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Conserved domains on  [gi|148708550|gb|EDL40497|]
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neurofibromatosis 2, isoform CRA_e, partial [Mus musculus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 221-317 2.41e-63

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


:

Pssm-ID: 270015  Cd Length: 97  Bit Score: 202.89  E-value: 2.41e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 221 MYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 300
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 148708550 301 ILQLCIGNHDLFMRRRK 317
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 28-227 2.11e-60

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: 199.06  E-value: 2.11e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550    28 TVRIVTMDAEM-EFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVLDHDVsKEEPVTFHFLAK 104
Cdd:smart00295   1 VLKVYLLDGTTlEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   105 FYPENaEEELVQEITQH-LFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINly 182
Cdd:smart00295  80 FYPPD-PNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD-- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 148708550   183 QMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 227
Cdd:smart00295 157 SRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 351-470 7.20e-24

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


:

Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 96.91  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  351 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 430
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 148708550  431 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 470
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
ERM_C super family cl38012
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 523-586 7.97e-17

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.


The actual alignment was detected with superfamily member pfam00769:

Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 75.31  E-value: 7.97e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148708550  523 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGgpSSKHNTIKKV 586
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQG--RDKYKTLRKI 62
PLN03086 super family cl29366
PRLI-interacting factor K; Provisional
 312-372 3.19e-03

PRLI-interacting factor K; Provisional


The actual alignment was detected with superfamily member PLN03086:

Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.24  E-value: 3.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148708550 312 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 372
Cdd:PLN03086   3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
 
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 ...
 221-317 2.41e-63

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


Pssm-ID: 270015  Cd Length: 97  Bit Score: 202.89  E-value: 2.41e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 221 MYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 300
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 148708550 301 ILQLCIGNHDLFMRRRK 317
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 28-227 2.11e-60

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: 199.06  E-value: 2.11e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550    28 TVRIVTMDAEM-EFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVLDHDVsKEEPVTFHFLAK 104
Cdd:smart00295   1 VLKVYLLDGTTlEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   105 FYPENaEEELVQEITQH-LFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINly 182
Cdd:smart00295  80 FYPPD-PNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD-- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 148708550   183 QMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 227
Cdd:smart00295 157 SRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 25-108 4.01e-53

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


Pssm-ID: 340706  Cd Length: 85  Bit Score: 175.65  E-value: 4.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  25 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHDVSKEEPVTFHFLA 103
Cdd:cd17186    1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQDVPKEEPVTFHFLA 80


                 ....*
gi 148708550 104 KFYPE 108
Cdd:cd17186   81 KFYPE 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 111-227 2.06e-33

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 123.53  E-value: 2.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  111 EEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWE 190
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 148708550  191 ERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 227
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
231-316 8.46e-28

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.57  E-value: 8.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  231 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 309
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 148708550  310 DLFMRRR 316
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 351-470 7.20e-24

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 96.91  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  351 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 430
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 148708550  431 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 470
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 523-586 7.97e-17

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: 75.31  E-value: 7.97e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148708550  523 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGgpSSKHNTIKKV 586
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQG--RDKYKTLRKI 62
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-481 8.42e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.05  E-value: 8.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 315 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 394
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 395 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 474
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                 ....*..
gi 148708550 475 QKLLEIA 481
Cdd:COG1196  435 EEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 322-563 9.82e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 9.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 322 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 401
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 481
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 482 TKPTYPPMNPIPPPLPPDIPSFDIIADslsfdfkDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERET 561
Cdd:COG1196  400 AQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472


                 ..
gi 148708550 562 AL 563
Cdd:COG1196  473 AL 474
PTZ00121 PTZ00121
MAEBL; Provisional
 315-589 3.08e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEVQQMKAQARE----EKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 387
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAA 1356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  388 LLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEADQLKQDLQEAR 467
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAEEKKKAD 1434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  468 EAERRA--KQKLLEIATKPTYPPMNPIPPPLPPDIPSfdiiADSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLN 545
Cdd:PTZ00121 1435 EAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAK---KKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 148708550  546 ELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKKVPEM 589
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 324-483 2.22e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 62.90  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 324 QQMKAQAREEKARKQMERQRlAREKQMREEAErtrdelERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 403
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQ-AEELQQKQAAE------QERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 404 AQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 482
Cdd:PRK09510 142 AAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216


                 .
gi 148708550 483 K 483
Cdd:PRK09510 217 K 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 322-554 1.83e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   322 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 401
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 481
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   482 TKPTYPPMNPIPPPLPPDIPSFDI---------IADSLSFDFKDTdmkrlSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 552
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLeglevridnLQERLSEEYSLT-----LEEAEALENKIEDDEEEARRRLKRLENKIK 982


                   ..
gi 148708550   553 AL 554
Cdd:TIGR02168  983 EL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-560 4.42e-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: 53.14  E-value: 4.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   307 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 379
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   380 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 453
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   454 KEADQLKQDLQEAREAERRAKQKLLEIA----------TKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKrls 523
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIEslaaeieeleELIEELESELEALLNERASLEEALALLRSELEELSEELR--- 904

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 148708550   524 mEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 560
Cdd:TIGR02168  905 -ELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
growth_prot_Scy NF041483
polarized growth protein Scy;
317-470 1.56e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 48.28  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  317 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 396
Cdd:NF041483  490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  397 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRL------MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 470
Cdd:NF041483  560 EETERAIAARQAEAAEELTR-----LHTEAEERLtaaeeaLADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
growth_prot_Scy NF041483
polarized growth protein Scy;
322-483 3.24e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.13  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  322 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 401
Cdd:NF041483  583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 476
Cdd:NF041483  660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                  ....*..
gi 148708550  477 LLEIATK 483
Cdd:NF041483  740 LLASARK 746
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 334-425 9.71e-04

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.73  E-value: 9.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 334 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 412
Cdd:cd06503   29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106

                         90
                 ....*....|...
gi 148708550 413 EMQRIKAtAIRTE 425
Cdd:cd06503  107 EKEKALA-ELRKE 118
growth_prot_Scy NF041483
polarized growth protein Scy;
338-479 9.86e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  338 QMERQRLARE-KQMREEA----ERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAA--- 408
Cdd:NF041483  439 QEEARRLRGEaEQLRAEAvaegERIRGEARREAVQQIEEaARTAEELLTKAKADADELRSTATAESERVRTEAIERAttl 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  409 --EAEQEMQRIKATA--IRTEEEKRLMEQKVlEAEVLALKMAEESE-----RRAKEADQLKQDLQEAREAERRAKQKLLE 479
Cdd:NF041483  519 rrQAEETLERTRAEAerLRAEAEEQAEEVRA-AAERAARELREETEraiaaRQAEAAEELTRLHTEAEERLTAAEEALAD 597
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 312-372 3.19e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.24  E-value: 3.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148708550 312 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 372
Cdd:PLN03086   3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
growth_prot_Scy NF041483
polarized growth protein Scy;
326-471 6.28e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.81  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  326 MKAQARE--EKARKQMERQRlareKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAqiTEEEAKL- 402
Cdd:NF041483  518 LRRQAEEtlERTRAEAERLR----AEAEEQAEEVRAAAERAARELREETERAIAA--RQAEAAEELTRLH--TEAEERLt 589

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  403 -----LAQKAAEAE-------QEMQRIKATAirTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDL--QEARE 468
Cdd:NF041483  590 aaeeaLADARAEAErirreaaEETERLRTEA--AERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLrsEAAAE 667


                  ...
gi 148708550  469 AER 471
Cdd:NF041483  668 AER 670
 
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 ...
 221-317 2.41e-63

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


Pssm-ID: 270015  Cd Length: 97  Bit Score: 202.89  E-value: 2.41e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 221 MYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 300
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 148708550 301 ILQLCIGNHDLFMRRRK 317
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 28-227 2.11e-60

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: 199.06  E-value: 2.11e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550    28 TVRIVTMDAEM-EFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVLDHDVsKEEPVTFHFLAK 104
Cdd:smart00295   1 VLKVYLLDGTTlEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   105 FYPENaEEELVQEITQH-LFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINly 182
Cdd:smart00295  80 FYPPD-PNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD-- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 148708550   183 QMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 227
Cdd:smart00295 157 SRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 25-108 4.01e-53

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


Pssm-ID: 340706  Cd Length: 85  Bit Score: 175.65  E-value: 4.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  25 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHDVSKEEPVTFHFLA 103
Cdd:cd17186    1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQDVPKEEPVTFHFLA 80


                 ....*
gi 148708550 104 KFYPE 108
Cdd:cd17186   81 KFYPE 85
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 27-108 1.52e-42

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins; The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that play an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Merlin, which is highly related to the members of the ezrin, radixin, and moesin (ERM) protein family that are directly attached to and functionally linked with NHE1, is included in this family.


Pssm-ID: 340617  Cd Length: 83  Bit Score: 147.43  E-value: 1.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  27 FTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKD-TVAWLKMDKKVLDHDVSKEEPVTFHFLAKF 105
Cdd:cd17097    1 INVRVTTMDAELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKgRVAWLKPDKKVLTQDVSKNNTLKFFFLVKF 80


                 ...
gi 148708550 106 YPE 108
Cdd:cd17097   81 YPE 83
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 111-227 2.06e-33

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 123.53  E-value: 2.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  111 EEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWE 190
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 148708550  191 ERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 227
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 28-108 3.31e-30

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


Pssm-ID: 340707 [Multi-domain]  Cd Length: 83  Bit Score: 113.33  E-value: 3.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  28 TVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFY 106
Cdd:cd17187    2 NVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVdSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKFY 81


                 ..
gi 148708550 107 PE 108
Cdd:cd17187   82 PE 83
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 119-219 6.75e-30

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


Pssm-ID: 271216  Cd Length: 99  Bit Score: 113.11  E-value: 6.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 119 TQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWEERITAWYA 198
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLK--QRKPEEWEKRIVELHK 78

                         90       100
                 ....*....|....*....|.
gi 148708550 199 EHRGRARDEAEMEYLKIAQDL 219
Cdd:cd14473   79 KLRGLSPAEAKLKYLKIARKL 99
FERM_C pfam09380
FERM C-terminal PH-like domain;
231-316 8.46e-28

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.57  E-value: 8.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  231 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 309
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 148708550  310 DLFMRRR 316
Cdd:pfam09380  79 TFFRLRR 85
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 25-108 8.98e-26

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and similar proteins; Ezrin, also termed cytovillin, or villin-2, or p81, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Ezrin is a tyrosine kinase substrate that functions as a cross-linker between actin cytoskeleton and plasma membrane. It has been implicated in the regulation of the proliferation, apoptosis, adhesion, invasion, metastasis and angiogenesis of cancer cells.


