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Conserved domains on  [gi|731218501|ref|XP_010623545|]
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ezrin isoform X2 [Fukomys damarensis]

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 1.27e-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: 1.27e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  64 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 143
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 731218501 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 4.52e-33

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: 119.61  E-value: 4.52e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 731218501  374 DDRNEEKRITEAEKNERVQRQLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 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 1.06e-19

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: 84.20  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  201 KEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQ 280
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 731218501  281 LATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDL 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.
 5-70 2.17e-10

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: 58.05  E-value: 2.17e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 731218501    5 SSPSSQIPLESSFLIRVMDQHKLtrDQWEERIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 70
Cdd:pfam00373  54 SHTSEYLSLESFLPKQLLRKMKS--KELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
 
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 1.27e-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: 1.27e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  64 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 143
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 731218501 144 ILQLCMGNHELYMRRRK 160
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
FERM_C pfam09380
FERM C-terminal PH-like domain;
74-159 7.30e-34

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 121.98  E-value: 7.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   74 NKKGTDLWLGVDALGLNIYEKDDKLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILQLCMGNH 152
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 731218501  153 ELYMRRR 159
Cdd:pfam09380  79 TFFRLRR 85
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 374-450 4.52e-33

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: 119.61  E-value: 4.52e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 731218501  374 DDRNEEKRITEAEKNERVQRQLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 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 1.06e-19

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: 84.20  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  201 KEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQ 280
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 731218501  281 LATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDL 320
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-411 2.63e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.28  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 162 DTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLED 241
Cdd:COG1196  223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 242 ERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLV 321
Cdd:COG1196  303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 322 KTKEELHLVMTAPPPPPPPVYEPASyhVQENLQEEGAEpmgYSAELSSEGILDDRNEEKRITEAEKNERVQRQLLTLSNE 401
Cdd:COG1196  383 ELAEELLEALRAAAELAAQLEELEE--AEEALLERLER---LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        250
                 ....*....|
gi 731218501 402 LSQARDENKR 411
Cdd:COG1196  458 EEALLELLAE 467
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-329 1.34e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 165 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERK 244
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 245 RAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVKTK 324
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490


                 ....*
gi 731218501 325 EELHL 329
Cdd:COG1196  491 ARLLL 495
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 5-70 2.17e-10

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 58.05  E-value: 2.17e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 731218501    5 SSPSSQIPLESSFLIRVMDQHKLtrDQWEERIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 70
Cdd:pfam00373  54 SHTSEYLSLESFLPKQLLRKMKS--KELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 27-70 4.02e-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: 53.45  E-value: 4.02e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 731218501    27 LTRDQWEERIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 70
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-450 7.42e-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: 7.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   171 AQAREEKHQKQLERQQ----LETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQralQLEDERKRA 246
Cdd:TIGR02168  662 TGGSAKTNSSILERRReieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS---ALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   247 QEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVKTKEE 326
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   327 LHLVMTAPPPPPPPVYEPASYHVQ-----ENLQEEGAEpmgYSAELSSEGILDDRNEEKRITEAEKNERVQRQLLTLSNE 401
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDleeqiEELSEDIES---LAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 731218501   402 LSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 450
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 167-308 7.85e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.96  E-value: 7.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 167 QQMKAQAREEKHQKQLERQQlETEKKRRETVEREKEQMLrEKEelmlRLQDYEEKTKKAEKELSDQIQ-------RALQL 239
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQ-AEELQQKQAAEQERLKQL-EKE----RLAAQEQKKQAEEAAKQAALKqkqaeeaAAKAA 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 240 EDERKRAQEEAERLEAdrvAALQAKEELERQA-ADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEE 308
Cdd:PRK09510 143 AAAKAKAEAEAKRAAA---AAKKAAAEAKKKAeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
PTZ00121 PTZ00121
MAEBL; Provisional
 158-411 7.36e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 7.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  158 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRREtvEREKEQMLREKEElmlrlqdyeekTKKAEKELSDQIQRAL 237
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE--EAKKADEAKKKAE-----------EAKKADEAKKKAEEAK 1496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  238 QLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQ 317
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  318 DDLVKTKEELHLVMTAPPPPPPPVYEPASYHVQENLQEE-----GAEPMGYSAELSSEGILDDRNEEKRITEAEKNERVQ 392
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656

                         250
                  ....*....|....*....
gi 731218501  393 RQLLTLSNELSQARDENKR 411
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKK 1675
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-408 1.23e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   172 QAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRalqLEDERKRAQEEAE 251
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR---LEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   252 RLEADRVAA-------LQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVKTK 324
Cdd:TIGR02168  313 NLERQLEELeaqleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   325 EELHLVMTAPPPPPPPVyePASYHVQENLQEEGAEPMGYSAELSSEGILDDRNEEKRITE--AEKNERVQRQLLTLSNEL 402
Cdd:TIGR02168  393 LQIASLNNEIERLEARL--ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQEELERLEEALEELREEL 470


                   ....*.
gi 731218501   403 SQARDE 408
Cdd:TIGR02168  471 EEAEQA 476
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 24-62 4.82e-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: 4.82e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 731218501  24 QHKLTRDQWEERIQVWHAEHRGMLKDNAMLEYLKIAQDL 62
Cdd:cd14473   61 LKQRKPEEWEKRIVELHKKLRGLSPAEAKLKYLKIARKL 99
 
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 1.27e-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: 1.27e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  64 MYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKR 143
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 731218501 144 ILQLCMGNHELYMRRRK 160
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
FERM_C pfam09380
FERM C-terminal PH-like domain;
74-159 7.30e-34

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 121.98  E-value: 7.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   74 NKKGTDLWLGVDALGLNIYEKDDKLtpKIGFPWSEIRNISFNDKKFVIKPIDKKAPD-FVFYAPRLRINKRILQLCMGNH 152
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSEEtLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 731218501  153 ELYMRRR 159
Cdd:pfam09380  79 TFFRLRR 85
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 374-450 4.52e-33

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: 119.61  E-value: 4.52e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 731218501  374 DDRNEEKRITEAEKNERVQRQLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 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 1.06e-19

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: 84.20  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  201 KEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQ 280
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 731218501  281 LATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDL 320
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
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 731218501  66 GINYFEIKNK--KGTDLWLGVDALGLNIYEKDDKlTPKIGFPWSEIRNISFN-DKKFVIKPIDKKAPDFVFYAPRLRINK 142
Cdd:cd00836    1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEDKQSKLLFQTPSRQAK 79

                         90
                 ....*....|....
gi 731218501 143 RILQLCMGNHELYM 156
Cdd:cd00836   80 EIWKLIVGYHRFLL 93
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 1.40e-13

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


Pssm-ID: 270012  Cd Length: 113  Bit Score: 66.99  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  66 GINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPID-KKAPD-------------F 131
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDpRRNSHrsrrtfqsssvsvH 80

                         90       100
                 ....*....|....*....|....*....
gi 731218501 132 VFYAPRLRINKRILQLCMGNHELYMRRRK 160
Cdd:cd13191   81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQ 109
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-411 2.63e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.28  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 162 DTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLED 241
Cdd:COG1196  223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 242 ERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLV 321
Cdd:COG1196  303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 322 KTKEELHLVMTAPPPPPPPVYEPASyhVQENLQEEGAEpmgYSAELSSEGILDDRNEEKRITEAEKNERVQRQLLTLSNE 401
Cdd:COG1196  383 ELAEELLEALRAAAELAAQLEELEE--AEEALLERLER---LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        250
                 ....*....|
gi 731218501 402 LSQARDENKR 411
Cdd:COG1196  458 EEALLELLAE 467
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 70-161 9.27e-12

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


Pssm-ID: 270008  Cd Length: 103  Bit Score: 61.19  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  70 FEIKNKKGTDLWLGVDALGLNIYE-KDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLC 148
Cdd:cd13187    8 YREKKSSTLSLWLGICSRGIIIYEeKNGARTPVLRFPWRETQKISFDKKKFTIESRGGSGIKHTFYTDSYKKSQYLLQLC 87

                         90
                 ....*....|....*
gi 731218501 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 2.15e-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: 2.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  73 KNKKGTD--LWLGVDALGLNIY-EKDDKLTPKIGFPWSEIRNISFNDKKFVIKPiDKKAPDFVFYAPRLRINKRILQLCM 149
Cdd:cd13185   12 KSKKETPgsVLLGITAKGIQIYqESDGEQQLLRTFPWSNIGKLSFDRKKFEIRP-EGSLRKLTYYTSSDEKSKYLLALCR 90


                 ....*...
gi 731218501 150 GNHELYMR 157
Cdd:cd13185   91 ETHQFSMA 98
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-329 1.34e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 165 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERK 244
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 245 RAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVKTK 324
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490


                 ....*
gi 731218501 325 EELHL 329
Cdd:COG1196  491 ARLLL 495
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 5-70 2.17e-10

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 58.05  E-value: 2.17e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 731218501    5 SSPSSQIPLESSFLIRVMDQHKLtrDQWEERIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 70
Cdd:pfam00373  54 SHTSEYLSLESFLPKQLLRKMKS--KELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-443 2.95e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 179 QKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERKRAQE-------EAE 251
Cdd:COG1196  219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyellaELA 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 252 RLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVKTKEELHLVM 331
Cdd:COG1196  299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 332 TAPPPPPPPVYEPASYHVQENLQEEGAEpmgysAELSSEGILDDRNEEKRITEAEKNERVQRQLLTLSNELSQARDENKR 411
Cdd:COG1196  379 EELEELAEELLEALRAAAELAAQLEELE-----EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                        250       260       270
                 ....*....|....*....|....*....|..
gi 731218501 412 THNDIIHNENMRQgRDKYKTLRQIRQGNTKQR 443
Cdd:COG1196  454 LEEEEEALLELLA-ELLEEAALLEAALAELLE 484
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 58-122 2.65e-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: 2.65e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 731218501  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 731218501  51 AMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTpkiGFPWSEIRNISFNDKKF---VIKPIDKK 127
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFilhVMQKEEKK 77


                 .
gi 731218501 128 A 128
Cdd:cd13192   78 H 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 150-327 1.34e-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: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 150 GNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKEL 229
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 230 SDQIQRALQLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEW 309
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                        170
                 ....*....|....*...
gi 731218501 310 QHRAREAQDDLVKTKEEL 327
Cdd:COG1196  462 LELLAELLEEAALLEAAL 479
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 27-70 4.02e-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: 53.45  E-value: 4.02e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 731218501    27 LTRDQWEERIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYF 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 2.46e-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: 2.46e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 731218501  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 7.42e-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: 7.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   171 AQAREEKHQKQLERQQ----LETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQralQLEDERKRA 246
Cdd:TIGR02168  662 TGGSAKTNSSILERRReieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS---ALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   247 QEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVKTKEE 326
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   327 LHLVMTAPPPPPPPVYEPASYHVQ-----ENLQEEGAEpmgYSAELSSEGILDDRNEEKRITEAEKNERVQRQLLTLSNE 401
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDleeqiEELSEDIES---LAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 731218501   402 LSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM 450
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 167-308 7.85e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.96  E-value: 7.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 167 QQMKAQAREEKHQKQLERQQlETEKKRRETVEREKEQMLrEKEelmlRLQDYEEKTKKAEKELSDQIQ-------RALQL 239
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQ-AEELQQKQAAEQERLKQL-EKE----RLAAQEQKKQAEEAAKQAALKqkqaeeaAAKAA 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 240 EDERKRAQEEAERLEAdrvAALQAKEELERQA-ADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEE 308
Cdd:PRK09510 143 AAAKAKAEAEAKRAAA---AAKKAAAEAKKKAeAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209
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 4.04e-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: 45.01  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  65 YGINYFEIKNKKGTDLWLGVDALGLNIYEkdDKLtpKIG-FPWSEIRNISFNDKKFVIK----PIDKKAPDFVFYAPRLR 139
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYR--DRL--RINrFAWPKVLKISYKRNNFYIKirpgEFEQYETTIGFKLPNHR 76

                         90
                 ....*....|...
gi 731218501 140 INKRILQLCMGNH 152
Cdd:cd13184   77 AAKRLWKVCVEHH 89
PTZ00121 PTZ00121
MAEBL; Provisional
 158-411 7.36e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 7.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  158 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRREtvEREKEQMLREKEElmlrlqdyeekTKKAEKELSDQIQRAL 237
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE--EAKKADEAKKKAE-----------EAKKADEAKKKAEEAK 1496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  238 QLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQ 317
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  318 DDLVKTKEELHLVMTAPPPPPPPVYEPASYHVQENLQEE-----GAEPMGYSAELSSEGILDDRNEEKRITEAEKNERVQ 392
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656

                         250
                  ....*....|....*....
gi 731218501  393 RQLLTLSNELSQARDENKR 411
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKK 1675
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 65-157 7.57e-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: 44.20  E-value: 7.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  65 YGINYFEIKNKKGTDLWLGVDALGlnIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPdFVFYAPRLRINKRI 144
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEG--IFVKHDNGRPPVFFRWEDIKNVINHKRTFSIECQNSEET-VQFQFEDAETAKYV 77

                         90
                 ....*....|...
gi 731218501 145 LQLCMGNHELYMR 157
Cdd:cd13188   78 WKLCVLQHKFYRQ 90
PTZ00121 PTZ00121
MAEBL; Provisional
 158-436 1.22e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  158 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELM----LRLQDYEEKTKKAEKELSDQI 233
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEA 1612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  234 QRAlqlEDERKRAQE-EAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKialLEEARRRKENEVEEWQHR 312
Cdd:PTZ00121 1613 KKA---EEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK---KAEEDKKKAEEAKKAEED 1686

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  313 AREAQDDLVKTKEELHLVMTAPPPPPPPVYEPASYHVQENLQEEGAEPMGYSAELSSEgilddRNEEKRITEAEKNeRVQ 392
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK-----KAEEAKKDEEEKK-KIA 1760

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 731218501  393 RQLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIR 436
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-408 1.23e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   172 QAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRalqLEDERKRAQEEAE 251
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR---LEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   252 RLEADRVAA-------LQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVKTK 324
Cdd:TIGR02168  313 NLERQLEELeaqleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   325 EELHLVMTAPPPPPPPVyePASYHVQENLQEEGAEPMGYSAELSSEGILDDRNEEKRITE--AEKNERVQRQLLTLSNEL 402
Cdd:TIGR02168  393 LQIASLNNEIERLEARL--ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelQEELERLEEALEELREEL 470


                   ....*.
gi 731218501   403 SQARDE 408
Cdd:TIGR02168  471 EEAEQA 476
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 164-320 1.50e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   164 IEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRAL----QL 239
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarleRL 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   240 EDERKRAQEEAERL-----EADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAR 314
Cdd:TIGR02168  413 EDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492


                   ....*.
gi 731218501   315 EAQDDL 320
Cdd:TIGR02168  493 SLERLQ 498
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 157-316 1.53e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 157 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKE-QMLREKEELML-----------RLQDYEEKTKK 224
Cdd:COG4942   67 LARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlYRLGRQPPLALllspedfldavRRLQYLKYLAP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 225 AEKELSDQIQRALQ-LEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKE 303
Cdd:COG4942  147 ARREQAEELRADLAeLAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226

                        170
                 ....*....|...
gi 731218501 304 NEVEEWQHRAREA 316
Cdd:COG4942  227 ALIARLEAEAAAA 239
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-327 1.59e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   165 EVQQMKAQAREEKHQKQ----LERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLE 240
Cdd:TIGR02168  709 ELEEELEQLRKELEELSrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   241 DERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDL 320
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868


                   ....*..
gi 731218501   321 VKTKEEL 327
Cdd:TIGR02168  869 EELESEL 875
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 174-331 1.89e-05

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.87  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  174 REEKHQKQLERQQLETEKKRRETVEREKEqmlREKEELMLRLQDYEEKTKKAEKELSDQiQRALQLEDERKRAQEEAERL 253
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQ---RRFEEIRLRKQRLEEERQRQEEEERKQ-RLQLQAAQERARQQQEEFRR 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  254 EADRVAALQAKEELERQAADQiKSQEQLATELAEYTAKIALLEEARR----RKENEVEEwqHRAREAQDDLVKTKEELHL 329
Cdd:pfam15709 431 KLQELQRKKQQEEAERAEAEK-QRQKELEMQLAEEQKRLMEMAEEERleyqRQKQEAEE--KARLEAEERRQKEEEAARL 507


                  ..
gi 731218501  330 VM 331
Cdd:pfam15709 508 AL 509
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-326 2.57e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 165 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAE-----KELSDQIQRALQL 239
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelAELPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 240 EDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQ-EQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQD 318
Cdd:COG4717  155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234


                 ....*...
gi 731218501 319 DLVKTKEE 326
Cdd:COG4717  235 ELEAAALE 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 158-416 2.88e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 2.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   158 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKK------RRETVERE-------KEQMLREKEELMLRLQDYEEKTKK 224
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAeryqalLKEKREYEgyellkeKEALERQKEAIERQLASLEEELEK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   225 AEKELSDQIQRALQLEDERKRAQEEAERLEADRVAALQAK--------EELERQAADQIKSQEQLATELAEYTAKIALLE 296
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLL 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   297 EARRRKENEVEEWQHRAREAQDDLVKTKEELHLvmtapppppppvyepasyhVQENLQEEGAEpmgySAELSSEgiLDDR 376
Cdd:TIGR02169  336 AEIEELEREIEEERKRRDKLTEEYAELKEELED-------------------LRAELEEVDKE----FAETRDE--LKDY 390

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 731218501   377 NEEKRITEAEKNErVQRQLLTLSNELSQARDENKRTHNDI 416
Cdd:TIGR02169  391 REKLEKLKREINE-LKRELDRLQEELQRLSEELADLNAAI 429
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 163-329 3.42e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   163 TIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDE 242
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   243 RKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVK 322
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884


                   ....*..
gi 731218501   323 TKEELHL 329
Cdd:TIGR02168  885 LEEALAL 891
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-406 4.24e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 4.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   158 RRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQmlrekEELMLRLQDYEEKTKKAEKELSDQIQRAL 237
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-----EELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   238 QLEDERKRAQEEAERLE------ADRVAALQAK-EELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQ 310
Cdd:TIGR02168  313 NLERQLEELEAQLEELEskldelAEELAELEEKlEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   311 HRAREAQDDLVKTKEELHLVMTAPPPPPPPVYEPASYHVQENLQEEGAEPMGYSAELSSEGILDDRNEEKRITEAEKNER 390
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472

                          250
                   ....*....|....*.
gi 731218501   391 VQRQLLTLSNELSQAR 406
Cdd:TIGR02168  473 AEQALDAAERELAQLQ 488
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 24-62 4.82e-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: 4.82e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 731218501  24 QHKLTRDQWEERIQVWHAEHRGMLKDNAMLEYLKIAQDL 62
Cdd:cd14473   61 LKQRKPEEWEKRIVELHKKLRGLSPAEAKLKYLKIARKL 99
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 170-325 7.32e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  170 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKelsdQIQRALQLEDERKRAQEE 249
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQ----QVERLRQQEEERKRKKLE 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  250 AERLEADRvaalQAKEELERQAADQiksqeqlatELAEytAKIALLEEARRRK--ENEVEEWQ------HRAREAQDDLV 321
Cdd:pfam17380 479 LEKEKRDR----KRAEEQRRKILEK---------ELEE--RKQAMIEEERKRKllEKEMEERQkaiyeeERRREAEEERR 543


                  ....
gi 731218501  322 KTKE 325
Cdd:pfam17380 544 KQQE 547
PRK12704 PRK12704
phosphodiesterase; Provisional
 166-291 8.45e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 8.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 166 VQQMKAQAREEKHQKQLERQqlETEKKRRETVERE----------KEQMLREKEElmlRLQDYEEKTKKAEKELSDQIQR 235
Cdd:PRK12704  44 LEEAKKEAEAIKKEALLEAK--EEIHKLRNEFEKElrerrnelqkLEKRLLQKEE---NLDRKLELLEKREEELEKKEKE 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 731218501 236 ALQLEDERKRAQEEAERLEADRVAAL-----------------QAKEELERQAADQIKSQEQLATELAEYTAK 291
Cdd:PRK12704 119 LEQKQQELEKKEEELEELIEEQLQELerisgltaeeakeilleKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 156-327 9.61e-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: 45.06  E-value: 9.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   156 MRRRKPDTIEVQQMKAQAREEK-----HQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELS 230
Cdd:TIGR02169  203 LRREREKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   231 D-------QIQRAL--------QLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALL 295
Cdd:TIGR02169  283 DlgeeeqlRVKEKIgeleaeiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362

                          170       180       190
                   ....*....|....*....|....*....|..
gi 731218501   296 EEARRRKENEVEEWQHRAREAQDDLVKTKEEL 327
Cdd:TIGR02169  363 KEELEDLRAELEEVDKEFAETRDELKDYREKL 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 191-420 1.13e-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: 44.66  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   191 KKRREtverEKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERKRAQEEAERLEADRVAALQAK-EELER 269
Cdd:TIGR02168  171 KERRK----ETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREElEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   270 QAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHR---AREAQDDLVKTKEEL-----HLVMTAPPPPPPPV 341
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILrerlaNLERQLEELEAQLE 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   342 YEPASY-HVQENLQEEGAEPMGYSAELSSEGILDDRNEEKRITEAEKNERVQRQLLTLSNELSQARDENKRTHNDIIHNE 420
Cdd:TIGR02168  327 ELESKLdELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 153-316 1.35e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.17  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  153 ELYMRRRKPDTIEVQQMKAQAREEKHQKQLER-QQLETEKKRRETVEREKEQMLREKEELMLRLQdyEEKTKKAEKELSD 231
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELeQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQ--LQAAQERARQQQE 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  232 QIQRALQlEDERKRAQEEAERLEADRvaalQAKEELERQAADQIKSQEQLATElaEYTAKIALLEEARRRKENEVEEWQH 311
Cdd:pfam15709 427 EFRRKLQ-ELQRKKQQEEAERAEAEK----QRQKELEMQLAEEQKRLMEMAEE--ERLEYQRQKQEAEEKARLEAEERRQ 499


                  ....*
gi 731218501  312 RAREA 316
Cdd:pfam15709 500 KEEEA 504
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 177-446 1.61e-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: 43.96  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  177 KHQKQL-ERQQLET-EKKRRETVEREKEQMLREKE---ELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERKRAQEEAE 251
Cdd:pfam17380 279 QHQKAVsERQQQEKfEKMEQERLRQEKEEKAREVErrrKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  252 RLEADRV------AALQAKEELERQAADQIKSQEQLATELaEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVKTKE 325
Cdd:pfam17380 359 KRELERIrqeeiaMEISRMRELERLQMERQQKNERVRQEL-EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  326 ELHLVMTAPPPPPPPVYEPASYHVQENLQEEGAEPMGYSAELSSEGILDDRNEEKR--ITEAEKNERvQRQLLTLSNELS 403
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkILEKELEER-KQAMIEEERKRK 516

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 731218501  404 QARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQgntKQRIDE 446
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEE---RRRIQE 556
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
184-328 1.77e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  184 RQQLETEKKRRETVE---------REKEQMLREKEELMLRLQDYEEKTK-----KAEKELSDQIQRALQ----LEDERKR 245
Cdd:COG4913   241 HEALEDAREQIELLEpirelaeryAAARERLAELEYLRAALRLWFAQRRlelleAELEELRAELARLEAelerLEARLDA 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  246 AQEEAERLEADRVAA-LQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDDLVKTK 324
Cdd:COG4913   321 LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400


                  ....
gi 731218501  325 EELH 328
Cdd:COG4913   401 EALE 404
PTZ00121 PTZ00121
MAEBL; Provisional
 139-331 2.23e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  139 RINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQlERQQLETEKKRRETVEREKEQMLREKEELMLRLQDY 218
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE-EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  219 EEKTKKAEKelsdQIQRALQLEDERKRAQEEAERL--EADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLE 296
Cdd:PTZ00121 1667 AKKAEEDKK----KAEEAKKAEEDEKKAAEALKKEaeEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 731218501  297 ----EARRRKENEVEEWQHRAREAQDDLVKTKEELHLVM 331
Cdd:PTZ00121 1743 kkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 162-310 2.32e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 162 DTIEVQQMKAQAREEKHQKQLERQQlETEKKRRETVEREKEQMLREK---------------EELMLRLQDYEEKTKKAE 226
Cdd:COG3883   54 NELQAELEALQAEIDKLQAEIAEAE-AEIEERREELGERARALYRSGgsvsyldvllgsesfSDFLDRLSALSKIADADA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 227 KELSDQIQRALQLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEV 306
Cdd:COG3883  133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212


                 ....
gi 731218501 307 EEWQ 310
Cdd:COG3883  213 AAAA 216
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 161-326 2.50e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.91  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  161 PDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDyeektkkaekelsdqiQRALQLE 240
Cdd:TIGR02794  52 ANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE----------------QAAKQAE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  241 DERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIAllEEARRRKENEVEEWQHRAREAQDDL 320
Cdd:TIGR02794 116 EKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA--EEAKKKAEAEAKAKAEAEAKAKAEE 193


                  ....*.
gi 731218501  321 VKTKEE 326
Cdd:TIGR02794 194 AKAKAE 199
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-331 3.00e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 181 QLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERKRAQEEAERLEADRVAA 260
Cdd:COG1196  665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 261 LQAKEELERQAADQIKSQEQLATELAEYTAKIALL--------EEARRRKEneveewQHRAREAQ-DDLVKTKEELHLVM 331
Cdd:COG1196  745 EELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaiEEYEELEE------RYDFLSEQrEDLEEARETLEEAI 818
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 151-328 3.78e-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: 43.12  E-value: 3.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   151 NHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETE--KKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKE 228
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   229 LSDQIQRALQLEDERKRAQEEAERLEA------DRVAALQAKEELERQAADQIKSQEqLATELAEYTAKIALLEEARRRK 302
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEArlerleDRRERLQQEIEELLKKLEEAELKE-LQAELEELEEELEELQEELERL 459

                          170       180
                   ....*....|....*....|....*.
gi 731218501   303 ENEVEEWQHRAREAQDDLVKTKEELH 328
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELA 485
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
162-320 4.15e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  162 DTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRAL-QLE 240
Cdd:COG4913   265 AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeQLE 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  241 DERKRAQEEAERLEADRVAALQAKEELERQAADQIKS----QEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREA 316
Cdd:COG4913   345 REIERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424


                  ....
gi 731218501  317 QDDL 320
Cdd:COG4913   425 EAEI 428
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 158-328 6.95e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   158 RRKPDTIEVQQMKAQAREEKHQKQLERQ---------QLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKE 228
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDKLlaeieelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   229 LSDQIQRALQLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEE 308
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466

                          170       180
                   ....*....|....*....|
gi 731218501   309 WQHRAREAQDDLVKTKEELH 328
Cdd:TIGR02169  467 YEQELYDLKEEYDRVEKELS 486
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 75-148 7.43e-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: 7.43e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 731218501  75 KKGTDLWLGVDALGLnIYEKDDKLTPKIGFPWSEIRNISFND-----KKFVIKPIDkKAPDFVFYAPRLRINKRILQLC 148
Cdd:cd00900   13 TKRVEGTLYITSDRL-ILRDKNDGGLELSIPISDIVNVNVSPqgpssRYLVLVLKD-RGEFVGFSFPKEEDAIEISDAL 89
PTZ00121 PTZ00121
MAEBL; Provisional
 156-410 7.60e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 7.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  156 MRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKK----RRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKEL-- 229
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKadeaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAkk 1541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  230 ------SDQIQRALQLED-ERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRK 302
Cdd:PTZ00121 1542 aeekkkADELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  303 ENEVEEWQHRAREAQDDLVKTKEELHLVMTAPPPPPPPVYEPASYHVQENLQEEGAEPMGYSAELSSEGILDDRNEEKRI 382
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701

                         250       260
                  ....*....|....*....|....*...
gi 731218501  383 TEAEKNERVQRQLLTLSNELSQARDENK 410
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENK 1729
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-316 8.71e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  165 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQiqrALQLEDERK 244
Cdd:COG4913   686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE---RFAAALGDA 762

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 731218501  245 RAQEEAERLEADRVAALQAKEELERQAADQIKS-QEQLATELAEYTAKIALLEEARRR----KENEVEEWQHRAREA 316
Cdd:COG4913   763 VERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALldrlEEDGLPEYEERFKEL 839
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 162-326 1.34e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 162 DTIEVQQMKAQAREEKHQKQLERQQLETEKKRREtVEREKEQMLREKEELMLRLQDYEEKTKKAEKE--------LSDQI 233
Cdd:COG3883   40 DALQAELEELNEEYNELQAELEALQAEIDKLQAE-IAEAEAEIEERREELGERARALYRSGGSVSYLdvllgsesFSDFL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 234 QRALQLE-------DERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEV 306
Cdd:COG3883  119 DRLSALSkiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198

                        170       180
                 ....*....|....*....|
gi 731218501 307 EEWQHRAREAQDDLVKTKEE 326
Cdd:COG3883  199 AELEAELAAAEAAAAAAAAA 218
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
184-319 1.52e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  184 RQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKkaekeLSDQIQRALQLEDERKRAQEEAERLEADRVAALQA 263
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-----ALQRLAEYSWDEIDVASAEREIAELEAELERLDAS 683

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 731218501  264 K---EELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAREAQDD 319
Cdd:COG4913   684 SddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 174-262 2.08e-03

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


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 39.90  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  174 REEKHQKQLERQQLETEKKRRETVEREKE--QMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERKRAQEEAE 251
Cdd:pfam15991  20 RERERKKQEQEAKMEEERLRREREEREKEdrMTLEETKEQILKLEKKLADLKEEKHQLFLQLKKVLHEDETRKRQLKEQS 99

                          90
                  ....*....|.
gi 731218501  252 RLEADRVAALQ 262
Cdd:pfam15991 100 ELFALQQAAAQ 110
PTZ00121 PTZ00121
MAEBL; Provisional
 156-449 2.28e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  156 MRRRKPDTIEVQ--QMKAQAREEKHQkqlERQQLETEKKRRETVEREKEqmlREKEELMLRLQDYEEKTKKAEKELSDQI 233
Cdd:PTZ00121 1069 DEGLKPSYKDFDfdAKEDNRADEATE---EAFGKAEEAKKTETGKAEEA---RKAEEAKKKAEDARKAEEARKAEDARKA 1142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  234 QRALQLEDERK----RAQEEAERLEADRVA-----ALQAKEELE-RQAADQIKSQEQLATELAEYTAKIALLEEARRRKE 303
Cdd:PTZ00121 1143 EEARKAEDAKRveiaRKAEDARKAEEARKAedakkAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARKAED 1222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  304 NEVEEWQHRAREAQddlvKTKEELHLVMTAPPPPPPPVYEPASY-HVQENLQEEGAEPMGYSAELSSEgilddrNEEKRI 382
Cdd:PTZ00121 1223 AKKAEAVKKAEEAK----KDAEEAKKAEEERNNEEIRKFEEARMaHFARRQAAIKAEEARKADELKKA------EEKKKA 1292

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 731218501  383 TEAEKNERVQR--QLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEA 449
Cdd:PTZ00121 1293 DEAKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 157-301 2.37e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 157 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRA 236
Cdd:COG1196  676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 731218501 237 LQLEDERKRAQEEAERLEADRVAA----LQAKEELERqaadqiksqeqLATELAEYTAKIALLEEARRR 301
Cdd:COG1196  756 LPEPPDLEELERELERLEREIEALgpvnLLAIEEYEE-----------LEERYDFLSEQREDLEEARET 813
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
168-327 2.57e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 168 QMKAQArEEKHQKQLERQQLETEKKRRET------VEREKEQMLREKEELMLRLQDYEEKTKK----------------- 224
Cdd:PRK02224 191 QLKAQI-EEKEEKDLHERLNGLESELAELdeeierYEEQREQARETRDEADEVLEEHEERREEletleaeiedlretiae 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 225 -------AEKELSDQIQRALQLEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEE 297
Cdd:PRK02224 270 terereeLAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349

                        170       180       190
                 ....*....|....*....|....*....|
gi 731218501 298 ARRRKENEVEEWQHRAREAQDDLVKTKEEL 327
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAV 379
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-314 3.28e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 165 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVErEKEQMLREKEELMLRLQDYEEKTKKaekeLSDQIQRALQLEDERK 244
Cdd:COG4717   99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELA 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 731218501 245 RAQEEAERLEAD-RVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRAR 314
Cdd:COG4717  174 ELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 165-424 3.34e-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: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  165 EVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMlREKEELMLRLQDYEE------KTKKAEKELSDQIQRALQ 238
Cdd:pfam17380 338 EQERMAMERERELERIRQEERKRELERIRQEEIAMEISRM-RELERLQMERQQKNErvrqelEAARKVKILEEERQRKIQ 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  239 ---LEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLatelaeytAKIALLEEARRRKENEVEEWQHRARE 315
Cdd:pfam17380 417 qqkVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV--------ERLRQQEEERKRKKLELEKEKRDRKR 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  316 AQDDLVKTKEElhlvmTAPPPPPPPVYEPASYHVQENLQEEGAEPMgYSAELSSEGilddRNEEKRITEAEKNERVQRQL 395
Cdd:pfam17380 489 AEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAI-YEEERRREA----EEERRKQQEMEERRRIQEQM 558

                         250       260       270
                  ....*....|....*....|....*....|.
gi 731218501  396 LTLSNELS--QARDENKRTHNDIIHNENMRQ 424
Cdd:pfam17380 559 RKATEERSrlEAMEREREMMRQIVESEKARA 589
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
162-449 3.91e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 162 DTIEVQQMKAQAREEKHQKQLE-----RQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRA 236
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEeheerREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 237 -----------LQLEDERKRAQEEAERLEADRVAALQAKEELE--RQAADQIKSQ-EQLATELAEYTAKIALLEEARRRK 302
Cdd:PRK02224 303 glddadaeaveARREELEDRDEELRDRLEECRVAAQAHNEEAEslREDADDLEERaEELREEAAELESELEEAREAVEDR 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 303 ENEVEEWQHRAREAQDDLVKTKEELhlvmtapppppppvyEPASYHvQENLQEEGAEPMGYSAELSSegilDDRNEEKRI 382
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDL---------------GNAEDF-LEELREERDELREREAELEA----TLRTARERV 442

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 383 TEAEK----------------------NERVQRQLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQgNT 440
Cdd:PRK02224 443 EEAEAlleagkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE-DL 521


                 ....*....
gi 731218501 441 KQRIDEFEA 449
Cdd:PRK02224 522 EELIAERRE 530
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 731218501  65 YGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIgfPWSEIRNISFNDKKF 119
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERI--PYTAIQMATSSGRVF 53
mukB PRK04863
chromosome partition protein MukB;
166-313 4.43e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  166 VQQMKAQ----AREEKHQKQLERQQLETEKK--RRETVEREKEQMLREKEELMLRLQDYeektkkaekeLSDQIQRALQL 239
Cdd:PRK04863  515 LQQLRMRlselEQRLRQQQRAERLLAEFCKRlgKNLDDEDELEQLQEELEARLESLSES----------VSEARERRMAL 584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  240 EDERKRAQEEAERLEADRVAALQAKEELER---QAADQIKSQE-------QLATELAEYTAKIALLEEARRRKENEVEEW 309
Cdd:PRK04863  585 RQQLEQLQARIQRLAARAPAWLAAQDALARlreQSGEEFEDSQdvteymqQLLERERELTVERDELAARKQALDEEIERL 664


                  ....
gi 731218501  310 QHRA 313
Cdd:PRK04863  665 SQPG 668
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 157-321 6.59e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.63  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 157 RRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREK-----------------EELMLRLQDYE 219
Cdd:PRK09510  81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKqaeeaaakaaaaakakaEAEAKRAAAAA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 220 EKTKKAEKELSDQIQRALQLEDERKRAQEEAERlEADRVAALQAKEELERQAADQIKsqEQLATELAEYTAKIALLEEAR 299
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAEAEAKKKAAAEAK--KKAAAEAKAAAAKAAAEAKAA 237

                        170       180
                 ....*....|....*....|..
gi 731218501 300 RRKENEVEEWQHRAREAQDDLV 321
Cdd:PRK09510 238 AEKAAAAKAAEKAAAAKAAAEV 259
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 169-327 7.33e-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: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   169 MKAQAREEKHQKQLER------QQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDE 242
Cdd:TIGR02169  694 QSELRRIENRLDELSQelsdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   243 RKRAQEEAERLEAD----RVAALQAK-EELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEVEEWQHRA---R 314
Cdd:TIGR02169  774 LHKLEEALNDLEARlshsRIPEIQAElSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiE 853

                          170
                   ....*....|...
gi 731218501   315 EAQDDLVKTKEEL 327
Cdd:TIGR02169  854 KEIENLNGKKEEL 866
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 157-326 8.33e-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: 38.57  E-value: 8.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  157 RRRKPDTIEVQQMKAQ---AREEKHQKQLERQQLETEKKRRETVEREKE-QMLREKEELMLRLQDYEEKTKKAEKELSDQ 232
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEqeeARQREVRRLEEERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQ 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501  233 IQRALQLE-DERKRAQeeaerLEADRVAALQAKEELERQAADQIKSQEQLAtelaeytakialleEARRRKENEVEEwqh 311
Cdd:pfam17380 493 RRKILEKElEERKQAM-----IEEERKRKLLEKEMEERQKAIYEEERRREA--------------EEERRKQQEMEE--- 550

                         170
                  ....*....|....*
gi 731218501  312 rAREAQDDLVKTKEE 326
Cdd:pfam17380 551 -RRRIQEQMRKATEE 564
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 159-326 9.01e-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: 38.51  E-value: 9.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   159 RKPDTIEVQQMKAQAREEKhqkqlERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSD------- 231
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEK-----LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlsh 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501   232 ----QIQRALQ-LEDERKRAQEEAERLEADRVAALQAKEELERQAADQIKSQEQLATELAEYTAKIALLEEARRRKENEV 306
Cdd:TIGR02169  791 sripEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870

                          170       180
                   ....*....|....*....|
gi 731218501   307 EEWQHRAREAQDDLVKTKEE 326
Cdd:TIGR02169  871 EELEAALRDLESRLGDLKKE 890
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-325 9.46e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 9.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 167 QQMKAQAREEKHQKQLER--QQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELSDQIQRALQLEDERK 244
Cdd:COG1196  401 QLEELEEAEEALLERLERleEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 245 RAQEEAERLEADRVAALQAKEELE-----RQAADQIKSQEQLATELA-----EYTAKIALLEEARRRKENEVEEWQHRAR 314
Cdd:COG1196  481 ELLEELAEAAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAvligvEAAYEAALEAALAAALQNIVVEDDEVAA 560

                        170
                 ....*....|.
gi 731218501 315 EAQDDLVKTKE 325
Cdd:COG1196  561 AAIEYLKAAKA 571
PRK12704 PRK12704
phosphodiesterase; Provisional
 170-326 9.72e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 9.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 170 KAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEEKTKKAEKELsdqIQRALQLEDERKRAQEE 249
Cdd:PRK12704  32 KIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRL---LQKEENLDRKLELLEKR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731218501 250 AERLEADRVAALQAKEELERQAADQ---IKSQEQLATELAEYTAkiallEEARRRKENEVEEwqhRAREAQDDLVKTKEE 326
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELeelIEEQLQELERISGLTA-----EEAKEILLEKVEE---EARHEAAVLIKEIEE 180
 
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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