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Conserved domains on  [gi|701404033|ref|XP_009969620|]
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ezrin isoform X2 [Tyto alba]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 64-160 1.61e-75

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


:

Pssm-ID: 270015  Cd Length: 97  Bit Score: 231.01  E-value: 1.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  64 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 143
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 701404033 144 ILQLCMGNHELYMRRRK 160
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 374-450 8.04e-34

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


:

Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 121.54  E-value: 8.04e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701404033  374 NDRNEEKRVTEAEKNERVQQQLRALTDELAQARDENKRTHNDIIHSENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 450
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 201-320 2.92e-16

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: 74.57  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  201 KEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQ 280
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 701404033  281 LATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDL 320
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_M super family cl47539
FERM central domain; This domain is the central structural domain of the FERM domain.
 24-70 2.19e-09

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


The actual alignment was detected with superfamily member pfam00373:

Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 54.97  E-value: 2.19e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 701404033   24 QHKLSREQWEERIQVWHAEHSGMLKENAMLEYLKIAQDLEMYGINYF 70
Cdd:pfam00373  71 LRKMKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-238 2.55e-03

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 2.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701404033 162 DTIEVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQ 238
Cdd:COG4942  158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
 
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 ...
 64-160 1.61e-75

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


Pssm-ID: 270015  Cd Length: 97  Bit Score: 231.01  E-value: 1.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  64 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 143
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 701404033 144 ILQLCMGNHELYMRRRK 160
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 374-450 8.04e-34

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


Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 121.54  E-value: 8.04e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701404033  374 NDRNEEKRVTEAEKNERVQQQLRALTDELAQARDENKRTHNDIIHSENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 450
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_C pfam09380
FERM C-terminal PH-like domain;
74-159 1.60e-33

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 121.21  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   74 NKKGTDLWLGVDALGLNIYEKDDKLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILQLCMGNH 152
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 701404033  153 ELYMRRR 159
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 201-320 2.92e-16

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: 74.57  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  201 KEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQ 280
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 701404033  281 LATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDL 320
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-327 6.13e-11

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: 6.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 165 EVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERR 244
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 245 RAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTK 324
Cdd:COG1196  362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441


                 ...
gi 701404033 325 EEL 327
Cdd:COG1196  442 EAL 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-411 2.18e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 165 EVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERR 244
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 245 RAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTK 324
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 325 EELHLVMTAPPPPPPPvyepvnyhvHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQQLRALTDELAQ 404
Cdd:COG1196  393 RAAAELAAQLEELEEA---------EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463


                 ....*..
gi 701404033 405 ARDENKR 411
Cdd:COG1196  464 LLAELLE 470
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 24-70 2.19e-09

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 54.97  E-value: 2.19e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 701404033   24 QHKLSREQWEERIQVWHAEHSGMLKENAMLEYLKIAQDLEMYGINYF 70
Cdd:pfam00373  71 LRKMKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 27-70 1.48e-08

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: 54.61  E-value: 1.48e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 701404033    27 LSREQWEERIQVWHAEHSGMLKENAMLEYLKIAQDLEMYGINYF 70
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-450 7.36e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 7.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   171 AQAREEKHQKQLERQQ-LENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEE 249
Cdd:TIGR02168  662 TGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   250 AERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTKEELHL 329
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   330 VMTAPPPPPPPV--YEPVNYHVHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQQLRALTDELAQARD 407
Cdd:TIGR02168  822 LRERLESLERRIaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 701404033   408 ENKRTHNDIIHSENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 450
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 167-308 1.24e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.11  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 167 QQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQmlrEKEellvRLQEYEVKTQKAE--KELSDQIQRAIQLEEERR 244
Cdd:PRK09510  70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQL---EKE----RLAAQEQKKQAEEaaKQAALKQKQAEEAAAKAA 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701404033 245 RAQEEAERLEADRLAAL--QAKEELERQTM-DQIKSQEQLATELAEYTAKIALLEEARRRKESEVEE 308
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAakKAAAEAKKKAEaEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 24-62 4.96e-05