Pssm-ID: 340759  Cd Length: 85  Bit Score: 100.83  E-value: 8.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  25 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDVSKEEPVTFHFLA 103
Cdd:cd17239    1 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVdNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 80


                 ....*
gi 148708550 104 KFYPE 108
Cdd:cd17239   81 KFYPE 85
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 26-108 6.67e-24

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and similar proteins; Moesin, also termed membrane-organizing extension spike protein, is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Moesin is involved in mitotic spindle function through stabilizing cell shape and microtubules at the cell cortex. It is required for the formation of F-actin networks that mediate endosome biogenesis or maturation and transport through the degradative pathway.


Pssm-ID: 340757  Cd Length: 84  Bit Score: 95.58  E-value: 6.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  26 TFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYtiKDTVA---WLKMDKKVLDHDVSKEEPVTFHFL 102
Cdd:cd17237    1 TISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQY--QDTKGfstWLKLNKKVTAQDVRKESPLLFKFR 78


                 ....*.
gi 148708550 103 AKFYPE 108
Cdd:cd17237   79 AKFYPE 84
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 351-470 7.20e-24

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 96.91  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  351 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 430
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 148708550  431 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 470
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 29-108 4.34e-23

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and similar proteins; Radixin is a member of the ezrin/radixin/moesin (ERM) family of cytoskeletal proteins that plays an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. The C-terminal domain can fold back to bind to the FERM domain forming an autoinhibited conformation. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Radixin plays important roles in cell polarity, cell motility, invasion and tumor progression. It mediates the binding of F-actin to the plasma membrane after a conformational activation through Akt2-dependent phosphorylation at Thr564. It is also involved in reversal learning and short-term memory by regulating synaptic GABAA receptor density.


Pssm-ID: 340758 [Multi-domain]  Cd Length: 83  Bit Score: 93.26  E-value: 4.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  29 VRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYP 107
Cdd:cd17238    3 VRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVdSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFP 82


                 .
gi 148708550 108 E 108
Cdd:cd17238   83 E 83
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 523-586 7.97e-17

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: 75.31  E-value: 7.97e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148708550  523 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGgpSSKHNTIKKV 586
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQG--RDKYKTLRKI 62
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 223-313 3.56e-16

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


Pssm-ID: 275389  Cd Length: 93  Bit Score: 73.95  E-value: 3.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 223 GVNYFTIRNK--KGTELLLGVDALGLHIYDPENRlTPKISFPWNEIRNISYS-DKEFTIKPLDK-KIDVFKFNSSKlRVN 298
Cdd:cd00836    1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEdKQSKLLFQTPS-RQA 78

                         90
                 ....*....|....*
gi 148708550 299 KLILQLCIGNHDLFM 313
Cdd:cd00836   79 KEIWKLIVGYHRFLL 93
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 27-105 7.00e-15

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 69.92  E-value: 7.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  27 FTVRIVTMD-AEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVLDHdVSKEEPVTFHFLAK 104
Cdd:cd01765    1 ISCRVRLLDgTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKhWLDLDKKISKQ-LKRSGPYQFYFRVK 79


                 .
gi 148708550 105 F 105
Cdd:cd01765   80 F 80
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-481 8.42e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.05  E-value: 8.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 315 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 394
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 395 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 474
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                 ....*..
gi 148708550 475 QKLLEIA 481
Cdd:COG1196  435 EEEEEEE 441
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 223-318 1.42e-13

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


Pssm-ID: 270012  Cd Length: 113  Bit Score: 67.37  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 223 GVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKK--------------IDVF 288
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRrnshrsrrtfqsssVSVH 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 148708550 289 KFNSSKLRVNKLILQLCIGNHDLFMRRRKA 318
Cdd:cd13191   81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQS 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 322-563 9.82e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 9.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 322 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 401
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 481
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 482 TKPTYPPMNPIPPPLPPDIPSFDIIADslsfdfkDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERET 561
Cdd:COG1196  400 AQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472


                 ..
gi 148708550 562 AL 563
Cdd:COG1196  473 AL 474
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 314-483 2.54e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 2.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 393
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 394 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 473
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                        170
                 ....*....|
gi 148708550 474 KQKLLEIATK 483
Cdd:COG1196  469 LEEAALLEAA 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-570 9.89e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 9.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 310 DLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 389
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 390 AEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREA 469
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 470 ERRAKQKLLEIATkptyPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKT 549
Cdd:COG1196  395 AAELAAQLEELEE----AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                        250       260
                 ....*....|....*....|.
gi 148708550 550 EIEALKLKERETALDVLHSES 570
Cdd:COG1196  471 EAALLEAALAELLEELAEAAA 491
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 35-109 1.98e-11

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


Pssm-ID: 340720  Cd Length: 89  Bit Score: 60.29  E-value: 1.98e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148708550  35 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYtIKDT--VAWLKMDKKVLDHDVSKEE-PVTFHFLAKFYPEN 109
Cdd:cd17200   12 DRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITF-IDDTgqSNWLQLDHRVLDHDLPKKSgPVTLYFAVRFYIES 88
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 314-483 2.22e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 393
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 394 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 473
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        170
                 ....*....|
gi 148708550 474 KQKLLEIATK 483
Cdd:COG1196  483 LEELAEAAAR 492
PTZ00121 PTZ00121
MAEBL; Provisional
 315-589 3.08e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEVQQMKAQARE----EKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 387
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAA 1356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  388 LLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEADQLKQDLQEAR 467
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAEEKKKAD 1434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  468 EAERRA--KQKLLEIATKPTYPPMNPIPPPLPPDIPSfdiiADSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLN 545
Cdd:PTZ00121 1435 EAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAK---KKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 148708550  546 ELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKKVPEM 589
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 31-91 4.51e-11

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


Pssm-ID: 430570  Cd Length: 63  Bit Score: 58.37  E-value: 4.51e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148708550   31 IVTMDA-EMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDV 91
Cdd:pfam09379   1 VRLLDGtVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLdDNGEHRWLDLSKRLSKQAP 63
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 35-107 1.89e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and pleckstrin domain-containing protein 1 (FARP1) and similar proteins; This family includes the F1 sub-domain of FERM, RhoGEF and pleckstrin domain-containing proteins FARP1, FARP2, and FERM domain-containing protein 7 (FRMD7). FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340618  Cd Length: 85  Bit Score: 57.22  E-value: 1.89e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148708550  35 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHdVSKEEPVTFHFLAKFYP 107
Cdd:cd17098   10 DTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTdPEGNKCWLDPEKPILRQ-VKRPKDVVFKFVVKFYT 82
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 324-483 2.22e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 62.90  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 324 QQMKAQAREEKARKQMERQRlAREKQMREEAErtrdelERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 403
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQ-AEELQQKQAAE------QERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 404 AQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 482
Cdd:PRK09510 142 AAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216


                 .
gi 148708550 483 K 483
Cdd:PRK09510 217 K 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 316-562 3.23e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 3.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 316 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQI 395
Cdd:COG1196  213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 396 TEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQ 475
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 476 KLLEIATKptyppmnpippPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 555
Cdd:COG1196  373 ELAEAEEE-----------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441


                 ....*..
gi 148708550 556 LKERETA 562
Cdd:COG1196  442 EALEEAA 448
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 35-109 4.09e-10

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


Pssm-ID: 340623  Cd Length: 91  Bit Score: 56.52  E-value: 4.09e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148708550  35 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHDVSK---EEPVTFHFLAKFYPEN 109
Cdd:cd17103   12 DRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDeTGHYNWLQLDKRVLDHEFPKkwsSGPLVLHFAVKFYVES 90
RA_FERM_F0_F1_like cd01768
Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 ...
 29-103 6.77e-10

Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 sub-domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting, directly or indirectly, with Ras proteins and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras protein is a small GTPase that is involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon. The FERM domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, also known as the N-terminal Ubl-like structural domain of the FERM domain (FERM_N), which is structurally similar to Ub. Some FERM domain-containing proteins contain an N-terminal region, which also has the beta-grasp Ub-like fold, precedes the FERM domain and has been referred to as the F0 domain.


Pssm-ID: 340467  Cd Length: 110  Bit Score: 56.79  E-value: 6.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  29 VRIVTM-----DAEMEFNCEMKWKGKDLFDLVCRTLGLR-----------ETWFFGLQYTIKDTVA-------------- 78
Cdd:cd01768    2 LKIFGAglasgANYKSVLATARSTARELVAEALERYGLAgspgggpgessCVDAFALCDALGRPAAagvgsgewraehlr 81

                         90       100
                 ....*....|....*....|....*....
gi 148708550  79 WLKMDKKV----LDHDVSKEEPVTFHFLA 103
Cdd:cd01768   82 VLGDSERPllvqELWRARPGWARRFELRG 110
PTZ00121 PTZ00121
MAEBL; Provisional
 315-560 9.94e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 9.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-EATMANEALMRSEETADLLAEKA 393
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEA 1612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  394 QiTEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESeRRAKEADQLKQDLQEAREAERRA 473
Cdd:PTZ00121 1613 K-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-KKAEEDKKKAEEAKKAEEDEKKA 1690

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  474 KQKLLEIATKPTYPPMNPIppplppdipsfdiiadslsfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEA 553
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKK----------------------KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748


                  ....*..
gi 148708550  554 LKLKERE 560
Cdd:PTZ00121 1749 AKKDEEE 1755
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 314-476 4.47e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 58.66  E-value: 4.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 393
Cdd:PRK09510  81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 394 QITEEEAKLLAQKAAEAEQEmQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 473
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAA-AEAKKKAEAEAAAKAAAEAKK-KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAA 238


