
Cdd:TIGR02169  866 LEEELEELEaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALeeELSEIEDPKGEDEE 945

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505830   453 QQKAQMVQEDLEKTRAELKTAMSTphvAEPAENEQDEQDENGAEASADL---RADAMAKDRSEEERTTEAEKNER 524
Cdd:TIGR02169  946 IPEEELSLEDVQAELQRVEEEIRA---LEPVNMLAIQEYEEVLKRLDELkekRAKLEEERKAILERIEEYEKKKR 1017
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
354-540 3.05e-04

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 43.43  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 354 LMERL--KQIEEQTKKAQQELE----EQTRRALELEQERKRAQSEAEklAKERQEAEEAKEALLQASRDQKKTQEQLALE 427
Cdd:PRK07735  22 ARKRLvaKHGAEISKLEEENREkekaLPKNDDMTIEEAKRRAAAAAK--AKAAALAKQKREGTEEVTEEEKAKAKAKAAA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 428 MAELTARisqlEMARQKKE-----SEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQD-EQDENGAEASADL 501
Cdd:PRK07735 100 AAKAKAA----ALAKQKREgteevTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDkEKAKAKAAAAAKA 175

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 967505830 502 RADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANAR 540
Cdd:PRK07735 176 KAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAK 214
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
356-555 3.18e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQ---SEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELT 432
Cdd:PRK02224 220 EEIERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 433 A--------------RISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTphvAEPAENEQDEQDENGAEAS 498
Cdd:PRK02224 300 AeaglddadaeaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER---AEELREEAAELESELEEAR 376

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 967505830 499 ADLRADAMAKDRSEEERTTEAEK-------NERVQKHLKALTSELANARDESKKTANDMIHAEN 555
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELREREAELEATLRTARE 440
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
354-451 3.53e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKE----ALLQASRDQKKTQEQLALEMA 429
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelrALLEERFAAALGDAVERELRE 769

                          90       100
                  ....*....|....*....|..
gi 967505830  430 ELTARISQLEMARQKKESEAVE 451
Cdd:COG4913   770 NLEERIDALRARLNRAEEELER 791
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 356-545 4.22e-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: 4.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLakeRQEAEEAKEALlqasRDQKKTQEQLALEMAELTARI 435
Cdd:TIGR02169  294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL---LAEIEELEREI----EEERKRRDKLTEEYAELKEEL 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   436 SQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELktamstphvaEPAENEQDEQDENGAEASADLRADAMAKDRSEEER 515
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREI----------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436

                          170       180       190
                   ....*....|....*....|....*....|
gi 967505830   516 TTEAEKNERVQKHLKALTSELANARDESKK 545
Cdd:TIGR02169  437 NELEEEKEDKALEIKKQEWKLEQLAADLSK 466
PRK12704 PRK12704
phosphodiesterase; Provisional
 359-551 4.47e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 359 KQIEEQTKKAQQELEEQTrraLELEQERKRAQSEAEKLAKERQEAEEAKEALLQasrdQKKtqEQLALEMAELtarisql 438
Cdd:PRK12704  42 RILEEAKKEAEAIKKEAL---LEAKEEIHKLRNEFEKELRERRNELQKLEKRLL----QKE--ENLDRKLELL------- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 439 emarQKKESEAVEWQQKAQMVQEDLEKTRAELKTamstphvaepAENEQDEQDENGAEASADlRADAMAKDRSEEERTTE 518
Cdd:PRK12704 106 ----EKREEELEKKEKELEQKQQELEKKEEELEE----------LIEEQLQELERISGLTAE-EAKEILLEKVEEEARHE 170

                        170       180       190
                 ....*....|....*....|....*....|...
gi 967505830 519 AeknervQKHLKALTSElanARDESKKTANDMI 551
Cdd:PRK12704 171 A------AVLIKEIEEE---AKEEADKKAKEIL 194
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 356-461 4.48e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKER-QEAEEAKEALLQASRDQKKtQEQLALEMAELTAR 434
Cdd:PRK00409 534 QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAiKEAKKEADEIIKELRQLQK-GGYASVKAHELIEA 612

                         90       100
                 ....*....|....*....|....*..
gi 967505830 435 ISQLEMARQKKESEAVEWQQKAQMVQE 461
Cdd:PRK00409 613 RKRLNKANEKKEKKKKKQKEKQEELKV 639
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 313-547 5.15e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 43.01  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 313 KAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQieeqtKKAQQELEEQTRRALELEQERKRAQSE 392
Cdd:PRK05035 450 EAKARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKA-----KKAAATQPIVIKAGARPDNSAVIAARE 524

