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Conserved domains on  [gi|7328175|emb|CAB82418|]
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hypothetical protein, partial [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 244-340 1.01e-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: 231.01  E-value: 1.01e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  244 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 323
Cdd:cd13194   1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                        90
                ....*....|....*..
gi 7328175  324 ILQLCMGNHELYMRRRK 340
Cdd:cd13194  81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 51-250 2.52e-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: 197.13  E-value: 2.52e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175      51 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVD-NKGFPTWLKLDKKVSAQEVRKEnPLQFKFRAKF 128
Cdd:smart00295   2 LKVYLLDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     129 YPEDVaEELIQDITQ-KLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVH-KSGYLSSERLIPQRVMDQhk 206
Cdd:smart00295  81 YPPDP-NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS-- 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 7328175     207 LTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 250
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 554-630 3.86e-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: 3.86e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7328175    554 DDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL 630
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 381-500 5.80e-31

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: 116.94  E-value: 5.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    381 KEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQ 460
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 7328175    461 LAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDL 500
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
 
Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 244-340 1.01e-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: 231.01  E-value: 1.01e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  244 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 323
Cdd:cd13194   1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                        90
                ....*....|....*..
gi 7328175  324 ILQLCMGNHELYMRRRK 340
Cdd:cd13194  81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 51-250 2.52e-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: 197.13  E-value: 2.52e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175      51 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVD-NKGFPTWLKLDKKVSAQEVRKEnPLQFKFRAKF 128
Cdd:smart00295   2 LKVYLLDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     129 YPEDVaEELIQDITQ-KLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVH-KSGYLSSERLIPQRVMDQhk 206
Cdd:smart00295  81 YPPDP-NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS-- 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 7328175     207 LTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 250
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 47-131 3.58e-57

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: 187.12  E-value: 3.58e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   47 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 126
Cdd:cd17239   1 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 80


                ....*
gi 7328175  127 KFYPE 131
Cdd:cd17239  81 KFYPE 85
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 554-630 3.86e-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: 3.86e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7328175    554 DDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL 630
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 132-250 8.90e-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: 127.77  E-value: 8.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    132 DVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLtrDQ 211
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKS--KE 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 7328175    212 WEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 250
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
254-339 5.26e-33

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 121.59  E-value: 5.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    254 NKKGTDLWLGVDALGLNIYEKDDKLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILQLCMGNH 332
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 7328175    333 ELYMRRR 339
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 381-500 5.80e-31

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: 116.94  E-value: 5.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    381 KEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQ 460
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 7328175    461 LAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDL 500
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 345-591 7.72e-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: 7.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  425 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 504
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  505 EELHLVMTAPPpppppvyepvsyHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQ 584
Cdd:COG1196 393 RAAAELAAQLE------------ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460


                ....*..
gi 7328175  585 ARDENKR 591
Cdd:COG1196 461 LLELLAE 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 345-509 8.80e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.51  E-value: 8.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  425 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 504
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490


                ....*
gi 7328175  505 EELHL 509
Cdd:COG1196 491 ARLLL 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 351-627 5.79e-11

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: 65.85  E-value: 5.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     351 AQAREEKHQKQLERQQ-LETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEE 429
Cdd:TIGR02168  662 TGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     430 AERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHL 509
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     510 VMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNER--VQRQLLTLSSELSQARD 587
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERasLEEALALLRSELEELSE 901

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 7328175     588 ENKRthndiiHNENMRQGRDKYKTLRQI------RQGNTKQRIDEF 627
Cdd:TIGR02168  902 ELRE------LESKRSELRRELEELREKlaqlelRLEGLEVRIDNL 941
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 345-508 1.80e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     345 EVQQMKAQAREEKHQKQLERQQLETE----KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLE 420
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     421 EERKRAQEEAERLEAdrmaalrakeELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKED---EVEEWQHRAKEAQ 497
Cdd:TIGR02168  845 EQIEELSEDIESLAA----------EIEELEELIEELESELEALLNERASLEEALALLRSELEElseELRELESKRSELR 914

                          170
                   ....*....|.
gi 7328175     498 DDLVKTKEELH 508
Cdd:TIGR02168  915 RELEELREKLA 925
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 347-504 1.87e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.82  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   347 QQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQmmrEKEELmLRLQDYEEKTKKAERELSEQIQ----RALQLEEE 422
Cdd:PRK09510  70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQL---EKERL-AAQEQKKQAEEAAKQAALKQKQaeeaAAKAAAAA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   423 RKRAQEEAERLEAdrmAALRAKEELERQA-VDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEveewqhrAKEAQDDLV 501
Cdd:PRK09510 146 KAKAEAEAKRAAA---AAKKAAAEAKKKAeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAE-------AKKKAAAEA 215


                 ...
gi 7328175   502 KTK 504
Cdd:PRK09510 216 KKK 218
PTZ00121 PTZ00121
MAEBL; Provisional
 338-591 8.35e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 8.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    338 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRREtvEREKEQMMREKEElmlRLQDYEEKTKKAErELSEQIQRAL 417
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE--EAKKADEAKKKAE---EAKKADEAKKKAE-EAKKKADEAK 1503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    418 QLEEERKRAqEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAElaeytaKIALLEEARRRKEDEVEEWQHRAKEAQ 497
Cdd:PTZ00121 1504 KAAEAKKKA-DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD------ELKKAEELKKAEEKKKAEEAKKAEEDK 1576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    498 DDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDE-----GAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQ 572
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656

                         250
                  ....*....|....*....
gi 7328175    573 RQLLTLSSELSQARDENKR 591
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKK 1675
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 371-467 1.80e-06

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 47.43  E-value: 1.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  371 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQL-EEERKRAQEEAERlEADRMAAlRAKEELER 449
Cdd:cd06503  29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEaEKIKEEILAEAKE-EAERILE-QAKAEIEQ 106

                        90       100
                ....*....|....*....|..
gi 7328175  450 ---QAVDQIKSQ-EQLAAELAE 467
Cdd:cd06503 107 ekeKALAELRKEvADLAVEAAE 128
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 363-462 3.02e-03

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.77  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   363 ERQQLETEKKRRETVEREKEQMMREK--------EELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAE--R 432
Cdd:NF033838 303 EKKVAEAEKKVEEAKKKAKDQKEEDRrnyptntyKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVEskK 382

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 7328175   433 LEADRMAAL-----RAKEELERQAVDQIKSQEQLA 462
Cdd:NF033838 383 AEATRLEKIktdrkKAEEEAKRKAAEEDKVKEKPA 417
 
Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 244-340 1.01e-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: 231.01  E-value: 1.01e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  244 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 323
Cdd:cd13194   1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                        90
                ....*....|....*..
gi 7328175  324 ILQLCMGNHELYMRRRK 340
Cdd:cd13194  81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 51-250 2.52e-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: 197.13  E-value: 2.52e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175      51 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVD-NKGFPTWLKLDKKVSAQEVRKEnPLQFKFRAKF 128
Cdd:smart00295   2 LKVYLLDGTtLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDpDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     129 YPEDVaEELIQDITQ-KLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVH-KSGYLSSERLIPQRVMDQhk 206
Cdd:smart00295  81 YPPDP-NQLKEDPTRlNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLDS-- 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 7328175     207 LTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 250
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 47-131 3.58e-57

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: 187.12  E-value: 3.58e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   47 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 126
Cdd:cd17239   1 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 80


                ....*
gi 7328175  127 KFYPE 131
Cdd:cd17239  81 KFYPE 85
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 49-131 3.38e-56

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


Pssm-ID: 340707 [Multi-domain]  Cd Length: 83  Bit Score: 184.60  E-value: 3.38e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKF 128
Cdd:cd17187   1 VNVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVDSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKF 80


                ...
gi 7328175  129 YPE 131
Cdd:cd17187  81 YPE 83
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 49-131 3.66e-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: 154.90  E-value: 3.66e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKF 128
Cdd:cd17238   1 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKF 80


                ...
gi 7328175  129 YPE 131
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 ...
 49-131 5.52e-43

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: 148.97  E-value: 5.52e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKF 128
Cdd:cd17097   1 INVRVTTMDAELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVAWLKPDKKVLTQDVSKNNTLKFFFLVKF 80


                ...
gi 7328175  129 YPE 131
Cdd:cd17097  81 YPE 83
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 49-131 5.74e-43

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: 149.13  E-value: 5.74e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKF 128
Cdd:cd17237   2 ISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKF 81


                ...
gi 7328175  129 YPE 131
Cdd:cd17237  82 YPE 84
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 47-131 1.35e-38

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


Pssm-ID: 340706  Cd Length: 85  Bit Score: 137.13  E-value: 1.35e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   47 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 126
Cdd:cd17186   1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDSKGTVAWLKMDKKVLDQDVPKEEPVTFHFLA 80


                ....*
gi 7328175  127 KFYPE 131
Cdd:cd17186  81 KFYPE 85
RA_FERM_F0_F1_like cd01768
Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 ...
 50-126 2.64e-37

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: 134.60  E-value: 2.64e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   50 NVRVTTM-----DAELEFAIQPNTTGKQLFDQVVKTIGLR-----------EVWYFGLHYVDNK-------------GFP 100
Cdd:cd01768   1 VLKIFGAglasgANYKSVLATARSTARELVAEALERYGLAgspgggpgessCVDAFALCDALGRpaaagvgsgewraEHL 80

                        90       100       110
                ....*....|....*....|....*....|
gi 7328175  101 TWLKLDKKVSAQ----EVRKENPLQFKFRA 126
Cdd:cd01768  81 RVLGDSERPLLVqelwRARPGWARRFELRG 110
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 554-630 3.86e-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: 3.86e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7328175    554 DDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL 630
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 132-250 8.90e-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: 127.77  E-value: 8.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    132 DVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLtrDQ 211
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLRKMKS--KE 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 7328175    212 WEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 250
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
254-339 5.26e-33

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 121.59  E-value: 5.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    254 NKKGTDLWLGVDALGLNIYEKDDKLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILQLCMGNH 332
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 7328175    333 ELYMRRR 339
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 381-500 5.80e-31

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: 116.94  E-value: 5.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    381 KEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQ 460
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 7328175    461 LAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDL 500
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 142-242 2.57e-30

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: 114.27  E-value: 2.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  142 TQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLtrDQWEDRIQVWHA 221
Cdd:cd14473   1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQRKP--EEWEKRIVELHK 78

                        90       100
                ....*....|....*....|.
gi 7328175  222 EHRGMLKDNAMLEYLKIAQDL 242
Cdd:cd14473  79 KLRGLSPAEAKLKYLKIARKL 99
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 49-128 8.42e-22

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: 89.57  E-value: 8.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 127
Cdd:cd01765   1 ISCRVRLLDgTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKHWLDLDKKISKQ-LKRSGPYQFYFRVK 79


                .
gi 7328175  128 F 128
Cdd:cd01765  80 F 80
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 246-336 1.10e-18

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


Pssm-ID: 275389  Cd Length: 93  Bit Score: 81.27  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  246 GINYFEIKNK--KGTDLWLGVDALGLNIYEKDDKlTPKIGFPWSEIRNISFN-DKKFVIKPIDKKAPDFVFYAPRLRINK 322
Cdd:cd00836   1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEDKQSKLLFQTPSRQAK 79

                        90
                ....*....|....
gi 7328175  323 RILQLCMGNHELYM 336
Cdd:cd00836  80 EIWKLIVGYHRFLL 93
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 53-112 2.81e-17

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


Pssm-ID: 430570  Cd Length: 63  Bit Score: 76.09  E-value: 2.81e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7328175     53 VTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQ 112
Cdd:pfam09379   1 VRLLDGtVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNGEHRWLDLSKRLSKQ 61
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 49-132 3.71e-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: 73.79  E-value: 3.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 127
Cdd:cd17098   1 LHVKVQMLDdTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKCWLDPEKPILRQ-VKRPKDVVFKFVVK 79


                ....*
gi 7328175  128 FYPED 132
Cdd:cd17098  80 FYTPD 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 345-591 7.72e-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: 7.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  425 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 504
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  505 EELHLVMTAPPpppppvyepvsyHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQ 584
Cdd:COG1196 393 RAAAELAAQLE------------ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460


                ....*..
gi 7328175  585 ARDENKR 591
Cdd:COG1196 461 LLELLAE 467
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 246-340 1.21e-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: 67.37  E-value: 1.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  246 GINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPID-KKAPD-------------F 311
Cdd:cd13191   1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDpRRNSHrsrrtfqsssvsvH 80

                        90       100
                ....*....|....*....|....*....
gi 7328175  312 VFYAPRLRINKRILQLCMGNHELYMRRRK 340
Cdd:cd13191  81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQ 109
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 345-509 8.80e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.51  E-value: 8.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  425 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 504
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490


                ....*
gi 7328175  505 EELHL 509
Cdd:COG1196 491 ARLLL 495
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 250-341 9.30e-12

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


Pssm-ID: 270008  Cd Length: 103  Bit Score: 61.96  E-value: 9.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  250 FEIKNKKGTDLWLGVDALGLNIYE-KDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLC 328
Cdd:cd13187   8 YREKKSSTLSLWLGICSRGIIIYEeKNGARTPVLRFPWRETQKISFDKKKFTIESRGGSGIKHTFYTDSYKKSQYLLQLC 87

                        90
                ....*....|....*
gi 7328175  329 MGNHE--LYMRRRKP 341
Cdd:cd13187  88 SAQHKfhIQMRSRQS 102
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 253-337 1.38e-11

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


Pssm-ID: 270006  Cd Length: 107  Bit Score: 61.55  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  253 KNKKGTD--LWLGVDALGLNIY-EKDDKLTPKIGFPWSEIRNISFNDKKFVIKPiDKKAPDFVFYAPRLRINKRILQLCM 329
Cdd:cd13185  12 KSKKETPgsVLLGITAKGIQIYqESDGEQQLLRTFPWSNIGKLSFDRKKFEIRP-EGSLRKLTYYTSSDEKSKYLLALCR 90