                 ...
gi 148708550 474 KQK 476
Cdd:PRK09510 239 EKA 241
PTZ00121 PTZ00121
MAEBL; Provisional
 315-560 6.14e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 6.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEVQQMKAQAREEkARKQMERQRLAREKQMREEAERTRDELERRllqmKEEATMANEALMRSEEtADLLAEKAQ 394
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKADEAKKKAEE-AKKKADEAK 1503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  395 ITEEEAKLL--------AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 466
Cdd:PTZ00121 1504 KAAEAKKKAdeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  467 REAERRAKQKLLEIAtkPTYPPMNPIPPPLPPDIPSFDIIADSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNE 546
Cdd:PTZ00121 1584 EEAKKAEEARIEEVM--KLYEEEKKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                         250
                  ....*....|....
gi 148708550  547 LKTEIEALKLKERE 560
Cdd:PTZ00121 1659 NKIKAAEEAKKAEE 1672
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 25-109 6.58e-09

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


Pssm-ID: 340627  Cd Length: 91  Bit Score: 53.12  E-value: 6.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  25 KTFTVRIVTMDaEMEFNCEMK------WKGKDLFDLVCRTLGLRETWFFGLQYTIKDT-VAWLKMDKKVLDHDVSKEEPV 97
Cdd:cd17107    1 EEFYCEIVLLD-ESELILTIQqdgiksSKGSVVLDVVFQHLNLLETDYFGLRYIDRQHqTHWLDPAKTLSEQLKLIGPPY 79

                         90
                 ....*....|..
gi 148708550  98 TFHFLAKFYPEN 109
Cdd:cd17107   80 TLYFGVKFYAED 91
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 37-109 8.20e-09

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


Pssm-ID: 340621  Cd Length: 97  Bit Score: 52.95  E-value: 8.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  37 EMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYtIKDT-------------VA---WLKMDKKVLDHdvsKEEPVTFH 100
Cdd:cd17101   13 RLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAV-LKDGeyffldpdtklskYApkgWKSEAKKGLKG---GKPVFTLY 88


                 ....*....
gi 148708550 101 FLAKFYPEN 109
Cdd:cd17101   89 FRVKFYVDN 97
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 313-483 1.20e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.12  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 313 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMRSEETADLLAEK 392
Cdd:PRK09510  67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEEAAKQAALKQKQAEEAAAKAAAA 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 393 AQI-TEEEAKLLAQKAAEAEQEMqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 471
Cdd:PRK09510 145 AKAkAEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA 221

                        170
                 ....*....|..
gi 148708550 472 RAKQKLLEIATK 483
Cdd:PRK09510 222 EAKAAAAKAAAE 233
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 221-312 1.58e-08

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


Pssm-ID: 270010  Cd Length: 95  Bit Score: 52.31  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 221 MYGVNYFTIRNKKGTELLLGVDALGLHIYdpENRLtpKIS-FPWNEIRNISYSDKEFTI----KPLDKKIDVFKFNSSKL 295
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVF--QNGI--RINtFPWSKIVKISFKRKQFFIqlrrEPNESRDTILGFNMLSY 76

                         90
                 ....*....|....*..
gi 148708550 296 RVNKLILQLCIGNHDLF 312
Cdd:cd13189   77 RACKNLWKSCVEHHTFF 93
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 322-554 1.83e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   322 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 401
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 481
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   482 TKPTYPPMNPIPPPLPPDIPSFDI---------IADSLSFDFKDTdmkrlSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 552
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLeglevridnLQERLSEEYSLT-----LEEAEALENKIEDDEEEARRRLKRLENKIK 982


                   ..
gi 148708550   553 AL 554
Cdd:TIGR02168  983 EL 984
PTZ00121 PTZ00121
MAEBL; Provisional
 315-560 7.12e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 7.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEvQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR---------LLQMKEEATMANEALMRSEET 385
Cdd:PTZ00121 1404 KKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeeakkaeeAKKKAEEAKKADEAKKKAEEA 1482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  386 ADllAEKAQITEEEAKLLAQKAAEAEQEMQriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRaKEADQLKQdLQE 465
Cdd:PTZ00121 1483 KK--ADEAKKKAEEAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK-KKADELKK-AEE 1556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  466 AREAE--RRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRlsMEIEKEKVEYMEKSKHLQEQ 543
Cdd:PTZ00121 1557 LKKAEekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKK 1634

                         250
                  ....*....|....*..
gi 148708550  544 LNELKTEIEALKLKERE 560
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEE 1651
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 222-312 7.40e-08

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: 50.40  E-value: 7.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 222 YGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK-------PLDKKIDvFKFNSSk 294
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRIN---RFAWPKVLKISYKRNNFYIKirpgefeQYETTIG-FKLPNH- 75

                         90
                 ....*....|....*...
gi 148708550 295 lRVNKLILQLCIGNHDLF 312
Cdd:cd13184   76 -RAAKRLWKVCVEHHTFF 92
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 208-287 9.60e-08

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


Pssm-ID: 270013  Cd Length: 105  Bit Score: 50.47  E-value: 9.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 208 AEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTI---KPLDKK 284
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFILhvmQKEEKK 77


                 ...
gi 148708550 285 IDV 287
Cdd:cd13192   78 HTL 80
PTZ00121 PTZ00121
MAEBL; Provisional
 310-573 1.22e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  310 DLFMRRRKADSL---EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR-----LLQMKEEATMANEALMR 381
Cdd:PTZ00121 1575 DKNMALRKAEEAkkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkveqLKKKEAEEKKKAEELKK 1654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  382 SEETADLLAEKAQITEEEAKLLAQKAAEAEQEmQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEE----SERRAKEAD 457
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElkkaEEENKIKAE 1733

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  458 QLKQDLQEAREAERRAKQKLLEiATKPTYPPMNPIPPPLPPDIPSFDIIADSLsfdfKDTDMKRlSMEIEKEKVEYMEKS 537
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEEL----DEEDEKR-RMEVDKKIKDIFDNF 1807

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 148708550  538 KHLQEQLNELKTEIEALKLKERETALDVLHSESSDR 573
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 316-476 1.24e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 316 RKADSLEVQQMKAQAREEKARKQMERQRlarekqmrEEAERTRDELERRLLQMKEEATMAN--EALMRSEETADLL---- 389
Cdd:COG3883   51 EEYNELQAELEALQAEIDKLQAEIAEAE--------AEIEERREELGERARALYRSGGSVSylDVLLGSESFSDFLdrls 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 390 -------AEKAQITE--EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLK 460
Cdd:COG3883  123 alskiadADADLLEElkADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202

                        170
                 ....*....|....*.
gi 148708550 461 QDLQEAREAERRAKQK 476
Cdd:COG3883  203 AELAAAEAAAAAAAAA 218
PTZ00121 PTZ00121
MAEBL; Provisional
 315-560 1.69e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAE-----------RTRDELERRLLQMKEEATMANEALMRSE 383
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkadeakkaeeaKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  384 ETADllAEKAQITEEEAKLLAQKAAEAEQ--------------EMQRIKATAIRTEEEKRLMEQKVLEAE-----VLALK 444
Cdd:PTZ00121 1562 EKKK--AEEAKKAEEDKNMALRKAEEAKKaeearieevmklyeEEKKMKAEEAKKAEEAKIKAEELKKAEeekkkVEQLK 1639

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  445 MAEESERRakEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSfdiiadslsfdfKDTDMKRLSM 524
Cdd:PTZ00121 1640 KKEAEEKK--KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK------------KEAEEAKKAE 1705

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 148708550  525 EIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 560
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 47-106 1.76e-07

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


Pssm-ID: 340622  Cd Length: 82  Bit Score: 48.78  E-value: 1.76e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148708550  47 KGKDLFDLVCRTLGLRETWFFGLQYTikDTVA---WLKMDKKVLDHdVSKEEPVTFHFLAKFY 106
Cdd:cd17102   23 KGQFLLDYVCNYLNLLEKDYFGLRYV--DTEKqrhWLDPNKSIYKQ-LKGVPPYVLCFRVKFY 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 330-573 2.17e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 330 AREEKARKQME--RQRLAR--------EKQM---REEAERTR------DELERR-----LLQMKE-EATMANEALMRSEE 384
Cdd:COG1196  172 ERKEEAERKLEatEENLERledilgelERQLeplERQAEKAEryrelkEELKELeaellLLKLRElEAELEELEAELEEL 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 385 TADLLAEKAQITEEEAKL---------LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKE 455
Cdd:COG1196  252 EAELEELEAELAELEAELeelrleleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 456 ADQLKQDLQEAREAERRAKQKLLEIATKptypPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYME 535
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 148708550 536 KSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDR 573
Cdd:COG1196  408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 35-109 2.78e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4A (FRMD4A); FRMD4A is a cytohesin adaptor involved in cell structure, transport and signaling. It promotes the growth of cancer cells in tongue, head and neck squamous cell carcinomas. It also regulates tau secretion by activating cytohesin-Arf6 signaling through connecting cytohesin family Arf6-specific guanine-nucleotide exchange factors (GEFs) and Par-3 at primordial adherens junctions during epithelial polarization. As a genetic risk factor for late-onset Alzheimer's disease (AD), FRMD4A may play a role in amyloidogenic and tau-related pathways in AD. FRMD4A contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340719  Cd Length: 89  Bit Score: 48.42  E-value: 2.78e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148708550  35 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDT-VAWLKMDKKVLDHDVSKEE-PVTFHFLAKFYPEN 109
Cdd:cd17199   12 DRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGhLNWLQLDRRVLEHDFPKKSgPVVLYFCVRFYIES 88
PTZ00121 PTZ00121
MAEBL; Provisional
 320-560 3.51e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  320 SLEVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLlAEKAQITEEE 399
Cdd:PTZ00121 1184 AEEVRKAEELRKAEDARK-AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN-EEIRKFEEAR 1261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  400 AKLLAQKAAEAEQEMQRiKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLE 479
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEAR-KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  480 IATKPTYPPMNPIPPplppdipsfdiiADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKER 559
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAA------------ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408


                  .
gi 148708550  560 E 560
Cdd:PTZ00121 1409 E 1409
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 320-476 4.03e-07

