NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|348533462|ref|XP_003454224|]
View 

merlin [Oreochromis niloticus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 216-312 8.80e-63

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: 201.73  E-value: 8.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 216 MYGVNYFLIRNKKGTDLLLGVDALGLHIYEPDNKLTPKCSFPWNEIRNISYSDKEFTIKPLDKKANVFKFNSSRLRVNKL 295
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 348533462 296 ILQLCIGNHDLFMRRRR 312
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-222 3.87e-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: 195.98  E-value: 3.87e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462    24 VRISTM-ESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRYNIKDTVA--WLKMDKKVLDQEVpKEEPIIFHFLAKF 100
Cdd:smart00295   2 LKVYLLdGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   101 YPENaEEELVQDITQH-LFFLQVKKKILEEEIHCPPEASVLLASYAVHAEYGDYDPAVH-KPGFLAEEELLPKRVINlyQ 178
Cdd:smart00295  81 YPPD-PNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD--S 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 348533462   179 MTPEMWEERITACYAEHRGRTRDEAEMEYLKIAQDLDMYGVNYF 222
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 515-591 7.17e-28

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: 106.52  E-value: 7.17e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348533462  515 SMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERETPLDIIHNQNTEQGTSKHSNFKKLTLQSTKSRVAFFEEL 591
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 346-465 5.90e-24

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: 96.91  E-value: 5.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  346 REEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRL 425
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 348533462  426 MEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSE 465
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
PTZ00266 super family cl31758
NIMA-related protein kinase; Provisional
 309-361 2.87e-03

NIMA-related protein kinase; Provisional


The actual alignment was detected with superfamily member PTZ00266:

Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 40.88  E-value: 2.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 348533462  309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERAR-DELERRLI 361
Cdd:PTZ00266  459 RIERLEREERERLERERMERIERERLERERLERERLERDRLERDRlDRLERERV 512
 
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 ...
 216-312 8.80e-63

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: 201.73  E-value: 8.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 216 MYGVNYFLIRNKKGTDLLLGVDALGLHIYEPDNKLTPKCSFPWNEIRNISYSDKEFTIKPLDKKANVFKFNSSRLRVNKL 295
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 348533462 296 ILQLCIGNHDLFMRRRR 312
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-222 3.87e-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: 195.98  E-value: 3.87e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462    24 VRISTM-ESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRYNIKDTVA--WLKMDKKVLDQEVpKEEPIIFHFLAKF 100
Cdd:smart00295   2 LKVYLLdGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   101 YPENaEEELVQDITQH-LFFLQVKKKILEEEIHCPPEASVLLASYAVHAEYGDYDPAVH-KPGFLAEEELLPKRVINlyQ 178
Cdd:smart00295  81 YPPD-PNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD--S 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 348533462   179 MTPEMWEERITACYAEHRGRTRDEAEMEYLKIAQDLDMYGVNYF 222
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 20-103 4.45e-49

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: 164.86  E-value: 4.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  20 KTFNVRISTMESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRYNI-KDTVAWLKMDKKVLDQEVPKEEPIIFHFLA 98
Cdd:cd17186    1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQDVPKEEPVTFHFLA 80


                 ....*
gi 348533462  99 KFYPE 103
Cdd:cd17186   81 KFYPE 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 106-222 3.08e-34

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 125.84  E-value: 3.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  106 EEELVQDITQHLFFLQVKKKILEEEIHCPPEASVLLASYAVHAEYGDYDPAVHKPGFLAEEELLPKRVINlyQMTPEMWE 185
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 348533462  186 ERITACYAEHRGRTRDEAEMEYLKIAQDLDMYGVNYF 222
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 515-591 7.17e-28

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: 106.52  E-value: 7.17e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348533462  515 SMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERETPLDIIHNQNTEQGTSKHSNFKKLTLQSTKSRVAFFEEL 591
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-311 5.05e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 104.64  E-value: 5.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  226 NKKGTDLLLGVDALGLHIYEPDNKLTPkcSFPWNEIRNISYSDKEFTIKPLDKKA-NVFKFNSSRLRVNKLILQLCIGNH 304
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKILN--LFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 348533462  305 DLFMRRR 311
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 346-465 5.90e-24

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: 96.91  E-value: 5.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  346 REEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRL 425
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 348533462  426 MEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSE 465
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-474 5.93e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.36  E-value: 5.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 310 RRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQ 389
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 390 IAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAK 469
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                 ....*
gi 348533462 470 NKLLE 474
Cdd:COG1196  435 EEEEE 439
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 319-471 1.55e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.12  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 319 QQMKAQAREERARKQVERQRLQ--REKQLREEAERARDELERRLIQLQ-----DEADMANEALLRSEQTADLLAEKAQI- 390
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQAEelQQKQAAEQERLKQLEKERLAAQEQkkqaeEAAKQAALKQKQAEEAAAKAAAAAKAk 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 391 AEEEAKLLAQKAAEAETEMqriKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKN 470
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225


                 .
gi 348533462 471 K 471
Cdd:PRK09510 226 A 226
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 306-552 3.08e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 3.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   306 LFMRRRRVDSLEVQQMKAQ------AREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEAL--LRS 377
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAErykelkAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeeLRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   378 E----------QTADLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQK-----------MLEAKMV 436
Cdd:TIGR02168  275 EvseleeeieeLQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAeelaeleekleELKEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   437 ALK-MAEESERRAKEAEQLKQDLLEARDSERRA----KNKLLEITSKAVYMSPGL-APDSMPQDVSFSRENLSFDFKDTD 510
Cdd:TIGR02168  355 SLEaELEELEAELEELESRLEELEEQLETLRSKvaqlELQIASLNNEIERLEARLeRLEDRRERLQQEIEELLKKLEEAE 434

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 348533462   511 MKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERE 552
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
PTZ00121 PTZ00121
MAEBL; Provisional
 310-590 1.42e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  310 RRRVDSLEVQQMKAQAREERARKQVER-QRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  389 QiAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEE---SERRAKEAEQLKQDLLEARDSE 465
Cdd:PTZ00121 1613 K-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakkAEEDKKKAEEAKKAEEDEKKAA 1691

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  466 RRAKNKLLEitSKAVYMSPGLAPDSMPQDVSFSRENLSFDFKDTDMKRLSMEiEKEKVEYMEKSKHLQEQLNELKTEIES 545
Cdd:PTZ00121 1692 EALKKEAEE--AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEK 1768

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 348533462  546 LKLKERETPLDIIHNQNTEQGTSKHSNFKKlTLQSTKSRVAFFEE 590
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRMEVDK-KIKDIFDNFANIIE 1812
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 309-472 3.65e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 3.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   389 QIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERraKEAEQLKQDLLEARDSERRA 468
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR--EELEEAEQALDAAERELAQL 487


                   ....
gi 348533462   469 KNKL 472
Cdd:TIGR02168  488 QARL 491
growth_prot_Scy NF041483
polarized growth protein Scy;
317-467 1.86e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.90  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  317 EVQQMKAQAREERARKQVERQRLQREKQlrEEAERARDELERRLIQLQDEADMANEALlRSEQTADLLAEKAQIAEEEAK 396
Cdd:NF041483  583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348533462  397 LLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMA-EESERRAKEAEQLKQDLLEARDSERR 467
Cdd:NF041483  660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETLGSARAEADQERE 731
growth_prot_Scy NF041483
polarized growth protein Scy;
321-467 1.84e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.82  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  321 MKAQARE--ERARKQVERQRLQREKQ---LREEAERA----RDELERRLIQLQDEADM--------ANEALLRSEQT-AD 382
Cdd:NF041483  518 LRRQAEEtlERTRAEAERLRAEAEEQaeeVRAAAERAarelREETERAIAARQAEAAEeltrlhteAEERLTAAEEAlAD 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  383 LLAEKAQI---AEEEAKLLAQKAAE--------AETEMQRIKVTAIRGQEERRlmeqkmLEAKMVALKMAEESerrAKEA 451
Cdd:NF041483  598 ARAEAERIrreAAEETERLRTEAAErirtlqaqAEQEAERLRTEAAADASAAR------AEGENVAVRLRSEA---AAEA 668

                         170
                  ....*....|....*.
gi 348533462  452 EQLKQdllEARDSERR 467
Cdd:NF041483  669 ERLKS---EAQESADR 681
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 309-361 2.87e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 40.88  E-value: 2.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 348533462  309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERAR-DELERRLI 361
Cdd:PTZ00266  459 RIERLEREERERLERERMERIERERLERERLERERLERDRLERDRlDRLERERV 512
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
317-558 3.17e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAK 396
Cdd:COG4372   60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 397 LLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMV----ALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKL 472
Cdd:COG4372  140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 473 LEITSKAVYMSPGLAPDSMPQDVSFSRENLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERE 552
Cdd:COG4372  220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299


                 ....*.
gi 348533462 553 TPLDII 558
Cdd:COG4372  300 LLLNLA 305
DegS pfam05384
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU ...
 319-370 4.59e-03

Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU two-component regulatory system of Bacillus subtilis controls various processes that characterize the transition from the exponential to the stationary growth phase, including the induction of extracellular degradative enzymes, expression of late competence genes and down-regulation of the sigma D regulon. The family also contains one sequence Swiss:Q8R9D3 from Thermoanaerobacter tengcongensis which are described as sensory transduction histidine kinases.


Pssm-ID: 428449 [Multi-domain]  Cd Length: 159  Bit Score: 38.23  E-value: 4.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 348533462  319 QQMKaQAREERARKQVERQRLQ-REKQLREEaeraRDELERRLIQLQDEADMA 370
Cdd:pfam05384  77 EDIK-EAYEEAKDLQVELALLReREKQLRER----RDELERRLKNLKETIERA 124
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 330-420 7.15e-03

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: 37.03  E-value: 7.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 330 ARKQVERQRLQREKQLREEAERARDELERRLIQLQDEAD-MANEALLRSEQTADLLAEKAQiaEEEAKLLAQKAAEAETE 408
Cdd:cd06503   30 EREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQeIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQE 107

                         90
                 ....*....|..
gi 348533462 409 MQRIKvTAIRGQ 420
Cdd:cd06503  108 KEKAL-AELRKE 118
 
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 ...
 216-312 8.80e-63

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: 201.73  E-value: 8.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 216 MYGVNYFLIRNKKGTDLLLGVDALGLHIYEPDNKLTPKCSFPWNEIRNISYSDKEFTIKPLDKKANVFKFNSSRLRVNKL 295
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 348533462 296 ILQLCIGNHDLFMRRRR 312
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 24-222 3.87e-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: 195.98  E-value: 3.87e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462    24 VRISTM-ESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRYNIKDTVA--WLKMDKKVLDQEVpKEEPIIFHFLAKF 100
Cdd:smart00295   2 LKVYLLdGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVKF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   101 YPENaEEELVQDITQH-LFFLQVKKKILEEEIHCPPEASVLLASYAVHAEYGDYDPAVH-KPGFLAEEELLPKRVINlyQ 178
Cdd:smart00295  81 YPPD-PNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD--S 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 348533462   179 MTPEMWEERITACYAEHRGRTRDEAEMEYLKIAQDLDMYGVNYF 222
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 20-103 4.45e-49

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: 164.86  E-value: 4.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  20 KTFNVRISTMESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRYNI-KDTVAWLKMDKKVLDQEVPKEEPIIFHFLA 98
Cdd:cd17186    1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQDVPKEEPVTFHFLA 80


                 ....*
gi 348533462  99 KFYPE 103
Cdd:cd17186   81 KFYPE 85
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 22-103 4.35e-41