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 393 AEKLAKeRQEAEEAKEAllqASRDQKKTQEQLALEMAeltarisQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKT 472
Cdd:PRK05035 525 ARKAQA-RARQAEKQAA---AAADPKKAAVAAAIARA-------KAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKK 593

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967505830 473 AMSTPHVAEPAENEQDEQDENGAEASADLRADA--MAKDRSEEERTTEAEKNERVQKhlkaltselANARDESKKTA 547
Cdd:PRK05035 594 AAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAkkAEQQANAEPEEPVDPRKAAVAA---------AIARAKARKAA 661
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 348-542 6.63e-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: 6.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   348 EREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQ-KKTQEQLAL 426
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   427 EMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKtamSTPHVAEPAENEQDEQDENGAEASADLRADAM 506
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA---ELKEELEDLRAELEEVDKEFAETRDELKDYRE 392

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 967505830   507 AKDRSEEERTTEAEKNERVQKHLKALTSELANARDE 542
Cdd:TIGR02169  393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
314-470 6.76e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 314 AQAREEKHQKQMERAMLENEKKKREMAEKEKEKierekeelMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEA 393
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEK--------LLQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967505830 394 EKLAKERQEAEEAKEALLQASRDQKKTQEQlalEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAEL 470
Cdd:COG4717  163 EELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 15-75 7.70e-04

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


Pssm-ID: 340712  Cd Length: 87  Bit Score: 38.85  E-value: 7.70e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 967505830  15 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQ 75
Cdd:cd17192    7 RIQLLNNEfVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQ 68
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 308-519 7.99e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 7.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEelmERLKQIEEQTKKAQQELEEQTRRALELEQERK 387
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 388 RAQSEAEKLAKERQ------------------EAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEA 449
Cdd:COG4942  101 AQKEELAELLRALYrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 450 VEWQQKaqmvQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEA 519
Cdd:COG4942  181 AELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
358-544 8.15e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 358 LKQIEEQTKKAQQELE-----------EQTRRALELEQERKRAQSEAEKLA--KERQE--------AEEAKEALLQASR- 415
Cdd:PRK02224 435 LRTARERVEEAEALLEagkcpecgqpvEGSPHVETIEEDRERVEELEAELEdlEEEVEeveerlerAEDLVEAEDRIERl 514

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 416 -DQKKTQEQLALE----MAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMStphvaEPAENEQDEQ 490
Cdd:PRK02224 515 eERREDLEELIAErretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS-----KLAELKERIE 589

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 967505830 491 DENGAEASADLRADAMAK-DRSEEERTTEAEKNERVQKHLKAL---TSELANARDESK 544
Cdd:PRK02224 590 SLERIRTLLAAIADAEDEiERLREKREALAELNDERRERLAEKrerKRELEAEFDEAR 647
Ermin pfam20491
Ermin; This is a cytoskeletal protein exclusively expressed in oligodendrocytes that plays a ...
 383-584 8.30e-04

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: 41.75  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  383 EQERKRAQ-------SEAEKLAKERQEAEE-------AKEALLQASRDQKKTQEQLALEMAELTAriSQLEMARQKKESE 448
Cdd:pfam20491  58 QEERRKLQgnmllnsSMEDKMLKENPEEKLfivhkaiTDLSLQETSADEMTFREGHQWEKIPLSG--SNQEIRRQKERIT 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  449 AVEWQQKAQMVQEDLEKTRAELK-TAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQK 527
Cdd:pfam20491 136 EQPLKEEEDEDRKNKGHQAAEIEwLGFRKPSQADMLHSKHDEEQKVWDEEIDDDDDDNCNNDEDEVRVIEFKKKHEEVSQ 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967505830  528 HLK----ALTSELANARDESKKTANDMIHAENMRLGRDKYK-----TLRQIRQGNTKQRIDEFESM 584
Cdd:pfam20491 216 FKEegdaSEDSPLSSASSQAVTPDEQPTLGKKSDISRNAYSryntiSYRKIRKGNTKQRIDEFESM 281
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 354-542 9.65e-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: 9.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQsEAEKLAKERQEAEEAkeALLQASRDQKKTQEQLALEMAELTA 433
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   434 RISQLEMARQKKESEAVEWQQKAQMVQEDLEK----TRAELKTAMSTPHVA-EPAENEQDEQDENGAEASADLRADAMAK 508
Cdd:TIGR02169  252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEiASLERSIAEKERELEDAEERLAKLEAEI 331