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: 42.23  E-value: 4.96e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 701404033  24 QHKLSREQWEERIQVWHAEHSGMLKENAMLEYLKIAQDL 62
Cdd:cd14473   61 LKQRKPEEWEKRIVELHKKLRGLSPAEAKLKYLKIARKL 99
PTZ00121 PTZ00121
MAEBL; Provisional
 174-441 2.88e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  174 REEKHQKQLERQQLENEKKKRETIEREKEQMLREKEEllVRLQEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEEAERL 253
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  254 EADRLAALQAKEELERQTMDQIKSQEQLATELAEytakiALLEEARRRKESEveewQIRAKEAQEdlVKTKEELHLVmta 333
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE-----ALKKEAEEAKKAE----ELKKKEAEE--KKKAEELKKA--- 1724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  334 pppppppvyEPVNYHVHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQQLRALTDELAQARDENKRTH 413
Cdd:PTZ00121 1725 ---------EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795

                         250       260
                  ....*....|....*....|....*...
gi 701404033  414 NDiihsenmRQGRDKYKTLRQIRQGNTK 441
Cdd:PTZ00121 1796 VD-------KKIKDIFDNFANIIEGGKE 1816
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 176-408 9.41e-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: 41.97  E-value: 9.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   176 EKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRL----QEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEEAE 251
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   252 RLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTKEELHLVM 331
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   332 TAPPPPPPPVYEPVNY-----HVHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTE--AEKNERVQQQLRALTDELAQ 404
Cdd:TIGR02168  393 LQIASLNNEIERLEARlerleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQEELERLEEALEELREELEE 472


                   ....
gi 701404033   405 ARDE 408
Cdd:TIGR02168  473 AEQA 476
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-238 2.55e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 2.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701404033 162 DTIEVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQ 238
Cdd:COG4942  158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
 
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 ...
 64-160 1.61e-75

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


Pssm-ID: 270015  Cd Length: 97  Bit Score: 231.01  E-value: 1.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  64 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 143
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 701404033 144 ILQLCMGNHELYMRRRK 160
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 374-450 8.04e-34

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


Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 121.54  E-value: 8.04e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701404033  374 NDRNEEKRVTEAEKNERVQQQLRALTDELAQARDENKRTHNDIIHSENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 450
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
FERM_C pfam09380
FERM C-terminal PH-like domain;
74-159 1.60e-33

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 121.21  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   74 NKKGTDLWLGVDALGLNIYEKDDKLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILQLCMGNH 152
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 701404033  153 ELYMRRR 159
Cdd:pfam09380  79 TFFRLRR 85
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 66-156 6.97e-19

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


Pssm-ID: 275389  Cd Length: 93  Bit Score: 81.27  E-value: 6.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  66 GINYFEIKNK--KGTDLWLGVDALGLNIYEKDDKlTPKIGFPWSEIRNISFN-DKKFVIKPIDKKAPDFVFYAPRLRINK 142
Cdd:cd00836    1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEDKQSKLLFQTPSRQAK 79

                         90
                 ....*....|....
gi 701404033 143 RILQLCMGNHELYM 156
Cdd:cd00836   80 EIWKLIVGYHRFLL 93
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 201-320 2.92e-16

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: 74.57  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  201 KEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQ 280
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 701404033  281 LATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDL 320
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 66-160 1.97e-13

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


Pssm-ID: 270012  Cd Length: 113  Bit Score: 66.60  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  66 GINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPID-KKAPD-------------F 131
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDpRRNSHrsrrtfqsssvsvH 80

                         90       100
                 ....*....|....*....|....*....
gi 701404033 132 VFYAPRLRINKRILQLCMGNHELYMRRRK 160
Cdd:cd13191   81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQ 109
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 70-161 1.21e-11