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: 143.19  E-value: 4.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  22 FNVRISTMESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQEVPKEEPIIFHFLAKF 100
Cdd:cd17097    1 INVRVTTMDAELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYeNKKGRVAWLKPDKKVLTQDVSKNNTLKFFFLVKF 80


                 ...
gi 348533462 101 YPE 103
Cdd:cd17097   81 YPE 83
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 106-222 3.08e-34

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 125.84  E-value: 3.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  106 EEELVQDITQHLFFLQVKKKILEEEIHCPPEASVLLASYAVHAEYGDYDPAVHKPGFLAEEELLPKRVINlyQMTPEMWE 185
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 348533462  186 ERITACYAEHRGRTRDEAEMEYLKIAQDLDMYGVNYF 222
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 114-214 2.97e-31

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: 116.96  E-value: 2.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 114 TQHLFFLQVKKKILEEEIHCPPEASVLLASYAVHAEYGDYDPAVHKPGFLAEEELLPKRVINlyQMTPEMWEERITACYA 193
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLK--QRKPEEWEKRIVELHK 78

                         90       100
                 ....*....|....*....|.
gi 348533462 194 EHRGRTRDEAEMEYLKIAQDL 214
Cdd:cd14473   79 KLRGLSPAEAKLKYLKIARKL 99
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 23-103 2.64e-30

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: 113.72  E-value: 2.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  23 NVRISTMESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQEVPKEEPIIFHFLAKFY 101
Cdd:cd17187    2 NVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYvDSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKFY 81


                 ..
gi 348533462 102 PE 103
Cdd:cd17187   82 PE 83
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 515-591 7.17e-28

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: 106.52  E-value: 7.17e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348533462  515 SMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERETPLDIIHNQNTEQGTSKHSNFKKLTLQSTKSRVAFFEEL 591
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-311 5.05e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 104.64  E-value: 5.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  226 NKKGTDLLLGVDALGLHIYEPDNKLTPkcSFPWNEIRNISYSDKEFTIKPLDKKA-NVFKFNSSRLRVNKLILQLCIGNH 304
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKILN--LFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 348533462  305 DLFMRRR 311
Cdd:pfam09380  79 TFFRLRR 85
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 20-103 3.56e-26

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: 101.99  E-value: 3.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  20 KTFNVRISTMESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQEVPKEEPIIFHFLA 98
Cdd:cd17239    1 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYvDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 80


                 ....*
gi 348533462  99 KFYPE 103
Cdd:cd17239   81 KFYPE 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 346-465 5.90e-24

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: 96.91  E-value: 5.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  346 REEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRL 425
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 348533462  426 MEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSE 465
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 21-103 1.46e-23

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: 94.81  E-value: 1.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  21 TFNVRISTMESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQEVPKEEPIIFHFLAK 99
Cdd:cd17237    1 TISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYqDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAK 80


                 ....
gi 348533462 100 FYPE 103
Cdd:cd17237   81 FYPE 84
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 23-103 9.06e-23

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: 92.49  E-value: 9.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  23 NVRISTMESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQEVPKEEPIIFHFLAKFY 101
Cdd:cd17238    2 NVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYvDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFF 81


                 ..
gi 348533462 102 PE 103
Cdd:cd17238   82 PE 83
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 218-308 8.76e-16

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: 72.79  E-value: 8.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 218 GVNYFLIRNK--KGTDLLLGVDALGLHIYEPDNKlTPKCSFPWNEIRNISYS-DKEFTIKPLDK-KANVFKFNSSRlRVN 293
Cdd:cd00836    1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEdKQSKLLFQTPS-RQA 78

                         90
                 ....*....|....*
gi 348533462 294 KLILQLCIGNHDLFM 308
Cdd:cd00836   79 KEIWKLIVGYHRFLL 93
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-474 5.93e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 75.36  E-value: 5.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 310 RRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQ 389
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 390 IAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAK 469
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                 ....*
gi 348533462 470 NKLLE 474
Cdd:COG1196  435 EEEEE 439
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 31-100 2.70e-13

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: 65.30  E-value: 2.70e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348533462  31 SDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRYNIKDTVA-WLKMDKKVLDQeVPKEEPIIFHFLAKF 100
Cdd:cd01765   11 TELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKhWLDLDKKISKQ-LKRSGPYQFYFRVKF 80
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 317-479 3.22e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAK 396
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 397 LLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEIT 476
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448


                 ...
gi 348533462 477 SKA 479
Cdd:COG1196  449 EEE 451
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 218-313 1.33e-12

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: 64.29  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 218 GVNYFLIRNKKGTDLLLGVDALGLHIYEPDNKLTPKCSFPWNEIRNISYSDKEFTIKPLDKKANVFKFNSSRLR------ 291
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRRNSHRSRRTFQSssvsvh 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 348533462 292 --------VNKLILQLCIGNHDLFMRRRRV 313
Cdd:cd13191   81 vwygqtpaLCKTIWSMAIAQHQFYLDRKQS 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-479 5.17e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 5.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 389 QIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRA 468
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                        170
                 ....*....|.
gi 348533462 469 KNKLLEITSKA 479
Cdd:COG1196  413 LERLERLEEEL 423
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 33-104 8.23e-12

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: 61.53  E-value: 8.23e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 348533462  33 LEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQEVPK---EEPIIFHFLAKFYPEN 104
Cdd:cd17103   15 LEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYeDETGHYNWLQLDKRVLDHEFPKkwsSGPLVLHFAVKFYVES 90
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 30-84 1.43e-11

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: 59.91  E-value: 1.43e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 348533462   30 ESDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQ 84
Cdd:pfam09379   6 GTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFlDDNGEHRWLDLSKRLSKQ 61
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-479 2.30e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 389 QIAEEEAKLLAQKAAEAETEMQRIkvtairgQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRA 468
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475

                        170
                 ....*....|.
gi 348533462 469 KNKLLEITSKA 479
Cdd:COG1196  476 EAALAELLEEL 486
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 33-104 6.62e-11

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: 59.11  E-value: 6.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  33 LEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRYnIKDT-------------VA---WLKMDKKVLDQEVPkeePIIFHF 96
Cdd:cd17101   14 LQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAV-LKDGeyffldpdtklskYApkgWKSEAKKGLKGGKP---VFTLYF 89


                 ....*...
gi 348533462  97 LAKFYPEN 104
Cdd:cd17101   90 RVKFYVDN 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 273-475 1.02e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 273 IKPLDKKANV---FKFNSSRLRVNKLILQLcignhdLFMRRRRVDSLEVQQMKAQAREERARKQVERQRLQREK-QLREE 348
Cdd:COG1196  202 LEPLERQAEKaerYRELKEELKELEAELLL------LKLRELEAELEELEAELEELEAELEELEAELAELEAELeELRLE 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 349 AERARDELERRL----IQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKlLAQKAAEAETEMQRIKVTAIRGQEERR 424
Cdd:COG1196  276 LEELELELEEAQaeeyELLAELARLEQDIARLEERRRELEERLEELEEELAE-LEEELEELEEELEELEEELEEAEEELE 354

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 348533462 425 LMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEI 475
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-474 1.13e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQ-----TADL 383
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEeleelEEEL 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 384 LAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKmlEAKMVALKMAEESERRAKEAEQLKQDLLEARD 463
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA--EELLEALRAAAELAAQLEELEEAEEALLERLE 417

                        170
                 ....*....|.
gi 348533462 464 SERRAKNKLLE 474
Cdd:COG1196  418 RLEEELEELEE 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 317-480 1.37e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAK 396
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 397 LLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEIT 476
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455


                 ....
gi 348533462 477 SKAV 480
Cdd:COG1196  456 EEEE 459
RA_FERM_F0_F1_like cd01768
Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 ...
 23-98 2.70e-10

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: 57.94  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  23 NVRISTM-----ESDLEFSCEVKWKGKDLFDLVCRTLGLR-----------ETWFFGLRY--------------NIKDTV 72
Cdd:cd01768    1 VLKIFGAglasgANYKSVLATARSTARELVAEALERYGLAgspgggpgessCVDAFALCDalgrpaaagvgsgeWRAEHL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 348533462  73 AWLKMDKKVLDQ----EVPKEEPIIFHFLA 98
Cdd:cd01768   81 RVLGDSERPLLVqelwRARPGWARRFELRG 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 319-479 1.05e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 319 QQMKAQAREERARKQVERQRLQrEKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKLL 398
Cdd:COG1196  308 EERRRELEERLEELEEELAELE-EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 399 AQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEITSK 478
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466


                 .
gi 348533462 479 A 479
Cdd:COG1196  467 E 467
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 301-565 1.40e-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: 60.91  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  301 IGNHDLFMRRRRVDSLEVQQMKAQAREERARKQVERQRlqREKQLREEAERARDELERRLIQLQDEADMANEallrseqt 380
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR--KVKILEEERQRKIQQQKVEMEQIRAEQEEARQ-------- 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  381 adllaEKAQIAEEEAKLLAQKAAEAETEMQRiKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERR--AKEAEQLKQDL 458
Cdd:pfam17380 435 -----REVRRLEEERAREMERVRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAM 508

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  459 LEaRDSERRAKNKLLEITSKAVYmspglapdsmpqdvsfsrenlsfdfkdTDMKRLSMEIEKEKVEYMEKSKHLQEQL-- 536
Cdd:pfam17380 509 IE-EERKRKLLEKEMEERQKAIY---------------------------EEERRREAEEERRKQQEMEERRRIQEQMrk 560

                         250       260       270
                  ....*....|....*....|....*....|
gi 348533462  537 -NELKTEIESLKlKERETPLDIIHNQNTEQ 565
Cdd:pfam17380 561 aTEERSRLEAME-REREMMRQIVESEKARA 589
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 31-102 1.62e-09

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: 54.91  E-value: 1.62e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 348533462  31 SDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQeVPKEEPIIFHFLAKFYP 102
Cdd:cd17098   11 TVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFtDPEGNKCWLDPEKPILRQ-VKRPKDVVFKFVVKFYT 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-479 1.63e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 310 RRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALlrSEQTADLLAEKAQ 389
Cdd:COG1196  219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--EEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 390 IAEEEAKL---------LAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLE 460
Cdd:COG1196  297 LARLEQDIarleerrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376

                        170
                 ....*....|....*....
gi 348533462 461 ARDSERRAKNKLLEITSKA 479
Cdd:COG1196  377 AEEELEELAEELLEALRAA 395
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 33-104 1.85e-09

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: 54.89  E-value: 1.85e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348533462  33 LEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRYnIKDT--VAWLKMDKKVLDQEVPKEE-PIIFHFLAKFYPEN 104
Cdd:cd17200   15 LELLVQPKLLSRELLDLVASHFNLKEKEYFGITF-IDDTgqSNWLQLDHRVLDHDLPKKSgPVTLYFAVRFYIES 88
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 42-101 3.94e-09

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: 53.40  E-value: 3.94e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 348533462  42 KGKDLFDLVCRTLGLRETWFFGLRYniKDTVA---WLKMDKKVLDQeVPKEEPIIFHFLAKFY 101
Cdd:cd17102   23 KGQFLLDYVCNYLNLLEKDYFGLRY--VDTEKqrhWLDPNKSIYKQ-LKGVPPYVLCFRVKFY 82
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 30-104 4.51e-09

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: 53.89  E-value: 4.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  30 ESDLEFSCEVKW----KGKDLFDLVCRTLGLRETWFFGLRYNIKDT-VAWLKMDKKVLDQEVPKEEPIIFHFLAKFYPEN 104
Cdd:cd17107   12 ESELILTIQQDGikssKGSVVLDVVFQHLNLLETDYFGLRYIDRQHqTHWLDPAKTLSEQLKLIGPPYTLYFGVKFYAED 91
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 221-309 8.73e-09