                ....*...
gi 7328175  330 GNHELYMR 337
Cdd:cd13185  91 ETHQFSMA 98
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 59-129 2.51e-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: 59.95  E-value: 2.51e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7328175   59 ELEFaiQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAKFY 129
Cdd:cd17102  15 CCEF--KKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQRHWLDPNKSIYKQ-LKGVPPYVLCFRVKFY 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 330-507 4.67e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 4.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  330 GNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAEREL 409
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  410 SEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQavdqiksQEQLAAELAEYTAKIALLEEARRRKEDEVEEW 489
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                       170
                ....*....|....*...
gi 7328175  490 QHRAKEAQDDLVKTKEEL 507
Cdd:COG1196 455 EEEEEALLELLAELLEEA 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 351-627 5.79e-11

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: 65.85  E-value: 5.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     351 AQAREEKHQKQLERQQ-LETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEE 429
Cdd:TIGR02168  662 TGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     430 AERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHL 509
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     510 VMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNER--VQRQLLTLSSELSQARD 587
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERasLEEALALLRSELEELSE 901

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 7328175     588 ENKRthndiiHNENMRQGRDKYKTLRQI------RQGNTKQRIDEF 627
Cdd:TIGR02168  902 ELRE------LESKRSELRRELEELREKlaqlelRLEGLEVRIDNL 941
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 57-133 1.45e-10

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


Pssm-ID: 340720  Cd Length: 89  Bit Score: 57.98  E-value: 1.45e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7328175   57 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEV-RKENPLQFKFRAKFYPEDV 133
Cdd:cd17200  12 DRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNWLQLDHRVLDHDLpKKSGPVTLYFAVRFYIESI 89
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 57-133 4.94e-10

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


Pssm-ID: 340623  Cd Length: 91  Bit Score: 56.52  E-value: 4.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   57 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKEN---PLQFKFRAKFYPEDV 133
Cdd:cd17103  12 DRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDETGHYNWLQLDKRVLDHEFPKKWssgPLVLHFAVKFYVESI 91
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 49-129 7.54e-10

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


Pssm-ID: 340628  Cd Length: 81  Bit Score: 55.82  E-value: 7.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 127
Cdd:cd17108   1 IQCKVILLDgTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQHWLDPTKKIKKQ-VKIGPPYTLRFRVK 79


                ..
gi 7328175  128 FY 129
Cdd:cd17108  80 FY 81
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 57-129 8.79e-10

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


Pssm-ID: 340624  Cd Length: 81  Bit Score: 55.35  E-value: 8.79e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7328175   57 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAKFY 129
Cdd:cd17104  10 SVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERLWLNLRNRISRQ-LPGPPPYRLRLRVKFF 81
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 345-508 1.80e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     345 EVQQMKAQAREEKHQKQLERQQLETE----KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLE 420
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     421 EERKRAQEEAERLEAdrmaalrakeELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKED---EVEEWQHRAKEAQ 497
Cdd:TIGR02168  845 EQIEELSEDIESLAA----------EIEELEELIEELESELEALLNERASLEEALALLRSELEElseELRELESKRSELR 914

                          170
                   ....*....|.
gi 7328175     498 DDLVKTKEELH 508
Cdd:TIGR02168  915 RELEELREKLA 925
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 347-504 1.87e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.82  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   347 QQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQmmrEKEELmLRLQDYEEKTKKAERELSEQIQ----RALQLEEE 422
Cdd:PRK09510  70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQL---EKERL-AAQEQKKQAEEAAKQAALKQKQaeeaAAKAAAAA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   423 RKRAQEEAERLEAdrmAALRAKEELERQA-VDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEveewqhrAKEAQDDLV 501
Cdd:PRK09510 146 KAKAEAEAKRAAA---AAKKAAAEAKKKAeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAE-------AKKKAAAEA 215


                 ...
gi 7328175   502 KTK 504
Cdd:PRK09510 216 KKK 218
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 354-496 2.63e-09

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: 59.97  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    354 REEKHQKQLERQQLETEKKRRETVEREKEqmmREKEELMLRLQDYEEKTKKAERELSEQI-------QRALQLEEE---- 422
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQ---RRFEEIRLRKQRLEEERQRQEEEERKQRlqlqaaqERARQQQEEfrrk 431

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175    423 -----RKRAQEEAERLEADRMaalRAKEELERQAVDQIKSQEQLAAELAEYTAKialLEEARRRKEDEVEEWQHRAKEA 496
Cdd:pfam15709 432 lqelqRKKQQEEAERAEAEKQ---RQKELEMQLAEEQKRLMEMAEEERLEYQRQ---KQEAEEKARLEAEERRQKEEEA 504
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 52-132 3.60e-09

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


Pssm-ID: 340721  Cd Length: 84  Bit Score: 53.73  E-value: 3.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   52 RVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFYP 130
Cdd:cd17201   5 KVTLLDGsEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKNWLDPSKEIKKQ--IRSGPWHFAFTVKFYP 82


                ..
gi 7328175  131 ED 132
Cdd:cd17201  83 PD 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 356-591 3.90e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 3.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  356 EKHQKQLERQQlETEKKRRETVEREKEqmmREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERkrAQEEAErLEA 435
Cdd:COG1196 199 ERQLEPLERQA-EKAERYRELKEELKE---LEAELLLLKLRELEAELEELEAELEELEAELEELEAEL--AELEAE-LEE 271

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  436 DRMAALRAKEELER---QAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMT 512
Cdd:COG1196 272 LRLELEELELELEEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175  513 APPPPPPPVYEpvsyhVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKR 591
Cdd:COG1196 352 ELEEAEAELAE-----AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 334-505 4.25e-09

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: 59.75  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    334 LYMRRRKPDTIEVQQMKAQAR----EEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLqdyeEKTKKAEREL 409
Cdd:pfam17380 383 LQMERQQKNERVRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM----ERVRLEEQER 458

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    410 SEQIQRALQLEEERKRAQEEAERLEADRMAAlrakEELERQAVDQiksqeqlaaELAEytAKIALLEEARRRK--EDEVE 487
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKRDRKRA----EEQRRKILEK---------ELEE--RKQAMIEEERKRKllEKEME 523

                         170       180
                  ....*....|....*....|....
gi 7328175    488 EWQ------HRAKEAQDDLVKTKE 505
Cdd:pfam17380 524 ERQkaiyeeERRREAEEERRKQQE 547
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 238-302 4.37e-09

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


Pssm-ID: 270014  Cd Length: 122  Bit Score: 54.66  E-value: 4.37e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7328175  238 IAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTpkiGFPWSEIRNISFNDKKFVIK 302
Cdd:cd13193   2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 51-129 5.65e-09

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


Pssm-ID: 340619  Cd Length: 85  Bit Score: 53.39  E-value: 5.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   51 VRVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFY 129
Cdd:cd17099   6 VRIQLLDNTvLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQLDKHAHEPLLYFGVMFY 85
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 57-133 6.56e-09

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: 53.43  E-value: 6.56e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7328175   57 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEV-RKENPLQFKFRAKFYPEDV 133
Cdd:cd17199  12 DRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRVLEHDFpKKSGPVVLYFCVRFYIESI 89
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 59-131 7.12e-09

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


Pssm-ID: 340621  Cd Length: 97  Bit Score: 53.33  E-value: 7.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   59 ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFpTWLKLDKKVSAQ------EVRKENPLQFK------FRA 126
Cdd:cd17101  13 RLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAVLKDGEY-FFLDPDTKLSKYapkgwkSEAKKGLKGGKpvftlyFRV 91


                ....*
gi 7328175  127 KFYPE 131
Cdd:cd17101  92 KFYVD 96
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 337-504 7.24e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 58.28  E-value: 7.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   337 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERElseqiqrA 416
Cdd:PRK09510  81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAE-------A 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   417 LQLEEERKRAQEEAERL---EADRMAALRAKEELERQAVDQIKSQEQLAAE-LAEYTAKIALLEEARRRKEDEVEEWQHR 492
Cdd:PRK09510 154 KRAAAAAKKAAAEAKKKaeaEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEaEAKKKAAAEAKKKAAAEAKAAAAKAAAE 233

                        170
                 ....*....|..
gi 7328175   493 AKEAQDDLVKTK 504
Cdd:PRK09510 234 AKAAAEKAAAAK 245
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
345-506 7.35e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 7.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEEL--MLRLQDYEEKTKKAERELSEQIQRALQLE-- 420
Cdd:COG4717  75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEer 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  421 -EERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQ-EQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQD 498
Cdd:COG4717 155 lEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234


                ....*...
gi 7328175  499 DLVKTKEE 506
Cdd:COG4717 235 ELEAAALE 242
PTZ00121 PTZ00121
MAEBL; Provisional
 338-591 8.35e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 8.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    338 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRREtvEREKEQMMREKEElmlRLQDYEEKTKKAErELSEQIQRAL 417
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE--EAKKADEAKKKAE---EAKKADEAKKKAE-EAKKKADEAK 1503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    418 QLEEERKRAqEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAElaeytaKIALLEEARRRKEDEVEEWQHRAKEAQ 497
Cdd:PTZ00121 1504 KAAEAKKKA-DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD------ELKKAEELKKAEEKKKAEEAKKAEEDK 1576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    498 DDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDE-----GAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQ 572
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656

                         250
                  ....*....|....*....
gi 7328175    573 RQLLTLSSELSQARDENKR 591
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKK 1675
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 345-509 9.61e-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: 58.53  E-value: 9.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     345 EVQQMKAQAREEKHQKQ----LERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLE 420
Cdd:TIGR02168  709 ELEEELEQLRKELEELSrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     421 EERKRAQEEAE--------------RLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEV 486
Cdd:TIGR02168  789 AQIEQLKEELKalrealdelraeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868

                          170       180
                   ....*....|....*....|...
gi 7328175     487 EEWQHRAKEAQDDLVKTKEELHL 509
Cdd:TIGR02168  869 EELESELEALLNERASLEEALAL 891
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 338-588 1.38e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 1.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     338 RRKPDTIEVQQMKAQ------AREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEK---TKKAERE 408
Cdd:TIGR02168  199 ERQLKSLERQAEKAErykelkAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKleeLRLEVSE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     409 LSEQI------------------QRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTA 470
Cdd:TIGR02168  279 LEEEIeelqkelyalaneisrleQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     471 KIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSE 550
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 7328175     551 GIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDE 588
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 231-308 1.60e-08

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


Pssm-ID: 270013  Cd Length: 105  Bit Score: 52.78  E-value: 1.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  231 AMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTpkiGFPWSEIRNISFNDKKF---VIKPIDKK 307
Cdd:cd13192   1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFilhVMQKEEKK 77


                .
gi 7328175  308 A 308
Cdd:cd13192  78 H 78
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 338-629 2.02e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 2.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     338 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKK------RRETVERE-------KEQMMREKEELMLRLQDYEEKTKK 404
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEgyellkeKEALERQKEAIERQLASLEEELEK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     405 AERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAK--------EELERQAVDQIKSQEQLAAELAEYTAKIALLE 476
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLL 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     477 EARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQ------------ESLQDEGAEPTGYS 544
Cdd:TIGR02169  336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyrekleklkreiNELKRELDRLQEEL 415

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     545 AELSSEGiRDDRNEEKRItEAEKNErVQRQLLTLSSELSQARDENKRTHNDIIHNEnmRQGRDKYKTLRQI--RQGNTKQ 622
Cdd:TIGR02169  416 QRLSEEL-ADLNAAIAGI-EAKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYE--QELYDLKEEYDRVekELSKLQR 490


                   ....*..
gi 7328175     623 RIDEFEA 629
Cdd:TIGR02169  491 ELAEAEA 497
PTZ00121 PTZ00121
MAEBL; Provisional
 336-610 3.87e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    336 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKK----RRETVEREKEQMMREKEELML--RLQDYEEKTKKAEREL 409
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKadeaKKAAEAKKKADEAKKAEEAKKadEAKKAEEAKKADEAKK 1541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    410 SEQIQRALQLEE-------ERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRK 482
Cdd:PTZ00121 1542 AEEKKKADELKKaeelkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    483 EDEVEEWQHRAKEAQDDLVKTKEElhlVMTAPPPPPPPVYEPVSyhvQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRI 562
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIK---AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 7328175    563 TEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYK 610
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 345-606 4.37e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 4.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     425 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQ---DDLV 501
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrlEDLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     502 KTKEELHLVMTAPPpppppvyepvsyHVQESLQDEGAEptgYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSE 581
Cdd:TIGR02168  845 EQIEELSEDIESLA------------AEIEELEELIEE---LESELEALLNERASLEEALALLRSELEELSEELRELESK 909

                          250       260
                   ....*....|....*....|....*
gi 7328175     582 LSQARDENKRThNDIIHNENMRQGR 606
Cdd:TIGR02168  910 RSELRRELEEL-REKLAQLELRLEG 933
PTZ00121 PTZ00121
MAEBL; Provisional
 336-511 4.79e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    336 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLEtEKKRRETVEREKEQMMREKEELMlrlQDYEEKTKKAErELSEQIQR 415
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-EKKKAEELKKAEEENKIKAAEEA---KKAEEDKKKAE-EAKKAEED 1686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    416 ALQLEEERKRAQEEAERLEAdrmaaLRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLE----EARRRKEDEVEEWQH 491
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEE-----LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDkkkaEEAKKDEEEKKKIAH 1761