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 52.16  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  320 SLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAtmANEALMRSEETADLLAEKAQITEEE 399
Cdd:TIGR02794  46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA--AAEKAAKQAEQAAKQAEEKQKQAEE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  400 AKLL----AQKAAEAEQEMQRIKATAIRTEEEKrlmeqkvleaevlALKMAEESERRAKEAD-QLKQDLQEAREAERRAK 474
Cdd:TIGR02794 124 AKAKqaaeAKAKAEAEAERKAKEEAAKQAEEEA-------------KAKAAAEAKKKAEEAKkKAEAEAKAKAEAEAKAK 190


                  ..
gi 148708550  475 QK 476
Cdd:TIGR02794 191 AE 192
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 30-106 4.36e-07

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


Pssm-ID: 340628  Cd Length: 81  Bit Score: 47.73  E-value: 4.36e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148708550  30 RIVTMD-AEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVlDHDVSKEEPVTFHFLAKFY 106
Cdd:cd17108    4 KVILLDgTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQhWLDPTKKI-KKQVKIGPPYTLRFRVKFY 81
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-560 4.42e-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: 53.14  E-value: 4.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   307 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 379
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   380 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 453
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   454 KEADQLKQDLQEAREAERRAKQKLLEIA----------TKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKrls 523
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIEslaaeieeleELIEELESELEALLNERASLEEALALLRSELEELSEELR--- 904

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 148708550   524 mEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 560
Cdd:TIGR02168  905 -ELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 30-107 4.89e-07

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


Pssm-ID: 340721  Cd Length: 84  Bit Score: 47.57  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  30 RIVTMDAEmEFNCEM--KWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVLDHdvSKEEPVTFHFLAKFY 106
Cdd:cd17201    5 KVTLLDGS-EYECEVekHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKnWLDPSKEIKKQ--IRSGPWHFAFTVKFY 81


                 .
gi 148708550 107 P 107
Cdd:cd17201   82 P 82
PRK12704 PRK12704
phosphodiesterase; Provisional
 315-474 5.39e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.47  E-value: 5.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 315 RRKADSLEVQQMKAQARE--EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEET------- 385
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRilEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENldrklel 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 386 -----ADLLAEKAQITEEEAKLLAQKA------AEAEQEMQRIkatAIRTEEE--KRLMEQKVLEAEVLALKMAEESERR 452
Cdd:PRK12704 105 lekreEELEKKEKELEQKQQELEKKEEeleeliEEQLQELERI---SGLTAEEakEILLEKVEEEARHEAAVLIKEIEEE 181

                        170       180
                 ....*....|....*....|..
gi 148708550 453 AKEadqlkqdlqearEAERRAK 474
Cdd:PRK12704 182 AKE------------EADKKAK 191
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 315-475 8.49e-07

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 51.38  E-value: 8.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETAD--LLAEK 392
Cdd:TIGR02794  69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAErkAKEEA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  393 AQITEEEAKllAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQDLQEAR---EA 469
Cdd:TIGR02794 149 AKQAEEEAK--AKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKA-KAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAaaaEA 225


                  ....*.
gi 148708550  470 ERRAKQ 475
Cdd:TIGR02794 226 ERKADE 231
PTZ00121 PTZ00121
MAEBL; Provisional
 316-560 9.21e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 9.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  316 RKADslEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAlmrseetadllAEKAQI 395
Cdd:PTZ00121 1206 RKAE--EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----------RRQAAI 1272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  396 TEEEAKllaqKAAEAEQEMQRIKATAIRTEEEKRLMEQkvleaevlALKMAEEserrAKEADQLKQDLQEAREAERRAKQ 475
Cdd:PTZ00121 1273 KAEEAR----KADELKKAEEKKKADEAKKAEEKKKADE--------AKKKAEE----AKKADEAKKKAEEAKKKADAAKK 1336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  476 KLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSlsfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 555
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE-----KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411


                  ....*
gi 148708550  556 LKERE 560
Cdd:PTZ00121 1412 KAAAA 1416
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 222-314 9.44e-07

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


Pssm-ID: 270009  Cd Length: 91  Bit Score: 47.28  E-value: 9.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 222 YGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKisFPWNEIRNISYSDKEFTIKPLDKKIDV-FKFNSSklRVNKL 300
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVF--FRWEDIKNVINHKRTFSIECQNSEETVqFQFEDA--ETAKY 76

                         90
                 ....*....|....
gi 148708550 301 ILQLCIGNHDLFMR 314
Cdd:cd13188   77 VWKLCVLQHKFYRQ 90
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 27-88 1.31e-06

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


Pssm-ID: 340619  Cd Length: 85  Bit Score: 46.46  E-value: 1.31e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148708550  27 FTVRIVTMDAE-MEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDK---KVLD 88
Cdd:cd17099    4 FVVRIQLLDNTvLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLrWVDLEKplkKQLD 70
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 322-474 1.40e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   322 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 401
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148708550   402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 474
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 314-585 1.46e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQM--------REEAERTR-DELERRLLQMKEEATMANEALMRSEE 384
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirqeerKRELERIRqEEIAMEISRMRELERLQMERQQKNER 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  385 TADLL--AEKAQITEEE------------AKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKvLEAEVLALKMAEESE 450
Cdd:pfam17380 394 VRQELeaARKVKILEEErqrkiqqqkvemEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE-RQQQVERLRQQEEER 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  451 RRAK-EADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADslsfdfkdtDMKRLSMEIEKE 529
Cdd:pfam17380 473 KRKKlELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE---------EERRREAEEERR 543

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148708550  530 KVEYMEKSKHLQEQL---NELKTEIEALKlKERETALDVLHSESSDRGGPSSKHNTIKK 585
Cdd:pfam17380 544 KQQEMEERRRIQEQMrkaTEERSRLEAME-REREMMRQIVESEKARAEYEATTPITTIK 601
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 322-479 2.03e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.19  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 322 EVQQMKAQAREEKaRKQMERQRLAREKQmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 401
Cdd:PRK09510 105 QLEKERLAAQEQK-KQAEEAAKQAALKQ-KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 402 LLAQKAAEAEQ---EMQRIKATAIRTEEEKRLMEQKvleAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 478
Cdd:PRK09510 183 AKKKAEAEAAAkaaAEAKKKAEAEAKKKAAAEAKKK---AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259


                 .
gi 148708550 479 E 479
Cdd:PRK09510 260 D 260
PTZ00121 PTZ00121
MAEBL; Provisional
 315-560 2.09e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEVQQMKAQARE------EKARKQMERQRLAREKQMREEAERTRDELERRL--LQMKEEATMANEALMRSEETA 386
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEeakkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAK 1522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  387 DllAEKAQITEEEAKLLAQKAAEAEQEMQRI-KATAIRTEEEKRLMEQKVLEAE--VLALKMAEES----ERRAKEADQL 459
Cdd:PTZ00121 1523 K--ADEAKKAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAkkaeEARIEEVMKL 1600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  460 K--------QDLQEAREAERRAKQ-------KLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSfdFKDTDMKRLSM 524
Cdd:PTZ00121 1601 YeeekkmkaEEAKKAEEAKIKAEElkkaeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA--KKAEEDKKKAE 1678

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 148708550  525 EIEKEKVEYMEKSKHLQEQLNElKTEIEALKLKERE 560
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAE 1713
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 230-314 4.26e-06

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: 45.76  E-value: 4.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 230 RNKKGTE--LLLGVDALGLHIYDP-ENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRvNKLILQLCI 306
Cdd:cd13185   12 KSKKETPgsVLLGITAKGIQIYQEsDGEQQLLRTFPWSNIGKLSFDRKKFEIRPEGSLRKLTYYTSSDEK-SKYLLALCR 90


                 ....*...
gi 148708550 307 GNHDLFMR 314
Cdd:cd13185   91 ETHQFSMA 98
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 29-107 5.04e-06

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


Pssm-ID: 340626  Cd Length: 84  Bit Score: 44.74  E-value: 5.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  29 VRIVTMDaEMEFNCEM--KWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWL---KMDKKVLdhdvsKEEPVTFHFL 102
Cdd:cd17106    4 CKVLLLD-GTEYTCEVekRAKGQVLFDKVCEHLNLLEKDYFGLTYRdAQDQKNWLdpaKEIKKQI-----RSGPWLFSFN 77


                 ....*
gi 148708550 103 AKFYP 107
Cdd:cd17106   78 VKFYP 82
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 35-106 5.42e-06

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


Pssm-ID: 340624  Cd Length: 81  Bit Score: 44.57  E-value: 5.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148708550  35 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMdKKVLDHDVSKEEPVTFHFLAKFY 106
Cdd:cd17104   10 SVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTgPKGERLWLNL-RNRISRQLPGPPPYRLRLRVKFF 81
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 332-472 5.86e-06

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 46.57  E-value: 5.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  332 EEKARKQMERQRLAREKQMREEAERTRDELERRLLQmKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAE 411
Cdd:pfam05672  10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRK-EELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEER 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148708550  412 QEMQRikatairteEEKRLMEQKVLEAEVlalKMAEESERRAKEADQLKQDLQEAREAERR 472
Cdd:pfam05672  89 EQREQ---------EEQERLQKQKEEAEA---KAREEAERQRQEREKIMQQEEQERLERKK 137
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
322-483 6.79e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 6.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 322 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEeatmANEALMRSEETADLLAEKAQITEEEAK 401
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK----LLQLLPLYQELEALEAELAELPERLEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 402 LLAQKA--AEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 478
Cdd:COG4717  151 LEERLEelRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                 ....*
gi 148708550 479 EIATK 483
Cdd:COG4717  231 QLENE 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
315-477 6.87e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 6.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEvqQMKAQARE-EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAEKA 393
Cdd:COG4913   248 REQIELLE--PIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL------ERLEARLD 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  394 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALKMAEESERRA-----KEADQLKQDLQEA 466
Cdd:COG4913   320 ALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRarLEALLAALGLPLPASAEEfaalrAEAAALLEALEEE 399

                         170
                  ....*....|.
gi 148708550  467 REAERRAKQKL 477
Cdd:COG4913   400 LEALEEALAEA 410
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
314-485 7.36e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 7.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 314 RRRKADSLEVQQMKAQARE-----EKARKQMERQRLARE--KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETA 386
Cdd:PRK02224 272 REREELAEEVRDLRERLEEleeerDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 387 DLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQ----- 461
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreael 431