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: 53.47  E-value: 8.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 221 YFLIRNKKGTD--LLLGVDALGLHIYEP-DNKLTPKCSFPWNEIRNISYSDKEFTIKPLDKKANVFKFNSSRLRvNKLIL 297
Cdd:cd13185    8 YRLRKSKKETPgsVLLGITAKGIQIYQEsDGEQQLLRTFPWSNIGKLSFDRKKFEIRPEGSLRKLTYYTSSDEK-SKYLL 86

                         90
                 ....*....|..
gi 348533462 298 QLCIGNHDLFMR 309
Cdd:cd13185   87 ALCRETHQFSMA 98
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 319-471 1.55e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.12  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 319 QQMKAQAREERARKQVERQRLQ--REKQLREEAERARDELERRLIQLQ-----DEADMANEALLRSEQTADLLAEKAQI- 390
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQAEelQQKQAAEQERLKQLEKERLAAQEQkkqaeEAAKQAALKQKQAEEAAAKAAAAAKAk 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 391 AEEEAKLLAQKAAEAETEMqriKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKN 470
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225


                 .
gi 348533462 471 K 471
Cdd:PRK09510 226 A 226
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 306-552 3.08e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 3.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   306 LFMRRRRVDSLEVQQMKAQ------AREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEAL--LRS 377
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAErykelkAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeeLRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   378 E----------QTADLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQK-----------MLEAKMV 436
Cdd:TIGR02168  275 EvseleeeieeLQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAeelaeleekleELKEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   437 ALK-MAEESERRAKEAEQLKQDLLEARDSERRA----KNKLLEITSKAVYMSPGL-APDSMPQDVSFSRENLSFDFKDTD 510
Cdd:TIGR02168  355 SLEaELEELEAELEELESRLEELEEQLETLRSKvaqlELQIASLNNEIERLEARLeRLEDRRERLQQEIEELLKKLEEAE 434

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 348533462   511 MKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERE 552
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 216-307 6.08e-08

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


Pssm-ID: 270010  Cd Length: 95  Bit Score: 50.77  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 216 MYGVNYFLIRNKKGTDLLLGVDALGLHIYEpdnKLTPKCSFPWNEIRNISYSDKEFTI----KPLDKKANVFKFNSSRLR 291
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQ---NGIRINTFPWSKIVKISFKRKQFFIqlrrEPNESRDTILGFNMLSYR 77

                         90
                 ....*....|....*.
gi 348533462 292 VNKLILQLCIGNHDLF 307
Cdd:cd13189   78 ACKNLWKSCVEHHTFF 93
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 203-282 7.63e-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: 50.47  E-value: 7.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 203 AEMEYLKIAQDLDMYGVNYFLIRNKKGTDLLLGVDALGLHIYEpDNKLTPkcSFPWNEIRNISYSDKEFTI---KPLDKK 279
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQ-GGKRVH--HFRWNDITKFNYEGKMFILhvmQKEEKK 77


                 ...
gi 348533462 280 ANV 282
Cdd:cd13192   78 HTL 80
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 217-307 1.36e-07

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: 49.63  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 217 YGVNYFLIRNKKGTDLLLGVDALGLHIYEPDNKLTpkcSFPWNEIRNISYSDKEFTIK-------PLDKKANvFKFNSSr 289
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRIN---RFAWPKVLKISYKRNNFYIKirpgefeQYETTIG-FKLPNH- 75

                         90
                 ....*....|....*...
gi 348533462 290 lRVNKLILQLCIGNHDLF 307
Cdd:cd13184   76 -RAAKRLWKVCVEHHTFF 92
PTZ00121 PTZ00121
MAEBL; Provisional
 310-590 1.42e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  310 RRRVDSLEVQQMKAQAREERARKQVER-QRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  389 QiAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEE---SERRAKEAEQLKQDLLEARDSE 465
Cdd:PTZ00121 1613 K-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakkAEEDKKKAEEAKKAEEDEKKAA 1691

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  466 RRAKNKLLEitSKAVYMSPGLAPDSMPQDVSFSRENLSFDFKDTDMKRLSMEiEKEKVEYMEKSKHLQEQLNELKTEIES 545
Cdd:PTZ00121 1692 EALKKEAEE--AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEK 1768

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 348533462  546 LKLKERETPLDIIHNQNTEQGTSKHSNFKKlTLQSTKSRVAFFEE 590
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRMEVDK-KIKDIFDNFANIIE 1812
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 309-452 2.50e-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: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIqLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:pfam17380 444 RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEM 522

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348533462  389 Q-----IAEEEAKLLAQKAAEAETEMQ---RIKVTAIRGQEERRLMEQKMLEAKMvaLKMAEESERRAKEAE 452
Cdd:pfam17380 523 EerqkaIYEEERRREAEEERRKQQEMEerrRIQEQMRKATEERSRLEAMEREREM--MRQIVESEKARAEYE 592
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 309-472 3.65e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 3.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   389 QIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERraKEAEQLKQDLLEARDSERRA 468
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR--EELEEAEQALDAAERELAQL 487


                   ....
gi 348533462   469 KNKL 472
Cdd:TIGR02168  488 QARL 491
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 217-309 3.82e-07

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: 48.05  E-value: 3.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 217 YGVNYFLIRNKKGTDLLLGVDALGLHIYEPDNKLTPKcsFPWNEIRNISYSDKEFTIKPLDKKANV-FKFNSSRLRvnKL 295
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVF--FRWEDIKNVINHKRTFSIECQNSEETVqFQFEDAETA--KY 76

                         90
                 ....*....|....
gi 348533462 296 ILQLCIGNHDLFMR 309
Cdd:cd13188   77 VWKLCVLQHKFYRQ 90
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
310-416 4.99e-07

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 51.97  E-value: 4.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 310 RRRVDSLEVQQMKAQAREERARKQVER-QRLQRE----KQLREEAERARDELERRLIQLQDEADMANEALlrsEQTADLL 384
Cdd:COG1566  109 EAEIAAAEAQLAAAQAQLDLAQRELERyQALYKKgavsQQELDEARAALDAAQAQLEAAQAQLAQAQAGL---REEEELA 185

                         90       100       110
                 ....*....|....*....|....*....|..
gi 348533462 385 AEKAQIAEEEAKLlaqkaAEAETEMQRIKVTA 416
Cdd:COG1566  186 AAQAQVAQAEAAL-----AQAELNLARTTIRA 212
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 319-471 5.20e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.12  E-value: 5.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 319 QQMKAQAReeRARKQVERQRLQREKQLREEAerarDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKLL 398
Cdd:PRK09510  68 QQQQKSAK--RAEEQRKKKEQQQAEELQQKQ----AAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348533462 399 AQKA-AEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVA---LKMAEESERRAKEAEQLKQDLLEARDSERRAKNK 471
Cdd:PRK09510 142 AAAAkAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAeakKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKK 218
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 317-468 5.24e-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: 52.16  E-value: 5.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTAD--LLAEKAQIAEEE 394
Cdd:TIGR02794  76 QAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAErkAKEEAAKQAEEE 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 348533462  395 AKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRA 468
Cdd:TIGR02794 156 AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKA 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-428 6.64e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 6.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSLEVQQMKAQAREERARKQVER--QRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAE 386
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 348533462 387 KAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQ 428
Cdd:COG1196  457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 319-471 6.90e-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: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  319 QQMKAQAREERAR-KQVERQRLQREKQLREEAERARDELERrlIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKl 397
Cdd:TIGR02794  57 QQKKPAAKKEQERqKKLEQQAEEAEKQRAAEQARQKELEQR--AAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAK- 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 348533462  398 laqKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNK 471
Cdd:TIGR02794 134 ---AKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAK 204
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
316-547 7.85e-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: 7.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  316 LEVQQMKAQARE--------ERARKQVERQRLQRE--KQLREEAERaRDELERRLIQLQDEADMANeaLLRSEQTADLLA 385
Cdd:COG4913   218 LEEPDTFEAADAlvehfddlERAHEALEDAREQIEllEPIRELAER-YAAARERLAELEYLRAALR--LWFAQRRLELLE 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  386 EKAQIAEEEAKLLAQKAAEAETEMQRIkvtairgQEERRLMEQKMLEAKmvalkmAEESERRAKEAEQLKQDLLEARDSE 465
Cdd:COG4913   295 AELEELRAELARLEAELERLEARLDAL-------REELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRR 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  466 RRAKNKLLEItskavymspGLAPDSMPQDVSFSRENLSfDFKDtDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIES 545
Cdd:COG4913   362 ARLEALLAAL---------GLPLPASAEEFAALRAEAA-ALLE-ALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430


                  ..
gi 348533462  546 LK 547
Cdd:COG4913   431 LE 432
PTZ00121 PTZ00121
MAEBL; Provisional
 317-552 8.80e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEAllrsEQTADLLAEKAQIAEEEAK 396
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA----RRQAAIKAEEARKADELKK 1285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  397 LLAQKAAEaetemqrikvtAIRGQEERRLMEQkmLEAKMVALKMAEESERRAKEAEQlKQDLLEARDSERRAKNKLLEIT 476
Cdd:PTZ00121 1286 AEEKKKAD-----------EAKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAE 1351

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 348533462  477 SKAVymspglapdsmPQDVSFSRENLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERE 552
Cdd:PTZ00121 1352 AEAA-----------ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 33-104 8.83e-07

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: 47.27  E-value: 8.83e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 348533462  33 LEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQEVPKEE-PIIFHFLAKFYPEN 104
Cdd:cd17199   15 LELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFtDETGHLNWLQLDRRVLEHDFPKKSgPVVLYFCVRFYIES 88
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 34-102 9.09e-07

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: 46.80  E-value: 9.09e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348533462  34 EFSCEV--KWKGKDLFDLVCRTLGLRETWFFGLRYNIKDTVA-WLKMDKKVLDQevPKEEPIIFHFLAKFYP 102
Cdd:cd17201   13 EYECEVekHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKnWLDPSKEIKKQ--IRSGPWHFAFTVKFYP 82
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 34-102 9.79e-07

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


Pssm-ID: 340626  Cd Length: 84  Bit Score: 47.05  E-value: 9.79e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348533462  34 EFSCEV--KWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQevPKEEPIIFHFLAKFYP 102
Cdd:cd17106   13 EYTCEVekRAKGQVLFDKVCEHLNLLEKDYFGLTYrDAQDQKNWLDPAKEIKKQ--IRSGPWLFSFNVKFYP 82
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 34-102 1.09e-06

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


Pssm-ID: 340722  Cd Length: 84  Bit Score: 46.89  E-value: 1.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348533462  34 EFSC--EVKWKGKDLFDLVCRTLGLRETWFFGLRYNIK-DTVAWLKMDKKVLDQevPKEEPIIFHFLAKFYP 102
Cdd:cd17202   13 EYSCdlEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSaNQKNWLDSTKEIKRQ--IRRLPWLFTFNVKFYP 82
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 318-546 1.65e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   318 VQQMKAQAREERARKQVER----QRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEE 393
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   394 EAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLL 473
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   474 EITSKAVYMSPGLAP------------DSMPQDVSFSRENLSFDFKDTdmkrlSMEIEKEKVEYMEKSKHLQEQLNELKT 541
Cdd:TIGR02168  905 ELESKRSELRRELEElreklaqlelrlEGLEVRIDNLQERLSEEYSLT-----LEEAEALENKIEDDEEEARRRLKRLEN 979