                         170       180
                  ....*....|....*....|
gi 7328175    492 RAKEAQDDLVKTKEELHLVM 511
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVI 1781
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 68-132 4.97e-08

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


Pssm-ID: 340627  Cd Length: 91  Bit Score: 50.80  E-value: 4.97e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7328175   68 TTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPED 132
Cdd:cd17107  27 SKGSVVLDVVFQHLNLLETDYFGLRYIDRQHQTHWLDPAKTLSEQLKLIGPPYTLYFGVKFYAED 91
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 51-132 8.41e-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: 50.13  E-value: 8.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   51 VRVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFY 129
Cdd:cd17106   4 CKVLLLDGtEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQKNWLDPAKEIKKQ--IRSGPWLFSFNVKFY 81


                ...
gi 7328175  130 PED 132
Cdd:cd17106  82 PPD 84
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
347-508 8.97e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 8.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   347 QQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRA 426
Cdd:COG4913  242 EALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   427 QEEAERLEADRMAA-LRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKE 505
Cdd:COG4913  322 REELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                 ...
gi 7328175   506 ELH 508
Cdd:COG4913  402 ALE 404
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 57-132 1.05e-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: 49.81  E-value: 1.05e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7328175   57 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAKFYPED 132
Cdd:cd17188  11 DSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNVWLELLKPITKQ-IKNPKELIFKFTVKFFPVD 85
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 345-511 1.16e-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: 54.57  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    345 EVQQMKAQAREEKHQKQ--LERQQLETEKKRRETVEREKEqmmREKEELMLRLQDYEEKTKKAERELSEQiQRALQLEEE 422
Cdd:pfam15709 344 EMRRLEVERKRREQEEQrrLQQEQLERAEKMREELELEQQ---RRFEEIRLRKQRLEEERQRQEEEERKQ-RLQLQAAQE 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    423 RKRAQEEAERLEADRMAALRAKEELERQAVDQiKSQEQLAAELAEYTAKIALLEEARR----RKEDEVEEwqHRAKEAQD 498
Cdd:pfam15709 420 RARQQQEEFRRKLQELQRKKQQEEAERAEAEK-QRQKELEMQLAEEQKRLMEMAEEERleyqRQKQEAEE--KARLEAEE 496

                         170
                  ....*....|...
gi 7328175    499 DLVKTKEELHLVM 511
Cdd:pfam15709 497 RRQKEEEAARLAL 509
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
350-500 1.19e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   350 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEEL---MLRLQDYEEKTKKAERELSEQI-----QRALQLEE 421
Cdd:COG4913  266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLeaeLERLEARLDALREELDELEAQIrgnggDRLEQLER 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   422 ERKRAQEEAERLEADRMAALRAKEELERQAVDQIKS----QEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQ 497
Cdd:COG4913  346 EIERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425


                 ...
gi 7328175   498 DDL 500
Cdd:COG4913  426 AEI 428
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
348-629 1.26e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 55.05  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   348 QMKAQArEEKHQKQLERQQLETEKKRRET------VEREKEQMMREKEELMLRLQDYEEK---------------TKKAE 406
Cdd:PRK02224 191 QLKAQI-EEKEEKDLHERLNGLESELAELdeeierYEEQREQARETRDEADEVLEEHEERreeletleaeiedlrETIAE 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   407 ---------RELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELE------RQAVDQIKSQEQLAAELAE-YTA 470
Cdd:PRK02224 270 terereelaEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEdrdeelRDRLEECRVAAQAHNEEAEsLRE 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   471 KIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPV------YEPVSYHvQESLQDEGAEPTGYS 544
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFgdapvdLGNAEDF-LEELREERDELRERE 428

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   545 AELSS--EGIRDDRNEEKRITEA----------EKNERVQR------QLLTLSSELSQARDENKRTHNDIIHNENMRQGR 606
Cdd:PRK02224 429 AELEAtlRTARERVEEAEALLEAgkcpecgqpvEGSPHVETieedreRVEELEAELEDLEEEVEEVEERLERAEDLVEAE 508

                        330       340
                 ....*....|....*....|...
gi 7328175   607 DKYKTLRQIRQgNTKQRIDEFEA 629
Cdd:PRK02224 509 DRIERLEERRE-DLEELIAERRE 530
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 345-506 1.47e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:TIGR02169  834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     425 RAQEEAERLEADRMAALRAKEELERQA------VDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQD 498
Cdd:TIGR02169  914 KKRKRLSELKAKLEALEEELSEIEDPKgedeeiPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993


                   ....*...
gi 7328175     499 DLVKTKEE 506
Cdd:TIGR02169  994 KRAKLEEE 1001
PTZ00121 PTZ00121
MAEBL; Provisional
 338-626 2.01e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    338 RRKPDTIEVQQMKAQAREEKhQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA- 416
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAe 1367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    417 ---LQLEEERKRAQEEAERLEADRMAalrakEELERQAVDQIKSQEQL-AAELAEYTAKIALLEEARRRKEDEVEEWQHR 492
Cdd:PTZ00121 1368 aaeKKKEEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELkKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    493 AKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQ 572
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 7328175    573 RqlltlSSELSQArdENKRTHNDIIHNENMRQGrDKYKTLRQIRQGNTKQRIDE 626
Cdd:PTZ00121 1523 K-----ADEAKKA--EEAKKADEAKKAEEKKKA-DELKKAEELKKAEEKKKAEE 1568
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 337-496 2.22e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 2.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  337 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKE-QMMREKEELML-----------RLQDYEEKTKK 404
Cdd:COG4942  67 LARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlYRLGRQPPLALllspedfldavRRLQYLKYLAP 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  405 AERELSEQIQRALQ-LEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKE 483
Cdd:COG4942 147 ARREQAEELRADLAeLAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                       170
                ....*....|...
gi 7328175  484 DEVEEWQHRAKEA 496
Cdd:COG4942 227 ALIARLEAEAAAA 239
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 363-630 2.37e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     363 ERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADrmaalr 442
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED------ 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     443 aKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEewQHRAKEAQDDLVKTKEElHLVMTAPPPPPPPVY 522
Cdd:TIGR02169  746 -LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEE-VSRIEARLREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     523 EPVSYHvQESLQDEGAEPTGYSAELSS-EGIRDDRNEEKRITEAEKNERV---QRQLLTLSSELSQARDENKRTHNDIih 598
Cdd:TIGR02169  822 NRLTLE-KEYLEKEIQELQEQRIDLKEqIKSIEKEIENLNGKKEELEEELeelEAALRDLESRLGDLKKERDELEAQL-- 898

                          250       260       270
                   ....*....|....*....|....*....|..
gi 7328175     599 nENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL 630
Cdd:TIGR02169  899 -RELERKIEELEAQIEKKRKRLSELKAKLEAL 929
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 52-132 2.52e-07

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


Pssm-ID: 340723  Cd Length: 84  Bit Score: 48.78  E-value: 2.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   52 RVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFYP 130
Cdd:cd17203   5 KVTLLDgSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQKNWLDPAKEIKKQ--IRSGAWQFSFNVKFYP 82


                ..
gi 7328175  131 ED 132
Cdd:cd17203  83 PD 84
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 344-500 2.63e-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: 53.91  E-value: 2.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     344 IEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAL----QL 419
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarleRL 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     420 EEERKRAQEEAERL-----EADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAK 494
Cdd:TIGR02168  413 EDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492


                   ....*.
gi 7328175     495 EAQDDL 500
Cdd:TIGR02168  493 SLERLQ 498
PRK12704 PRK12704
phosphodiesterase; Provisional
 345-471 2.71e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 53.63  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   345 EVQQMKAQAREEKHQKQLERQQLETE--------KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRa 416
Cdd:PRK12704  65 EIHKLRNEFEKELRERRNELQKLEKRllqkeenlDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE- 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7328175   417 lqLEEERKRAQEEAERLEADRMaalraKEELERQAVDQIKSQEQLAAELAEYTAK 471
Cdd:PRK12704 144 --LERISGLTAEEAKEILLEKV-----EEEARHEAAVLIKEIEEEAKEEADKKAK 191
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 331-508 2.86e-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: 53.91  E-value: 2.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     331 NHELYMRRRKPDTIEVQQMKAQAREEKHQKQLER--QQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAE-- 406
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEEleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEae 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     407 --------RELSEQIQRA----LQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQE-----QLAAELAEYT 469
Cdd:TIGR02168  367 leelesrlEELEEQLETLrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelkELQAELEELE 446

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 7328175     470 AKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELH 508
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 359-604 3.27e-07

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: 53.59  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    359 QKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRA------------ 426
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKiqqqkvemeqir 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    427 --QEEAERLEADRMAALRAKeELERQAVDQIKSQEQLaaelaeytAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 504
Cdd:pfam17380 427 aeQEEARQREVRRLEEERAR-EMERVRLEEQERQQQV--------ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL 497

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    505 EElhlvmTAPPPPPPPVYEPVSYHVQESLQDEGAeptgySAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELS- 583
Cdd:pfam17380 498 EK-----ELEERKQAMIEEERKRKLLEKEMEERQ-----KAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSr 567

                         250       260
                  ....*....|....*....|..
gi 7328175    584 -QARDENKRTHNDIIHNENMRQ 604
Cdd:pfam17380 568 lEAMEREREMMRQIVESEKARA 589
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 49-132 3.29e-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: 3.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 127
Cdd:cd17205   3 ITCRVSLLDGtDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAHWLDVTKSIKKQ-VKIGPPYCLHLRVK 81


                ....*
gi 7328175  128 FYPED 132
Cdd:cd17205  82 FYSSE 86
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 244-301 3.59e-07

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


Pssm-ID: 270010  Cd Length: 95  Bit Score: 48.46  E-value: 3.59e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7328175  244 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPkigFPWSEIRNISFNDKKFVI 301
Cdd:cd13189   1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINT---FPWSKIVKISFKRKQFFI 55
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 51-125 4.41e-07

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


Pssm-ID: 340450  Cd Length: 68  Bit Score: 47.32  E-value: 4.41e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7328175   51 VRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREvWYFGLHYVDnkgfpTWLKLDKKVSaqEVRKENPLQFKFR 125
Cdd:cd00196   1 VKVETPSlKKIVVAVPPSTTLRQVLEKVAKRIGLPP-DVIRLLFNG-----QVLDDLMTAK--QVGLEPGEELHFV 68
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 343-511 4.61e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 4.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  343 TIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEE 422
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  423 RKRAQEEAERLEADRMAALrakEELERQAVDQIKSQEQLAAELAEYTAKIALL--------EEArrrkeDEVEEwQHRAK 494
Cdd:COG1196 730 LEAEREELLEELLEEEELL---EEEALEELPEPPDLEELERELERLEREIEALgpvnllaiEEY-----EELEE-RYDFL 800

                       170
                ....*....|....*...
gi 7328175  495 EAQ-DDLVKTKEELHLVM 511
Cdd:COG1196 801 SEQrEDLEEARETLEEAI 818
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 52-132 5.23e-07

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


Pssm-ID: 340625  Cd Length: 83  Bit Score: 47.88  E-value: 5.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   52 RVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFYP 130
Cdd:cd17105   4 KVSLLDdTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKTWLDPAKEIKKQ--VHGGPWEFTFNVKFYP 81


                ..
gi 7328175  131 ED 132
Cdd:cd17105  82 PD 83
PTZ00121 PTZ00121
MAEBL; Provisional
 336-499 5.77e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 5.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    336 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELmlrlQDYEEKTKKAERELSEQIQR 415
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA----KKAEEDEKKAAEALKKEAEE 1700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    416 ALQLEEERKRAQEEAERLEADRMAALRAK---EELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHR 492
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKikaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780


                  ....*..
gi 7328175    493 AKEAQDD 499
Cdd:PTZ00121 1781 IEEELDE 1787
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 347-506 6.55e-07

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: 51.77  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    347 QQMKAQAR-EEKHQKQLERQQLETEKKRRETVEREKEQMMREKEElmlrlqdyeEKTKKAErelseqiQRALQLEEERKR 425
Cdd:TIGR02794  57 QQKKPAAKkEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE---------KAAKQAE-------QAAKQAEEKQKQ 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    426 AQEEAERLEADRMAAL------RAKEELERQAVDQIKSQEQLAAELAEytakiallEEARRRKEDEVEEWQHRAKEAQDD 499
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAeaeaerKAKEEAAKQAEEEAKAKAAAEAKKKA--------EEAKKKAEAEAKAKAEAEAKAKAE 192


                  ....*..
gi 7328175    500 LVKTKEE 506
Cdd:TIGR02794 193 EAKAKAE 199
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 52-132 7.60e-07

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


Pssm-ID: 340722  Cd Length: 84  Bit Score: 47.27  E-value: 7.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   52 RVTTMDA-ELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQevRKENPLQFKFRAKFYP 130
Cdd:cd17202   5 KVTLLDGtEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSANQKNWLDSTKEIKRQ--IRRLPWLFTFNVKFYP 82


                ..
gi 7328175  131 ED 132
Cdd:cd17202  83 PD 84
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
317-492 8.43e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 8.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   317 RLRINKRILQLCMGNHELYMRRRKpdtieVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELML-RL 395
Cdd:COG4913  266 AARERLAELEYLRAALRLWFAQRR-----LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdRL 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   396 QDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAErLEADRMAALRAKEELERQAVDQIksQEQLAAELAEYTAKIALL 475
Cdd:COG4913  341 EQLEREIERLERELEERERRRARLEALLAALGLPLP-ASAEEFAALRAEAAALLEALEEE--LEALEEALAEAEAALRDL 417

                        170
                 ....*....|....*..
gi 7328175   476 EEARRRKEDEVEEWQHR 492
Cdd:COG4913  418 RRELRELEAEIASLERR 434
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
387-496 9.47e-07