                        170       180
                 ....*....|....*....|....*.
gi 148708550 462 --DLQEAREAERRAkQKLLEIATKPT 485
Cdd:PRK02224 432 eaTLRTARERVEEA-EALLEAGKCPE 456
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 318-477 1.28e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.51  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  318 ADSLEVQQMKAQARE-EKARKQMERQRLARE--------KQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtADL 388
Cdd:PRK10929  104 TDALEQEILQVSSQLlEKSRQAQQEQDRAREisdslsqlPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQ-AES 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  389 LAEKAQITEEEaklLAQKAAEAEQEMQRIKATAIRTEEEK----------RLMEQKVLEAEvLALkmaEESERRAKEADQ 458
Cdd:PRK10929  183 AALKALVDELE---LAQLSANNRQELARLRSELAKKRSQQldaylqalrnQLNSQRQREAE-RAL---ESTELLAEQSGD 255

                         170
                  ....*....|....*....
gi 148708550  459 LKQDLQEAREAERRAKQKL 477
Cdd:PRK10929  256 LPKSIVAQFKINRELSQAL 274
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 230-318 1.36e-05

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


Pssm-ID: 270008  Cd Length: 103  Bit Score: 44.24  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 230 RNKK--GTELLLGVDALGLHIYDPEN-RLTPKISFPWNEIRNISYSDKEFTIKP--LDKKIDVFKFNSSKlrVNKLILQL 304
Cdd:cd13187    9 REKKssTLSLWLGICSRGIIIYEEKNgARTPVLRFPWRETQKISFDKKKFTIESrgGSGIKHTFYTDSYK--KSQYLLQL 86

                         90
                 ....*....|....*.
gi 148708550 305 CIGNH--DLFMRRRKA 318
Cdd:cd13187   87 CSAQHkfHIQMRSRQS 102
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 314-475 1.37e-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: 48.02  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMR-----EEAERTRDELERRLLQMKEEATMANEALMRSEETADL 388
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRlrkqrLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  389 LAEKAQITEEEAKllaqkaaEAEQEMQRIKATAIR-TEEEKRLME----------QKVLEAEVLALKMAEESERRAKEAD 457
Cdd:pfam15709 433 QELQRKKQQEEAE-------RAEAEKQRQKELEMQlAEEQKRLMEmaeeerleyqRQKQEAEEKARLEAEERRQKEEEAA 505

                         170
                  ....*....|....*...
gi 148708550  458 QLKQDlQEAREAERRAKQ 475
Cdd:pfam15709 506 RLALE-EAMKQAQEQARQ 522
growth_prot_Scy NF041483
polarized growth protein Scy;
317-470 1.56e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 48.28  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  317 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 396
Cdd:NF041483  490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  397 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRL------MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 470
Cdd:NF041483  560 EETERAIAARQAEAAEELTR-----LHTEAEERLtaaeeaLADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 222-279 1.59e-05

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: 44.16  E-value: 1.59e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148708550 222 YGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPwnEIRNISYSDKEFTIK 279
Cdd:cd13195    1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERIPYT--AIQMATSSGRVFTLT 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 314-473 2.03e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 314 RRRKADSLEVQQMKAQAREEKARKQMER--QRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 391
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 392 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAE-----VLALKMAEESERRAKEADQLKQDLQEA 466
Cdd:COG1196  457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAY 536


                 ....*..
gi 148708550 467 REAERRA 473
Cdd:COG1196  537 EAALEAA 543
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 303-485 2.70e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.04  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  303 QLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQR---LAREKQM----REEAERTRDELErrlLQMKEEATMA 375
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRleeQERQQQVerlrQQEEERKRKKLE---LEKEKRDRKR 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  376 NEALMRSEETADLLAEKAQITEEEAKllaQKAAEAEQEMQRikaTAIRTEEEKRLM-EQKVLEAEVLALKMAEESERRAK 454
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERK---RKLLEKEMEERQ---KAIYEEERRREAeEERRKQQEMEERRRIQEQMRKAT 562

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 148708550  455 EADQLKQDLQEARE-----AERRAKQKLLEIATKPT 485
Cdd:pfam17380 563 EERSRLEAMEREREmmrqiVESEKARAEYEATTPIT 598
PRK12705 PRK12705
hypothetical protein; Provisional
 300-473 2.75e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.01  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 300 LILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKarkqmERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAL 379
Cdd:PRK12705  12 LLIGLLLGVLVVLLKKRQRLAKEAERILQEAQKEA-----EEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 380 MRSEEtaDLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL--MEQKVLEAEVLALKMAEESERRAKEAD 457
Cdd:PRK12705  87 VQKEE--QLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVagLTPEQARKLLLKLLDAELEEEKAQRVK 164

                        170
                 ....*....|....*.
gi 148708550 458 QLKQDLQEarEAERRA 473
Cdd:PRK12705 165 KIEEEADL--EAERKA 178
growth_prot_Scy NF041483
polarized growth protein Scy;
322-483 3.24e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.13  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  322 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 401
Cdd:NF041483  583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 476
Cdd:NF041483  660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                  ....*..
gi 148708550  477 LLEIATK 483
Cdd:NF041483  740 LLASARK 746
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 32-107 3.68e-05

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


Pssm-ID: 340722  Cd Length: 84  Bit Score: 42.27  E-value: 3.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148708550  32 VTMDAEMEFNC--EMKWKGKDLFDLVCRTLGLRETWFFGLQYTIK-DTVAWLKMDKKVLDHdvSKEEPVTFHFLAKFYP 107
Cdd:cd17202    6 VTLLDGTEYSCdlEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSaNQKNWLDSTKEIKRQ--IRRLPWLFTFNVKFYP 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 314-466 3.99e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDE--LERRLLQMKEEATMANEALMRSEETADLLAE 391
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErlEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148708550 392 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 466
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
322-481 4.13e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 4.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 322 EVQQMKAQAREEKARKQMERQ-RLAREKQMREEAERTRDELERRLLQMKEEATmanealmRSEETADLLAEKA-QITEEE 399
Cdd:COG2268  202 RIAEAEAERETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEER-------REAETARAEAEAAyEIAEAN 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 400 AKLLAQKAAEAEQEMQRIKATAIRTE-EEKRLMEQKVLEAEVLALKMA--EESERRAKEADQLKQdlQEAREAERRAKQK 476
Cdd:COG2268  275 AEREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEaeAEAEAEAIRAKGLAE--AEGKRALAEAWNK 352


                 ....*
gi 148708550 477 LLEIA 481
Cdd:COG2268  353 LGDAA 357
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
315-419 5.58e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.42  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 315 RRKADSLEVQQMKAQAREEKARKQMER-QRLARE----KQMREEAERTRDELERRLLQMKEEATMANEALmrsEETADLL 389
Cdd:COG1566  109 EAEIAAAEAQLAAAQAQLDLAQRELERyQALYKKgavsQQELDEARAALDAAQAQLEAAQAQLAQAQAGL---REEEELA 185

                         90       100       110
                 ....*....|....*....|....*....|
gi 148708550 390 AEKAQITEEEAKLlaqKAAEAEQEMQRIKA 419
Cdd:COG1566  186 AAQAQVAQAEAAL---AQAELNLARTTIRA 212
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 336-560 5.89e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.27  E-value: 5.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  336 RKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMrsEETADLLAEKAQIteeeakllaqkAAEAEQEMQ 415
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERR--RKLEEAEKARQAEM--DRQAAIYAEQERM-----------AMERERELE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  416 RikataIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERraKQKLLEIATKPTYPPMNPIPPP 495
Cdd:pfam17380 352 R-----IRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR--KVKILEEERQRKIQQQKVEMEQ 424

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148708550  496 LPPDIPsfdiiadslsfDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 560
Cdd:pfam17380 425 IRAEQE-----------EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLE 478
PTZ00121 PTZ00121
MAEBL; Provisional
 322-560 6.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  322 EVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAQITEEEAK 401
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARK-AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA--RKAEDAKKAEAARKAEEVRKA 1190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 481
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148708550  482 TKPTYPPMNPIPPPLPPDIPSFDiiadslsfDFKDTDMKRLSMEIeKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 560
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEEKKKAD--------EAKKAEEKKKADEA-KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-482 6.91e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 310 DLFMRRRKADSLEVQQMKAQAREEKARkqmerQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 389
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALL-----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 390 AEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQK---------------------VLEAEVLALKMAEE 448
Cdd:COG1196  462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvkaalllaglrglagavaVLIGVEAAYEAALE 541

                        170       180       190
                 ....*....|....*....|....*....|....
gi 148708550 449 SERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 482
Cdd:COG1196  542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 333-479 6.93e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 45.66  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  333 EKARKQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEET-ADLLAEKAQITEEEAKLLAQKAAeae 411
Cdd:pfam07888  51 EAANRQREKEK-ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKyKELSASSEELSEEKDALLAQRAA--- 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148708550  412 qEMQRIKataiRTEEEKRLMEQKVLEAEVLALKMAEESERRAKeadQLKQDlqearEAERRAKQKLLE 479
Cdd:pfam07888 127 -HEARIR----ELEEDIKTLTQRVLERETELERMKERAKKAGA---QRKEE-----EAERKQLQAKLQ 181
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 314-479 7.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 7.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 393
Cdd:COG1196  676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 394 QITEEEAKLLAQKAAEAEQEMQRIKA---TAIrtEEEKRLMEQKV-LEAEvlalkmaeeserrakeadqlKQDLQEAREA 469
Cdd:COG1196  756 LPEPPDLEELERELERLEREIEALGPvnlLAI--EEYEELEERYDfLSEQ--------------------REDLEEARET 813

                        170
                 ....*....|....*...
gi 148708550 470 --------ERRAKQKLLE 479
Cdd:COG1196  814 leeaieeiDRETRERFLE 831
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 327-589 7.25e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 7.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   327 KAQAREEKARKQMERQRLAR-----EKQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtadLLAEKAQITEEEAK 401
Cdd:pfam02463  171 KKEALKKLIEETENLAELIIdleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK---LNEERIDLLQELLR 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 481
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   482 TKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLnELKTEIEALKLKERET 561
Cdd:pfam02463  328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA-KLKEEELELKSEEEKE 406

                          250       260
                   ....*....|....*....|....*...
gi 148708550   562 ALDVLHSESSDRGGPSSKHNTIKKVPEM 589
Cdd:pfam02463  407 AQLLLELARQLEDLLKEEKKEELEILEE 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 312-554 8.41e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 8.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 312 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 391
Cdd:COG1196  565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 392 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 471
Cdd:COG1196  645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 472 RAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADslsFDFKDTDMKRLSMEIEK-EKV------EY---MEKSKHLQ 541
Cdd:COG1196  725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD---LEELERELERLEREIEAlGPVnllaieEYeelEERYDFLS 801

                        250
                 ....*....|...
gi 148708550 542 EQLNELKTEIEAL 554
Cdd:COG1196  802 EQREDLEEARETL 814
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 315-484 9.33e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 9.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 315 RRKADSLEVQQMKAQAREEKARKQMERQRlAREKQMREEAERTRDELERRLLQM--------------KEEATMANEALM 380
Cdd:COG4942   61 ERRIAALARRIRALEQELAALEAELAELE-KEIAELRAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQ 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 381 RSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLK 460
Cdd:COG4942  140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219

                        170       180
                 ....*....|....*....|....
gi 148708550 461 QDLQEAREAERRAKQKLLEIATKP 484
Cdd:COG4942  220 QEAEELEALIARLEAEAAAAAERT 243
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 312-479 9.42e-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: 45.43  E-value: 9.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   312 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAE 391
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI------EELEEL 867

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   392 KAQITEEEAKLLAQKAaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAER 471
Cdd:TIGR02168  868 IEELESELEALLNERA-SLEEALALLRSELEELSEELRELESKRSELR-------RELEELREKLAQLELRLEGLEVRID 939


                   ....*...
gi 148708550   472 RAKQKLLE 479
Cdd:TIGR02168  940 NLQERLSE 947
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 314-476 9.43e-05

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.84  E-value: 9.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  314 RRRKADSLEVQQMKAQAREEKARKQM-ERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEalmrsEETADLLAEK 392
Cdd:TIGR02794  89 ARQKELEQRAAAEKAAKQAEQAAKQAeEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE-----EEAKAKAAAE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  393 AQITEEEAKLLAQKAAEAEQEMQRiKATAirtEEEKRLMEQKVLEAEVLALKMAE-ESERRAKEADQLKQDLQEAREAER 471
Cdd:TIGR02794 164 AKKKAEEAKKKAEAEAKAKAEAEA-KAKA---EEAKAKAEAAKAKAAAEAAAKAEaEAAAAAAAEAERKADEAELGDIFG 239


                  ....*
gi 148708550  472 RAKQK 476
Cdd:TIGR02794 240 LASGS 244
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 314-485 1.06e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 45.32  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEaertrdelerrllqmkeeatmanealmRSEETADLLAEKA 393
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA---------------------------RHKKAAEARAAKD 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 394 Q--ITEEEAKLLAQKAAEAEQemqrikaTAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAer 471
Cdd:PRK05035 485 KdaVAAALARVKAKKAAATQP-------IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA-- 555

                        170
                 ....*....|....
gi 148708550 472 RAKQKLLEIATKPT 485
Cdd:PRK05035 556 RAKAKKAAQQAANA 569
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 322-483 1.28e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.94  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  322 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEAL----MRSEETADLLAEKAQITE 397
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQL--ERAEKMREELELEQQRRFEEIRLRKQRLeeerQRQEEEERKQRLQLQAAQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  398 EEAKLLAQKAAEAEQEMQRIKAT--AIRTEEEKRL---MEQKVLEAEVLALKMAEES-----ERRAKEADQLKQDLQEAR 467
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRKKQQeeAERAEAEKQRqkeLEMQLAEEQKRLMEMAEEErleyqRQKQEAEEKARLEAEERR 498

                         170
                  ....*....|....*.
gi 148708550  468 EAERRAKQKLLEIATK 483
Cdd:pfam15709 499 QKEEEAARLALEEAMK 514
PTZ00491 PTZ00491
major vault protein; Provisional
 325-456 1.39e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 45.01  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 325 QMKAQAREEKARKQMERQRLarekQMREEAERTRdeleRRLLQMKEEATmANEALMRSEETADLLAEKAQITEEeaklla 404
Cdd:PTZ00491 669 RHQAELLEQEARGRLERQKM----HDKAKAEEQR----TKLLELQAESA-AVESSGQSRAEALAEAEARLIEAE------ 733

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148708550 405 qkaAEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLAlKMAEESERRAKEA 456
Cdd:PTZ00491 734 ---AEVEQAELRAKALRIEAEAElEKLRKRQELELEYEQ-AQNELEIAKAKEL 782
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
310-480 1.80e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 310 DLFMRRRKADSLEVQQMKAQAREEKARKQmERQRLAREKQMREEAERTRDELERRLLQMKEEAtmanEALMRSEETADLL 389
Cdd:COG4717   57 ELFKPQGRKPELNLKELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREEL----EKLEKLLQLLPLY 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 390 AEKAQItEEEAKLLAQKAAEAEQEMQRIKataiRTEEEKRLMEQKVLEAE-VLALKMAEESERRAKEADQLKQDLQEARE 468
Cdd:COG4717  132 QELEAL-EAELAELPERLEELEERLEELR----ELEEELEELEAELAELQeELEELLEQLSLATEEELQDLAEELEELQQ 206

                        170
                 ....*....|..
gi 148708550 469 AERRAKQKLLEI 480
Cdd:COG4717  207 RLAELEEELEEA 218
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 215-279 2.86e-04

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


Pssm-ID: 270014  Cd Length: 122  Bit Score: 40.79  E-value: 2.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148708550 215 IAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK 279
Cdd:cd13193    2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
315-478 2.89e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 315 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQM----REEAERTRDELERRLLQMKEEATMANEALmrsEETADLLA 390
Cdd:COG4717   94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPlyqeLEALEAELAELPERLEELEERLEELRELE---EELEELEA 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 391 EKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAE 470
Cdd:COG4717  171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ-------EELEELEEELEQLENELEAAALEE 243


                 ....*...
gi 148708550 471 RRAKQKLL 478
Cdd:COG4717  244 RLKEARLL 251
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 317-571 2.98e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   317 KADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQIT 396
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   397 EEEAKLLAQKAAEAEQEMQRIKATAIRTEE-----EKRLMEQKVLEAEVLALKMAEESER---RAKEADQLKQDLQEARE 468
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKE 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   469 AERRAKQKLLE--IATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDmKRLSmEIEKEKVEYMEKSKHLQEQLNE 546
Cdd:TIGR02169  830 YLEKEIQELQEqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE-SRLG-DLKKERDELEAQLRELERKIEE 907

                          250       260
                   ....*....|....*....|....*..
gi 148708550   547 LKTEIEALK--LKERETALDVLHSESS 571
Cdd:TIGR02169  908 LEAQIEKKRkrLSELKAKLEALEEELS 934
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
327-564 3.62e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 327 KAQAREEKARKQMERQRlAREKQMREEAERTRDELERR---LLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 403
Cdd:COG4372   35 KALFELDKLQEELEQLR-EELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 404 AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATK 483
Cdd:COG4372  114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 484 PTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETAL 563
Cdd:COG4372  194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273


                 .
gi 148708550 564 D 564
Cdd:COG4372  274 E 274
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 47-106 3.63e-04

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


Pssm-ID: 340724  Cd Length: 84  Bit Score: 39.42  E-value: 3.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148708550  47 KGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVlDHDVSKEEPVTFHFLAKFY 106
Cdd:cd17204   22 KGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAhWLDHTKPI-KKQIKIGPPYTLHFRIKYY 81
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 315-462 4.11e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.67  E-value: 4.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   315 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEA------ERTRDELERRLLQMKEEATMANEALmrsEETADL 388
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfartalKNARLDLRRLFDEKQSEKDKKNKAL---AERKDS 679

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148708550   389 LAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESER--RAKEADQLKQD 462
Cdd:pfam12128  680 ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRsgAKAELKALETW 755
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 322-464 4.30e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 4.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   322 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRD-------ELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 394
Cdd:TIGR02169  372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   395 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQ 464
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 359-460 4.43e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.15  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 359 DELERRLLQMKEEAtmanEALMRSEETADllAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEA 438
Cdd:COG0542  414 DELERRLEQLEIEK----EALKKEQDEAS--FERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487

                         90       100
                 ....*....|....*....|..
gi 148708550 439 EVLALKMAEESERRAKEADQLK 460
Cdd:COG0542  488 PELEKELAELEEELAELAPLLR 509
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 32-107 4.55e-04

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


Pssm-ID: 340625  Cd Length: 83  Bit Score: 39.41  E-value: 4.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148708550  32 VTMDAEMEFNCEMK--WKGKDLFDLVCRTLGLRETWFFGLQ-YTIKDTVAWLKMDKKVLDHdvSKEEPVTFHFLAKFYP 107
Cdd:cd17105    5 VSLLDDTVYECEVEkhAKGQDLFKKVCEHLNLLEEDYFGLAiWDSPTSKTWLDPAKEIKKQ--VHGGPWEFTFNVKFYP 81
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 35-106 4.61e-04

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


Pssm-ID: 340620  Cd Length: 86  Bit Score: 39.21  E-value: 4.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148708550  35 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQY----TIKDTVAWLKMDKKvLDHDVSKEEPVTFHFLAKFY 106
Cdd:cd17100   11 DTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFsddsPATDSMRWLDPLKP-IRKQIKGGPPYYLNFRVKFY 85
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 35-107 4.61e-04

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


Pssm-ID: 340709  Cd Length: 85  Bit Score: 39.40  E-value: 4.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148708550  35 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHdVSKEEPVTFHFLAKFYP 107
Cdd:cd17189   10 DTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDhRKVMVWLDLLKPIVKQ-IRRPKHVVLRFVVKFFP 82
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 320-480 4.91e-04

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.20  E-value: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  320 SLEVQQMkaqaREEKARKQMERQRLAREKQMREEAERTRDELERRLL-----QMKEEATMANEALMR------------- 381
Cdd:pfam07111 480 SLELEQL----REERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLsevaqQLEQELQRAQESLASvgqqlevarqgqq 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  382 --SEETADLLAEKAQITEEEAKLLAQKAAEAEQEM-QRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERrakeADQ 458
Cdd:pfam07111 556 esTEEAASLRQELTQQQEIYGQALQEKVAEVETRLrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER----NQE 631

                         170       180
                  ....*....|....*....|...
gi 148708550  459 LKQDLQEAREAE-RRAKQKLLEI 480
Cdd:pfam07111 632 LRRLQDEARKEEgQRLARRVQEL 654
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
328-480 5.76e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 328 AQAREEKARKQMERQRLAREKQMREEA-ERTRD--ELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLa 404
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERlERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL- 549

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148708550 405 qkaaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 480
Cdd:PRK02224 550 ----EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 35-107 6.19e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 7 (FRMD7); FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. It interacts with the Rho GTPase regulator, RhoGDIalpha, and activates the Rho subfamily member Rac1, which regulates reorganization of actin filaments and controls neuronal outgrowth. Mutations in the FRMD7 gene are responsible for the X-linked idiopathic congenital nystagmus (ICN), a disease which affects ocular motor control. FRMD7 contains a FERM domain, and a pleckstrin homology (PH) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340708  Cd Length: 86  Bit Score: 39.02  E-value: 6.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148708550  35 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQY-TIKDTVAWLKMDKKVLDHdVSKEEPVTFHFLAKFYP 107
Cdd:cd17188   11 DSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFrNHAGNNVWLELLKPITKQ-IKNPKELIFKFTVKFFP 83
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 321-481 6.32e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   321 LEVQQMKAQAREEKARKQMERQRLAREKQMRE--EAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEE 398
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   399 EAKLLAQKAAEAEQEMQRIKATAIRTEEE----KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 474
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486


                   ....*..
gi 148708550   475 QKLLEIA 481
Cdd:TIGR02169  487 KLQRELA 493
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 30-107 6.82e-04

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


Pssm-ID: 340723  Cd Length: 84  Bit Score: 38.77  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  30 RIVTMDAEmEFNCEM--KWKGKDLFDLVCRTLGLRETWFFGLQY-TIKDTVAWLKMDKKVLDHdvSKEEPVTFHFLAKFY 106
Cdd:cd17203    5 KVTLLDGS-EYTCEVekRSKGQVLFDKVCEHLNLLEKDYFGLTYrDSENQKNWLDPAKEIKKQ--IRSGAWQFSFNVKFY 81


                 .
gi 148708550 107 P 107
Cdd:cd17203   82 P 82
Rabaptin pfam03528
Rabaptin;
326-475 6.86e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 42.40  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  326 MKAQAREEKAR--KQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEaLMRSEETADLLAEKAQITEEEAKLL 403
Cdd:pfam03528 113 MKETVREYEVQfhRRLEQER-AQWNQYRESAEREIADLRRRLSEGQEEENLEDE-MKKAQEDAEKLRSVVMPMEKEIAAL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  404 AQKAAEAEQEMQRIKATAIRT-----EEEKRLMEQKVLEAEVLALK---MAEESERRAKEADQLKQDLQEAREAERRAKQ 475
Cdd:pfam03528 191 KAKLTEAEDKIKELEASKMKElnhylEAEKSCRTDLEMYVAVLNTQksvLQEDAEKLRKELHEVCHLLEQERQQHNQLKH 270
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 315-573 8.63e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.65  E-value: 8.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   315 RRKADSLEVQQMKAQAREEKARKQMERQRLA--REKQMREEAERTRDELERRLLQMKEEATMANEalMRSEETADLLAEK 392
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLaqVLKENKEEEKEKKLQEEELKLLAKEEEELKSE--LLKLERRKVDDEE 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   393 AQITEEEAKLLAQKAAEAEQEmqrIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERR 472
Cdd:pfam02463  315 KLKESEKEKKKAEKELKKEKE---EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   473 AKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 552
Cdd:pfam02463  392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471

                          250       260
                   ....*....|....*....|.
gi 148708550   553 ALKLKERETALDVLHSESSDR 573
Cdd:pfam02463  472 DLLKETQLVKLQEQLELLLSR 492
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
294-473 9.29e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  294 KLRVNKLILQLCIGNHDLFMRRRKADSL--EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTR--------DELER 363
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQRRLELLeaELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLER 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  364 RLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMqrikatairtEEEKRLMEQKVLEAEVLAL 443
Cdd:COG4913   346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL----------EEELEALEEALAEAEAALR 415

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 148708550  444 KMAEESERRAKEADQLKQ-------DLQEAREAERRA 473
Cdd:COG4913   416 DLRRELRELEAEIASLERrksnipaRLLALRDALAEA 452
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 334-425 9.71e-04

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.73  E-value: 9.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 334 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 412
Cdd:cd06503   29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106

                         90
                 ....*....|...
gi 148708550 413 EMQRIKAtAIRTE 425
Cdd:cd06503  107 EKEKALA-ELRKE 118
growth_prot_Scy NF041483
polarized growth protein Scy;
338-479 9.86e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  338 QMERQRLARE-KQMREEA----ERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAA--- 408
Cdd:NF041483  439 QEEARRLRGEaEQLRAEAvaegERIRGEARREAVQQIEEaARTAEELLTKAKADADELRSTATAESERVRTEAIERAttl 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  409 --EAEQEMQRIKATA--IRTEEEKRLMEQKVlEAEVLALKMAEESE-----RRAKEADQLKQDLQEAREAERRAKQKLLE 479
Cdd:NF041483  519 rrQAEETLERTRAEAerLRAEAEEQAEEVRA-AAERAARELREETEraiaaRQAEAAEELTRLHTEAEERLTAAEEALAD 597
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
308-483 1.55e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 41.12  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 308 NHDLFMRRRKAdslevqqmkAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAT--MANEALMRSEET 385
Cdd:PRK07735   4 EKDLEDLKKEA---------ARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 386 ADLLAEKAQITEEEAKLLAQKAAEAEQemqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQE 465
Cdd:PRK07735  75 AKQKREGTEEVTEEEKAKAKAKAAAAA-----KAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREG 149

                        170
                 ....*....|....*...
gi 148708550 466 AREAERRAKQKLLEIATK 483
Cdd:PRK07735 150 TEEVTEEEEETDKEKAKA 167
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 313-471 1.58e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  313 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRseETADLLAEK 392
Cdd:pfam13868  30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ--EREQMDEIV 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148708550  393 AQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 471
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 316-469 1.61e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.14  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  316 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERtrdelerrllqMKEEATMANEALMRSEETADLLAEKAQI 395
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK-----------QQEAKNLPKPADTSSPKEDKQVAENQKR 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148708550  396 TEEEAKLLAQKAAEAEQEMQRIKATAIRTE--EEKRLMEQKVLEAEVLALKMAEESERRAKEAD-QLKQDLQEAREA 469
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQEskASEKEAEDKELEAQKKREPVAEDLQKTKPQVEaQPTSLNEDAIDS 358
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 315-563 2.33e-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: 41.21  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   315 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMR---------------------------EEAERTRDELERRLLQ 367
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqallkekreyegyellkekealerqkEAIERQLASLEEELEK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   368 MKEEATMANEALMRSEETADLLAEKAQ-ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVL----- 441
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkll 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   442 --ALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDM 519
Cdd:TIGR02169  336 aeIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 148708550   520 KRLSMEIEKEKveymEKSKHLQEQLNELKTEIE--ALKLKERETAL 563
Cdd:TIGR02169  416 QRLSEELADLN----AAIAGIEAKINELEEEKEdkALEIKKQEWKL 457
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
330-473 2.54e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  330 AREEKARKQMERQRLAREkqmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKL------- 402
Cdd:COG4913   608 NRAKLAALEAELAELEEE---LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerldass 684

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148708550  403 -----LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLalkmAEESERRAKEADQLKQDLQEAREAERRA 473
Cdd:COG4913   685 ddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFA 756
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 28-106 2.81e-03

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


Pssm-ID: 340725  Cd Length: 86  Bit Score: 37.33  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  28 TVRIVTMDA-EMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVlDHDVSKEEPVTFHFLAKF 105
Cdd:cd17205    4 TCRVSLLDGtDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAhWLDVTKSI-KKQVKIGPPYCLHLRVKF 82


                 .
gi 148708550 106 Y 106
Cdd:cd17205   83 Y 83
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 312-372 3.19e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.24  E-value: 3.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148708550 312 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 372
Cdd:PLN03086   3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 338-480 3.30e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  338 QMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQemqri 417
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQ----- 401

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148708550  418 kataiRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 480
Cdd:pfam15709 402 -----RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEM 459
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 318-450 3.34e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 318 ADSLEVQQMKAQArEEKARKQmeRQRLAREKQMREEAERTRDELERRLLQMKEEatmanEALMRSEetadlLAEKAQITE 397
Cdd:PRK00409 513 EDKEKLNELIASL-EELEREL--EQKAEEAEALLKEAEKLKEELEEKKEKLQEE-----EDKLLEE-----AEKEAQQAI 579

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148708550 398 EEAKLLAQKAAEAEQEMQRIKATAIR---TEEEKRLMEQKVLEAEVLALKMAEESE 450
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKaheLIEARKRLNKANEKKEKKKKKQKEKQE 635
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 315-483 3.34e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   315 RRKADSLEVQQMKAQAREEKARKQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 394
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELS-EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   395 ITEEEAKLLAQKAAEAEQEMQRikatairteEEKRLMEQKVLEAEV--LALKMAEESERRAKEADQLKQDLQEAREAERR 472
Cdd:TIGR02168  951 LTLEEAEALENKIEDDEEEARR---------RLKRLENKIKELGPVnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021

                          170
                   ....*....|.
gi 148708550   473 AKQKLLEIATK 483
Cdd:TIGR02168 1022 AIEEIDREARE 1032
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 331-480 3.42e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   331 REEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQI--TEEEAKLLAQKA 407
Cdd:TIGR00618  368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLAHAKKQQelQQRYAELCAAAI 447

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148708550   408 AEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 480
Cdd:TIGR00618  448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 311-573 3.93e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   311 LFMRRRKADSLEVQQMKAQAREEK--ARKQMERQRLARE-KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETAD 387
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAERYKELkaELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   388 LLAEkaqiteeeaklLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAR 467
Cdd:TIGR02168  275 EVSE-----------LEEEIEELQKELYALANEISRLEQQKQILRERLANLE-------RQLEELEAQLEELESKLDELA 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550   468 EAERRAKQKLLEIATKPT-----YPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTdmkRLSMEIEKEKVEYMEKSK-HLQ 541
Cdd:TIGR02168  337 EELAELEEKLEELKEELEsleaeLEELEAELEELESRLEELEEQLETLRSKVAQL---ELQIASLNNEIERLEARLeRLE 413

                          250       260       270
                   ....*....|....*....|....*....|..
gi 148708550   542 EQLNELKTEIEALKLKERETALDVLHSESSDR 573
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAELKELQAELEEL 445
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 319-461 4.32e-03

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


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 39.71  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  319 DSLEVQQMKAQAREEKARKQMERQR-----LAREKQMREEAERTRDELERRLLQMKEEATMANEAL-----------MRS 382
Cdd:pfam00529  61 DSAEAQLAKAQAQVARLQAELDRLQaleseLAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLarrrvlapiggISR 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  383 EEtadLLAEKAQITEEEAKLLAqkaaeAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEvlaLKMAEESERRAKEADQLKQ 461
Cdd:pfam00529 141 ES---LVTAGALVAQAQANLLA-----TVAQLDQIYVQITQSAAEnQAEVRSELSGAQ---LQIAEAEAELKLAKLDLER 209
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
319-480 4.53e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 319 DSLEVQQMKAQAREEKARKQMERQRLARE------------KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETA 386
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREeletleaeiedlRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 387 DLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEE-KRLMEQkvleaevlALKMAEESERRAKEADQLKQDLQE 465
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaESLRED--------ADDLEERAEELREEAAELESELEE 374

                        170
                 ....*....|....*
gi 148708550 466 AREAERRAKQKLLEI 480
Cdd:PRK02224 375 AREAVEDRREEIEEL 389
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
322-564 4.59e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 322 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 401
Cdd:COG4372   46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 402 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALKMAEESERRAKEADQLKQDLQEAREA----ERRAKQ 475
Cdd:COG4372  126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLesLQEELAALEQELQALSEAEAEQALDELLKEANRNaekeEELAEA 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 476 KLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 555
Cdd:COG4372  206 EKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285


                 ....*....
gi 148708550 556 LKERETALD 564
Cdd:COG4372  286 EALEEAALE 294
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 327-468 5.01e-03

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


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 38.86  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  327 KAQAREEKARkQMERQrLAREKQMREEAERTRDELERRLlqmkeeaTMANEALMRSEETADLLAEKAQITEEEAKLLAQK 406
Cdd:pfam00261  86 RALKDEEKME-ILEAQ-LKEAKEIAEEADRKYEEVARKL-------VVVEGDLERAEERAELAESKIVELEEELKVVGNN 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148708550  407 AAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalKMAEESERRA----KEADQLKQDLQEARE 468
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAE----TRAEFAERSVqkleKEVDRLEDELEAEKE 218
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 330-461 6.05e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  330 AREEKARKQMER--QRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLaeKAQITEEEAK----LL 403
Cdd:COG3096   529 RQQQNAERLLEEfcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL--RARIKELAARapawLA 606

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  404 AQKAAE--AEQEMQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQ 461
Cdd:COG3096   607 AQDALErlREQSGEALADSQEVTAAMQQLLERER-EATVERDELAARKQALESQIERLSQ 665
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
315-480 6.13e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  315 RRKADSLEVQQMKAQAREEKARKQME--RQRLAREKQMRE---------EAERTRDELERRLlqmkEEATMANEALMRSE 383
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDalQERREALQRLAEyswdeidvaSAEREIAELEAEL----ERLDASSDDLAALE 691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  384 ETADLL-AEKAQITEEEAKL------LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLAlkmAEESERRAKEA 456
Cdd:COG4913   692 EQLEELeAELEELEEELDELkgeigrLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA---ALGDAVERELR 768

                         170       180
                  ....*....|....*....|....
gi 148708550  457 DQLKQDLQEAREAERRAKQKLLEI 480
Cdd:COG4913   769 ENLEERIDALRARLNRAEEELERA 792
growth_prot_Scy NF041483
polarized growth protein Scy;
326-471 6.28e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.81  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  326 MKAQARE--EKARKQMERQRlareKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAqiTEEEAKL- 402
Cdd:NF041483  518 LRRQAEEtlERTRAEAERLR----AEAEEQAEEVRAAAERAARELREETERAIAA--RQAEAAEELTRLH--TEAEERLt 589

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  403 -----LAQKAAEAE-------QEMQRIKATAirTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDL--QEARE 468
Cdd:NF041483  590 aaeeaLADARAEAErirreaaEETERLRTEA--AERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLrsEAAAE 667


                  ...
gi 148708550  469 AER 471
Cdd:NF041483  668 AER 670
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 334-423 6.50e-03

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


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 37.46  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 334 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAtmaneALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQE 413
Cdd:COG0711   30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEA-----AEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAE 104

                         90
                 ....*....|
gi 148708550 414 MQRIKATAIR 423
Cdd:COG0711  105 IEQERAKALA 114
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 319-479 7.56e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 39.22  E-value: 7.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  319 DSLEVQQMKAQAREEKARKQMERQRLAREKQMR-EEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITE 397
Cdd:pfam05262 175 DSISDKKVVEALREDNEKGVNFRRDMTDLKEREsQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  398 EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVL------ALKMAEESERRAKEADQLKQDLQEAREAER 471
Cdd:pfam05262 255 QEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALkakdhkAFDLKQESKASEKEAEDKELEAQKKREPVA 334


                  ....*...
gi 148708550  472 RAKQKLLE 479
Cdd:pfam05262 335 EDLQKTKP 342
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 313-479 7.86e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.75  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  313 MRRRKADSLEVQQMKAQAREEKARKQMERQR-LAREKQMREEAERTRDELERRLLQMKEEATMANEALMrseetaDLLAE 391
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEkLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL------EYLKE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  392 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQ---KVLEAEVLA---LKMAEESERRAKEADQLKQDLQE 465
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDElraKLYQEEQERkerQKEREEAEKKARQRQELQQAREE 243

                         170
                  ....*....|....
gi 148708550  466 AREAERRAKQKLLE 479
Cdd:pfam13868 244 QIELKERRLAEEAE 257
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 313-424 8.22e-03

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.33  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  313 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEK 392
Cdd:pfam05672  35 LEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEA 114

                          90       100       110
                  ....*....|....*....|....*....|..
gi 148708550  393 AQITEEEAKLLAQKAAEAEQEMQRIKATAIRT 424
Cdd:pfam05672 115 ERQRQEREKIMQQEEQERLERKKRIEEIMKRT 146
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 342-484 8.46e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 38.67  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  342 QRLAREKQMREEAERTRDELERRLLQMKEEATmanealmrseetADLLAEKAQITEEEAKLLAQKAA-EAEQEMQRIKat 420
Cdd:TIGR02794  50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAE------------KQRAAEQARQKELEQRAAAEKAAkQAEQAAKQAE-- 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148708550  421 airtEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKP 484
Cdd:TIGR02794 116 ----EKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA 175
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 330-419 8.59e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 37.06  E-value: 8.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 330 AREEKARKQME---RQRLAREKQMREEAERTRDELERRLLQMKEEAtmanealmrseetadllaeKAQITEEEAKLLAQK 406
Cdd:PRK05759  45 AAAERAKKELElaqAKYEAQLAEARAEAAEIIEQAKKRAAQIIEEA-------------------KAEAEAEAARIKAQA 105

                         90
                 ....*....|...
gi 148708550 407 AAEAEQEMQRIKA 419
Cdd:PRK05759 106 QAEIEQERKRARE 118
Caldesmon pfam02029
Caldesmon;
314-480 8.63e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.08  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQM--------------KEEATMANEAL 379
Cdd:pfam02029 168 EVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTtkrrqgglsqsqerEEEAEVFLEAE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  380 MRSEETADLLAEKAqitEEEAKLLAQKAAEAEQEMQRIKataiRTEEEKRlmeqKVLEAEVLALKmAEESERRAKEAD-- 457
Cdd:pfam02029 248 QKLEELRRRRQEKE---SEEFEKLRQKQQEAELELEELK----KKREERR----KLLEEEEQRRK-QEEAERKLREEEek 315

                         170       180
                  ....*....|....*....|....*.
gi 148708550  458 -QLKQDLQEAR--EAERRakQKLLEI 480
Cdd:pfam02029 316 rRMKEEIERRRaeAAEKR--QKLPED 339
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 313-414 8.84e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 313 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKqmrEEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEK 392
Cdd:COG3883  135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211

                         90       100
                 ....*....|....*....|..
gi 148708550 393 AQITEEEAKLLAQKAAEAEQEM 414
Cdd:COG3883  212 AAAAAAAAAAAAAAAAAAAAAA 233
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 314-417 9.52e-03

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


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 37.71  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550  314 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 393
Cdd:pfam09756   1 KKLGAKKRAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEKLKS 80

                          90       100
                  ....*....|....*....|....
gi 148708550  394 QITEEEAKLLAQKAAEAEQEMQRI 417
Cdd:pfam09756  81 QFVVEEEGTDKLSAEDESQLLEDF 104
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
321-470 9.56e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 9.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 321 LEVQQMKAQAREEKARKQMERQRLA----REKQMREEAERTRDELERRLLQMKEEATMANEALMRseetadLLAEKAQIT 396
Cdd:COG3206  231 ARAELAEAEARLAALRAQLGSGPDAlpelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA------LRAQIAALR 304

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148708550 397 EEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAE-ESERRAKEA--DQLKQDLQEAREAE 470
Cdd:COG3206  305 AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEVARElyESLLQRLEEARLAE 381
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 364-476 9.72e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.63  E-value: 9.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148708550 364 RLLQMKEEATMANEALMRSEET-ADLLAEKAQITEEEAKLLAQKAaEAEQEMQRIKATAIR--TEEEKRLMEQKVLEAEV 440
Cdd:PRK09510  66 RQQQQQKSAKRAEEQRKKKEQQqAEELQQKQAAEQERLKQLEKER-LAAQEQKKQAEEAAKqaALKQKQAEEAAAKAAAA 144

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 148708550 441 LALKMAEESERRAKEADQLKQDLQEAREAERRAKQK 476
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAA 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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