                   ....*
gi 348533462   542 EIESL 546
Cdd:TIGR02168  980 KIKEL 984
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
310-474 1.71e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  310 RRRVDSLEvqQMKAQARE-ERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAE-- 386
Cdd:COG4913   248 REQIELLE--PIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREel 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  387 ---KAQIAE---EEAKLLAQKAAEAETEMQRIKvtairgQEERRLMEQ-KMLEAKMVA-----LKMAEESERRAKEAEQL 454
Cdd:COG4913   326 delEAQIRGnggDRLEQLEREIERLERELEERE------RRRARLEALlAALGLPLPAsaeefAALRAEAAALLEALEEE 399

                         170       180
                  ....*....|....*....|
gi 348533462  455 KQDLLEARDSERRAKNKLLE 474
Cdd:COG4913   400 LEALEEALAEAEAALRDLRR 419
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-552 2.70e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 2.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQ--------------DEADMANEALLRSEQTAD 382
Cdd:TIGR02168  706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkelteleaeieeleERLEEAEEELAEAEAEIE 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   383 LLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEAR 462
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   463 DSERRAKNKLLEITSKAvymspglapDSMPQDVSFSRENLsfDFKDTDMKrlsmEIEKEKVEYMEKSKHLQEQLNELKTE 542
Cdd:TIGR02168  866 ELIEELESELEALLNER---------ASLEEALALLRSEL--EELSEELR----ELESKRSELRRELEELREKLAQLELR 930

                          250
                   ....*....|
gi 348533462   543 IESLKLKERE 552
Cdd:TIGR02168  931 LEGLEVRIDN 940
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
317-547 3.03e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.42  E-value: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAK 396
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 397 LLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKmvalKMAEESERRAKEAEQLKQDLLEARDsERRAKNKLLEIT 476
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELR----ERFGDAPVDLGNAEDFLEELREERD-ELREREAELEAT 434

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 477 SKAV---------YMSPGLAPDSmPQDVSFSRENLSFDFKDTDMKRLSMEIE--KEKVEYMEKSKHLQEQLNELKTEIES 545
Cdd:PRK02224 435 LRTArerveeaeaLLEAGKCPEC-GQPVEGSPHVETIEEDRERVEELEAELEdlEEEVEEVEERLERAEDLVEAEDRIER 513


                 ..
gi 348533462 546 LK 547
Cdd:PRK02224 514 LE 515
PTZ00121 PTZ00121
MAEBL; Provisional
 310-552 3.38e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  310 RRRVDSLEVQQMKAQARE----ERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLA 385
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  386 EKAQIAEEEAKLLAQKAAEAETEMQRIKVTAirgqEERRLMEQ---KMLEAKMVA--LKMAEESERRAKEAEQLKQDLLE 460
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKA----EEKKKADEakkKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKK 1432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  461 ARDSERRA--KNKLLEITSKAvymspglapdsmpqDVSFSRENLSfdfKDTDMKRLSMEIeKEKVEYMEKSKHLQEQLNE 538
Cdd:PTZ00121 1433 ADEAKKKAeeAKKADEAKKKA--------------EEAKKAEEAK---KKAEEAKKADEA-KKKAEEAKKADEAKKKAEE 1494

                         250
                  ....*....|....
gi 348533462  539 LKTEIESLKLKERE 552
Cdd:PTZ00121 1495 AKKKADEAKKAAEA 1508
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 311-488 7.26e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.67  E-value: 7.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 311 RRVDSLEVQQMKAQAREERARKQVErqRLQRE-KQLREEAERARDELERRLIQLQDEADMAN--EALLRSEQTADLL--- 384
Cdd:COG3883   44 AELEELNEEYNELQAELEALQAEID--KLQAEiAEAEAEIEERREELGERARALYRSGGSVSylDVLLGSESFSDFLdrl 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 385 --------AEKAQIAE--EEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQL 454
Cdd:COG3883  122 salskiadADADLLEElkADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201

                        170       180       190
                 ....*....|....*....|....*....|....
gi 348533462 455 KQDLLEARDSERRAKNKLLEITSKAVYMSPGLAP 488
Cdd:COG3883  202 EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-461 1.19e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDE-LERRLIQLQDEADMANEALLRSEQT-ADLLAE 386
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErLEEELEELEEALAELEEEEEEEEEAlEEAAEE 450

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348533462 387 KAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEA 461
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
PTZ00121 PTZ00121
MAEBL; Provisional
 309-569 1.36e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  309 RRRRVDSLEVQQMKAQAREERARKQvERQRLQREKQLREEAERARDElerRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVE---QLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  389 QIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQ---KMLEAKMVALKM-AEESERRAKeAEQLKQdllEARDS 464
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkKEAEEKKKAEELkKAEEENKIK-AEEAKK---EAEED 1742

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  465 ERRAKNKLLEITSKAVYMSPGLAPDSMPQDVSFSRENLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 544
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN 1822

                         250       260
                  ....*....|....*....|....*
gi 348533462  545 SLKLKERETPLDIIHNQNTEQGTSK 569
Cdd:PTZ00121 1823 DSKEMEDSAIKEVADSKNMQLEEAD 1847
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 35-102 1.40e-05

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: 43.64  E-value: 1.40e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  35 FSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQ-EVPKEepIIFHFLAKFYP 102
Cdd:cd17188   16 FVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFrNHAGNNVWLELLKPITKQiKNPKE--LIFKFTVKFFP 83
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 221-311 1.41e-05

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: 44.24  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 221 YFLIRNKK--GTDLLLGVDALGLHIYEPDNKL-TPKCSFPWNEIRNISYSDKEFTIKPLDKKANVFKFNSSRLRVNKLIL 297
Cdd:cd13187    5 HRVYREKKssTLSLWLGICSRGIIIYEEKNGArTPVLRFPWRETQKISFDKKKFTIESRGGSGIKHTFYTDSYKKSQYLL 84

                         90
                 ....*....|....*.
gi 348533462 298 QLCIGNH--DLFMRRR 311
Cdd:cd13187   85 QLCSAQHkfHIQMRSR 100
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
312-424 1.60e-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: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  312 RVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIA 391
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389

                          90       100       110
                  ....*....|....*....|....*....|...
gi 348533462  392 EEEAKLLAQKAAEAETEMQRIKVTAIRGQEERR 424
Cdd:COG4913   390 AALLEALEEELEALEEALAEAEAALRDLRRELR 422
growth_prot_Scy NF041483
polarized growth protein Scy;
317-467 1.86e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.90  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  317 EVQQMKAQAREERARKQVERQRLQREKQlrEEAERARDELERRLIQLQDEADMANEALlRSEQTADLLAEKAQIAEEEAK 396
Cdd:NF041483  583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348533462  397 LLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMA-EESERRAKEAEQLKQDLLEARDSERR 467
Cdd:NF041483  660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETLGSARAEADQERE 731
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-475 2.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 310 RRRVDSLEVQqmkaqareerARKQVERQRLQREKQLREEAERA--RDELERRLIQLQDEADMANEALLRSEQTADLLAEK 387
Cdd:COG1196  199 ERQLEPLERQ----------AEKAERYRELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAE 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 388 AQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAkmvALKMAEESERRAKEAEQ---LKQDLLEARDS 464
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL---EERLEELEEELAELEEEleeLEEELEELEEE 345

                        170
                 ....*....|.
gi 348533462 465 ERRAKNKLLEI 475
Cdd:COG1196  346 LEEAEEELEEA 356
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 34-102 2.50e-05

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: 43.01  E-value: 2.50e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348533462  34 EFSCEV--KWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQevPKEEPIIFHFLAKFYP 102
Cdd:cd17203   13 EYTCEVekRSKGQVLFDKVCEHLNLLEKDYFGLTYrDSENQKNWLDPAKEIKKQ--IRSGAWQFSFNVKFYP 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 323-546 2.57e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 323 AQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKLLAQKA 402
Cdd:COG1196  581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 403 AEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEITSKAVYM 482
Cdd:COG1196  661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 348533462 483 SPGLAPDSMPQDVSFSRENLSFDFKDTDMKRLSMEIEK-EKV------EY---MEKSKHLQEQLNELKTEIESL 546
Cdd:COG1196  741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlGPVnllaieEYeelEERYDFLSEQREDLEEARETL 814
PTZ00121 PTZ00121
MAEBL; Provisional
 308-552 2.92e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  308 MRRRRVDSLEVQQMKAQARE----ERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMAneallRSEQTADL 383
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA-----KKAAEAKK 1510

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  384 LAEKAQIAEEeakllAQKAAEAETEMQRIKVTAIRGQEERRLMEQKmleAKMVALKMAEESER--RAKEAEQLKQDLLEA 461
Cdd:PTZ00121 1511 KADEAKKAEE-----AKKADEAKKAEEAKKADEAKKAEEKKKADEL---KKAEELKKAEEKKKaeEAKKAEEDKNMALRK 1582

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  462 RDSERRAKNKLLEITSKAVYMSPGLAPDSM--PQDVSFSRENLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNEL 539
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659

                         250
                  ....*....|...
gi 348533462  540 KTEIESLKLKERE 552
Cdd:PTZ00121 1660 KIKAAEEAKKAEE 1672
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 328-562 3.04e-05

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: 47.36  E-value: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   328 ERARKQVERQRLQREKQLREeAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKLLAQKAAEAET 407
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAE-LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   408 EMQRIkvtairgQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEITSKAvymspgla 487
Cdd:TIGR02168  755 ELTEL-------EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-------- 819

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348533462   488 pdsmpQDVSFSRENLSFDFKDTdmkrlsmeiEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERETPLDIIHNQN 562
Cdd:TIGR02168  820 -----ANLRERLESLERRIAAT---------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 310-468 3.81e-05

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: 45.88  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  310 RRRVDSLEVQQMKAQAReerarkqveRQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAE--- 386
Cdd:pfam00529  57 QAALDSAEAQLAKAQAQ---------VARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIdla 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  387 ------------KAQIAEEEAKLLAQKA--AEAETEMQRIKVTAIRGQEERRlmeqkmleaKMVALKMAEESERRAKEAE 452
Cdd:pfam00529 128 rrrvlapiggisRESLVTAGALVAQAQAnlLATVAQLDQIYVQITQSAAENQ---------AEVRSELSGAQLQIAEAEA 198

                         170
                  ....*....|....*.
gi 348533462  453 QLKQDLLEARDSERRA 468
Cdd:pfam00529 199 ELKLAKLDLERTEIRA 214
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 331-552 4.42e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.66  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  331 RKQVERQRLQREKQLREEAERARDELERRliQLQDEADMANEALLrsEQTADLLAEKAQIA-EEEAKLLAQKAAEAETEM 409
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERR--RKLEEAEKARQAEM--DRQAAIYAEQERMAmERERELERIRQEERKREL 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  410 QRIKvtairgQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEItskavymspglapd 489
Cdd:pfam17380 363 ERIR------QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM-------------- 422

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 348533462  490 smpQDVSFSRENLsfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERE 552
Cdd:pfam17380 423 ---EQIRAEQEEA----RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLE 478
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 314-445 4.65e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.36  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 314 DSLEVQQMKAqaREERARKQVErQRLQREKQLREEAERARDELERRLIQLQDEadmanEALLRSEQtadllAEKAQIAEE 393
Cdd:PRK00409 514 DKEKLNELIA--SLEELERELE-QKAEEAEALLKEAEKLKEELEEKKEKLQEE-----EDKLLEEA-----EKEAQQAIK 580