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 50.21  E-value: 9.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  387 EKEELMLR--LQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRA-KEELERQAVDQIKSQEQLAA 463
Cdd:COG1842  22 EDPEKMLDqaIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERKAELEAQAE 101

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 7328175  464 EL----AEYTAKIALLEEARRRKEDEVEEWQHRAKEA 496
Cdd:COG1842 102 ALeaqlAQLEEQVEKLKEALRQLESKLEELKAKKDTL 138
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 347-485 1.03e-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: 51.00  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    347 QQMKAQAREEKHQKQLERQQLETEKKRRETvEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAL--QLEEERK 424
Cdd:TIGR02794  79 EAEKQRAAEQARQKELEQRAAAEKAAKQAE-QAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAakQAEEEAK 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175    425 R-----AQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAEL---AEYTAKIALLEEARRRKEDE 485
Cdd:TIGR02794 158 AkaaaeAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAkaaAEAAAKAEAEAAAAAAAEAE 226
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 49-132 1.10e-06

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


Pssm-ID: 340710  Cd Length: 85  Bit Score: 46.71  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLqFKFRAK 127
Cdd:cd17190   1 LQLRVKLLDnTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWIWLEPMKLIVKQVRRPKNTK-LRLAVK 79


                ....*
gi 7328175  128 FYPED 132
Cdd:cd17190  80 FFPPD 84
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 48-132 1.47e-06

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


Pssm-ID: 340709  Cd Length: 85  Bit Score: 46.34  E-value: 1.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   48 PINVRVTTmDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 127
Cdd:cd17189   2 PIKVQMLD-DTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMVWLDLLKPIVKQ-IRRPKHVVLRFVVK 79


                ....*
gi 7328175  128 FYPED 132
Cdd:cd17189  80 FFPPD 84
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 349-507 1.75e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     349 MKAQAREEKHQKQLER------QQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEE 422
Cdd:TIGR02169  694 QSELRRIENRLDELSQelsdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     423 RKRAQEEAERLEAD----RMAALRAK-EELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKE-- 495
Cdd:TIGR02169  774 LHKLEEALNDLEARlshsRIPEIQAElSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSie 853

                          170
                   ....*....|...
gi 7328175     496 -AQDDLVKTKEEL 507
Cdd:TIGR02169  854 kEIENLNGKKEEL 866
PTZ00121 PTZ00121
MAEBL; Provisional
 339-505 1.77e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    339 RKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEqmmrEKEELMLRLQDYEEKTKKAERELSEQIQRALQ 418
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE----EKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    419 LEEERKRAQEEaeRLEADRmaaLRAKEELERQAVDQIKSQEQLAAELAEYTAKIAllEEARR----RKEDEVEEW--QHR 492
Cdd:PTZ00121 1663 AAEEAKKAEED--KKKAEE---AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA--EEKKKaeelKKAEEENKIkaEEA 1735

                         170
                  ....*....|...
gi 7328175    493 AKEAQDDLVKTKE 505
Cdd:PTZ00121 1736 KKEAEEDKKKAEE 1748
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 351-551 1.79e-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: 1.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  351 AQAREEKHQKQLERQQLETEKkrrETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEE- 429
Cdd:COG3883  12 AFADPQIQAKQKELSELQAEL---EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEl 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  430 AERLEA------------------------DRMAALRAKEELERQAVDQIKS-QEQLAAELAEYTAKIALLEEARRRKED 484
Cdd:COG3883  89 GERARAlyrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKAdKAELEAKKAELEAKLAELEALKAELEA 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7328175  485 EVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEG 551
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 371-467 1.80e-06

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 47.43  E-value: 1.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  371 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQL-EEERKRAQEEAERlEADRMAAlRAKEELER 449
Cdd:cd06503  29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEaEKIKEEILAEAKE-EAERILE-QAKAEIEQ 106

                        90       100
                ....*....|....*....|..
gi 7328175  450 ---QAVDQIKSQ-EQLAAELAE 467
Cdd:cd06503 107 ekeKALAELRKEvADLAVEAAE 128
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 49-129 1.87e-06

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


Pssm-ID: 340724  Cd Length: 84  Bit Score: 46.35  E-value: 1.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   49 INVRVTTMD-AELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQeVRKENPLQFKFRAK 127
Cdd:cd17204   1 LTCRVLLLDgTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAHWLDHTKPIKKQ-IKIGPPYTLHFRIK 79


                ..
gi 7328175  128 FY 129
Cdd:cd17204  80 YY 81
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 337-481 2.73e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  337 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA 416
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  417 LQLEEERKRAQEEAERLEAdRMAAL-----RAKEELERqavdqiksqeqLAAELAEYTAKIALLEEARRR 481
Cdd:COG1196 756 LPEPPDLEELERELERLER-EIEALgpvnlLAIEEYEE-----------LEERYDFLSEQREDLEEARET 813
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 351-588 3.13e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.76  E-value: 3.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  351 AQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQE 428
Cdd:COG4942  18 QADAAAEAEAELEqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  429 EAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELH 508
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  509 LVMTAPPPPpppvyepvsyhvQESLQDEGAEPTGYSAELSsegiRDDRNEEKRITEAEKNE-RVQRQLLTLSSELSQARD 587
Cdd:COG4942 178 ALLAELEEE------------RAALEALKAERQKLLARLE----KELAELAAELAELQQEAeELEALIARLEAEAAAAAE 241


                .
gi 7328175  588 E 588
Cdd:COG4942 242 R 242
PTZ00121 PTZ00121
MAEBL; Provisional
 336-629 3.85e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    336 MRRRKPDTIEVQ--QMKAQAREEKHQkqlERQQLETEKKRRETVEREKEqmmREKEELMLRLQDYEEKTKKAERELSEQI 413
Cdd:PTZ00121 1069 DEGLKPSYKDFDfdAKEDNRADEATE---EAFGKAEEAKKTETGKAEEA---RKAEEAKKKAEDARKAEEARKAEDARKA 1142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    414 QRALQLEEERK----RAQEEAERLE-------ADRMAALRAKEELeRQAVDQIKSQEQLAAELAEYTAKIALLEEARRRK 482
Cdd:PTZ00121 1143 EEARKAEDAKRveiaRKAEDARKAEearkaedAKKAEAARKAEEV-RKAEELRKAEDARKAEAARKAEEERKAEEARKAE 1221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    483 EDEVEEWQHRAKEAQddlvKTKEElhlvmtAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKR- 561
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAK----KDAEE------AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKk 1291

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    562 ITEAEKNERVQR--QLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEA 629
Cdd:PTZ00121 1292 ADEAKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 342-488 4.30e-06

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: 48.38  E-value: 4.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  342 DTIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKA---------ERELS 410
Cdd:COG1579  20 DRLEHRLKELPAELAELEDELAalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIE 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7328175  411 EQIQRALQLEEERKRAQEEAERLEAdrmAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEE 488
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEE---ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 371-467 4.69e-06

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


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 46.70  E-value: 4.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  371 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAL-QLEEERKRAQEEAERlEADRMAAlRAKEELER 449
Cdd:COG0711  30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARkEAEAIAEEAKAEAEA-EAERIIA-QAEAEIEQ 107

                        90       100
                ....*....|....*....|..
gi 7328175  450 ---QAVDQIKSQ-EQLAAELAE 467
Cdd:COG0711 108 eraKALAELRAEvADLAVAIAE 129
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 62-129 5.06e-06

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


Pssm-ID: 340714  Cd Length: 84  Bit Score: 44.91  E-value: 5.06e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175   62 FAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNK-GFPTWLKLDKKVSAQeVRKENPLQFKFRAKFY 129
Cdd:cd17194  16 FKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLADDStDNPRWLDPNKPIRKQ-LKRGSPHNLNFRVKFF 83
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 345-497 5.08e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 5.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKE----ELMLRLQDYEEKTKKAERELSEQIQRALQLE 420
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaETRDELKDYREKLEKLKREINELKRELDRLQ 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     421 EERKRAQEEAERLEADRMAALRAKEELE---RQAVDQIKSQE----QLAAELAEYTAKIALLEEARRRKEDEVEEWQHR- 492
Cdd:TIGR02169  413 EELQRLSEELADLNAAIAGIEAKINELEeekEDKALEIKKQEwkleQLAADLSKYEQELYDLKEEYDRVEKELSKLQREl 492


                   ....*.
gi 7328175     493 -AKEAQ 497
Cdd:TIGR02169  493 aEAEAQ 498
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 345-506 5.35e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 5.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  425 RAQEE-AERLEA-------------------------------------DRMAALRA-KEELERQAVDQIKSQEQLAAEL 465
Cdd:COG4942 101 AQKEElAELLRAlyrlgrqpplalllspedfldavrrlqylkylaparrEQAEELRAdLAELAALRAELEAERAELEALL 180

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7328175  466 AEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEE 506
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 357-626 5.96e-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: 49.35  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    357 KHQKQL-ERQQLET-EKKRRETVEREKEQMMREKE--------------ELMLRLQDYEEKTKKA---ERELSEQIQRAL 417
Cdd:pfam17380 279 QHQKAVsERQQQEKfEKMEQERLRQEKEEKAREVErrrkleeaekarqaEMDRQAAIYAEQERMAmerERELERIRQEER 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    418 QLEEERKRAQEEAerLEADRMaalrakEELERQAVDQIKSQEQLAAELaEYTAKIALLEEARRRK----EDEVEEWQHRA 493
Cdd:pfam17380 359 KRELERIRQEEIA--MEISRM------RELERLQMERQQKNERVRQEL-EAARKVKILEEERQRKiqqqKVEMEQIRAEQ 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    494 KEAQDDLVKTKEElhlvMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKR--ITEAEKNERv 571
Cdd:pfam17380 430 EEARQREVRRLEE----ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkILEKELEER- 504

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 7328175    572 QRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQgntKQRIDE 626
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE---RRRIQE 556
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 245-332 7.43e-06

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


Pssm-ID: 270005  Cd Length: 94  Bit Score: 44.62  E-value: 7.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  245 YGINYFEIKNKKGTDLWLGVDALGLNIYEkdDKLtpKIG-FPWSEIRNISFNDKKFVIK----PIDKKAPDFVFYAPRLR 319
Cdd:cd13184   1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYR--DRL--RINrFAWPKVLKISYKRNNFYIKirpgEFEQYETTIGFKLPNHR 76

                        90
                ....*....|...
gi 7328175  320 INKRILQLCMGNH 332
Cdd:cd13184  77 AAKRLWKVCVEHH 89
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 376-507 9.90e-06

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: 47.23  E-value: 9.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  376 TVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAErleadrmaALRAKEELERQAVDQI 455
Cdd:COG1579  14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE--------EVEARIKKYEEQLGNV 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7328175  456 KSQEQLAA---ELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEEL 507
Cdd:COG1579  86 RNNKEYEAlqkEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL 140
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 245-337 1.07e-05

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


Pssm-ID: 270009  Cd Length: 91  Bit Score: 44.20  E-value: 1.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  245 YGINYFEIKNKKGTDLWLGVDALGlnIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPdFVFYAPRLRINKRI 324
Cdd:cd13188   1 YGEESFPAKDEQGNEVLIGASLEG--IFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEET-VQFQFEDAETAKYV 77

                        90
                ....*....|...
gi 7328175  325 LQLCMGNHELYMR 337
Cdd:cd13188  78 WKLCVLQHKFYRQ 90
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 57-129 1.73e-05

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


Pssm-ID: 340620  Cd Length: 86  Bit Score: 43.45  E-value: 1.73e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7328175   57 DAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGF---PTWLKLDKKVSAQeVRKENPLQFKFRAKFY 129
Cdd:cd17100  11 DTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPAtdsMRWLDPLKPIRKQ-IKGGPPYYLNFRVKFY 85
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
338-609 2.06e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   338 RRKPDTIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVER------------EKEQMMREKEELMLRLQDYEEKTK 403
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRlaeyswdeidvaSAEREIAELEAELERLDASSDDLA 688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   404 KAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVD-QIKSQEQLAAELAEYtakiaLLEEARRRK 482
Cdd:COG4913  689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEER-----FAAALGDAV 763

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   483 EDEVEEW-QHRAKEAQDDLVKTKEELHLVMTAppppPPPVYEPVSYHVQESLQDEGAeptgYSAELSSegIRDDR--NEE 559
Cdd:COG4913  764 ERELRENlEERIDALRARLNRAEEELERAMRA----FNREWPAETADLDADLESLPE----YLALLDR--LEEDGlpEYE 833

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 7328175   560 KRITEAeKNERVQRQLLTLSSELSQARDENKRTHNDIihNENMRQ---GRDKY 609
Cdd:COG4913  834 ERFKEL-LNENSIEFVADLLSKLRRAIREIKERIDPL--NDSLKRipfGPGRY 883
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 336-471 2.10e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.81  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    336 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMM-REKEELMLRLQDYEEKTKKAERELSEQiQ 414
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILeKELEERKQAMIEEERKRKLLEKEMEER-Q 526