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


Pssm-ID: 270008  Cd Length: 103  Bit Score: 61.19  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  70 FEIKNKKGTDLWLGVDALGLNIYE-KDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLC 148
Cdd:cd13187    8 YREKKSSTLSLWLGICSRGIIIYEeKNGARTPVLRFPWRETQKISFDKKKFTIESRGGSGIKHTFYTDSYKKSQYLLQLC 87

                         90
                 ....*....|....*
gi 701404033 149 MGNHE--LYMRRRKP 161
Cdd:cd13187   88 SAQHKfhIQMRSRQS 102
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 73-157 2.37e-11

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


Pssm-ID: 270006  Cd Length: 107  Bit Score: 60.40  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  73 KNKKGTD--LWLGVDALGLNIY-EKDDKLTPKIGFPWSEIRNISFNDKKFVIKPiDKKAPDFVFYAPRLRINKRILQLCM 149
Cdd:cd13185   12 KSKKETPgsVLLGITAKGIQIYqESDGEQQLLRTFPWSNIGKLSFDRKKFEIRP-EGSLRKLTYYTSSDEKSKYLLALCR 90


                 ....*...
gi 701404033 150 GNHELYMR 157
Cdd:cd13185   91 ETHQFSMA 98
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-327 6.13e-11

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: 6.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 165 EVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERR 244
Cdd:COG1196  282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 245 RAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTK 324
Cdd:COG1196  362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441


                 ...
gi 701404033 325 EEL 327
Cdd:COG1196  442 EAL 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-327 1.82e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 165 EVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERR 244
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 245 RAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTK 324
Cdd:COG1196  369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448


                 ...
gi 701404033 325 EEL 327
Cdd:COG1196  449 EEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 164-327 3.45e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 164 IEVQQMKAQAREEKHQKQLERQQLENEkkkRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEER 243
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 244 RRAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKT 323
Cdd:COG1196  375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454


                 ....
gi 701404033 324 KEEL 327
Cdd:COG1196  455 EEEE 458
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-411 2.18e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 165 EVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERR 244
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 245 RAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTK 324
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 325 EELHLVMTAPPPPPPPvyepvnyhvHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQQLRALTDELAQ 404
Cdd:COG1196  393 RAAAELAAQLEELEEA---------EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463


                 ....*..
gi 701404033 405 ARDENKR 411
Cdd:COG1196  464 LLAELLE 470
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 24-70 2.19e-09

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 54.97  E-value: 2.19e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 701404033   24 QHKLSREQWEERIQVWHAEHSGMLKENAMLEYLKIAQDLEMYGINYF 70
Cdd:pfam00373  71 LRKMKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 58-122 2.25e-09

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


Pssm-ID: 270014  Cd Length: 122  Bit Score: 55.04  E-value: 2.25e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 701404033  58 IAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTpkiGFPWSEIRNISFNDKKFVIK 122
Cdd:cd13193    2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 51-128 9.14e-09

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


Pssm-ID: 270013  Cd Length: 105  Bit Score: 52.78  E-value: 9.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  51 AMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTpkiGFPWSEIRNISFNDKKF---VIKPIDKK 127
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFilhVMQKEEKK 77


                 .
gi 701404033 128 A 128
Cdd:cd13192   78 H 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 150-327 1.27e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 150 GNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKEL 229
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 230 SDQIQRAIQLEEERRRAQEEAERLEADRLAALQAKEELERQtmdqiksQEQLATELAEYTAKIALLEEARRRKESEVEEW 309
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                        170
                 ....*....|....*...
gi 701404033 310 QIRAKEAQEDLVKTKEEL 327
Cdd:COG1196  455 EEEEEALLELLAELLEEA 472
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-329 1.39e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 165 EVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERR 244
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 245 RAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTK 324
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490


                 ....*
gi 701404033 325 EELHL 329
Cdd:COG1196  491 ARLLL 495
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 27-70 1.48e-08

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: 54.61  E-value: 1.48e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 701404033    27 LSREQWEERIQVWHAEHSGMLKENAMLEYLKIAQDLEMYGINYF 70
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 64-121 2.77e-07

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


Pssm-ID: 270010  Cd Length: 95  Bit Score: 48.46  E-value: 2.77e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 701404033  64 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPkigFPWSEIRNISFNDKKFVI 121
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVFQNGIRINT---FPWSKIVKISFKRKQFFI 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-450 7.36e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 7.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   171 AQAREEKHQKQLERQQ-LENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEE 249
Cdd:TIGR02168  662 TGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   250 AERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTKEELHL 329
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   330 VMTAPPPPPPPV--YEPVNYHVHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQQLRALTDELAQARD 407
Cdd:TIGR02168  822 LRERLESLERRIaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 701404033   408 ENKRTHNDIIHSENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 450
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 65-152 3.52e-06

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


Pssm-ID: 270005  Cd Length: 94  Bit Score: 45.39  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  65 YGINYFEIKNKKGTDLWLGVDALGLNIYEkdDKLtpKIG-FPWSEIRNISFNDKKFVIK----PIDKKAPDFVFYAPRLR 139
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYR--DRL--RINrFAWPKVLKISYKRNNFYIKirpgEFEQYETTIGFKLPNHR 76

                         90
                 ....*....|...
gi 701404033 140 INKRILQLCMGNH 152
Cdd:cd13184   77 AAKRLWKVCVEHH 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-418 4.39e-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: 49.28  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   165 EVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERR 244
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   245 RAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQ---EDLV 321
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrlEDLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   322 KTKEELHLVMTAPPPPPPPVYEPVNYHvHDNLQDEGSEYPAYSAELSSegiRNDRNEEKRVTEAEKNERVQ---QQLRAL 398
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALAL---LRSELEELSEELRELESKRSelrRELEEL 920

                          250       260
                   ....*....|....*....|
gi 701404033   399 TDELAQARDENKRTHNDIIH 418
Cdd:TIGR02168  921 REKLAQLELRLEGLEVRIDN 940
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 65-157 9.11e-06

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


Pssm-ID: 270009  Cd Length: 91  Bit Score: 43.82  E-value: 9.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  65 YGINYFEIKNKKGTDLWLGVDALGlnIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPdFVFYAPRLRINKRI 144
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEG--IFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEET-VQFQFEDAETAKYV 77

                         90
                 ....*....|...
gi 701404033 145 LQLCMGNHELYMR 157
Cdd:cd13188   78 WKLCVLQHKFYRQ 90
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 158-446 1.03e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   158 RRKPDTIEVQQMKAQAREEKHQKQLERQQLENEK---------KKRET----IEREKEQMLREKEELLVRLQEYEVKTQK 224
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqallkEKREYegyeLLKEKEALERQKEAIERQLASLEEELEK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   225 AEKELSDQIQRAIQLEEERRRAQEEAERLEADRLAALQAK--------EELERQTMDQIKSQEQLATELAEYTAKIALLE 296
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLL 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   297 EARRRKESEVEEWQIRAKEAQEDLVKTKEELHLVMTapppppppvyepvnyhvhdNLQDEGSEYPAYSAELSSEGIRNDR 376
Cdd:TIGR02169  336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA-------------------ELEEVDKEFAETRDELKDYREKLEK 396

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701404033   377 NEEKRVTEAEKNERVQQQLRALTDELAQARDENKRTHNDIIHSEN-MRQGRDKYKTLRQIRQGNTKQRIDE 446
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQLAADLSKY 467
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 167-308 1.24e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.11  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 167 QQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQmlrEKEellvRLQEYEVKTQKAE--KELSDQIQRAIQLEEERR 244
Cdd:PRK09510  70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQL---EKE----RLAAQEQKKQAEEaaKQAALKQKQAEEAAAKAA 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701404033 245 RAQEEAERLEADRLAAL--QAKEELERQTM-DQIKSQEQLATELAEYTAKIALLEEARRRKESEVEE 308
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAakKAAAEAKKKAEaEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
PRK12704 PRK12704
phosphodiesterase; Provisional
 165-291 1.40e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 165 EVQQMKAQAREEKHQKQLERQQLENE-KKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKeLSDQIQRAIQLEEER 243
Cdd:PRK12704  65 EIHKLRNEFEKELRERRNELQKLEKRlLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEK-KEEELEELIEEQLQE 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 701404033 244 RRAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAK 291
Cdd:PRK12704 144 LERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
PTZ00121 PTZ00121
MAEBL; Provisional
 156-308 2.03e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  156 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQlENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQR 235
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKE-AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA 1690

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701404033  236 AIQLEEERRraqeeaerlEADRLAALQAKEELERQTMDQIKSQEQLATELAEyTAKIALLEEARRRKESEVEE 308
Cdd:PTZ00121 1691 AEALKKEAE---------EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE-EAKKEAEEDKKKAEEAKKDE 1753
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 24-62 4.96e-05

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: 42.23  E-value: 4.96e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 701404033  24 QHKLSREQWEERIQVWHAEHSGMLKENAMLEYLKIAQDL 62
Cdd:cd14473   61 LKQRKPEEWEKRIVELHKKLRGLSPAEAKLKYLKIARKL 99
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-327 9.42e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 9.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 165 EVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEEL--LVRLQEYEVKTQKAEKELSDQIQRAIQLEEE 242
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 243 RRRAQEEAERLEADRLAALQAKEELERQtmdQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVK 322
Cdd:COG4717  155 LEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231


                 ....*
gi 701404033 323 TKEEL 327
Cdd:COG4717  232 LENEL 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-410 1.80e-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: 44.28  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   165 EVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERR 244
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   245 RAQEEAERLEADRLAALQAKEELERQtmdqiksQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTK 324
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQ-------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   325 EELHLVMtapppppppvyepvnyhvhdnLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQQLRALTDELAQ 404
Cdd:TIGR02168  442 LEELEEE---------------------LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500


                   ....*.
gi 701404033   405 ARDENK 410
Cdd:TIGR02168  501 LEGFSE 506
PRK12704 PRK12704
phosphodiesterase; Provisional
 170-326 2.57e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 170 KAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELsdqIQRAIQLEEERRRAQEE 249
Cdd:PRK12704  32 KIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRL---LQKEENLDRKLELLEKR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 250 AERLEADRLAALQAKEELE--RQTMDQIKSQEQLATE-LAEYTAkiallEEARRRKESEVEEwQIRAKEAQedLVKTKEE 326
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEkkEEELEELIEEQLQELErISGLTA-----EEAKEILLEKVEE-EARHEAAV--LIKEIEE 180
PTZ00121 PTZ00121
MAEBL; Provisional
 174-441 2.88e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  174 REEKHQKQLERQQLENEKKKRETIEREKEQMLREKEEllVRLQEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEEAERL 253
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  254 EADRLAALQAKEELERQTMDQIKSQEQLATELAEytakiALLEEARRRKESEveewQIRAKEAQEdlVKTKEELHLVmta 333
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE-----ALKKEAEEAKKAE----ELKKKEAEE--KKKAEELKKA--- 1724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  334 pppppppvyEPVNYHVHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQQLRALTDELAQARDENKRTH 413
Cdd:PTZ00121 1725 ---------EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795

                         250       260
                  ....*....|....*....|....*...
gi 701404033  414 NDiihsenmRQGRDKYKTLRQIRQGNTK 441
Cdd:PTZ00121 1796 VD-------KKIKDIFDNFANIIEGGKE 1816
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 167-424 3.82e-04

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: 42.80  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  167 QQMKAQAREEKHQKQLERQQLENEKKKRE-------TIEREKEQMLREKEELLVRLQEYEVK---TQKAEKELSDQIQRA 236
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQaemdrqaAIYAEQERMAMERERELERIRQEERKrelERIRQEEIAMEISRM 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  237 IQLEEERRRAQEEAERLEADRLAALQAK---EELERQTMDQIKSQEQLATELAE-YTAKIALLEEARRRKESEVEEWQIR 312
Cdd:pfam17380 378 RELERLQMERQQKNERVRQELEAARKVKileEERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEERAREMERVRLEEQE 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  313 AKEAQEDLVKTKEELH---LVMTAPPPPPPPVYEPVNYHVHDNLQDEG--------------SEYPAYSAELSSEGIRND 375
Cdd:pfam17380 458 RQQQVERLRQQEEERKrkkLELEKEKRDRKRAEEQRRKILEKELEERKqamieeerkrklleKEMEERQKAIYEEERRRE 537

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 701404033  376 RNEEKRV-TEAEKNERVQQQLRALTDELA--QARDENKRTHNDIIHSENMRQ 424
Cdd:pfam17380 538 AEEERRKqQEMEERRRIQEQMRKATEERSrlEAMEREREMMRQIVESEKARA 589
PTZ00121 PTZ00121
MAEBL; Provisional
 158-430 4.43e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  158 RRKPDTIEVQQMKAQAREEKHQKQLERQQLENEKKKREtiEREKEQMLREKEELLVRLQEYEVKTQKAEK--ELSDQIQR 235
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE--EAKKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEE 1494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  236 AIQLEEERRRAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKE 315
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  316 AQEDLVKTKEELHLVMTAPPPPPPPVYEPVNYHVHDNLQDEgSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQQL 395
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 701404033  396 RALTDELAQARDENKRTHNDIIHSENMRQGRDKYK 430
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 75-148 6.67e-04

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


Pssm-ID: 275390  Cd Length: 89  Bit Score: 38.53  E-value: 6.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701404033  75 KKGTDLWLGVDALGLnIYEKDDKLTPKIGFPWSEIRNISFND-----KKFVIKPIDkKAPDFVFYAPRLRINKRILQLC 148
Cdd:cd00900   13 TKRVEGTLYITSDRL-ILRDKNDGGLELSIPISDIVNVNVSPqgpssRYLVLVLKD-RGEFVGFSFPKEEDAIEISDAL 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 176-408 9.41e-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: 41.97  E-value: 9.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   176 EKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRL----QEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEEAE 251
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   252 RLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKTKEELHLVM 331
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   332 TAPPPPPPPVYEPVNY-----HVHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTE--AEKNERVQQQLRALTDELAQ 404
Cdd:TIGR02168  393 LQIASLNNEIERLEARlerleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQEELERLEEALEELREELEE 472


                   ....
gi 701404033   405 ARDE 408
Cdd:TIGR02168  473 AEQA 476
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 137-318 1.06e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  137 RLRINKRILQlcmgnHELYMRRRKPDTIEVQQMKAQAREEKHQKQLE---RQQLENEKKKRETIE--REKEQMLREKEEl 211
Cdd:pfam17380 358 RKRELERIRQ-----EEIAMEISRMRELERLQMERQQKNERVRQELEaarKVKILEEERQRKIQQqkVEMEQIRAEQEE- 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  212 lvrlqEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEEAERLEADRLaalQAKEELERQTMDQIKSQEQ----LATELAE 287
Cdd:pfam17380 432 -----ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK---RKKLELEKEKRDRKRAEEQrrkiLEKELEE 503

                         170       180       190
                  ....*....|....*....|....*....|...
gi 701404033  288 ytAKIALLEEARRRK--ESEVEEWQIRAKEAQE 318
Cdd:pfam17380 504 --RKQAMIEEERKRKllEKEMEERQKAIYEEER 534
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 158-327 1.19e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   158 RRKPDTIEVQQMKAQAREEKHQKQLERQ---------QLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKE 228
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDKLlaeieelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   229 LSDQIQRAIQLEEERRRAQEeaerlEADRLaalqaKEELERQTMDqiksQEQLATELAEYTAKIALLEEARRRKESEVEE 308
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKR-----ELDRL-----QEELQRLSEE----LADLNAAIAGIEAKINELEEEKEDKALEIKK 452

                          170
                   ....*....|....*....
gi 701404033   309 WQIRAKEAQEDLVKTKEEL 327
Cdd:TIGR02169  453 QEWKLEQLAADLSKYEQEL 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-331 1.74e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 181 QLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERRRAQEEAERLEADRLAA 260
Cdd:COG1196  665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 261 LQAKEELERQTMDQIKSQEQLATELAEYTAKIALL-----------EEARRRKESEVEEwqirakeaQEDLVKTKEELHL 329
Cdd:COG1196  745 EELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyEELEERYDFLSEQ--------REDLEEARETLEE 816


                 ..
gi 701404033 330 VM 331
Cdd:COG1196  817 AI 818
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 159-326 2.42e-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: 40.44  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   159 RKPDTIEVQQMKAQAREEKhqkqlERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSD------- 231
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEK-----LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlsh 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   232 ----QIQRAIQ-LEEERRRAQEEAERLEAdRLAALQAKEELERQTMDQIKSQEQLATE-LAEYTAKIALLEEARRRKESE 305
Cdd:TIGR02169  791 sripEIQAELSkLEEEVSRIEARLREIEQ-KLNRLTLEKEYLEKEIQELQEQRIDLKEqIKSIEKEIENLNGKKEELEEE 869

                          170       180
                   ....*....|....*....|.
gi 701404033   306 VEEWQIRAKEAQEDLVKTKEE 326
Cdd:TIGR02169  870 LEELEAALRDLESRLGDLKKE 890
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-238 2.55e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 2.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 701404033 162 DTIEVQQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQ 238
Cdd:COG4942  158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 162-313 2.95e-03

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


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 39.71  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  162 DTIEVQQMKAQAREEKHQKQLERQQLenEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSD-QIQRAIQL- 239
Cdd:pfam00529  61 DSAEAQLAKAQAQVARLQAELDRLQA--LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrRVLAPIGGi 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701404033  240 -EEERRRAQEEAERLEADRLAALQAKEELERQ-TMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRA 313
Cdd:pfam00529 139 sRESLVTAGALVAQAQANLLATVAQLDQIYVQiTQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRA 214
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 169-327 3.44e-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: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   169 MKAQAREEKHQKQLeRQQLENEKKKRETIEREKEQMLREK-------EELLVRLQEYEVKTQKAEKELSDQIQRAIQLEE 241
Cdd:TIGR02169  694 QSELRRIENRLDEL-SQELSDASRKIGEIEKEIEQLEQEEeklkerlEELEEDLSSLEQEIENVKSELKELEARIEELEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   242 ERRRAQEEAERLEAD----RLAALQAK-EELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKE- 315
Cdd:TIGR02169  773 DLHKLEEALNDLEARlshsRIPEIQAElSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSi 852

                          170
                   ....*....|....
gi 701404033   316 --AQEDLVKTKEEL 327
Cdd:TIGR02169  853 ekEIENLNGKKEEL 866
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 177-326 3.96e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  177 KHQKQL-ERQQLEN-EKKKRETIEREKEQMLREKEELLvRLQEYEVKTQKA----------EKELSDQIQRAIQLEEERR 244
Cdd:pfam17380 279 QHQKAVsERQQQEKfEKMEQERLRQEKEEKAREVERRR-KLEEAEKARQAEmdrqaaiyaeQERMAMERERELERIRQEE 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  245 RAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELaEYTAKIALLEEARRRK--ESEVEEWQIRAK--EAQEDL 320
Cdd:pfam17380 358 RKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQEL-EAARKVKILEEERQRKiqQQKVEMEQIRAEqeEARQRE 436


                  ....*.
gi 701404033  321 VKTKEE 326
Cdd:pfam17380 437 VRRLEE 442
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 65-119 4.35e-03

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


Pssm-ID: 270016  Cd Length: 111  Bit Score: 36.84  E-value: 4.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 701404033  65 YGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIgfPWSEIRNISFNDKKF 119
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERI--PYTAIQMATSSGRVF 53
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 156-327 6.73e-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: 38.90  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   156 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLENEKKKretIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQR 235
Cdd:TIGR02169  289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   236 AIQLEEERRRAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKE 315
Cdd:TIGR02169  366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445

                          170
                   ....*....|..
gi 701404033   316 AQEDLVKTKEEL 327
Cdd:TIGR02169  446 KALEIKKQEWKL 457
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 165-411 8.46e-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: 38.80  E-value: 8.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   165 EVQQMKAQAREEKHQ-KQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEER 243
Cdd:pfam02463  769 LSLKEKELAEEREKTeKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   244 RRAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQEDLVKT 323
Cdd:pfam02463  849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE 928

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033   324 KEELHLVMTAPPPPPPPVYEPVNYHVHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQQLRALTDELA 403
Cdd:pfam02463  929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008


                   ....*...
gi 701404033   404 QARDENKR 411
Cdd:pfam02463 1009 RAIIEETC 1016
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
162-449 9.50e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 9.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 162 DTIEVQQMKAQAREEKHQKQLERQQlenekKKRETIEREKEqmlrEKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEE 241
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHE-----ERREELETLEA----EIEDLRETIAETEREREELAEEVRDLRERLEELEE 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 242 ERRRAQEEAERLEADRLAALQAKEELE------RQTMDQIKSQEQLATELAE-YTAKIALLEEARRRKESEVEEWQIRAK 314
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEdrdeelRDRLEECRVAAQAHNEEAEsLREDADDLEERAEELREEAAELESELE 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 315 EAQEDLVKTKEELHLVMTAPPPPPPPV------YEPVNYHvHDNLQDEGSEYPAYSAELSS--EGIRNDRNEEKRVTEAE 386
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFgdapvdLGNAEDF-LEELREERDELREREAELEAtlRTARERVEEAEALLEAG 452

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701404033 387 K----------------NERVQQQLRALTDELAQARDENKRTHNDIIHSENMRQGRDKYKTLRQIRQgNTKQRIDEFEA 449
Cdd:PRK02224 453 KcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE-DLEELIAERRE 530
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 167-327 9.75e-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: 38.21  E-value: 9.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 167 QQMKAQAREEKHQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAIQLEEERRRA 246
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033 247 QEEAERLEADRLAALQAKEE----------------------LERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKES 304
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRqpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                        170       180
                 ....*....|....*....|...
gi 701404033 305 EVEEwQIRAKEAQEDLVKTKEEL 327
Cdd:COG4942  179 LLAE-LEEERAALEALKAERQKL 200
PTZ00121 PTZ00121
MAEBL; Provisional
 158-446 9.77e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  158 RRKPDTIEVQQMKAQAREEKhQKQLERQQLENEKKKRETIEREKEQMLREKEELLVRLQEYEVKTQKAEKELSDQIQRAI 237
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  238 QLEEERRRAQEEAERLEADRLAALQAKEELERQTMDQIKSQEQLATELAEYTAKIALLEEARRRKESEVEEWQIRAKEAQ 317
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701404033  318 EDLVKTKEELHLVMTAPPPPPPPVYEPVNYHVHDNLQDEGSEYPAYSAELSSEGIRNDRNEEKRVTEAEKNERVQQqlra 397
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK---- 1523

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 701404033  398 lTDELAQArdENKRTHNDIIHSENMRQGrDKYKTLRQIRQGNTKQRIDE 446
Cdd:PTZ00121 1524 -ADEAKKA--EEAKKADEAKKAEEKKKA-DELKKAEELKKAEEKKKAEE 1568
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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