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 348533462 394 EAKLLAQKAAEAETEMQRIKVTAIRGQ---EERRLMEQKMLEAKMVALKMAEESE 445
Cdd:PRK00409 581 EAKKEADEIIKELRQLQKGGYASVKAHeliEARKRLNKANEKKEKKKKKQKEKQE 635
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 328-478 4.84e-05

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: 46.04  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  328 ERARKQVERQRlQREKQLREEAERARDELERRLIQLQDEADMANE----------------ALLRSEQTADLLAEKAQIA 391
Cdd:pfam07888  51 EAANRQREKEK-ERYKRDREQWERQRRELESRVAELKEELRQSREkheeleekykelsassEELSEEKDALLAQRAAHEA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  392 -----EEEAKLLAQKAAEAETEMQRIKVTAIR--GQEERRLMEQKMLEAKMVALKmaEESERRAKEAEQLKQDLLEARDS 464
Cdd:pfam07888 130 rirelEEDIKTLTQRVLERETELERMKERAKKagAQRKEEEAERKQLQAKLQQTE--EELRSLSKEFQELRNSLAQRDTQ 207

                         170
                  ....*....|....
gi 348533462  465 ERRAKNKLLEITSK 478
Cdd:pfam07888 208 VLQLQDTITTLTQK 221
PTZ00121 PTZ00121
MAEBL; Provisional
 317-552 5.00e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  317 EVQQMKAQAREERARKqVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEAlLRSEQTADllAEKAQIAEEEAK 396
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARK-AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA-RKAEDAKK--AEAARKAEEVRK 1189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  397 LLAQKAAEaetEMQRIKvTAIRGQEERRLMEQKMLE--AKMVALKMAEESERRAKEAEQLKqdllEARDSERRAKNKLLE 474
Cdd:PTZ00121 1190 AEELRKAE---DARKAE-AARKAEEERKAEEARKAEdaKKAEAVKKAEEAKKDAEEAKKAE----EERNNEEIRKFEEAR 1261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  475 ITSKAVYMSPGLAPDSMPQDVSFSRENL--SFDFKDTDMKRLSMEIeKEKVEYMEKSKHLQEQLNELKTEIESLKLKERE 552
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKkkADEAKKAEEKKKADEA-KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340
PTZ00121 PTZ00121
MAEBL; Provisional
 310-552 5.04e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 5.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  310 RRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERrliqlQDEADMANEALLRSEQTAdllAEKAQ 389
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK-----AEEAKKADEAKKAEEAKK---ADEAK 1540

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  390 IAEEEAKL-LAQKAAEAETEMQRIKVTAIRGQEERRLM------EQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEAR 462
Cdd:PTZ00121 1541 KAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMalrkaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  463 DSERRAKNkllEITSKAVYMSPGLAPDSMPQDVSFSRENLSFDFKDTDMKRLSMEiEKEKVEYMEKS----KHLQEQLN- 537
Cdd:PTZ00121 1621 KAEELKKA---EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE-DKKKAEEAKKAeedeKKAAEALKk 1696

                         250
                  ....*....|....*..
gi 348533462  538 --ELKTEIESLKLKERE 552
Cdd:PTZ00121 1697 eaEEAKKAEELKKKEAE 1713
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 38-101 5.12e-05

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: 41.87  E-value: 5.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 348533462  38 EVKW----KGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMdKKVLDQEVPKEEPIIFHFLAKFY 101
Cdd:cd17104   14 EVEVdpkaNGQECLDKVCQKLGIIEKDYFGLQYtGPKGERLWLNL-RNRISRQLPGPPPYRLRLRVKFF 81
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 298-495 5.62e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.27  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  298 QLCIGNHDLFMRRRRVDSLEVQQMKAQAREERARKQVERQRLQrEKQLREEAERAR-DELERRLIQLQDEADMANEALLR 376
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE-EQERQQQVERLRqQEEERKRKKLELEKEKRDRKRAE 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  377 SEQ----TADLLAEKAQIAEEEAKllaQKAAEAETEMQRikvTAIRGQEERRLME------QKMLEAKMVALKMAEESER 446
Cdd:pfam17380 491 EQRrkilEKELEERKQAMIEEERK---RKLLEKEMEERQ---KAIYEEERRREAEeerrkqQEMEERRRIQEQMRKATEE 564

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 348533462  447 RAKEAEQLKQDLLEARDSERRAKNKLLEITSKAVYMSPGLAPDS---MPQDV 495
Cdd:pfam17380 565 RSRLEAMEREREMMRQIVESEKARAEYEATTPITTIKPIYRPRIseyQPPDV 616
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
309-449 6.03e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 45.63  E-value: 6.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSLEVQQMKAQAREERA--RKQVERQRLQREKQLREEAERARDELERRL--------IQLQDEADMANEALLRSE 378
Cdd:COG2268  230 QEREIETARIAEAEAELAKKKAeeRREAETARAEAEAAYEIAEANAEREVQRQLeiaerereIELQEKEAEREEAELEAD 309

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348533462 379 QTADLLAEKAQI-AEEEAKLLAQKA---AEAETEMQRIKVTAIRGQEERRLMEQKMLEakMVALKMAEESERRAK 449
Cdd:COG2268  310 VRKPAEAEKQAAeAEAEAEAEAIRAkglAEAEGKRALAEAWNKLGDAAILLMLIEKLP--EIAEAAAKPLEKIDK 382
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 22-101 6.53e-05

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: 41.83  E-value: 6.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  22 FNVRISTME-SDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDK---KVLDQEvpKEEPIIFhF 96
Cdd:cd17099    4 FVVRIQLLDnTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYvNKKGQLRWVDLEKplkKQLDKH--AHEPLLY-F 80


                 ....*
gi 348533462  97 LAKFY 101
Cdd:cd17099   81 GVMFY 85
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
304-431 6.57e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 6.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 304 HDLFMRRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMAN--------EALL 375
Cdd:COG4717  116 EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlslateEELQ 195

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 348533462 376 RSEQTADLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKML 431
Cdd:COG4717  196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
323-437 6.66e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 6.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  323 AQAREERARKQVERQRLQRE-------KQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEE-- 393
Cdd:COG4913   664 ASAEREIAELEAELERLDASsddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDla 743

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 348533462  394 --------EAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVA 437
Cdd:COG4913   744 rlelrallEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
PTZ00491 PTZ00491
major vault protein; Provisional
 320-456 6.68e-05

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 46.16  E-value: 6.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 320 QMKAQAREERARKQVERQRLQRekqlREEAERARdeleRRLIQLQDEadmaNEALLRSEQ-TADLLAE-KAQIAEEEAKL 397
Cdd:PTZ00491 669 RHQAELLEQEARGRLERQKMHD----KAKAEEQR----TKLLELQAE----SAAVESSGQsRAEALAEaEARLIEAEAEV 736

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 398 laqKAAEAETEMQRI-KVTAIRGQEERRLMEQKMlEAKMVALKMAEESERRAKEAEQLKQ 456
Cdd:PTZ00491 737 ---EQAELRAKALRIeAEAELEKLRKRQELELEY-EQAQNELEIAKAKELADIEATKFER 792
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 323-554 7.47e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 7.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 323 AQAREE---RARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLL-AEKAQIAEEEAKLL 398
Cdd:COG4942   17 AQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeAELAELEKEIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 399 AQKAAEAETEMQRIKVTAIRGQEER---RLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEI 475
Cdd:COG4942   97 AELEAQKEELAELLRALYRLGRQPPlalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 348533462 476 TSKAvymspglapdsmpQDVSFSRENLSFDFKDTdmKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERETP 554
Cdd:COG4942  177 EALL-------------AELEEERAALEALKAER--QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
310-472 8.84e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 45.25  E-value: 8.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 310 RRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERardELERRLIQLQD-EADMANEALLRSEQTADLLAEKA 388
Cdd:COG2268  191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQER---EIETARIAEAEaELAKKKAEERREAETARAEAEAA 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 389 -QIAEEEAKLLAQKAAEAETEMQRIKVTAIRgQEERRLMEQKMLEAKMVALKMAEESERRAkEAEQLKQDLL---EARDS 464
Cdd:COG2268  268 yEIAEANAEREVQRQLEIAEREREIELQEKE-AEREEAELEADVRKPAEAEKQAAEAEAEA-EAEAIRAKGLaeaEGKRA 345


                 ....*...
gi 348533462 465 ERRAKNKL 472
Cdd:COG2268  346 LAEAWNKL 353
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
317-473 9.03e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 9.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQAREERARKQVERQRLQREKQL------REEAERARDELERRLIQLQDEADMANEALlrsEQTADLLAEKAQI 390
Cdd:COG4717   99 ELEEELEELEAELEELREELEKLEKLLQLlplyqeLEALEAELAELPERLEELEERLEELRELE---EELEELEAELAEL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 391 AEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKmvalkmaEESERRAKEAEQLKQDLLEARDSERRAKN 470
Cdd:COG4717  176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ-------EELEELEEELEQLENELEAAALEERLKEA 248


                 ...
gi 348533462 471 KLL 473
Cdd:COG4717  249 RLL 251
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
317-480 1.06e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAK 396
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 397 LLAQKAAEAETEMQRIKVTAIRgQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEIT 476
Cdd:COG4717  155 LEELRELEEELEELEAELAELQ-EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233


                 ....
gi 348533462 477 SKAV 480
Cdd:COG4717  234 NELE 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-558 1.07e-04

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: 45.43  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMAneallrSEQTADLlaeKAQIAEEEAK 396
Cdd:TIGR02168  790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL------EEQIEEL---SEDIESLAAE 860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   397 LLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAE--QLKQDLLEARDSERRAKNKLLE 474
Cdd:TIGR02168  861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREleELREKLAQLELRLEGLEVRIDN 940

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   475 ITSK--AVYMSPGLAPDSMPQDVSFSRENLsfdfkDTDMKRLSMEIEK---EKVEYMEKSKHLQEQLNELKTEIESLKlK 549
Cdd:TIGR02168  941 LQERlsEEYSLTLEEAEALENKIEDDEEEA-----RRRLKRLENKIKElgpVNLAAIEEYEELKERYDFLTAQKEDLT-E 1014


                   ....*....
gi 348533462   550 ERETPLDII 558
Cdd:TIGR02168 1015 AKETLEEAI 1023
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 309-410 1.11e-04

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: 44.94  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  309 RRRRVDSLEVQQMKAQAREERARKQVER-----QRLQREKQlREEAERARDELERRL---IQLQDE----ADMANEALL- 375
Cdd:pfam15709 400 RQRQEEEERKQRLQLQAAQERARQQQEEfrrklQELQRKKQ-QEEAERAEAEKQRQKeleMQLAEEqkrlMEMAEEERLe 478

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 348533462  376 ------RSEQTADLLAEKAQIAEEEAKLLAQKAAEAETEMQ 410
Cdd:pfam15709 479 yqrqkqEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQ 519
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 309-457 1.16e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSLEVQQMKAQAREERARKQverqrlqrEKQLREEAERARDELERRLIQLQDEADMAN-EALLRSEQTADLL--- 384
Cdd:COG4942   67 LARRIRALEQELAALEAELAELEKE--------IAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVrrl 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 385 --------AEKAQIAE--EEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQL 454
Cdd:COG4942  139 qylkylapARREQAEElrADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218


                 ...
gi 348533462 455 KQD 457
Cdd:COG4942  219 QQE 221
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 350-476 1.24e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 350 ERARD---ELERRLIQLQDEADMANEAL-LRSEQT---ADLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEE 422
Cdd:COG1196  189 ERLEDilgELERQLEPLERQAEKAERYReLKEELKeleAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 348533462 423 RRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEIT 476
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 307-377 1.41e-04