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7328175    415 RALQLEEERKRAQEEAERL------------------EADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAK 471
Cdd:pfam17380 527 KAIYEEERRREAEEERRKQqemeerrriqeqmrkateERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 338-481 2.20e-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: 47.15  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    338 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRREtVEREKEQMMRE---KEELMLRLQDYEEKTKKAERELSEQIQ 414
Cdd:TIGR02794  83 QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ-AEEAKAKQAAEakaKAEAEAERKAKEEAAKQAEEEAKAKAA 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7328175    415 RALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRR 481
Cdd:TIGR02794 162 AEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERK 228
PRK12704 PRK12704
phosphodiesterase; Provisional
 350-506 2.97e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   350 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELmlrlqdyEEKTKKAERELSEQIQRALQLEEERKRAQEE 429
Cdd:PRK12704  32 KIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-------EKELRERRNELQKLEKRLLQKEENLDRKLEL 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175   430 AERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALL--EEARRRKEDEVEEwqhRAKEAQDDLVKTKEE 506
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLtaEEAKEILLEKVEE---EARHEAAVLIKEIEE 180
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 339-506 3.53e-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: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     339 RKPDTIEVQQMKAQAREEKhqkqlERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSE------- 411
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEK-----LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlsh 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     412 ----QIQRALQ-LEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEV 486
Cdd:TIGR02169  791 sripEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                          170       180
                   ....*....|....*....|
gi 7328175     487 EEWQHRAKEAQDDLVKTKEE 506
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKE 890
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 342-461 3.77e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.74  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   342 DTIEVQQMKAqaREEKHQKQLERQQLETEKKRRET------VEREKEQMMREKEELMLRL-QDYEEKTKKAERELSEQIQ 414
Cdd:PRK00409 514 DKEKLNELIA--SLEELERELEQKAEEAEALLKEAeklkeeLEEKKEKLQEEEDKLLEEAeKEAQQAIKEAKKEADEIIK 591

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 7328175   415 RALQLEEERKRAQEEAERLEADRmaALR-AKEELERQAVDQIKSQEQL 461
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARK--RLNkANEKKEKKKKKQKEKQEEL 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 360-488 3.98e-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: 3.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     360 KQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELseqiqraLQLEEERKRAQEEAERLEADRMA 439
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-------RDLESRLGDLKKERDELEAQLRE 900

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 7328175     440 ALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEE 488
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 345-451 3.99e-05

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 44.26  E-value: 3.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDyEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:pfam05672  30 EEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAE-EEAEEREQREQEEQERLQKQKEEAEA 108

                          90       100
                  ....*....|....*....|....*..
gi 7328175    425 RAQEEAERLEADRmAALRAKEELERQA 451
Cdd:pfam05672 109 KAREEAERQRQER-EKIMQQEEQERLE 134
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 395-497 4.20e-05

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: 45.06  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    395 LQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAAL-RAKEELERQAVDQIKSQEQLAAEL-------- 465
Cdd:pfam04012  31 IRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALtKGNEELAREALAEKKSLEKQAEALetqlaqqr 110

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 7328175    466 ---AEYTAKIALLEEARRRKEDEVEEWQHRAKEAQ 497
Cdd:pfam04012 111 savEQLRKQLAALETKIQQLKAKKNLLKARLKAAK 145
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 345-488 4.56e-05

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


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 45.90  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    345 EVQQMKAQAREEKHQKQLERQQLETEKKRREtverekEQMMREKEELMLRLQDYEEkTKKAERELSEQIQRAL-QLEEER 423
Cdd:pfam09787  51 ELRQERDLLREEIQKLRGQIQQLRTELQELE------AQQQEEAESSREQLQELEE-QLATERSARREAEAELeRLQEEL 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7328175    424 KRAQEEAERLEADRMAALRAKE-ELERQAvDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEE 488
Cdd:pfam09787 124 RYLEEELRRSKATLQSRIKDREaEIEKLR-NQLTSKSQSSSSQSELENRLHQLTETLIQKQTMLEA 188
PTZ00121 PTZ00121
MAEBL; Provisional
 344-626 4.66e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    344 IEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAlqleEER 423
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA----EEK 1289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    424 KRAQEEAERLEADRMAALRAKEELERQAvDQIKSQEQLAAELAEYTAKIAllEEARrrKEDEVEewQHRAKEAQDDLVKT 503
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKKKA--EEAK--KAAEAA--KAEAEAAADEAEAA 1362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    504 KEELHLVMTAPPPPPPPVyEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELS 583
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKA-DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 7328175    584 QAR--DENKRTHNDIIHNENM-RQGRDKYKTLRQIRQGNTKQRIDE 626
Cdd:PTZ00121 1442 EAKkaDEAKKKAEEAKKAEEAkKKAEEAKKADEAKKKAEEAKKADE 1487
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 357-505 4.99e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.71  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     357 KHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQ-------DYEEKTKKAERELSEQIQRALQLEEERKRAQ 427
Cdd:pfam01576  549 RLQRELEalTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsNLEKKQKKFDQMLAEEKAISARYAEERDRAE 628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     428 EEAERLEADRMA-------ALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDL 500
Cdd:pfam01576  629 AEAREKETRALSlaraleeALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL 708


                   ....*
gi 7328175     501 VKTKE 505
Cdd:pfam01576  709 QATED 713
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 333-450 5.10e-05

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


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 45.08  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    333 ELYMRRRKPDTIEVQQMKA-----QAREEKHQKQLERQQLETEKKRRETVEREK------EQMMREKEELmlRLQDYEEK 401
Cdd:pfam13904  38 LTYARKLEGLKLERQPLEAyenwlAAKQRQRQKELQAQKEEREKEEQEAELRKRlakekyQEWLQRKARQ--QTKKREES 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7328175    402 TKKAERELS-------------EQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQ 450
Cdd:pfam13904 116 HKQKAAESAskslakperkvsqEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQERK 177
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
339-504 5.48e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 5.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  339 RKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQ 418
Cdd:COG4372  19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  419 LEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQD 498
Cdd:COG4372  99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178


                ....*.
gi 7328175  499 DLVKTK 504
Cdd:COG4372 179 AEAEQA 184
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 342-490 6.41e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 6.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  342 DTIEVQQMKAQAREEKHQKQLERQQlETEKKRRETVEREKEQMMREK---------------EELMLRLQDYEEKTKKAE 406
Cdd:COG3883  54 NELQAELEALQAEIDKLQAEIAEAE-AEIEERREELGERARALYRSGgsvsyldvllgsesfSDFLDRLSALSKIADADA 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  407 RELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEV 486
Cdd:COG3883 133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212


                ....
gi 7328175  487 EEWQ 490
Cdd:COG3883 213 AAAA 216
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 343-500 6.56e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 6.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  343 TIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAEREL----SEQIQRA 416
Cdd:COG1579  14 ELDSELDRLEHRLKELPAELAelEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKEYEA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  417 LQLEEER-KRAQEEAERLEADRMAALRAKEELERQAvdqiksQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKE 495
Cdd:COG1579  94 LQKEIESlKRRISDLEDEILELMERIEELEEELAEL------EAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167


                ....*
gi 7328175  496 AQDDL 500
Cdd:COG1579 168 LAAKI 172
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 350-478 6.72e-05

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


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 45.90  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    350 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLqdyEEKTKKAERELSEQIQRALQ---------LE 420
Cdd:pfam09731 291 HAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARL---EEVRAADEAQLRLEFEREREeiresyeekLR 367

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7328175    421 EERKRAQEEAErlEADRMAALRAKEELERQAVDQIKS-----QEQLAAELAEYTAKIALLEEA 478
Cdd:pfam09731 368 TELERQAEAHE--EHLKDVLVEQEIELQREFLQDIKEkveeeRAGRLLKLNELLANLKGLEKA 428
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 340-506 6.76e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 6.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  340 KPDTIEVQQMKAQAREEKHQKQLER--QQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQ----- 412
Cdd:COG3883  24 ELSELQAELEAAQAELDALQAELEElnEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvs 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  413 --------------IQRALQLE-------EERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAK 471
Cdd:COG3883 104 yldvllgsesfsdfLDRLSALSkiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183

                       170       180       190
                ....*....|....*....|....*....|....*
gi 7328175  472 IALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEE 506
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 351-500 6.97e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 6.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  351 AQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEA 430
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  431 ERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARrrkEDEVEEWQHRAKEAQDDL 500
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE---PPDLEELERELERLEREI 776
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 350-454 7.85e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 46.10  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    350 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEqiqraLQLEEERKRAQEE 429
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQ-----LQEKAAETSQERK 215

                          90       100
                  ....*....|....*....|....*..
gi 7328175    430 AERLEADRMAA--LRAKEELERQAVDQ 454
Cdd:PRK11448  216 QKRKEITDQAAkrLELSEEETRILIDQ 242
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
345-597 8.79e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 8.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:COG4372  39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  425 RAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKED-----EVEEWQHRAKEAQDD 499
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEaeaeqALDELLKEANRNAEK 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  500 LVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLS 579
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278

                       250
                ....*....|....*...
gi 7328175  580 SELSQARDENKRTHNDII 597
Cdd:COG4372 279 EIAALELEALEEAALELK 296
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 354-435 1.04e-04

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


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 44.53  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    354 REEKHQKQLERQQLETEKKRRETVEREKEQMM--REKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAE 431
Cdd:pfam15991  20 RERERKKQEQEAKMEEERLRREREEREKEDRMtlEETKEQILKLEKKLADLKEEKHQLFLQLKKVLHEDETRKRQLKEQS 99


                  ....
gi 7328175    432 RLEA 435
Cdd:pfam15991 100 ELFA 103
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
342-486 1.44e-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: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   342 DTIEVQQMKAQAREEKHQKQLER---QQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQ 418
Cdd:COG4913  312 ERLEARLDALREELDELEAQIRGnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175   419 LEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKI-ALLEEARRRKEDEV 486
Cdd:COG4913  392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrDALAEALGLDEAEL 460
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 378-586 1.56e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  378 EREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAA----LRAKEELERQAVD 453
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeiEERREELGERARA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  454 QIKSQEQL--------AAELAEYTAKIALLE---EARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPpppvy 522
Cdd:COG3883  95 LYRSGGSVsyldvllgSESFSDFLDRLSALSkiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----- 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7328175  523 epvsyhvQESLQDEGAEPTGYSAELSSEgiRDDRNEEKRITEAEKNERVQRQLLTLSSELSQAR 586
Cdd:COG3883 170 -------KAELEAQQAEQEALLAQLSAE--EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 52-112 1.66e-04

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


Pssm-ID: 340712  Cd Length: 87  Bit Score: 40.78  E-value: 1.66e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7328175   52 RVTTMDAE-LEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQ 112
Cdd:cd17192   7 RIQLLNNEfVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQ 68
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 425-592 2.03e-04

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


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 43.95  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    425 RAQEEAERLEADRMAALRAKEELERqavdQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTK 504
Cdd:pfam00529  55 DYQAALDSAEAQLAKAQAQVARLQA----ELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRR 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    505 eelhlvmtapppppppVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNER--------VQRQLL 576
Cdd:pfam00529 131 ----------------VLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAevrselsgAQLQIA 194

                         170
                  ....*....|....*.
gi 7328175    577 TLSSELSQARDENKRT 592
Cdd:pfam00529 195 EAEAELKLAKLDLERT 210
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
355-488 2.10e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   355 EEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAER---ELSEQIQRALQLEEERKRAQEEAE 431
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEErikELEEKEERLEELKKKLKELEKRLE 355

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175   432 RLEADRMAALRAKEELERqavdqiksQEQLAAELAEYTAK--IALLEEARRRKEdEVEE 488
Cdd:PRK03918 356 ELEERHELYEEAKAKKEE--------LERLKKRLTGLTPEklEKELEELEKAKE-EIEE 405
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
345-483 2.77e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEK------KRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQ 418
Cdd:COG4717  99 ELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE 178

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175  419 LEEERKRAQEEAE-RLE--ADRMAALRAKEELERQAVDQIKSQ-EQLAAELAEYTAKIALLEEARRRKE 483
Cdd:COG4717 179 LEELLEQLSLATEeELQdlAEELEELQQRLAELEEELEEAQEElEELEEELEQLENELEAAALEERLKE 247
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
332-466 2.99e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  332 HELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTK-KAERELS 410
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQ 195

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7328175  411 EQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQiKSQEQLAAELA 466
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARL 250
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 360-496 3.29e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    360 KQLERQQLETEKKRRETVEREKEQMmREKEELmlrlqdyeEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMA 439
Cdd:TIGR02794  50 QQANRIQQQKKPAAKKEQERQKKLE-QQAEEA--------EKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7328175    440 AlrakEELERQAvdqikSQEQLAAELAEytAKIALLEEARRRKEDE-----VEEWQHRAKEA 496
Cdd:TIGR02794 121 A----EEAKAKQ-----AAEAKAKAEAE--AERKAKEEAAKQAEEEakakaAAEAKKKAEEA 171
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
337-507 3.65e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   337 RRRKPDTIEVQQMKAQAREEKHQKQLER--------QQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERE 408
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERaedlveaeDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   409 LSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQA--VDQIKSQEQLAAELAEYTAKIALLEEARRRK---- 482
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRtlLAAIADAEDEIERLREKREALAELNDERRERlaek 632

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 7328175   483 ------------EDEVEEWQHRAKEAQDDLVKTKEEL 507
Cdd:PRK02224 633 rerkreleaefdEARIEEAREDKERAEEYLEQVEEKL 669
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 336-436 3.81e-04

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


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 41.32  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    336 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRET-VEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQ 414
Cdd:pfam15236  48 ERKRQKALEHQNAIKKQLEEKERQKKLEEERRRQEEQEEEErLRREREEEQKQFEEERRKQKEKEEAMTRKTQALLQAMQ 127

                          90       100
                  ....*....|....*....|....*
gi 7328175    415 RALQL---EEERKRAQEEAERLEAD 436
Cdd:pfam15236 128 KAQELaqrLKQEQRIRELAEKGHDT 152
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
350-507 4.01e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   350 KAQAREEKHQKQLERQQLETEKKRRETVEREKE-QMMREKEELMLRLQDYEEKTKKAERELSEQIQRalqLEEERKRAQE 428
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR---LEEEINGIEE 328