                          170       180       190
                   ....*....|....*....|....*....|....
gi 967505830   509 DRSEEERTTEAEKNERVQKHLKALTSELANARDE 542
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 354-522 9.90e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 9.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAK---EALLQAS---------------- 414
Cdd:COG3883   49 LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVsylDVLLGSEsfsdfldrlsalskia 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 415 -------RDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQ 487
Cdd:COG3883  129 dadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 967505830 488 DEQDENGAEASADLRADAMAKDRSEEERTTEAEKN 522
Cdd:COG3883  209 EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 25-92 1.06e-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: 1.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967505830  25 FAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFS-TWLKLNKKVTAQdVRKESPLLFKFRAKFY 92
Cdd:cd17193   16 FKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSVDSpRWLEPSKPIRKQ-LKGGFPCSLHFRVRFF 83
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 357-451 1.10e-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: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  357 RLKQIEEQTKKAQQELEEqtrraleLEQERKRAQSEAEKLAKERQEAEEAKEALLQ------------------ASRDQK 418
Cdd:pfam10168 562 RVKLLKLQKEQQLQELQS-------LEEERKSLSERAEKLAEKYEEIKDKQEKLMRrckkvlqrlnsqlpvlsdAEREMK 634

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 967505830  419 KTQEQLALEMAELTARISQLE--MARQKKESEAVE 451
Cdd:pfam10168 635 KELETINEQLKHLANAIKQAKkkMNYQRYQIAKSQ 669
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 366-527 1.19e-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: 41.86  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  366 KKAQQELEE--QTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEmarq 443
Cdd:COG3096   495 QTARELLRRyrSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE---- 570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  444 KKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRAdAMAKdRSEEERTTEAEKNE 523
Cdd:COG3096   571 EQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTA-AMQQ-LLEREREATVERDE 648


                  ....
gi 967505830  524 RVQK 527
Cdd:COG3096   649 LAAR 652
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 354-475 1.26e-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: 40.68  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEakeaLLQASRDQK------KTQEQLALE 427
Cdd:COG1579   29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----QLGNVRNNKeyealqKEIESLKRR 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 967505830 428 MAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMS 475
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
356-570 1.42e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARI 435
Cdd:COG4372   52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 436 SQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQ--DEQDENGAEASADLRADAMAKDRSEE 513
Cdd:COG4372  132 KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQalDELLKEANRNAEKEEELAEAEKLIES 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 967505830 514 ERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIR 570
Cdd:COG4372  212 LPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 358-549 1.53e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 41.47  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 358 LKQIEEQTKKAqqeleEQTRRALELEQERkraqseaekLAKERQEAEE-AKEAllqASRDQKKTQEQLALEMAELTARIS 436
Cdd:PRK05035 438 IRAIEQEKKKA-----EEAKARFEARQAR---------LEREKAAREArHKKA---AEARAAKDKDAVAAALARVKAKKA 500

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 437 QLEMARQKKESEAVEwqQKAQMVQEDLEKTRAElktamstphvAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERT 516
Cdd:PRK05035 501 AATQPIVIKAGARPD--NSAVIAAREARKAQAR----------ARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAAN 568

                        170       180       190
                 ....*....|....*....|....*....|...
gi 967505830 517 TEAEKNERVQKHLKALTSELANARDESKKTAND 549
Cdd:PRK05035 569 AEAEEEVDPKKAAVAAAIARAKAKKAAQQAASA 601
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 326-474 1.54e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 326 ERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEE 405
Cdd:COG1196  667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505830 406 AKEALLQASRDQKKTQEQLALEMAELTARISQLE----MARQkkESEAVEwQQKAQMVQ--EDLEKTRAELKTAM 474
Cdd:COG1196  747 LLEEEALEELPEPPDLEELERELERLEREIEALGpvnlLAIE--EYEELE-ERYDFLSEqrEDLEEARETLEEAI 818
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
363-535 1.60e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  363 EQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALlqasrdqKKTQEQLALEMAELTARISQLEMAR 442
Cdd:COG4913   664 ASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDEL-------KGEIGRLEKELEQAEEELDELQDRL 736

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  443 QKKESEAVEWQqkaqmvQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRaDAMAKDRSE-----EERTT 517
Cdd:COG4913   737 EAAEDLARLEL------RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE-RAMRAFNREwpaetADLDA 809

                         170
                  ....*....|....*...
gi 967505830  518 EAEKNERVQKHLKALTSE 535
Cdd:COG4913   810 DLESLPEYLALLDRLEED 827
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 381-485 1.71e-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: 40.90  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 381 ELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQ 460
Cdd:COG4942  147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                         90       100
                 ....*....|....*....|....*
gi 967505830 461 EDLEKTRAELKTAMSTPHVAEPAEN 485
Cdd:COG4942  227 ALIARLEAEAAAAAERTPAAGFAAL 251
PRK12472 PRK12472
hypothetical protein; Provisional
 389-531 1.85e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.01  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 389 AQSEAEKLAKERQEA----EEAKEALLQASRDQKKtqeqlalemaeLTARISQLEmaRQKKESEavewqqkAQMVQEDle 464
Cdd:PRK12472 188 APARAETLAREAEDAaraaDEAKTAAAAAAREAAP-----------LKASLRKLE--RAKARAD-------AELKRAD-- 245

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505830 465 KTRAELKTAMSTPHvaepAENEQDEQDENGAEASADL---RADAMAKDRS-----EEERTTEAEKNERVQKHLKA 531
Cdd:PRK12472 246 KALAAAKTDEAKAR----AEERQQKAAQQAAEAATQLdtaKADAEAKRAAaaatkEAAKAAAAKKAETAKAATDA 316
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 208-262 1.87e-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: 1.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 967505830 208 YGVNYFSIKNKKGSELWLGVDALGLNIYeqNDRLTPKIGFPWSEIRNISFNDKKF 262
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGITIC--NDDFEVIERIPYTAIQMATSSGRVF 53
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
354-542 2.25e-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: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  354 LMERLKQIEE---QTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAE 430
Cdd:COG4913   673 LEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  431 ltARISQLemARQKKESEAVEWQQKAQMV-QEDLEKTRAELKTAMStphvaepAENEQDEQDENGAEASADLRADAMAK- 508
Cdd:COG4913   753 --ERFAAA--LGDAVERELRENLEERIDAlRARLNRAEEELERAMR-------AFNREWPAETADLDADLESLPEYLALl 821

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 967505830  509 DRSEEERTTEAE------KNERVQKHLKALTSELANARDE 542
Cdd:COG4913   822 DRLEEDGLPEYEerfkelLNENSIEFVADLLSKLRRAIRE 861
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
359-540 2.43e-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: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  359 KQIEEQTKKAQQELEE--QTRRALELEQERKRAQSEAEKLAKERQEAEEAKEAL------LQASRDQKKTQ------EQL 424
Cdd:COG4913   221 PDTFEAADALVEHFDDleRAHEALEDAREQIELLEPIRELAERYAAARERLAELeylraaLRLWFAQRRLElleaelEEL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  425 ALEMAELTARISQLEMARQKKESEAVE---------------WQQKAQMVQEDLEKTRAELKTAMSTPHVAE-PAENEQD 488
Cdd:COG4913   301 RAELARLEAELERLEARLDALREELDEleaqirgnggdrleqLEREIERLERELEERERRRARLEALLAALGlPLPASAE 380

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 967505830  489 EQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANAR 540
Cdd:COG4913   381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 354-444 2.53e-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: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 433
Cdd:COG4942  162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241

                         90
                 ....*....|.
gi 967505830 434 RISQLEMARQK 444
Cdd:COG4942  242 RTPAAGFAALK 252
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
390-577 2.58e-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: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  390 QSEAEKLAKERQEAEEAKEALLQASRDqkktQEQLALEMAELTARISQLEMARQKKESEaVEWQQkaqmVQEDLEKTRAE 469
Cdd:COG4913   606 FDNRAKLAALEAELAELEEELAEAEER----LEALEAELDALQERREALQRLAEYSWDE-IDVAS----AEREIAELEAE 676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  470 LKTAMSTPHVAEPAENEQDEQDENGAEASADLradamakDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTAND 549
Cdd:COG4913   677 LERLDASSDDLAALEEQLEELEAELEELEEEL-------DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749

                         170       180
                  ....*....|....*....|....*...
gi 967505830  550 miHAENMRLGRDKYKTLRQIRQGNTKQR 577
Cdd:COG4913   750 --LLEERFAAALGDAVERELRENLEERI 775
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 356-470 2.59e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 356 ERLKQIEEQTKKAQQELEEQTRR--ALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 433
Cdd:COG1196  665 GSRRELLAALLEAEAELEELAERlaEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 967505830 434 RISQLEMARQKKESEAVEWQQKAQMvqEDLEKTRAEL 470
Cdd:COG1196  745 EELLEEEALEELPEPPDLEELEREL--ERLEREIEAL 779
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 356-548 2.60e-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: 40.76  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKAQQELEEQtrralelEQERKRAQSEAEKLAKERQEA-EEAKEALLQASRDQKKTQEQLALEmaeltar 434
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKA-------QQKADFAQDNADKQRDEVRQKqQEAKNLPKPADTSSPKEDKQVAEN------- 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  435 isqlemarQKKESEavEWQQKAQMVQEDLEKtraelktamSTPHVAEPAENEQDEQDEngaeasadlradaMAKDRSEEE 514
Cdd:pfam05262 279 --------QKREIE--KAQIEIKKNDEEALK---------AKDHKAFDLKQESKASEK-------------EAEDKELEA 326

                         170       180       190
                  ....*....|....*....|....*....|....
gi 967505830  515 RTTEAEKNERVQKHLKALTSELANARDESKKTAN 548
Cdd:pfam05262 327 QKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSN 360
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 356-545 2.97e-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: 40.49  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQieEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLA-----KERQEAEEAKEALLQASRDQKKT-----QEQLA 425
Cdd:pfam17380 294 EKMEQ--ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiyaeQERMAMERERELERIRQEERKRElerirQEEIA 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  426 LEMAELTaRISQLEMARQKKES---EAVEWQQKAQMVQEDLEKTRAELKTAMstphvaEPAENEQDEQDENGAEASADLR 502
Cdd:pfam17380 372 MEISRMR-ELERLQMERQQKNErvrQELEAARKVKILEEERQRKIQQQKVEM------EQIRAEQEEARQREVRRLEEER 444

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 967505830  503 ADAMAKDRSEE-ERTTEAEKNERVQKHLKALTSELANARDESKK 545
Cdd:pfam17380 445 AREMERVRLEEqERQQQVERLRQQEEERKRKKLELEKEKRDRKR 488
mukB PRK04863
chromosome partition protein MukB;
354-473 3.26e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEAL---------LQASRDQKKTQEQL 424
Cdd:PRK04863  990 LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadsgaeERARARRDELHARL 1069

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 967505830  425 alemAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTA 473
Cdd:PRK04863 1070 ----SANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 357-550 3.88e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   357 RLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARIS 436
Cdd:pfam01576  490 RLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   437 QLEMARQKKESE----AVEWQQKAQMV------QEDLEKTRAELKTAMStphvaepaeNEQDEQDENGAEA-SADLRADA 505
Cdd:pfam01576  570 KLEKTKNRLQQElddlLVDLDHQRQLVsnlekkQKKFDQMLAEEKAISA---------RYAEERDRAEAEArEKETRALS 640

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 967505830   506 MAkdRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDM 550
Cdd:pfam01576  641 LA--RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHEL 683
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 354-458 4.45e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 354 LMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTA 433
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230

                         90       100
                 ....*....|....*....|....*
gi 967505830 434 RISQLEMARQKKESEAVEWQQKAQM 458
Cdd:COG4942  231 RLEAEAAAAAERTPAAGFAALKGKL 255
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
308-471 5.41e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELmERLKQIEEQTKKAQQELEEQTRRALELEQERK 387
Cdd:COG4717  348 ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEALD 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 388 RAQSEaEKLAKERQEAEEAKEALLQASRDQKKTQEQL--ALEMAELTARISQLEMARQKKESEAVEWqQKAQMVQEDLEK 465
Cdd:COG4717  427 EEELE-EELEELEEELEELEEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEW-AALKLALELLEE 504


                 ....*.
gi 967505830 466 TRAELK 471
Cdd:COG4717  505 AREEYR 510
mukB PRK04863
chromosome partition protein MukB;
354-454 5.77e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  354 LMERLKQIEEQTKKAQQELEEQ---TRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAE 430
Cdd:PRK04863  511 LAEQLQQLRMRLSELEQRLRQQqraERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590

                          90       100
                  ....*....|....*....|....
gi 967505830  431 LTARISQLemarqkkESEAVEWQQ 454
Cdd:PRK04863  591 LQARIQRL-------AARAPAWLA 607
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 356-542 5.94e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  356 ERLKQIEEQTKKA-------QQELEEQTRRALELEQERkRAQSEAEKLAKERQEAEEAKEALLQASRDQKK--TQEQLAL 426
Cdd:COG3096   382 ARLEAAEEEVDSLksqladyQQALDVQQTRAIQYQQAV-QALEKARALCGLPDLTPENAEDYLAAFRAKEQqaTEEVLEL 460

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  427 E--MAELTARISQLEMARQ--KKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHV-AEPAENEQDEQDENGAEASADL 501
Cdd:COG3096   461 EqkLSVADAARRQFEKAYElvCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLrAQLAELEQRLRQQQNAERLLEE 540

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 967505830  502 RADAMAKDRSEEERTTEAEknERVQKHLKALTSELANARDE 542
Cdd:COG3096   541 FCQRIGQQLDAAEELEELL--AELEAQLEELEEQAAEAVEQ 579
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 356-577 6.80e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.44  E-value: 6.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   356 ERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQ-EQLALEMAELTAR 434
Cdd:pfam12128  618 EKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERlNSLEAQLKQLDKK 697

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   435 ISQLEMARQKKESEA-VEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDengaeasadlradamaKDRSEE 513
Cdd:pfam12128  698 HQAWLEEQKEQKREArTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETW----------------YKRDLA 761

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505830   514 ERTTEAEKNERVQKHLKALTSELAN-ARDESKKTANDMIHAENMRLGRDKYKTlrQIRQGNTKQR 577
Cdd:pfam12128  762 SLGVDPDVIAKLKREIRTLERKIERiAVRRQEVLRYFDWYQETWLQRRPRLAT--QLSNIERAIS 824
mukB PRK04863
chromosome partition protein MukB;
364-513 6.85e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 6.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  364 QTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQ---EQLALEMAEltARISQLEM 440
Cdd:PRK04863  341 QTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladYQQALDVQQ--TRAIQYQQ 418

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967505830  441 ARQKKEsEAVEWQQKAQMVQEDLEKTRAELKtamstphvaepaeNEQDEQDENGAEASADLRADAMAKDRSEE 513
Cdd:PRK04863  419 AVQALE-RAKQLCGLPDLTADNAEDWLEEFQ-------------AKEQEATEELLSLEQKLSVAQAAHSQFEQ 477
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
308-542 7.01e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 7.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 387
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830 388 RAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTR 467
Cdd:COG4372  119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 967505830 468 AELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDE 542
Cdd:COG4372  199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 308-547 7.67e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.18  E-value: 7.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   308 EVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERK 387
Cdd:TIGR00618  177 QYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   388 RAQSEAEKLAKERQE--AEEAKEALLQASRDQKKTQEQLALEmaeltarISQLEMARQKKESEAVEWQQKAQMVQEDLEK 465
Cdd:TIGR00618  257 KKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLAAH-------IKAVTQIEQQAQRIHTELQSKMRSRAKLLMK 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830   466 TRAELKTAMSTPHVAEPAENEQDEQDENGAEAS-ADLRADAMAKDRSEEERT-TEAEKNERVQKHLKALTSELANARDES 543
Cdd:TIGR00618  330 RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvATSIREISCQQHTLTQHIhTLQQQKTTLTQKLQSLCKELDILQREQ 409


                   ....
gi 967505830   544 KKTA 547
Cdd:TIGR00618  410 ATID 413
DUF874 pfam05917
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ...
 360-430 9.22e-03

Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.


Pssm-ID: 283549 [Multi-domain]  Cd Length: 398  Bit Score: 38.68  E-value: 9.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967505830  360 QIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAE 430
Cdd:pfam05917 149 ELEQEKQKTNKSGIELANNQIKAEQEQQKTEQEKQKAEKEAIELEQEKQKTIKTQRDLIKEQKDFIKETEQ 219
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 354-439 9.80e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 36.46  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967505830  354 LMERLKQIEEQTKKAQQELEEQTRRALE------------------LEQERKRAQSEAEKLAKERQEAEEAKEALLQASR 415
Cdd:pfam07926  13 LKEEAADAEAQLQKLQEDLEKQAEIAREaqqnyerelvlhaedikaLQALREELNELKAEIAELKAEAESAKAELEESEE 92

                          90       100
                  ....*....|....*....|....
gi 967505830  416 DQKKTQEQLALEMAELTARISQLE 439
Cdd:pfam07926  93 SWEEQKKELEKELSELEKRIEDLN 116
 
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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