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 44.86  E-value: 1.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348533462 307 FMRRRRVDSLEvqqmkaqaREERARKQVERQRLQREKQLREEAERARDELE-----RRL--IQLQDEADMANEALLRS 377
Cdd:PLN03086   3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKADQQMQESLQA 72
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 310-453 1.42e-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: 44.83  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   310 RRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEA------ERARDELERRLIQLQDEADMANEALLRSEQTADl 383
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfartalKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN- 681

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   384 laEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQ 453
Cdd:pfam12128  682 --ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAEL 749
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 28-102 1.44e-04

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: 40.57  E-value: 1.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348533462  28 TMESDLEFSCEVK--WKGKDLFDLVCRTLGLRETWFFGLR-YNIKDTVAWLKMDKKVLDQevPKEEPIIFHFLAKFYP 102
Cdd:cd17105    6 SLLDDTVYECEVEkhAKGQDLFKKVCEHLNLLEEDYFGLAiWDSPTSKTWLDPAKEIKKQ--VHGGPWEFTFNVKFYP 81
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 210-274 1.53e-04

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: 41.56  E-value: 1.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348533462 210 IAQDLDMYGVNYFLIRNKKGTDLLLGVDALGLHIYEpdnKLTPKCSFPWNEIRNISYSDKEFTIK 274
Cdd:cd13193    2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQ---GFTKINTFSWAKIRKLSFKRKRFLIK 63
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 327-453 1.59e-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: 42.34  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  327 EERARKQVERQRLQREKQLREEAERARDELERRLiQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAKLLAQKaaEAE 406
Cdd:pfam05672  10 EEAARILAEKRRQAREQREREEQERLEKEEEERL-RKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEE--EAE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 348533462  407 TEMQRIKVTAIRGQEERRLMEQKMLEAkmvALKMAEESERRAKEAEQ 453
Cdd:pfam05672  87 EREQREQEEQERLQKQKEEAEAKAREE---AERQRQEREKIMQQEEQ 130
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-474 1.63e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:COG1196  666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 389 QIAEEEA---KLLAQKAAEAETEMQRIKvtairgqeeRRLmeqKMLEA-KMVALK-MAEESERRAKEAEQlKQDLLEARD 463
Cdd:COG1196  746 ELLEEEAleeLPEPPDLEELERELERLE---------REI---EALGPvNLLAIEeYEELEERYDFLSEQ-REDLEEARE 812

                        170
                 ....*....|....*....
gi 348533462 464 S--------ERRAKNKLLE 474
Cdd:COG1196  813 TleeaieeiDRETRERFLE 831
growth_prot_Scy NF041483
polarized growth protein Scy;
321-467 1.84e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 44.82  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  321 MKAQARE--ERARKQVERQRLQREKQ---LREEAERA----RDELERRLIQLQDEADM--------ANEALLRSEQT-AD 382
Cdd:NF041483  518 LRRQAEEtlERTRAEAERLRAEAEEQaeeVRAAAERAarelREETERAIAARQAEAAEeltrlhteAEERLTAAEEAlAD 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  383 LLAEKAQI---AEEEAKLLAQKAAE--------AETEMQRIKVTAIRGQEERRlmeqkmLEAKMVALKMAEESerrAKEA 451
Cdd:NF041483  598 ARAEAERIrreAAEETERLRTEAAErirtlqaqAEQEAERLRTEAAADASAAR------AEGENVAVRLRSEA---AAEA 668

                         170
                  ....*....|....*.
gi 348533462  452 EQLKQdllEARDSERR 467
Cdd:NF041483  669 ERLKS---EAQESADR 681
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 315-465 1.94e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 44.36  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  315 SLEVQQMkaqaREERARKQVERQR----LQRE-KQLREEAERARDELERRLIQLQDEADMANEALLR------------- 376
Cdd:pfam07111 480 SLELEQL----REERNRLDAELQLsahlIQQEvGRAREQGEAERQQLSEVAQQLEQELQRAQESLASvgqqlevarqgqq 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  377 --SEQTADLLAEKAQIAEEEAKLLAQKAAEAETEM-QRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERrakeAEQ 453
Cdd:pfam07111 556 esTEEAASLRQELTQQQEIYGQALQEKVAEVETRLrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER----NQE 631

                         170
                  ....*....|..
gi 348533462  454 LKQDLLEARDSE 465
Cdd:pfam07111 632 LRRLQDEARKEE 643
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 317-408 2.53e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 44.17  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQAREERARKQVERQRLQREKQLREeaERARDELERRLIQLQD---------EADMANEALLRSEQTADLLAEK 387
Cdd:PRK05035 440 AIEQEKKKAEEAKARFEARQARLEREKAARE--ARHKKAAEARAAKDKDavaaalarvKAKKAAATQPIVIKAGARPDNS 517

                         90       100
                 ....*....|....*....|.
gi 348533462 388 AQIAEEEAKLLAQKAAEAETE 408
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQ 538
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 313-484 2.56e-04

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.84  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  313 VDSLEVQQMKAQAREERArKQVERQRLQREKQLREEAERAR--DELERRLIQLQDEADMANEALLRSEQTADLLAEKAQI 390
Cdd:pfam05262 174 TDSISDKKVVEALREDNE-KGVNFRRDMTDLKERESQEDAKraQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  391 AEEEAKLLAQKAA-----EAETEMQRIKVTAIRGQEErrlMEQKMLEAKMVALKMAEESERRAKEAEQlkqdllEARDSE 465
Cdd:pfam05262 253 KQQEAKNLPKPADtsspkEDKQVAENQKREIEKAQIE---IKKNDEEALKAKDHKAFDLKQESKASEK------EAEDKE 323

                         170
                  ....*....|....*....
gi 348533462  466 RRAKNKLLEITSKAVYMSP 484
Cdd:pfam05262 324 LEAQKKREPVAEDLQKTKP 342
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 305-422 2.57e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 305 DLFMRRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLL 384
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 348533462 385 AEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEE 422
Cdd:COG1196  467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 217-290 2.95e-04

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: 40.70  E-value: 2.95e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348533462 217 YGVNYFLIRNKKGTDLLLGVDALGLHIYEPDnkLTPKCSFPWNEIRNISYSDKEFTIKPL----DKKANVFKFNSSRL 290
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDD--FEVIERIPYTAIQMATSSGRVFTLTYLsddgSVKVLEFKLPSTRA 76
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 317-466 3.04e-04

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: 43.79  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIqlqdeadmANEALLRSEQTADllaEKAQIAEEEAK 396
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRR--------FEEIRLRKQRLEE---ERQRQEEEERK 409

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 348533462  397 LLAQKAAEAETEMQrikvtaiRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAE-QLKQD---LLEARDSER 466
Cdd:pfam15709 410 QRLQLQAAQERARQ-------QQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEmQLAEEqkrLMEMAEEER 476
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 24-102 3.10e-04

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: 39.79  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  24 VRISTMESDLE-FSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY-NIKDTVAWLKMDKKVLDQeVPKEEPIIFHFLAKFY 101
Cdd:cd17189    3 IKVQMLDDTQEvFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFqDHRKVMVWLDLLKPIVKQ-IRRPKHVVLRFVVKFF 81


                 .
gi 348533462 102 P 102
Cdd:cd17189   82 P 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-546 3.18e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:COG1196  553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 389 QIAEEEAKLLAQKAAEAETEMQRIkvtAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRA 468
Cdd:COG1196  633 EAALRRAVTLAGRLREVTLEGEGG---SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348533462 469 KNKLLEITSKAVymspglapDSMPQDVSFSRENLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESL 546
Cdd:COG1196  710 AEAEEERLEEEL--------EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-101 3.65e-04

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: 39.64  E-value: 3.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 348533462  25 RISTME-SDLEFSCEVKWKGKDLFDLVCRTLGLRETWFFGLRYNIKDTVA-WLKMDKKVLDQeVPKEEPIIFHFLAKFY 101
Cdd:cd17205    6 RVSLLDgTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAhWLDVTKSIKKQ-VKIGPPYCLHLRVKFY 83
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 309-457 5.23e-04

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: 43.02  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLR-----EEAERARDELERRLIQLQDEADMANEALLRSEQTADL 383
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRlrkqrLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL 432

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348533462  384 LAEKAQIAEEEA-KLLAQKAAEAETEMQ---RIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQD 457
Cdd:pfam15709 433 QELQRKKQQEEAeRAEAEKQRQKELEMQlaeEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALE 510
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 305-416 7.09e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 7.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 305 DLFMRRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLrEEAERARDELERRLIQLQDEADMANEALlrseqtADLL 384
Cdd:COG3883  116 DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL-AELEALKAELEAAKAELEAQQAEQEALL------AQLS 188

                         90       100       110
                 ....*....|....*....|....*....|..
gi 348533462 385 AEKAQIAEEEAKLLAQKAAEAETEMQRIKVTA 416
Cdd:COG3883  189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 316-473 7.61e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 316 LEVQQMKAQAreERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEallrsEQTADLLAEKAQIAEEEA 395
Cdd:PRK09510 111 LAAQEQKKQA--EEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA-----EAKKKAEAEAAKKAAAEA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 396 KLLAQKAAEAETEMQ-RIKVTAIRGQEERRLMEQKML-EAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLL 473
Cdd:PRK09510 184 KKKAEAEAAAKAAAEaKKKAEAEAKKKAAAEAKKKAAaEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 310-570 7.65e-04

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: 42.80  E-value: 7.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   310 RRRVDSLEVQQ--MKAQAREERARKQVERQRLQRE-KQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLA- 385
Cdd:pfam15921  291 RSQANSIQSQLeiIQEQARNQNSMYMRQLSDLESTvSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSq 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   386 EKAQIAEEEAKLLA-----QKAAEAETEMQR----------IKVTAIRGQEERRLMEQKMLEAKMVALKMAEESE-RRAK 449
Cdd:pfam15921  371 ESGNLDDQLQKLLAdlhkrEKELSLEKEQNKrlwdrdtgnsITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQmERQM 450

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   450 EAEQLKQDLLEARDSERRAKNKLLEITSKAVYMSPGLAPDSMPQDVSFSRENLSFDFKDTDMKRLSMEIEK------EKV 523
Cdd:pfam15921  451 AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdLKL 530

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 348533462   524 EYMEKSKHLQEQLNELKTEIESLKLK--ERETPLDIIHNQ--NTEQGTSKH 570
Cdd:pfam15921  531 QELQHLKNEGDHLRNVQTECEALKLQmaEKDKVIEILRQQieNMTQLVGQH 581
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 325-553 1.17e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   325 AREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMAneallrSEQTADLLAEKAQIAEEEAKLlAQKAAE 404
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA------SRKIGEIEKEIEQLEQEEEKL-KERLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   405 AETEMQRIKvtaiRGQEERRlMEQKMLEAKMVALkmaeeseRRAKEAEQLKQDLLEARDSERRAKNKLLEITSkavymsp 484
Cdd:TIGR02169  742 LEEDLSSLE----QEIENVK-SELKELEARIEEL-------EEDLHKLEEALNDLEARLSHSRIPEIQAELSK------- 802

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348533462   485 glapdsmpQDVSFSRENLSFDFKDTDMKRLSME---IEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERET 553
Cdd:TIGR02169  803 --------LEEEVSRIEARLREIEQKLNRLTLEkeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 35-101 1.37e-03