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175   429 EAERLEADRmaalRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEEL 507
Cdd:PRK03918 329 RIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEI 403
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 401-488 4.04e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 43.13  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   401 KTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAAlrAKE--ELERQAVDqiksQEQLAAELAEYTAKIALLEEA 478
Cdd:PRK05431  15 KEALAKRGFPLDVDELLELDEERRELQTELEELQAERNAL--SKEigQAKRKGED----AEALIAEVKELKEEIKALEAE 88

                         90
                 ....*....|
gi 7328175   479 RRRKEDEVEE 488
Cdd:PRK05431  89 LDELEAELEE 98
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 357-449 4.05e-04

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


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 42.79  E-value: 4.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  357 KHQKQLERQQLETEKKRRETVErEKEQMMREKEELMLRLQDYEEKTKKAERELSEqiqralqLEEERKRAQEEAERLEaD 436
Cdd:COG4026 128 PEYNELREELLELKEKIDEIAK-EKEKLTKENEELESELEELREEYKKLREENSI-------LEEEFDNIKSEYSDLK-S 198

                        90
                ....*....|...
gi 7328175  437 RMAALRAKEELER 449
Cdd:COG4026 199 RFEELLKKRLLEV 211
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 354-471 4.10e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.57  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    354 REEKHQKQLERQQLEteKKRRETVEREKEQmmrekeelmlrlqdyeektkKAERELSEQIQRALQLEEERKRAQEEAERL 433
Cdd:PTZ00266  442 KENAHRKALEMKILE--KKRIERLEREERE--------------------RLERERMERIERERLERERLERERLERDRL 499

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 7328175    434 EADRMaalrakEELERQAVDQIKSQEQLAAELAEYTAK 471
Cdd:PTZ00266  500 ERDRL------DRLERERVDRLERDRLEKARRNSYFLK 531
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 345-465 4.11e-04

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.56  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREK-EQMMREKEELMLRLQDYEEKTKKAERELSEQIQR-ALQLEEE 422
Cdd:cd16269 170 EVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKaEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQlKEKMEEE 249

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7328175  423 RKRAQEEAErleadRMAALRAKEELERQAVDQIKSQEQLAAEL 465
Cdd:cd16269 250 RENLLKEQE-----RALESKLKEQEALLEEGFKEQAELLQEEI 287
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 342-444 4.24e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 4.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  342 DTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAlqlee 421
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL----- 232

                        90       100
                ....*....|....*....|...
gi 7328175  422 eRKRAQEEAERLEADRMAALRAK 444
Cdd:COG4942 233 -EAEAAAAAERTPAAGFAALKGK 254
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 371-467 4.47e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 41.30  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   371 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA-----LQLEEERKRAQEEAERLEAdrmaalRAKE 445
Cdd:PRK05759  34 EERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAkkraaQIIEEAKAEAEAEAARIKA------QAQA 107

                         90       100
                 ....*....|....*....|....*.
gi 7328175   446 ELER---QAVDQIKSQ-EQLAAELAE 467
Cdd:PRK05759 108 EIEQerkRAREELRKQvADLAVAGAE 133
mukB PRK04863
chromosome partition protein MukB;
352-493 7.22e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    352 QAREEKHQKQlERQQLE---TEKKRRETVEREKEQMMRE-----------KEELMLRLQDYEEKTKKAERELSEQIQRAL 417
Cdd:PRK04863  504 RLREQRHLAE-QLQQLRmrlSELEQRLRQQQRAERLLAEfckrlgknlddEDELEQLQEELEARLESLSESVSEARERRM 582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    418 QLEEERKRAQEEAERLEADRMAALRAKEELER------------QAVDQIksQEQLAAELAEYTAKIALLEEARRRKEDE 485
Cdd:PRK04863  583 ALRQQLEQLQARIQRLAARAPAWLAAQDALARlreqsgeefedsQDVTEY--MQQLLERERELTVERDELAARKQALDEE 660


                  ....*...
gi 7328175    486 VEEWQHRA 493
Cdd:PRK04863  661 IERLSQPG 668
PRK12705 PRK12705
hypothetical protein; Provisional
 334-508 7.45e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 42.39  E-value: 7.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   334 LYMRRRKPDTIEVQQMKAQAREEKhqkqlERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQI 413
Cdd:PRK12705  23 VLLKKRQRLAKEAERILQEAQKEA-----EEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   414 QRaLQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKiALLEEARRRKEDEVEEWQHRA 493
Cdd:PRK12705  98 EK-LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAE-LEEEKAQRVKKIEEEADLEAE 175

                        170
                 ....*....|....*
gi 7328175   494 KEAQDDLVKTKEELH 508
Cdd:PRK12705 176 RKAQNILAQAMQRIA 190
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 345-482 7.50e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 7.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETV--EREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEE 422
Cdd:COG1579  53 ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  423 RKRAQEEAERLEADRMAALrakEELERQAVDQIKSQEQLAAELAEYTakIALLEEARRRK 482
Cdd:COG1579 133 LAELEAELEEKKAELDEEL---AELEAELEELEAEREELAAKIPPEL--LALYERIRKRK 187
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 371-454 7.87e-04

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


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 39.99  E-value: 7.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    371 KKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA-----LQLEEERKRAQEEAERLEADRMAAL---- 441
Cdd:pfam00430  29 DKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAkkraeKLKEEIVAAAEAEAERIIEQAAAEIeqek 108

                          90
                  ....*....|....
gi 7328175    442 -RAKEELERQAVDQ 454
Cdd:pfam00430 109 dRALAELRQQVVAL 122
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 336-480 7.87e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 7.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     336 MRRRKPDTIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYE-------------- 399
Cdd:TIGR02169  851 SIEKEIENLNGKKEELEEELEELEAALRdlESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRkrlselkakleale 930

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     400 ------EKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIA 473
Cdd:TIGR02169  931 eelseiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010


                   ....*..
gi 7328175     474 LLEEARR 480
Cdd:TIGR02169 1011 EYEKKKR 1017
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 359-506 8.20e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.52  E-value: 8.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     359 QKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQ-----EEAERL 433
Cdd:pfam12128  662 KQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQlallkAAIAAR 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     434 EADRMAALRA-----KEELERQAVDQIKSQeQLAAELAEYTAKIallEEARRRkEDEVEEW----QHRAKEAQDDLVKTK 504
Cdd:pfam12128  742 RSGAKAELKAletwyKRDLASLGVDPDVIA-KLKREIRTLERKI---ERIAVR-RQEVLRYfdwyQETWLQRRPRLATQL 816


                   ..
gi 7328175     505 EE 506
Cdd:pfam12128  817 SN 818
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 346-443 8.30e-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: 8.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  346 VQQMKAQARE-EKHQKQLERQQLETEKKRRETVEREKEQmMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:COG4942 145 APARREQAEElRADLAELAALRAELEAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223

                        90
                ....*....|....*....
gi 7328175  425 RAQEEAERLEADRMAALRA 443
Cdd:COG4942 224 ELEALIARLEAEAAAAAER 242
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 405-503 8.73e-04

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


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 38.96  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    405 AERELseqiQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAvdqiksQEQLAAELAEYTAKIAllEEARRRKED 484
Cdd:pfam16999  11 AEREA----ALDQQIEAARKEAEREVEAAEAEAARILREAEAKAKAL------QAEYRQELAAETARIR--EEARARAEA 78

                          90
                  ....*....|....*....
gi 7328175    485 EVEEWQHRAKEAQDDLVKT 503
Cdd:pfam16999  79 EAQAVRTRAEGRLQQAVEL 97
PLN02316 PLN02316
synthase/transferase
 399-450 8.90e-04

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 42.55  E-value: 8.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7328175    399 EEKTKKAERELSEQIQRALQLEEERKRAQEEAERlEADRMaalRAKEELERQ 450
Cdd:PLN02316  252 EEKRRELEKLAKEEAERERQAEEQRRREEEKAAM-EADRA---QAKAEVEKR 299
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 352-450 9.18e-04

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.02  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    352 QAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRalqlEEERKRAQEEAE 431
Cdd:pfam05672  22 QAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEA----EEREQREQEEQE 97

                          90       100
                  ....*....|....*....|
gi 7328175    432 RLEADRMAA-LRAKEELERQ 450
Cdd:pfam05672  98 RLQKQKEEAeAKAREEAERQ 117
PTZ00121 PTZ00121
MAEBL; Provisional
 331-626 9.29e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    331 NHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAErels 410
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE---- 1325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    411 EQIQRAlqlEEERKRAQEEAERLEADRMAALRAKEELErqAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQ 490
Cdd:PTZ00121 1326 EAKKKA---DAAKKKAEEAKKAAEAAKAEAEAAADEAE--AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    491 HRAKEAQDDLVKTKEELHLVMTAPPPPPPPvyepvsYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNER 570
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEK------KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 7328175    571 VQRQlltlSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDE 626
Cdd:PTZ00121 1475 AKKK----AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
359-481 9.88e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 9.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  359 QKQLERQQLETEKkRRETVEREKEQMMREKEELMLRLQDYEEKTK--KAERELSEQIQRALQLEEERKRAQEEAERLEAd 436
Cdd:COG3206 163 EQNLELRREEARK-ALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEA- 240

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7328175  437 RMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRR 481
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSAR 285
PTZ00121 PTZ00121
MAEBL; Provisional
 339-454 1.09e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    339 RKPDTIEVQQMKAQAREEKHQKQLE--RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRA 416
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 7328175    417 LQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQ 454
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 317-507 1.10e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.27  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     317 RLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQ 396
Cdd:pfam02463  193 EELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     397 DYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIAlLE 476
Cdd:pfam02463  273 ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI-KR 351

                          170       180       190
                   ....*....|....*....|....*....|.
gi 7328175     477 EARRRKEDEVEEWQHRAKEAQDDLVKTKEEL 507
Cdd:pfam02463  352 EAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 347-496 1.17e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    347 QQMKAQAREEKHQKQLERQQLETEKK---RRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEER 423
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEkaeREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQER 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7328175    424 KRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEA 496
Cdd:pfam13868 218 KERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE 290
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
352-495 1.22e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   352 QAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAE 431
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7328175   432 RLEADRMAALRAKEELErQAVDQIKSQEQLAAELAEytaKIALLEEARRRKEDEVEEWQHRAKE 495
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEE---KIRELEERIEELKKEIEELEEKVKE 284
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 343-435 1.30e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  343 TIEVQQMKAQArEEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELmlrlqdyEEKTKKAERELSEQIQRALQLEEE 422
Cdd:cd16269 199 EIEAERAKAEA-AEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKM-------EEERENLLKEQERALESKLKEQEA 270

                        90
                ....*....|....*
gi 7328175  423 --RKRAQEEAERLEA 435
Cdd:cd16269 271 llEEGFKEQAELLQE 285
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
345-505 1.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEE-----------KTKKAERELsEQI 413
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEakakkeelerlKKRLTGLTP-EKL 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   414 QRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKS-------------QEQLAAELAEYTAKIALLEEARR 480
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgreltEEHRKELLEEYTAELKRIEKELK 469

                        170       180
                 ....*....|....*....|....*
gi 7328175   481 RKEDEVEEWQHRAKEAQDDLVKTKE 505
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESE 494
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 342-485 1.35e-03

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


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 41.25  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    342 DTIEVQQMKAQAReekhqkqleRQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELS---EQIQRALQ 418
Cdd:pfam00529  61 DSAEAQLAKAQAQ---------VARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAqaqIDLARRRV 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7328175    419 LEEE---RKRAQEEAERL----EADRMAALRAKEELERQAVDQIK-SQEQLAAELAEYTAKIALLEEARRRKEDE 485
Cdd:pfam00529 132 LAPIggiSRESLVTAGALvaqaQANLLATVAQLDQIYVQITQSAAeNQAEVRSELSGAQLQIAEAEAELKLAKLD 206
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
345-479 1.36e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERqqlETEKKRRETVEREKEQMMREKEELMlrlqdyEEKTKKAERELSEQIQRalqlEEERK 424
Cdd:COG2268 211 ETEIAIAQANREAEEAELEQ---EREIETARIAEAEAELAKKKAEERR------EAETARAEAEAAYEIAE----ANAER 277

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7328175  425 RAQEEAERLEADRMAALRAKEELERQAvdQIKSQEQLAAElAEYTAKIAlLEEAR 479
Cdd:COG2268 278 EVQRQLEIAEREREIELQEKEAEREEA--ELEADVRKPAE-AEKQAAEA-EAEAE 328
PRK12705 PRK12705
hypothetical protein; Provisional
 338-484 1.39e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.62  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   338 RRKPDTIEVQQMKAQAREEKHQKQLERqqletekKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRAL 417
Cdd:PRK12705  47 EEKLEAALLEAKELLLRERNQQRQEAR-------REREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSAREL 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7328175   418 QLEEERKRAQEEAERL------EADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKED 484
Cdd:PRK12705 120 ELEELEKQLDNELYRVagltpeQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRIASE 192
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 360-506 1.48e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   360 KQLERQQLETEKKRRETVEREKEQMMREkEELMlrlqdyeektkkaERELSEQiQRALQLEEERKRAQ------EEAERL 433
Cdd:PRK09510  62 EQYNRQQQQQKSAKRAEEQRKKKEQQQA-EELQ-------------QKQAAEQ-ERLKQLEKERLAAQeqkkqaEEAAKQ 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7328175   434 EADR-----MAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEE 506
Cdd:PRK09510 127 AALKqkqaeEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 255-328 1.50e-03

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


Pssm-ID: 275390  Cd Length: 89  Bit Score: 38.15  E-value: 1.50e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175  255 KKGTDLWLGVDALGLnIYEKDDKLTPKIGFPWSEIRNISFND-----KKFVIKPIDkKAPDFVFYAPRLRINKRILQLC 328
Cdd:cd00900  13 TKRVEGTLYITSDRL-ILRDKNDGGLELSIPISDIVNVNVSPqgpssRYLVLVLKD-RGEFVGFSFPKEEDAIEISDAL 89
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
368-506 1.63e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  368 ETEKKRRETVEREKEQMMREKEelmlRLQDYEEKTKKAERELSE--QIQRALQLEEERKRAQEEAERLEADRMAALrAKE 445
Cdd:COG2268 199 RDARIAEAEAERETEIAIAQAN----REAEEAELEQEREIETARiaEAEAELAKKKAEERREAETARAEAEAAYEI-AEA 273

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7328175  446 ELERQAvdqiksqeQLAAELAEYTAKIAlLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEE 506
Cdd:COG2268 274 NAEREV--------QRQLEIAEREREIE-LQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 365-477 1.74e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  365 QQLETEKKRRETVEREKEQMMREKEELML-RLQDYEEKTKKAERELSEqiqralqleeerKRAQEEAERLEADRMAALra 443
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFeRLAELRDELAELEEELEA------------LKARWEAEKELIEEIQEL-- 476

                        90       100       110
                ....*....|....*....|....*....|....
gi 7328175  444 KEELERQAVDQIKSQEQLAAELAEYTAKIALLEE 477
Cdd:COG0542 477 KEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 348-497 1.87e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    348 QMKAQAREEKhQKQLERQQLETEKKRRETVEREKEQMMREKEELM-------LRLQDYEEKTKKAERELSEQIQRALQLE 420
Cdd:pfam13868 115 QAEAEEKLEK-QRQLREEIDEFNEEQAEWKELEKEEEREEDERILeylkekaEREEEREAEREEIEEEKEREIARLRAQQ 193

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7328175    421 EERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQ 497
Cdd:pfam13868 194 EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQ 270
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 375-495 2.03e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 2.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  375 ETVEREKEQMMREKEELmlrlqdyeektKKAERELSEQiqRALQLEEERKRAQEEAErleadrmaALRAKEELERQAVDQ 454
Cdd:COG0542 414 DELERRLEQLEIEKEAL-----------KKEQDEASFE--RLAELRDELAELEEELE--------ALKARWEAEKELIEE 472

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7328175  455 IKSqeqLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKE 495
Cdd:COG0542 473 IQE---LKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 361-508 2.06e-03

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    361 QLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRalqLEEERKRAQEEAERLEADRMAA 440
Cdd:pfam07888  30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE---LKEELRQSREKHEELEEKYKEL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    441 LRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEA--------------QDDLVKTKEE 506
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeeaerkqlQAKLQQTEEE 186


                  ..
gi 7328175    507 LH 508
Cdd:pfam07888 187 LR 188
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 347-454 2.11e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.09  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    347 QQMKAQAREEKHQKQLERQQleteKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRalQLEEERKRA 426
Cdd:pfam15709 418 QERARQQQEEFRRKLQELQR----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ--KQEAEEKAR 491

                          90       100
                  ....*....|....*....|....*...
gi 7328175    427 QEEAERLEADRMAALRAKEELERQAVDQ 454
Cdd:pfam15709 492 LEAEERRQKEEEAARLALEEAMKQAQEQ 519
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 347-498 2.19e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.67  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    347 QQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRA 426
Cdd:pfam13868 173 AEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRL 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7328175    427 QEEAERLEADRMAALRAKEELERQavDQIKSQEQLAAELAEYTAKIALLEEARRRK----EDEVEEWQHRAKEAQD 498
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEI--EQEEAEKRRMKRLEHRRELEKQIEEREEQRaaerEEELEEGERLREEEAE 326
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
347-508 2.23e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  347 QQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQmmREKEELMLRLQDYEEKTKKAERELSEQIQRAlQLEEERKRA 426
Cdd:COG4717 361 EELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEELLEALDEE-ELEEELEEL 437

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  427 QEEAERLEADRMAALRAKEELErQAVDQIKSQEQLAAELAEYtakiallEEARRRKEDEVEEWQhRAKEAQDDLVKTKEE 506
Cdd:COG4717 438 EEELEELEEELEELREELAELE-AELEQLEEDGELAELLQEL-------EELKAELRELAEEWA-ALKLALELLEEAREE 508


                ..
gi 7328175  507 LH 508
Cdd:COG4717 509 YR 510
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
396-597 2.33e-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: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   396 QDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEaDRMAALRAKEELERQAVDqiksQEQLAAELAEYTAKIALL 475
Cdd:COG4913  606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEID----VASAEREIAELEAELERL 680

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   476 EEArrrkEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPvyepvsyhvQESLQDEGAEPTGYSAELSSEGIRDD 555
Cdd:COG4913  681 DAS----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE---------LEQAEEELDELQDRLEAAEDLARLEL 747

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 7328175   556 RNE-EKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDII 597
Cdd:COG4913  748 RALlEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 62-129 2.35e-03

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


Pssm-ID: 340713  Cd Length: 84  Bit Score: 37.53  E-value: 2.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175   62 FAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNK-GFPTWLKLDKKVSAQeVRKENPLQFKFRAKFY 129
Cdd:cd17193  16 FKVNKQDTGQVLLDMAYNHLGLTEREYFGLQHNEDSvDSPRWLEPSKPIRKQ-LKGGFPCSLHFRVRFF 83
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 333-463 2.62e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    333 ELYMRRRKPDTIEVQQMKAQAREEKHQKQLER-------------QQLETEKKRRETVEREK---EQMMREK-----EEL 391
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELeqqrrfeeirlrkQRLEEERQRQEEEERKQrlqLQAAQERarqqqEEF 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    392 MLRLQDYE-----EKTKKAERELSEQIQRALQLEEERKR---------------AQEEAERLEADRMAALRAKEELERQA 451
Cdd:pfam15709 429 RRKLQELQrkkqqEEAERAEAEKQRQKELEMQLAEEQKRlmemaeeerleyqrqKQEAEEKARLEAEERRQKEEEAARLA 508

                         170
                  ....*....|..
gi 7328175    452 VDQIKSQEQLAA 463
Cdd:pfam15709 509 LEEAMKQAQEQA 520
Ermin pfam20491
Ermin; This is a cytoskeletal protein exclusively expressed in oligodendrocytes that plays a ...
 424-630 2.65e-03

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


Pssm-ID: 466640 [Multi-domain]  Cd Length: 284  Bit Score: 40.21  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    424 KRAQEEAERLEA---------DRMAALRAKEEL--ERQAVDQIKSQEQLAAEL----AEYTAKIALL---EEARRRKEDE 485
Cdd:pfam20491  55 KGSQEERRKLQGnmllnssmeDKMLKENPEEKLfiVHKAITDLSLQETSADEMtfreGHQWEKIPLSgsnQEIRRQKERI 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    486 VEEwqhRAKEAQDDLVKTKEElhlvmTAPPPPPPPVYEPVSYHVQESLQDEgaEPTGYSAELSSE---GIRDDRNEEKRI 562
Cdd:pfam20491 135 TEQ---PLKEEEDEDRKNKGH-----QAAEIEWLGFRKPSQADMLHSKHDE--EQKVWDEEIDDDdddNCNNDEDEVRVI 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    563 TEAEKNERVQR--------QLLTLSSELSQARDENKR----THNDIIHNENMRQGRDKYktlRQIRQGNTKQRIDEFEAL 630
Cdd:pfam20491 205 EFKKKHEEVSQfkeegdasEDSPLSSASSQAVTPDEQptlgKKSDISRNAYSRYNTISY---RKIRKGNTKQRIDEFESM 281
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 361-500 2.87e-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: 41.09  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   361 QLERQQLETEKKRRETVEREKEqMMREKEELMLRLQDYEEKTKKAERELSeQIQRALQLEEERKRAQEE----AERLEAD 436
Cdd:COG3096  289 ELRRELFGARRQLAEEQYRLVE-MARELEELSARESDLEQDYQAASDHLN-LVQTALRQQEKIERYQEDleelTERLEEQ 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   437 RMAALRAKEELER---------QAVDQIKSQeqlaaeLAEY--------TAKIAL------LEEARRRKE------DEVE 487
Cdd:COG3096  367 EEVVEEAAEQLAEaearleaaeEEVDSLKSQ------LADYqqaldvqqTRAIQYqqavqaLEKARALCGlpdltpENAE 440

                        170
                 ....*....|...
gi 7328175   488 EWQHRAKEAQDDL 500
Cdd:COG3096  441 DYLAAFRAKEQQA 453
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
343-497 2.89e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  343 TIEVQQMkAQAREEKHQKQLERQQLETekkRRETVEREKEQMMREKEELML--RLQDYEEKTKKAERELSE--------- 411
Cdd:COG3206 215 KLLLQQL-SELESQLAEARAELAEAEA---RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAElsarytpnh 290

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  412 -QIQRAL-QLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEW 489
Cdd:COG3206 291 pDVIALRaQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370


                ....*...
gi 7328175  490 QHRAKEAQ 497
Cdd:COG3206 371 LQRLEEAR 378
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 382-470 2.89e-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: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  382 EQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAV---DQIKSQ 458
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEeleALIARL 232

                        90
                ....*....|..
gi 7328175  459 EQLAAELAEYTA 470
Cdd:COG4942 233 EAEAAAAAERTP 244
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 363-462 3.02e-03

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


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.77  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   363 ERQQLETEKKRRETVEREKEQMMREK--------EELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAE--R 432
Cdd:NF033838 303 EKKVAEAEKKVEEAKKKAKDQKEEDRrnyptntyKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVEskK 382

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 7328175   433 LEADRMAAL-----RAKEELERQAVDQIKSQEQLA 462
Cdd:NF033838 383 AEATRLEKIktdrkKAEEEAKRKAAEEDKVKEKPA 417
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 397-623 3.21e-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: 40.59  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     397 DYEEKTKKAERELSeQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIK-SQEQLAAEL-AEYTAKIAL 474
Cdd:pfam12128  594 EWAASEEELRERLD-KAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARlDLRRLFDEKqSEKDKKNKA 672

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     475 LEEARRRKEDEVEEWQHRAK----EAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSyhVQESLQDEG--AEPTGYSAELS 548
Cdd:pfam12128  673 LAERKDSANERLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALD--AQLALLKAAiaARRSGAKAELK 750

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7328175     549 SEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQ-ARDENKRTHNDIIHNENMRQGRDKYKTlrQIRQGNTKQR 623
Cdd:pfam12128  751 ALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERiAVRRQEVLRYFDWYQETWLQRRPRLAT--QLSNIERAIS 824
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
345-473 3.35e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 3.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  345 EVQQMKAQAREEKHQKQLERQQ---LETEKKRR------ETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQR 415
Cdd:COG2268 245 ELAKKKAEERREAETARAEAEAayeIAEANAERevqrqlEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE 324

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7328175  416 A-LQLEEERKRAQEEAERLEAdrMAAlrAKEELERQAVDQ--IKSQEQLAAELAEYTAKIA 473
Cdd:COG2268 325 AeAEAEAIRAKGLAEAEGKRA--LAE--AWNKLGDAAILLmlIEKLPEIAEAAAKPLEKID 381
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 345-483 3.39e-03

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.02  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERK 424
Cdd:pfam15558  43 KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRK 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 7328175    425 RAQEEaerleadrmaALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKE 483
Cdd:pfam15558 123 QCQEQ----------RLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQE 171
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 345-507 3.48e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    345 EVQQMKAQAREE--KHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKA------ERELSEQIQRA 416
Cdd:pfam13868  30 EKKRIKAEEKEEerRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyeeklqEREQMDEIVER 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    417 LQLEEERKRAQ--EEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAE-LAEYTAKIALLEEARRRKEDEVEEWQHRA 493
Cdd:pfam13868 110 IQEEDQAEAEEklEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEyLKEKAEREEEREAEREEIEEEKEREIARL 189

                         170
                  ....*....|....
gi 7328175    494 KEAQDDLVKTKEEL 507
Cdd:pfam13868 190 RAQQEKAQDEKAER 203
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 334-498 3.55e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     334 LYMRRRKPDTIEVQQMKAQAREEKHQ-----KQLERQQLETEKKRRETvEREKEQMMREKEELMLRLQDYEEKTKKAERE 408
Cdd:pfam15921  314 MYMRQLSDLESTVSQLRSELREAKRMyedkiEELEKQLVLANSELTEA-RTERDQFSQESGNLDDQLQKLLADLHKREKE 392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     409 LS---EQIQR--------ALQLEEERKRAQE---EAERLEA--------------DRMAALRAK-EELERQA--VDQIKS 457
Cdd:pfam15921  393 LSlekEQNKRlwdrdtgnSITIDHLRRELDDrnmEVQRLEAllkamksecqgqmeRQMAAIQGKnESLEKVSslTAQLES 472

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 7328175     458 -QEQLAAELAEYTAKIALLEEARRRKEDEVEEWQ--HRAKEAQD 498
Cdd:pfam15921  473 tKEMLRKVVEELTAKKMTLESSERTVSDLTASLQekERAIEATN 516
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 360-453 3.69e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 3.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  360 KQLERQ--QLETEKkrrETVEREKEQMMREK-EELMLRLQDYEEKTK------KAERELSEQIQRALQLEEERKRAQEEA 430
Cdd:COG0542 414 DELERRleQLEIEK---EALKKEQDEASFERlAELRDELAELEEELEalkarwEAEKELIEEIQELKEELEQRYGKIPEL 490

                        90       100
                ....*....|....*....|...
gi 7328175  431 ERLEADRMAALRAKEELERQAVD 453
Cdd:COG0542 491 EKELAELEEELAELAPLLREEVT 513
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 339-500 4.15e-03

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


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 39.24  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    339 RKPDTIEVQQMKAQAREEKHQKQLERqqletEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQ 418
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEE-----AEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    419 LEEERK----RAQEEAERLeadrmaalrakEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAK 494
Cdd:pfam00261  76 SERGRKvlenRALKDEEKM-----------EILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIV 144


                  ....*.
gi 7328175    495 EAQDDL 500
Cdd:pfam00261 145 ELEEEL 150
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 336-505 4.33e-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: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     336 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRL----QDYEEKTKKAERELSE 411
Cdd:pfam01576    7 MQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLaarkQELEEILHELESRLEE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     412 QIQRALQLEEERKRAQEEAERLEA--DRMAALRAKEELERQAVDqiksqeqlaAELAEYTAKIALLEEARRRKEDEVEEW 489
Cdd:pfam01576   87 EEERSQQLQNEKKKMQQHIQDLEEqlDEEEAARQKLQLEKVTTE---------AKIKKLEEDILLLEDQNSKLSKERKLL 157

                          170
                   ....*....|....*.
gi 7328175     490 QHRAKEAQDDLVKTKE 505
Cdd:pfam01576  158 EERISEFTSNLAEEEE 173
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 411-512 4.49e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 4.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  411 EQIQRAL-QLEEERKRAQEEAERLEADRMAALRAKEElerqavdqiKSQEQLAAELAEYTAKIALLEEARRRKEdEVEEW 489
Cdd:COG0542 414 DELERRLeQLEIEKEALKKEQDEASFERLAELRDELA---------ELEEELEALKARWEAEKELIEEIQELKE-ELEQR 483

                        90       100
                ....*....|....*....|...
gi 7328175  490 QHRAKEAQDDLVKTKEELHLVMT 512
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAP 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-507 4.88e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     317 RLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQARE--EKHQKQLERQQLETEKKRREtVEREKEQMMREKEELMLR 394
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdiESLAAEIEELEELIEELESE-LEALLNERASLEEALALL 892

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     395 LQDYEEKTKKaERELSEQIQRALQ----LEEERKRAQEEAERLEADRM---AALRAKEELERQAVDQIK-----SQEQLA 462
Cdd:TIGR02168  893 RSELEELSEE-LRELESKRSELRReleeLREKLAQLELRLEGLEVRIDnlqERLSEEYSLTLEEAEALEnkiedDEEEAR 971

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 7328175     463 AELAEYTAKIALLEEARRRKEDEVEEWQHR---AKEAQDDLVKTKEEL 507
Cdd:TIGR02168  972 RRLKRLENKIKELGPVNLAAIEEYEELKERydfLTAQKEDLTEAKETL 1019
PTZ00121 PTZ00121
MAEBL; Provisional
 356-603 5.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    356 EKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRL-QDYEEKTKKAERELSE-QIQRALQLEEERKRAQEEAERL 433
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVgQDEGLKPSYKDFDFDAkEDNRADEATEEAFGKAEEAKKT 1106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    434 EADRMAALRAKEELERQAVDQIKSQEQLAAELAEYtakialLEEARRRKEDEVEEWQHRAKEAQD-DLVKTKEELHLVMT 512
Cdd:PTZ00121 1107 ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK------AEEARKAEDAKRVEIARKAEDARKaEEARKAEDAKKAEA 1180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    513 APPPPPPPVYEPVSyHVQESLQDEGAEPtgYSAELSSEGIRdDRNEEKRITEAEKNERVQRQlltlssELSQARDENKRT 592
Cdd:PTZ00121 1181 ARKAEEVRKAEELR-KAEDARKAEAARK--AEEERKAEEAR-KAEDAKKAEAVKKAEEAKKD------AEEAKKAEEERN 1250

                         250
                  ....*....|.
gi 7328175    593 HNDIIHNENMR 603
Cdd:PTZ00121 1251 NEEIRKFEEAR 1261
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 362-458 5.41e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    362 LERQQLETEK----KRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADR 437
Cdd:TIGR04523 554 LKKENLEKEIdeknKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633

                          90       100
                  ....*....|....*....|.
gi 7328175    438 MAALRAKEELERQaVDQIKSQ 458
Cdd:TIGR04523 634 KNIKSKKNKLKQE-VKQIKET 653
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 352-497 5.44e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.72  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    352 QAREEKHQKQLE--RQQLETEKK---RRETVEREKEQMmrekEELMLRLQDYEEKTKKAERELSEQIQRA---LQLEEER 423
Cdd:pfam05557  13 QLQNEKKQMELEhkRARIELEKKasaLKRQLDRESDRN----QELQKRIRLLEKREAEAEEALREQAELNrlkKKYLEAL 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7328175    424 KRAQEEAERLEADrmaalrakeelERQAVDQIKSqeqlaaELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQ 497
Cdd:pfam05557  89 NKKLNEKESQLAD-----------AREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLK 145
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
407-507 5.73e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  407 RELSEQIQRALQLEEERKRAQEEAERLEAdRMAALRAKE----------ELERQAVDQIKSQEQLAAELAEYTAKIALLE 476
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEE-ELEELEAELeelreeleklEKLLQLLPLYQELEALEAELAELPERLEELE 152

                        90       100       110
                ....*....|....*....|....*....|.
gi 7328175  477 EarrrKEDEVEEWQHRAKEAQDDLVKTKEEL 507
Cdd:COG4717 153 E----RLEELRELEEELEELEAELAELQEEL 179
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 359-477 5.82e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 38.48  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    359 QKQLERQQLETEKKR-RETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQiqRALQLEEERKRAQEEAERleadr 437
Cdd:pfam09756   5 AKKRAKLELKEAKRQqREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEE--ERKQEEEQERKEQEEYEK----- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 7328175    438 maaLRAKEELERQAVDQIKS--QEQLAAELAEY--TAKIALLEE 477
Cdd:pfam09756  78 ---LKSQFVVEEEGTDKLSAedESQLLEDFINYikLKKVVLLEE 118
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 350-506 6.20e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 39.60  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    350 KAQAREEKHQKQLErqqLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEErkRAQEE 429
Cdd:pfam05262 215 AQQLKEELDKKQID---ADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIE--KAQIE 289

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7328175    430 AERLEADrmaALRAKEELERQAVDQIKSQEQLAaelaeytakialleearrrkEDEVEEWQHRAKEAQDDLVKTKEE 506
Cdd:pfam05262 290 IKKNDEE---ALKAKDHKAFDLKQESKASEKEA--------------------EDKELEAQKKREPVAEDLQKTKPQ 343
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 400-507 6.29e-03

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.81  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    400 EKTKKAERELSEQIQralQLEEERKRAQEEAERLEAD---RMAALRAKE-----------ELERQAVDQIKSQEQLAAEL 465
Cdd:pfam10174 547 EEAVRTNPEINDRIR---LLEQEVARYKEESGKAQAEverLLGILREVEnekndkdkkiaELESLTLRQMKEQNKKVANI 623

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 7328175    466 -----AEYTAKIALLEEARRRKEDEVEEWQHRA-KEAQDDLVKTKEEL 507
Cdd:pfam10174 624 khgqqEMKKKGAQLLEEARRREDNLADNSQQLQlEELMGALEKTRQEL 671
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 245-299 6.32e-03

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


Pssm-ID: 270016  Cd Length: 111  Bit Score: 36.84  E-value: 6.32e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7328175  245 YGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIgfPWSEIRNISFNDKKF 299
Cdd:cd13195   1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERI--PYTAIQMATSSGRVF 53
Caldesmon pfam02029
Caldesmon;
352-449 6.61e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.47  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    352 QAREEKHQKQLERQQLETEKKRR--ETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEE 429
Cdd:pfam02029 234 QEREEEAEVFLEAEQKLEELRRRrqEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKLREEE 313

                          90       100
                  ....*....|....*....|
gi 7328175    430 AERleadrmaalRAKEELER 449
Cdd:pfam02029 314 EKR---------RMKEEIER 324
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 337-498 6.65e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.13  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    337 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKR---RETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQI 413
Cdd:pfam13868  53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRqeeYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    414 QRALQLEEERKRAQEEAERLE-----------ADRMAALRAKEELERQAVDQIksQEQLAAELAEYTAKIALLEEARRRK 482
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEderileylkekAEREEEREAEREEIEEEKERE--IARLRAQQEKAQDEKAERDELRAKL 210

                         170
                  ....*....|....*.
gi 7328175    483 EDEVEEWQHRAKEAQD 498
Cdd:pfam13868 211 YQEEQERKERQKEREE 226
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
337-449 6.91e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.46  E-value: 6.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  337 RRRKPDTIEVQQMKAQAREEKHQKQLERQ--QLETEKKR-RETVEREKEQMMREKEELMLRLQDYEEKTKKaERELSEQI 413
Cdd:COG2433 393 EEPEAEREKEHEERELTEEEEEIRRLEEQveRLEAEVEElEAELEEKDERIERLERELSEARSEERREIRK-DREISRLD 471

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 7328175  414 QRALQLEEERKRAQEEAERLEA--DRMAALRAKEELER 449
Cdd:COG2433 472 REIERLERELEEERERIEELKRklERLKELWKLEHSGE 509
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 352-504 7.54e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 39.55  E-value: 7.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   352 QAREEKHQKQLERQQLETEKKRREtverekeqmmREKEElmlRlqdyEEKTKKAERELSEQIQRALQLEEERKRAQEEAE 431
Cdd:PRK05035 440 AIEQEKKKAEEAKARFEARQARLE----------REKAA---R----EARHKKAAEARAAKDKDAVAAALARVKAKKAAA 502

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   432 R-------LEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKI-ALLEEARRRKEDEVEEwqHRAKEAQDDLVKT 503
Cdd:PRK05035 503 TqpivikaGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVaAAIARAKAKKAAQQAA--NAEAEEEVDPKKA 580


                 .
gi 7328175   504 K 504
Cdd:PRK05035 581 A 581
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 386-481 8.67e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 37.63  E-value: 8.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175   386 REKEELMLRLQDYEEKTKKAERELSEQiqralqlEEERKRAQEEAERLEADRMA-ALRAKEELERQAVDQIKS-QEQLAA 463
Cdd:PRK07352  50 ERREAILQALKEAEERLRQAAQALAEA-------QQKLAQAQQEAERIRADAKArAEAIRAEIEKQAIEDMARlKQTAAA 122

                         90
                 ....*....|....*...
gi 7328175   464 ELAEYTAKIalLEEARRR 481
Cdd:PRK07352 123 DLSAEQERV--IAQLRRE 138
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 345-584 8.92e-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: 8.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     345 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKeqmmREKEELMLRLQDYEEKTKKAERELSEQIQ---------- 414
Cdd:TIGR00618  453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKK----AVVLARLLELQEEPCPLCGSCIHPNPARQdidnpgpltr 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     415 RALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKI----ALLEEARRRKEDEVEEWQ 490
Cdd:TIGR00618  529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpnlqNITVRLQDLTEKLSEAED 608

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175     491 HRAKEAQDDLVKTKEELHLVMTAPPPPpppvyepvsyHVQESLQDEGAEPTGYSAELSSEGIRdDRNEEKRITEAEKNER 570
Cdd:TIGR00618  609 MLACEQHALLRKLQPEQDLQDVRLHLQ----------QCSQELALKLTALHALQLTLTQERVR-EHALSIRVLPKELLAS 677

                          250
                   ....*....|....
gi 7328175     571 VQRQLLTLSSELSQ 584
Cdd:TIGR00618  678 RQLALQKMQSEKEQ 691
mukB PRK04863
chromosome partition protein MukB;
364-509 8.97e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 8.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    364 RQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELS---------EQIQRALQ-LEE--ERKRAQEEAE 431
Cdd:PRK04863  292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqtalrqqEKIERYQAdLEEleERLEEQNEVV 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    432 RLEADRMAALRAKEELERQAVDQIKSQ---EQLAAELAE-----YTAKIALLEEARRRKE------DEVEEWQHRAKEAQ 497
Cdd:PRK04863  372 EEADEQQEENEARAEAAEEEVDELKSQladYQQALDVQQtraiqYQQAVQALERAKQLCGlpdltaDNAEDWLEEFQAKE 451

                         170
                  ....*....|..
gi 7328175    498 DDLvkTKEELHL 509
Cdd:PRK04863  452 QEA--TEELLSL 461
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
 349-467 9.53e-03

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 38.81  E-value: 9.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175    349 MKAQAREEKHQKQLERQQ--------LETEKKRRETVEREKEQMMREKeelmlrlqdyEEKTKKAERELSEQIQRALQLE 420
Cdd:pfam07767 209 KKRLKEEEKLERVLEKIAesaataeaREEKRKTKAQRNKEKRRKEEER----------EAKEEKALKKKLAQLERLKEIA 278

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 7328175    421 EE-RKRAQEEAERLEADRMA---ALRAKEELERQAVDQIKSQE-----QLAAELAE 467
Cdd:pfam07767 279 KEiAEKEKEREEKAEARKREkrkKKKEEKKLRPRKLGKHKVPEpdlevQLPDELSG 334
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
350-613 9.69e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 38.87  E-value: 9.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  350 KAQAREEKHQKQLERQQLET-EKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQE 428
Cdd:COG3064   1 AQEALEEKAAEAAAQERLEQaEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  429 EAERLeadrmAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVE---EWQHRAKEAQDDLVKTKE 505
Cdd:COG3064  81 EAEKA-----AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKrkaEEERKAAEAEAAAKAEAE 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7328175  506 ELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQA 585
Cdd:COG3064 156 AARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALA 235

                       250       260
                ....*....|....*....|....*...
gi 7328175  586 RDENKRTHNDIIHNENMRQGRDKYKTLR 613
Cdd:COG3064 236 AVEATEEAALGGAEEAADLAAVGVLGAA 263
 
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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