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: 38.06  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348533462  35 FSCEVKWKGKDLFDLVCRTLGLRETWFFGLRY----NIKDTVAWLKMDKKVLDQeVPKEEPIIFHFLAKFY 101
Cdd:cd17100   16 FEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFsddsPATDSMRWLDPLKPIRKQ-IKGGPPYYLNFRVKFY 85
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 312-456 1.47e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.86  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  312 RVDSLEVQQMKAQAREER---ARKQVER--QRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLae 386
Cdd:COG3096   513 RLQQLRAQLAELEQRLRQqqnAERLLEEfcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL-- 590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  387 KAQIAEEEAK----LLAQKAAEAETEM------QRIKVTAIRGQEERRLMEQKMLEAKMVALKmaeesERRAKEAEQLKQ 456
Cdd:COG3096   591 RARIKELAARapawLAAQDALERLREQsgealaDSQEVTAAMQQLLEREREATVERDELAARK-----QALESQIERLSQ 665
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 311-563 1.58e-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: 41.50  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   311 RRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQlqdeADMANEALLRSEQTADLLAEKAQI 390
Cdd:pfam02463  672 TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL----ADRVQEAQDKINEELKLLKQKIDE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   391 AEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARD------- 463
Cdd:pfam02463  748 EEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEqllieqe 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   464 -SERRAKNKLLEITSKAVYMSPGLAPDSMPQDVSFSRENLSFDFKDTdmKRLSMEIEKEKVEYMEKSKHLQEQLNELKTE 542
Cdd:pfam02463  828 eKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL--KEEELEEQKLKDELESKEEKEKEEKKELEEE 905

                          250       260
                   ....*....|....*....|.
gi 348533462   543 IESLKLKERETPLDIIHNQNT 563
Cdd:pfam02463  906 SQKLNLLEEKENEIEERIKEE 926
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 354-455 1.93e-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: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 354 DELERRLIQLQDEAdmanEALLRSEQTADllAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEA 433
Cdd:COG0542  414 DELERRLEQLEIEK----EALKKEQDEAS--FERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487

                         90       100
                 ....*....|....*....|..
gi 348533462 434 KMVALKMAEESERRAKEAEQLK 455
Cdd:COG0542  488 PELEKELAELEEELAELAPLLR 509
Rabaptin pfam03528
Rabaptin;
318-553 1.93e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 40.86  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  318 VQQMKAQAREERARKQV---------ERQ---RLQREK----QLREEAERARDELERRLIQLQDEADMANEaLLRSEQTA 381
Cdd:pfam03528  95 IDEVKSQWQEEVASLQAimketvreyEVQfhrRLEQERaqwnQYRESAEREIADLRRRLSEGQEEENLEDE-MKKAQEDA 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  382 DLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRgqEERRLMEQKM---LEAKMVALKMAEESERRAKEAEQLKQDL 458
Cdd:pfam03528 174 EKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMK--ELNHYLEAEKscrTDLEMYVAVLNTQKSVLQEDAEKLRKEL 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  459 LEA---RDSERRAKNKLLEITSKAvymspglapdsmpQDVSFSRENLSFdfkdTDMKRLSMEIEKE---KVEYMEKSKHL 532
Cdd:pfam03528 252 HEVchlLEQERQQHNQLKHTWQKA-------------NDQFLESQRLLM----RDMQRMESVLTSEqlrQVEEIKKKDQE 314

                         250       260
                  ....*....|....*....|.
gi 348533462  533 QEQLNELKTEIESLKLKERET 553
Cdd:pfam03528 315 EHKRARTHKEKETLKSDREHT 335
PRK12704 PRK12704
phosphodiesterase; Provisional
 310-474 2.19e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 310 RRRVDSLEVQQMKAQARE--ERARKQVERQRLQRE-------KQLREEAER----ARDEL---ERRLIQLQDEADMANEA 373
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRilEEAKKEAEAIKKEALleakeeiHKLRNEFEKelreRRNELqklEKRLLQKEENLDRKLEL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 374 LLRSEQTADL----LAEKAQIAEEEAKLLAQKAAEAETEMQRIkvtAIRGQEERR--LMEQKMLEAKMVALKMAEESERR 447
Cdd:PRK12704 105 LEKREEELEKkekeLEQKQQELEKKEEELEELIEEQLQELERI---SGLTAEEAKeiLLEKVEEEARHEAAVLIKEIEEE 181

                        170       180
                 ....*....|....*....|....*..
gi 348533462 448 AKEaeqlkqdllearDSERRAKNKLLE 474
Cdd:PRK12704 182 AKE------------EADKKAKEILAQ 196
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 333-460 2.21e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.19  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  333 QVERQRLQREKQLREEAERARD--------------------ELERRLIQLQDEADMANEALLRSEQtADLLAEKAQIAE 392
Cdd:PRK10929  113 QVSSQLLEKSRQAQQEQDRAREisdslsqlpqqqtearrqlnEIERRLQTLGTPNTPLAQAQLTALQ-AESAALKALVDE 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348533462  393 EEaklLAQKAAEAETEMQRIKVTAIRGQEER----------RLMEQKMLEAKMvALkmaEESERRAKEAEQLKQDLLE 460
Cdd:PRK10929  192 LE---LAQLSANNRQELARLRSELAKKRSQQldaylqalrnQLNSQRQREAER-AL---ESTELLAEQSGDLPKSIVA 262
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
317-476 2.47e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAE-KAQIAEEEA 395
Cdd:COG4717  348 ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGElEELLEALDE 427

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 396 KLLAQKAAEAETEMQrikvtAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLleARDSERRAKNKLLEI 475
Cdd:COG4717  428 EELEEELEELEEELE-----ELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAEL--RELAEEWAALKLALE 500


                 .
gi 348533462 476 T 476
Cdd:COG4717  501 L 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 317-557 2.49e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEE-- 394
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEie 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   395 AKLLAQKAAEAETEMQRIKVTAIRGQE---ERRLMEQKMLEAKMVALKMAEESER---RAKEAEQLKQDLLEARDSERRA 468
Cdd:TIGR02169  755 NVKSELKELEARIEELEEDLHKLEEALndlEARLSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKEYLEKE 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   469 KNKLLEITSkavymspglapDSMPQDVSFSRENLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKL 548
Cdd:TIGR02169  835 IQELQEQRI-----------DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903


                   ....*....
gi 348533462   549 KERETPLDI 557
Cdd:TIGR02169  904 KIEELEAQI 912
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 330-470 2.66e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.21  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  330 ARKQVERQRLQREKQLREEAERArDELERRLIQLQdEADMANEALLRSEQTADLLAEKAQIAEEEAKLLAQKAAEAETEM 409
Cdd:TIGR02794  48 VAQQANRIQQQKKPAAKKEQERQ-KKLEQQAEEAE-KQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 348533462  410 QRIKVTAIRGQEERRlmEQKMLEAkmvALKMAEEsERRAKEAEQLKQDLLEAR---DSERRAKN 470
Cdd:TIGR02794 126 AKQAAEAKAKAEAEA--ERKAKEE---AAKQAEE-EAKAKAAAEAKKKAEEAKkkaEAEAKAKA 183
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 307-411 2.68e-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: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 307 FMRRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAE 386
Cdd:COG4942  134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213

                         90       100
                 ....*....|....*....|....*
gi 348533462 387 KAQIAEEEAKLLAQKAAEAETEMQR 411
Cdd:COG4942  214 ELAELQQEAEELEALIARLEAEAAA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
325-468 2.86e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  325 AREERARKQVERQRLQRE----KQLREEAERARDELERRLIQLQ-------DEADM--ANEALLRSEQT-ADLLAEKAQI 390
Cdd:COG4913   608 NRAKLAALEAELAELEEElaeaEERLEALEAELDALQERREALQrlaeyswDEIDVasAEREIAELEAElERLDASSDDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  391 AEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRL----MEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSER 466
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELeqaeEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767


                  ..
gi 348533462  467 RA 468
Cdd:COG4913   768 RE 769
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 309-361 2.87e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 40.88  E-value: 2.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 348533462  309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLREEAERAR-DELERRLI 361
Cdd:PTZ00266  459 RIERLEREERERLERERMERIERERLERERLERERLERDRLERDRlDRLERERV 512
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
310-475 3.06e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  310 RRRVDSLEVQQMKAQAREERARKQveRQRLQREKQLREE------AERARDELERRLIQL---QDEADMANEALLRSEQT 380
Cdd:COG4913   623 EEELAEAEERLEALEAELDALQER--REALQRLAEYSWDeidvasAEREIAELEAELERLdasSDDLAALEEQLEELEAE 700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  381 ADLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKmvaLKMAEESERRAKEAEQLKQDLLE 460
Cdd:COG4913   701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER---FAAALGDAVERELRENLEERIDA 777

                         170
                  ....*....|....*
gi 348533462  461 ARDSERRAKNKLLEI 475
Cdd:COG4913   778 LRARLNRAEEELERA 792
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
317-558 3.17e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQIAEEEAK 396
Cdd:COG4372   60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 397 LLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMV----ALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKL 472
Cdd:COG4372  140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 473 LEITSKAVYMSPGLAPDSMPQDVSFSRENLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERE 552
Cdd:COG4372  220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299


                 ....*.
gi 348533462 553 TPLDII 558
Cdd:COG4372  300 LLLNLA 305
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 309-396 3.36e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 309 RRRRVDSL-----EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADL 383
Cdd:COG4942  148 RREQAEELradlaELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227

                         90
                 ....*....|...
gi 348533462 384 LAEKAQIAEEEAK 396
Cdd:COG4942  228 LIARLEAEAAAAA 240
mukB PRK04863
chromosome partition protein MukB;
316-469 3.46e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  316 LEVQQMKA----QAReerarkqverQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADlLAEKAQIA 391
Cdd:PRK04863  406 LDVQQTRAiqyqQAV----------QALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS-VAQAAHSQ 474

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348533462  392 EEEAKLLAQKAAeAETEMQRIKVTAIrgQEERRLMEQKMLEAKMVALkmaeeserRAKEAEqLKQDLLEARDSERRAK 469
Cdd:PRK04863  475 FEQAYQLVRKIA-GEVSRSEAWDVAR--ELLRRLREQRHLAEQLQQL--------RMRLSE-LEQRLRQQQRAERLLA 540
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 305-464 3.46e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 40.37  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  305 DLFMRRRRVDSLEVQQMKAQAREERARKQVERQRLQREKQlREEAERARDELERRliqlQDEADMANEALLRSEQTADL- 383
Cdd:pfam05262 193 GVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKA-QQKADFAQDNADKQ----RDEVRQKQQEAKNLPKPADTs 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  384 --------------LAEKAQIAEEEAKLLAQKAAEAETEMQRIKVtairgQEERRLMEQKMLEAKMVALKMAEESERRAK 449
Cdd:pfam05262 268 spkedkqvaenqkrEIEKAQIEIKKNDEEALKAKDHKAFDLKQES-----KASEKEAEDKELEAQKKREPVAEDLQKTKP 342

                         170
                  ....*....|....*.
gi 348533462  450 EAE-QLKQDLLEARDS 464
Cdd:pfam05262 343 QVEaQPTSLNEDAIDS 358
PRK12705 PRK12705
hypothetical protein; Provisional
 295-473 4.19e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 295 LILQLCIGNHDLFMRRRRVDSLEVQQMKAQAREErarkqVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEAL 374
Cdd:PRK12705  12 LLIGLLLGVLVVLLKKRQRLAKEAERILQEAQKE-----AEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 375 LRSEQtaDLLAEKAQIAEEEAKLLAQKAAEAETEMQRIKVTAIRGQEERRLMEQKMLEAKMVALKMAeESERRAKEAEQL 454
Cdd:PRK12705  87 VQKEE--QLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLL-DAELEEEKAQRV 163

                        170
                 ....*....|....*....
gi 348533462 455 KQDLLEARDSERRAKNKLL 473
Cdd:PRK12705 164 KKIEEEADLEAERKAQNIL 182
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 316-461 4.31e-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: 39.63  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  316 LEVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADMA------NEALLRSEQTADLLAEKAQ 389
Cdd:pfam15558 100 AEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEAchkrqlKEREEQKKVQENNLSELLN 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348533462  390 iaEEEAKLLAQKAAEAETEMQR--IKVTAIRGQEER-RLMEQKMLEAKMVALKMAEESER---RAKEAEQLKQDLLEA 461
Cdd:pfam15558 180 --HQARKVLVDCQAKAEELLRRlsLEQSLQRSQENYeQLVEERHRELREKAQKEEEQFQRakwRAEEKEEERQEHKEA 255
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 42-101 4.43e-03

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: 36.33  E-value: 4.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348533462  42 KGKDLFDLVCRTLGLRETWFFGLRYNIKDTVA-WLKMDKKVLDQeVPKEEPIIFHFLAKFY 101
Cdd:cd17204   22 KGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAhWLDHTKPIKKQ-IKIGPPYTLHFRIKYY 81
DegS pfam05384
Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU ...
 319-370 4.59e-03

Sensor protein DegS; This is small family of Bacillus DegS proteins. The DegS-DegU two-component regulatory system of Bacillus subtilis controls various processes that characterize the transition from the exponential to the stationary growth phase, including the induction of extracellular degradative enzymes, expression of late competence genes and down-regulation of the sigma D regulon. The family also contains one sequence Swiss:Q8R9D3 from Thermoanaerobacter tengcongensis which are described as sensory transduction histidine kinases.


Pssm-ID: 428449 [Multi-domain]  Cd Length: 159  Bit Score: 38.23  E-value: 4.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 348533462  319 QQMKaQAREERARKQVERQRLQ-REKQLREEaeraRDELERRLIQLQDEADMA 370
Cdd:pfam05384  77 EDIK-EAYEEAKDLQVELALLReREKQLRER----RDELERRLKNLKETIERA 124
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 309-420 4.73e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.04  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  309 RRRRVDSLEVQQMKAQAREERARKQVERQRLQREkQLREEAERARDELErrlIQLQDEADMANEAL-LRSEQTADL---L 384
Cdd:PRK10929  185 LKALVDELELAQLSANNRQELARLRSELAKKRSQ-QLDAYLQALRNQLN---SQRQREAERALESTeLLAEQSGDLpksI 260

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 348533462  385 AEKAQIAEEEAKLLAQKA------------AEAETEMQRIKVTAIRGQ 420
Cdd:PRK10929  261 VAQFKINRELSQALNQQAqrmdliasqqrqAASQTLQVRQALNTLREQ 308
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
310-467 5.01e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 310 RRRVDSLE--VQQMKAQAR----EERArkQVERQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADL 383
Cdd:COG3206  188 RKELEEAEaaLEEFRQKNGlvdlSEEA--KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 384 LAEKAQIAEEEAKL--LAQKAAEAETEMQRIK--VTAIRGQ---EERRLMEQkmLEAKMVALKMAEESERRAKeaEQLKQ 456
Cdd:COG3206  266 QQLRAQLAELEAELaeLSARYTPNHPDVIALRaqIAALRAQlqqEAQRILAS--LEAELEALQAREASLQAQL--AQLEA 341

                        170
                 ....*....|.
gi 348533462 457 DLLEARDSERR 467
Cdd:COG3206  342 RLAELPELEAE 352
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 310-551 5.23e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 5.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   310 RRRVDSLEVQQMKAQAREERARKQVERQRLQREKQLReeaeraRDELERRLIQLqdeadmanEALLRSEQTADLLAEKAQ 389
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAER------YQALLKEKREY--------EGYELLKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   390 I------AEEEAKLLAQKAAEAETEMQRIKVTaiRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARD 463
Cdd:TIGR02169  242 IerqlasLEEELEKLTEEISELEKRLEEIEQL--LEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   464 SERRAKNKLLEITSKAVYMSpglAPDSMPQDVSFSRENLSFDFKDTDMKRLSM-----EIEKEKVEYMEKSKHLQEQLNE 538
Cdd:TIGR02169  320 AEERLAKLEAEIDKLLAEIE---ELEREIEEERKRRDKLTEEYAELKEELEDLraeleEVDKEFAETRDELKDYREKLEK 396

                          250
                   ....*....|...
gi 348533462   539 LKTEIESLKLKER 551
Cdd:TIGR02169  397 LKREINELKRELD 409
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 317-474 5.72e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 317 EVQQMKAQARE-ERARKQVERQRLQREKQLREeAERARDELERRLIQLQDEADMANEAL-LRSEQTADLLAE---KAQIA 391
Cdd:COG4942   42 ELAALKKEEKAlLKQLAALERRIAALARRIRA-LEQELAALEAELAELEKEIAELRAELeAQKEELAELLRAlyrLGRQP 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 392 EEEAKLLAQKAAEAETEMQRIK--VTAIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAK 469
Cdd:COG4942  121 PLALLLSPEDFLDAVRRLQYLKylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200


                 ....*
gi 348533462 470 NKLLE 474
Cdd:COG4942  201 LARLE 205
DUF6381 pfam19908
Family of unknown function (DUF6381); This entry represents a member of a biosynthetic gene ...
 318-352 5.78e-03

Family of unknown function (DUF6381); This entry represents a member of a biosynthetic gene cluster (BGC). This BGC (BGC0001558) is described by MIBiG as an example of the following biosynthetic class, polyketide, in particular the cosmomycin C biosynthetic gene cluster from Streptomyces sp. CNT302. This family appears to be predominantly found in actinobacteria.


Pssm-ID: 466229  Cd Length: 62  Bit Score: 35.64  E-value: 5.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 348533462  318 VQQMKAQARE-----ERARKQVERQRLQRE-KQLREEAERA 352
Cdd:pfam19908  11 AQQMREKAQEleeaaERATDPEERERLQEKaRRLREQSEQE 51
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
310-478 5.83e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 310 RRRVDSLEVQQMKAQAREERARKQVERQ-RLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKA 388
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEdRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA 560

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 389 QIAEEEAKLLAQKAAEAETEMQRIK-----VTAIR---------GQEERRLMEQKMLEAKMVAL---KMAEESERRAKEA 451
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKeriesLERIRtllaaiadaEDEIERLREKREALAELNDErreRLAEKRERKRELE 640

                        170       180
                 ....*....|....*....|....*...
gi 348533462 452 EQLKQDLLE-ARDSERRAKNKLLEITSK 478
Cdd:PRK02224 641 AEFDEARIEeAREDKERAEEYLEQVEEK 668
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 343-552 6.48e-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: 39.65  E-value: 6.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   343 KQLREEAERARDELERRLIQLQdeaDMANEaLLRSEQTADLLAEKAQiaeeeaKLLAQKAAEAETEmqrIKVTAIRGQEE 422
Cdd:TIGR02168  171 KERRKETERKLERTRENLDRLE---DILNE-LERQLKSLERQAEKAE------RYKELKAELRELE---LALLVLRLEEL 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   423 RrlmeqKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDSERRAKNKLLEITSKAVYMSPGLAPDsMPQDVSFSRENL 502
Cdd:TIGR02168  238 R-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-LEQQKQILRERL 311

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 348533462   503 SFDfkDTDMKRLSMEIE---KEKVEYMEKSKHLQEQLNELKTEIESLKLKERE 552
Cdd:TIGR02168  312 ANL--ERQLEELEAQLEeleSKLDELAEELAELEEKLEELKEELESLEAELEE 362
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 317-553 6.58e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 6.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   317 EVQQMKAQAREERARKQVERQRLQREKQLREEAERARDELERRLIQLQDEADManeallRSEQTADLLAEKAQIAEEEAK 396
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS------IEKEIENLNGKKEELEEELEE 872

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   397 LlaqKAAEAETEMQRIKVtairgQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQLKQDLLEARDserraknKLLEIT 476
Cdd:TIGR02169  873 L---EAALRDLESRLGDL-----KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE-------ELSEIE 937

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462   477 SKAVYMSPGLAPDSMPQDVSFSRENLSFD---FKDTDMKRLS--MEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKER 551
Cdd:TIGR02169  938 DPKGEDEEIPEEELSLEDVQAELQRVEEEiraLEPVNMLAIQeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017


                   ..
gi 348533462   552 ET 553
Cdd:TIGR02169 1018 EV 1019
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 330-420 7.15e-03

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: 37.03  E-value: 7.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 330 ARKQVERQRLQREKQLREEAERARDELERRLIQLQDEAD-MANEALLRSEQTADLLAEKAQiaEEEAKLLAQKAAEAETE 408
Cdd:cd06503   30 EREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQeIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQE 107

                         90
                 ....*....|..
gi 348533462 409 MQRIKvTAIRGQ 420
Cdd:cd06503  108 KEKAL-AELRKE 118
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
 336-453 7.37e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 39.06  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 336 RQRLQREKQLREEAERARDELERRLIQLQDEADMANEALLRSEQTADLLAEKAQiAEEEAKLLAQKAAEAETEMQRIKVT 415
Cdd:PRK00247 289 EQRAQYREKQKEKKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKTRTAEKNE-AKARKKEIAQKRRAAEREINREARQ 367

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 348533462 416 AIRGQEERRLMEQKMLEAKMVALKMAEESERRAKEAEQ 453
Cdd:PRK00247 368 ERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEE 405
PRK09039 PRK09039
peptidoglycan -binding protein;
291-410 7.81e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.79  E-value: 7.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462 291 RVNKLILQLcigNHDLFMRRRRVDSLEVQQmkAQAREERARKQVERQRLQrekQLREEAERARDELERRL----IQLQDE 366
Cdd:PRK09039  57 RLNSQIAEL---ADLLSLERQGNQDLQDSV--ANLRASLSAAEAERSRLQ---ALLAELAGAGAAAEGRAgelaQELDSE 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 348533462 367 ADMANEAL----LRSEQTADLlaeKAQIAEEEAKLLAQKAAEAETEMQ 410
Cdd:PRK09039 129 KQVSARALaqveLLNQQIAAL---RRQLAALEAALDASEKRDRESQAK 173
PTZ00121 PTZ00121
MAEBL; Provisional
 302-552 9.79e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 9.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  302 GNHDLFMRRRRVDSLEVQ-------QMKAQAREERARK------QVERQRLQREKQLREEAERARDELERRLIQLQDEAD 368
Cdd:PTZ00121 1036 GNNDDVLKEKDIIDEDIDgnhegkaEAKAHVGQDEGLKpsykdfDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEAR 1115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  369 MANEALLRSEQTADllAEKAQIAEEEAKL-LAQKAAEAE-TEMQRIKVTAIRGQEERRLMEQKMLEA--------KMVAL 438
Cdd:PTZ00121 1116 KAEEAKKKAEDARK--AEEARKAEDARKAeEARKAEDAKrVEIARKAEDARKAEEARKAEDAKKAEAarkaeevrKAEEL 1193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  439 KMAE-----------ESERRAKE---------------AEQLKQDLLEARDSERRAKNKLLEITSKAVYMSPGLAPDSMP 492
Cdd:PTZ00121 1194 RKAEdarkaeaarkaEEERKAEEarkaedakkaeavkkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK 1273

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 348533462  493 QDVSFSRENLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIESLKLKERE 552
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH