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Conserved domains on  [gi|1371986040|ref|NP_001348604|]
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merlin isoform 5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 175-271 1.65e-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: 1.65e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 175 MYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 254
Cdd:cd13194     1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                          90
                  ....*....|....*..
gi 1371986040 255 ILQLCIGNHDLFMRRRK 271
Cdd:cd13194    81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 23-181 7.42e-42

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: 148.98  E-value: 7.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040   23 TVRIVTMDAEM-EFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVKKQ--------------- 84
Cdd:smart00295   1 VLKVYLLDGTTlEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQdvksepltlyfrvkf 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040   85 -------------------------ILDEKVYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINlyQM 138
Cdd:smart00295  81 yppdpnqlkedptrlnllylqvrndILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD--SR 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1371986040  139 TPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 181
Cdd:smart00295 159 KLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 477-555 2.59e-23

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: 93.42  E-value: 2.59e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371986040 477 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGgpSSKHNTIKKLTLQSAKSRVAFFEEL 555
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQG--RDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 305-424 7.51e-23

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: 93.83  E-value: 7.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 305 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 384
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1371986040 385 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 424
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
PLN03086 super family cl29366
PRLI-interacting factor K; Provisional
 266-326 2.77e-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: 40.63  E-value: 2.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371986040 266 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 326
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 ...
 175-271 1.65e-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: 1.65e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 175 MYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 254
Cdd:cd13194     1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                          90
                  ....*....|....*..
gi 1371986040 255 ILQLCIGNHDLFMRRRK 271
Cdd:cd13194    81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 23-181 7.42e-42

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: 148.98  E-value: 7.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040   23 TVRIVTMDAEM-EFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVKKQ--------------- 84
Cdd:smart00295   1 VLKVYLLDGTTlEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQdvksepltlyfrvkf 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040   85 -------------------------ILDEKVYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINlyQM 138
Cdd:smart00295  81 yppdpnqlkedptrlnllylqvrndILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD--SR 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1371986040  139 TPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 181
Cdd:smart00295 159 KLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 20-84 5.55e-37

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: 131.74  E-value: 5.55e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371986040  20 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVKKQ 84
Cdd:cd17186     1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQ 66
FERM_C pfam09380
FERM C-terminal PH-like domain;
185-270 1.03e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.18  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 185 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 263
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 1371986040 264 DLFMRRR 270
Cdd:pfam09380  79 TFFRLRR 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 81-181 8.74e-27

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 104.66  E-value: 8.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  81 VKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWEERITAWYAEHRGRARD 160
Cdd:pfam00373  19 AKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELEKRVLEAHKNLRGLSAE 96

                          90       100
                  ....*....|....*....|.
gi 1371986040 161 EAEMEYLKIAQDLEMYGVNYF 181
Cdd:pfam00373  97 EAKLKYLQIAQSLPTYGVEFF 117
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 477-555 2.59e-23

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: 93.42  E-value: 2.59e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371986040 477 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGgpSSKHNTIKKLTLQSAKSRVAFFEEL 555
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQG--RDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 305-424 7.51e-23

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: 93.83  E-value: 7.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 305 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 384
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1371986040 385 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 424
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 269-435 1.61e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 269 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 348
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 349 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 428
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                  ....*..
gi 1371986040 429 QKLLEIA 435
Cdd:COG1196   435 EEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-517 1.48e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.74  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 276 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 355
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 356 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 435
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 436 TKPTYPPMNPIPPPLPPDIPSFDIIADslsfdfkDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERET 515
Cdd:COG1196   400 AQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472


                  ..
gi 1371986040 516 AL 517
Cdd:COG1196   473 AL 474
PTZ00121 PTZ00121
MAEBL; Provisional
 269-539 1.72e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.01  E-value: 1.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQARE----EKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 341
Cdd:PTZ00121  1277 ARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAA 1356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  342 LLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEADQLKQDLQEAR 421
Cdd:PTZ00121  1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAEEKKKAD 1434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  422 EAERRA--KQKLLEIATKPTYPPMNPIPPPLPPDIPSfdiiADSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLN 499
Cdd:PTZ00121  1435 EAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAK---KKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1371986040  500 ELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKK 539
Cdd:PTZ00121  1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 277-437 7.11e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 60.98  E-value: 7.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 277 VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKL 356
Cdd:PRK09510   61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAK 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 357 LAQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 435
Cdd:PRK09510  141 AAAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215


                  ..
gi 1371986040 436 TK 437
Cdd:PRK09510  216 KK 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-508 2.75e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  276 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 355
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  356 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 435
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  436 TKPTYPPMNPIPPPLPPDIPSFDI---------IADSLSFDFKDTdmkrlSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 506
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLeglevridnLQERLSEEYSLT-----LEEAEALENKIEDDEEEARRRLKRLENKIK 982


                   ..
gi 1371986040  507 AL 508
Cdd:TIGR02168  983 EL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 261-514 9.65e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 9.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  261 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 333
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  334 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 407
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  408 KEADQLKQDLQEAREAERRAKQKLLEIA----------TKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKrls 477
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIEslaaeieeleELIEELESELEALLNERASLEEALALLRSELEELSEELR--- 904

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1371986040  478 mEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 514
Cdd:TIGR02168  905 -ELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
growth_prot_Scy NF041483
polarized growth protein Scy;
271-424 4.41e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 46.74  E-value: 4.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  271 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 350
Cdd:NF041483   490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  351 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRL------MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 424
Cdd:NF041483   560 EETERAIAARQAEAAEELTR-----LHTEAEERLtaaeeaLADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
growth_prot_Scy NF041483
polarized growth protein Scy;
276-437 7.24e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 45.97  E-value: 7.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  276 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 355
Cdd:NF041483   583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  356 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 430
Cdd:NF041483   660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                   ....*..
gi 1371986040  431 LLEIATK 437
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 ...
 288-373 1.90e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 288 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 366
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106


                  ....*..
gi 1371986040 367 EMQRIKA 373
Cdd:cd06503   107 EKEKALA 113
growth_prot_Scy NF041483
polarized growth protein Scy;
292-433 2.57e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  292 QMERQRLARE-KQMREEA----ERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAA--- 362
Cdd:NF041483   439 QEEARRLRGEaEQLRAEAvaegERIRGEARREAVQQIEEaARTAEELLTKAKADADELRSTATAESERVRTEAIERAttl 518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  363 --EAEQEMQRIKATA--IRTEEEKRLMEQKVlEAEVLALKMAEESE-----RRAKEADQLKQDLQEAREAERRAKQKLLE 433
Cdd:NF041483   519 rrQAEETLERTRAEAerLRAEAEEQAEEVRA-AAERAARELREETEraiaaRQAEAAEELTRLHTEAEERLTAAEEALAD 597
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 266-326 2.77e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.63  E-value: 2.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371986040 266 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 326
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 ...
 175-271 1.65e-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: 1.65e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 175 MYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 254
Cdd:cd13194     1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                          90
                  ....*....|....*..
gi 1371986040 255 ILQLCIGNHDLFMRRRK 271
Cdd:cd13194    81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 23-181 7.42e-42

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: 148.98  E-value: 7.42e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040   23 TVRIVTMDAEM-EFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVKKQ--------------- 84
Cdd:smart00295   1 VLKVYLLDGTTlEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQdvksepltlyfrvkf 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040   85 -------------------------ILDEKVYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINlyQM 138
Cdd:smart00295  81 yppdpnqlkedptrlnllylqvrndILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD--SR 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1371986040  139 TPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 181
Cdd:smart00295 159 KLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 20-84 5.55e-37

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: 131.74  E-value: 5.55e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371986040  20 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVKKQ 84
Cdd:cd17186     1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQ 66
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 22-89 7.10e-31

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: 115.07  E-value: 7.10e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371986040  22 FTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKD-TVAWLKMDKKVKKQILDEK 89
Cdd:cd17097     1 INVRVTTMDAELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKgRVAWLKPDKKVLTQDVSKN 69
FERM_C pfam09380
FERM C-terminal PH-like domain;
185-270 1.03e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.18  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 185 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 263
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 1371986040 264 DLFMRRR 270
Cdd:pfam09380  79 TFFRLRR 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 81-181 8.74e-27

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 104.66  E-value: 8.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  81 VKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWEERITAWYAEHRGRARD 160
Cdd:pfam00373  19 AKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELEKRVLEAHKNLRGLSAE 96

                          90       100
                  ....*....|....*....|.
gi 1371986040 161 EAEMEYLKIAQDLEMYGVNYF 181
Cdd:pfam00373  97 EAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 81-173 1.04e-24

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: 98.47  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  81 VKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWEERITAWYAEHRGRARD 160
Cdd:cd14473     9 VKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLK--QRKPEEWEKRIVELHKKLRGLSPA 86

                          90
                  ....*....|...
gi 1371986040 161 EAEMEYLKIAQDL 173
Cdd:cd14473    87 EAKLKYLKIARKL 99
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 477-555 2.59e-23

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: 93.42  E-value: 2.59e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371986040 477 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGgpSSKHNTIKKLTLQSAKSRVAFFEEL 555
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQG--RDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 305-424 7.51e-23

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: 93.83  E-value: 7.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 305 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 384
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1371986040 385 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 424
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 23-84 4.29e-20

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: 84.83  E-value: 4.29e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371986040  23 TVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVKKQ 84
Cdd:cd17187     2 NVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVdSKGYSTWLKLNKKVLSQ 64
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 20-84 2.26e-17

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: 76.95  E-value: 2.26e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371986040  20 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVKKQ 84
Cdd:cd17239     1 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVdNKGFPTWLKLDKKVSAQ 66
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 177-267 3.00e-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: 3.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 177 GVNYFTIRNK--KGTELLLGVDALGLHIYDPENRlTPKISFPWNEIRNISYS-DKEFTIKPLDK-KIDVFKFNSSKlRVN 252
Cdd:cd00836     1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEdKQSKLLFQTPS-RQA 78

                          90
                  ....*....|....*
gi 1371986040 253 KLILQLCIGNHDLFM 267
Cdd:cd00836    79 KEIWKLIVGYHRFLL 93
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 21-84 2.43e-15

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: 71.31  E-value: 2.43e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371986040  21 TFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYtiKDTVA---WLKMDKKVKKQ 84
Cdd:cd17237     1 TISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQY--QDTKGfstWLKLNKKVTAQ 65
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 24-84 4.85e-15

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: 70.54  E-value: 4.85e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371986040  24 VRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVKKQ 84
Cdd:cd17238     3 VRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVdSKGYSTWLKLNKKVTQQ 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 269-435 1.61e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 269 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 348
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 349 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 428
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                  ....*..
gi 1371986040 429 QKLLEIA 435
Cdd:COG1196   435 EEEEEEE 441
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 22-91 4.49e-14

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: 67.61  E-value: 4.49e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371986040  22 FTVRIVTMD-AEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVKKQILDEKVY 91
Cdd:cd01765     1 ISCRVRLLDgTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKhWLDLDKKISKQLKRSGPY 72
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 177-272 1.55e-13

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


Pssm-ID: 270012  Cd Length: 113  Bit Score: 66.99  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 177 GVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKK--------------IDVF 242
Cdd:cd13191     1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRrnshrsrrtfqsssVSVH 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1371986040 243 KFNSSKLRVNKLILQLCIGNHDLFMRRRKA 272
Cdd:cd13191    81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQS 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 276-517 1.48e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.74  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 276 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 355
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 356 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 435
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 436 TKPTYPPMNPIPPPLPPDIPSFDIIADslsfdfkDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERET 515
Cdd:COG1196   400 AQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472


                  ..
gi 1371986040 516 AL 517
Cdd:COG1196   473 AL 474
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 26-85 3.98e-12

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: 61.45  E-value: 3.98e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371986040  26 IVTMDA-EMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVKKQI 85
Cdd:pfam09379   1 VRLLDGtVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLdDNGEHRWLDLSKRLSKQA 62
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 268-437 4.72e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 4.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 347
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 348 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 427
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                         170
                  ....*....|
gi 1371986040 428 KQKLLEIATK 437
Cdd:COG1196   469 LEEAALLEAA 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 264-524 1.60e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 264 DLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 343
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 344 AEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREA 423
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 424 ERRAKQKLLEIATkptyPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKT 503
Cdd:COG1196   395 AAELAAQLEELEE----AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                         250       260
                  ....*....|....*....|.
gi 1371986040 504 EIEALKLKERETALDVLHSES 524
Cdd:COG1196   471 EAALLEAALAELLEELAEAAA 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 268-437 3.82e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 347
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 348 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 427
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         170
                  ....*....|
gi 1371986040 428 KQKLLEIATK 437
Cdd:COG1196   483 LEELAEAAAR 492
PTZ00121 PTZ00121
MAEBL; Provisional
 269-539 1.72e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.01  E-value: 1.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQARE----EKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 341
Cdd:PTZ00121  1277 ARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAA 1356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  342 LLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEADQLKQDLQEAR 421
Cdd:PTZ00121  1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAEEKKKAD 1434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  422 EAERRA--KQKLLEIATKPTYPPMNPIPPPLPPDIPSfdiiADSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLN 499
Cdd:PTZ00121  1435 EAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAK---KKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1371986040  500 ELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKK 539
Cdd:PTZ00121  1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 270-516 5.39e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 270 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQI 349
Cdd:COG1196   213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 350 TEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQ 429
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 430 KLLEIATKptyppmnpippPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 509
Cdd:COG1196   373 ELAEAEEE-----------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441


                  ....*..
gi 1371986040 510 LKERETA 516
Cdd:COG1196   442 EALEEAA 448
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 277-437 7.11e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 60.98  E-value: 7.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 277 VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKL 356
Cdd:PRK09510   61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAK 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 357 LAQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 435
Cdd:PRK09510  141 AAAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215


                  ..
gi 1371986040 436 TK 437
Cdd:PRK09510  216 KK 217
PTZ00121 PTZ00121
MAEBL; Provisional
 269-514 1.80e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-EATMANEALMRSEETADLLAEKA 347
Cdd:PTZ00121  1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEA 1612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  348 QiTEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESeRRAKEADQLKQDLQEAREAERRA 427
Cdd:PTZ00121  1613 K-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-KKAEEDKKKAEEAKKAEEDEKKA 1690

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  428 KQKLLEIATKPTYPPMNPIppplppdipsfdiiadslsfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEA 507
Cdd:PTZ00121  1691 AEALKKEAEEAKKAEELKK----------------------KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748


                   ....*..
gi 1371986040  508 LKLKERE 514
Cdd:PTZ00121  1749 AKKDEEE 1755
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 22-85 3.61e-09

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


Pssm-ID: 340619  Cd Length: 85  Bit Score: 53.77  E-value: 3.61e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371986040  22 FTVRIVTMDAE-MEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVKKQI 85
Cdd:cd17099     4 FVVRIQLLDNTvLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLrWVDLEKPLKKQL 69
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 30-89 9.80e-09

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


Pssm-ID: 340618  Cd Length: 85  Bit Score: 52.60  E-value: 9.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371986040  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVKKQILDEK 89
Cdd:cd17098    10 DTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTdPEGNKCWLDPEKPILRQVKRPK 70
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 268-435 1.08e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.51  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 347
Cdd:PRK09510   81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 348 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA--REAER 425
Cdd:PRK09510  161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEakAAAEK 240

                         170
                  ....*....|
gi 1371986040 426 RAKQKLLEIA 435
Cdd:PRK09510  241 AAAAKAAEKA 250
PTZ00121 PTZ00121
MAEBL; Provisional
 269-514 1.12e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.23  E-value: 1.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQAREEkARKQMERQRLAREKQMREEAERTRDELERRllqmKEEATMANEALMRSEEtADLLAEKAQ 348
Cdd:PTZ00121  1430 KKKADEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKADEAKKKAEE-AKKKADEAK 1503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  349 ITEEEAKLL--------AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 420
Cdd:PTZ00121  1504 KAAEAKKKAdeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  421 REAERRAKQKLLEIAtkPTYPPMNPIPPPLPPDIPSFDIIADSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNE 500
Cdd:PTZ00121  1584 EEAKKAEEARIEEVM--KLYEEEKKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          250
                   ....*....|....
gi 1371986040  501 LKTEIEALKLKERE 514
Cdd:PTZ00121  1659 NKIKAAEEAKKAEE 1672
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 175-266 1.48e-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: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 175 MYGVNYFTIRNKKGTELLLGVDALGLHIYdpENRLtpKIS-FPWNEIRNISYSDKEFTI----KPLDKKIDVFKFNSSKL 249
Cdd:cd13189     1 LYGVELHSARDSNNLELQIGVSSAGILVF--QNGI--RINtFPWSKIVKISFKRKQFFIqlrrEPNESRDTILGFNMLSY 76

                          90
                  ....*....|....*..
gi 1371986040 250 RVNKLILQLCIGNHDLF 266
Cdd:cd13189    77 RACKNLWKSCVEHHTFF 93
RA_FERM_F0_F1_like cd01768
Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 ...
 24-90 2.45e-08

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: 52.17  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  24 VRIVTM-----DAEMEFNCEMKWKGKDLFDLVCRTLGLR-----------ETWFFGLQYTIKDTVA-------------- 73
Cdd:cd01768     2 LKIFGAglasgANYKSVLATARSTARELVAEALERYGLAgspgggpgessCVDAFALCDALGRPAAagvgsgewraehlr 81

                          90
                  ....*....|....*..
gi 1371986040  74 WLKMDKKVKKQILDEKV 90
Cdd:cd01768    82 VLGDSERPLLVQELWRA 98
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-508 2.75e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  276 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 355
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  356 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 435
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  436 TKPTYPPMNPIPPPLPPDIPSFDI---------IADSLSFDFKDTdmkrlSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 506
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLeglevridnLQERLSEEYSLT-----LEEAEALENKIEDDEEEARRRLKRLENKIK 982


                   ..
gi 1371986040  507 AL 508
Cdd:TIGR02168  983 EL 984
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 267-437 3.25e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 55.97  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 267 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMRSEETADLLAEK 346
Cdd:PRK09510   67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEEAAKQAALKQKQAEEAAAKAAAA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 347 AQI-TEEEAKLLAQKAAEAEQEMqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 425
Cdd:PRK09510  145 AKAkAEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA 221

                         170
                  ....*....|..
gi 1371986040 426 RAKQKLLEIATK 437
Cdd:PRK09510  222 EAKAAAAKAAAE 233
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 176-266 6.48e-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: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 176 YGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK-------PLDKKIDvFKFNSSk 248
Cdd:cd13184     1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRIN---RFAWPKVLKISYKRNNFYIKirpgefeQYETTIG-FKLPNH- 75

                          90
                  ....*....|....*...
gi 1371986040 249 lRVNKLILQLCIGNHDLF 266
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 ...
 162-241 8.82e-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: 8.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 162 AEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTI---KPLDKK 238
Cdd:cd13192     1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFILhvmQKEEKK 77


                  ...
gi 1371986040 239 IDV 241
Cdd:cd13192    78 HTL 80
PTZ00121 PTZ00121
MAEBL; Provisional
 269-514 1.29e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEvQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR---------LLQMKEEATMANEALMRSEET 339
Cdd:PTZ00121  1404 KKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeeakkaeeAKKKAEEAKKADEAKKKAEEA 1482

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  340 ADllAEKAQITEEEAKLLAQKAAEAEQEMQriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRaKEADQLKQdLQE 419
Cdd:PTZ00121  1483 KK--ADEAKKKAEEAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK-KKADELKK-AEE 1556

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  420 AREAE--RRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRlsMEIEKEKVEYMEKSKHLQEQ 497
Cdd:PTZ00121  1557 LKKAEekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKK 1634

                          250
                   ....*....|....*..
gi 1371986040  498 LNELKTEIEALKLKERE 514
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEE 1651
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 32-70 1.84e-07

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: 49.09  E-value: 1.84e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1371986040  32 EMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYtIKD 70
Cdd:cd17101    13 RLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAV-LKD 50
PTZ00121 PTZ00121
MAEBL; Provisional
 264-527 2.39e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  264 DLFMRRRKADSL---EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR-----LLQMKEEATMANEALMR 335
Cdd:PTZ00121  1575 DKNMALRKAEEAkkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkveqLKKKEAEEKKKAEELKK 1654

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  336 SEETADLLAEKAQITEEEAKLLAQKAAEAEQEmQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEE----SERRAKEAD 411
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElkkaEEENKIKAE 1733

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  412 QLKQDLQEAREAERRAKQKLLEiATKPTYPPMNPIPPPLPPDIPSFDIIADSLsfdfKDTDMKRlSMEIEKEKVEYMEKS 491
Cdd:PTZ00121  1734 EAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEEL----DEEDEKR-RMEVDKKIKDIFDNF 1807

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1371986040  492 KHLQEQLNELKTEIEALKLKERETALDVLHSESSDR 527
Cdd:PTZ00121  1808 ANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
PTZ00121 PTZ00121
MAEBL; Provisional
 269-514 3.20e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 3.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAE-----------RTRDELERRLLQMKEEATMANEALMRSE 337
Cdd:PTZ00121  1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkadeakkaeeaKKADEAKKAEEKKKADELKKAEELKKAE 1561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  338 ETADllAEKAQITEEEAKLLAQKAAEAEQ--------------EMQRIKATAIRTEEEKRLMEQKVLEAE-----VLALK 398
Cdd:PTZ00121  1562 EKKK--AEEAKKAEEDKNMALRKAEEAKKaeearieevmklyeEEKKMKAEEAKKAEEAKIKAEELKKAEeekkkVEQLK 1639

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  399 MAEESERRakEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSfdiiadslsfdfKDTDMKRLSM 478
Cdd:PTZ00121  1640 KKEAEEKK--KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK------------KEAEEAKKAE 1705

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1371986040  479 EIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 514
Cdd:PTZ00121  1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 270-430 4.31e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.14  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 270 RKADSLEVQQMKAQAREEKARKQMERQRlarekqmrEEAERTRDELERRLLQMKEEATMAN--EALMRSEETADLL---- 343
Cdd:COG3883    51 EEYNELQAELEALQAEIDKLQAEIAEAE--------AEIEERREELGERARALYRSGGSVSylDVLLGSESFSDFLdrls 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 344 -------AEKAQITE--EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLK 414
Cdd:COG3883   123 alskiadADADLLEElkADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202

                         170
                  ....*....|....*.
gi 1371986040 415 QDLQEAREAERRAKQK 430
Cdd:COG3883   203 AELAAAEAAAAAAAAA 218
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 284-527 4.45e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 4.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 284 AREEKARKQME--RQRLAR--------EKQM---REEAERTR------DELERR-----LLQMKE-EATMANEALMRSEE 338
Cdd:COG1196   172 ERKEEAERKLEatEENLERledilgelERQLeplERQAEKAEryrelkEELKELeaellLLKLRElEAELEELEAELEEL 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 339 TADLLAEKAQITEEEAKL---------LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKE 409
Cdd:COG1196   252 EAELEELEAELAELEAELeelrleleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 410 ADQLKQDLQEAREAERRAKQKLLEIATKptypPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYME 489
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1371986040 490 KSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDR 527
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
PTZ00121 PTZ00121
MAEBL; Provisional
 274-514 4.69e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 4.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  274 SLEVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLlAEKAQITEEE 353
Cdd:PTZ00121  1184 AEEVRKAEELRKAEDARK-AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN-EEIRKFEEAR 1261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  354 AKLLAQKAAEAEQEMQRiKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLE 433
Cdd:PTZ00121  1262 MAHFARRQAAIKAEEAR-KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  434 IATKPTYPPMNPIPPplppdipsfdiiADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKER 513
Cdd:PTZ00121  1341 AKKAAEAAKAEAEAA------------ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408


                   .
gi 1371986040  514 E 514
Cdd:PTZ00121  1409 E 1409
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-85 5.77e-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: 47.34  E-value: 5.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371986040  25 RIVTMD-AEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVKKQI 85
Cdd:cd17108     4 KVILLDgTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQhWLDPTKKIKKQV 66
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-85 6.72e-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: 47.19  E-value: 6.72e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371986040  25 RIVTMDAEmEFNCEM--KWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVKKQI 85
Cdd:cd17201     5 KVTLLDGS-EYECEVekHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKnWLDPSKEIKKQI 67
PRK12704 PRK12704
phosphodiesterase; Provisional
 269-428 7.72e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 51.70  E-value: 7.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 269 RRKADSLEVQQMKAQARE--EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEET------- 339
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRilEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENldrklel 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 340 -----ADLLAEKAQITEEEAKLLAQKA------AEAEQEMQRIKATairTEEE--KRLMEQKVLEAEVLALKMAEESERR 406
Cdd:PRK12704  105 lekreEELEKKEKELEQKQQELEKKEEeleeliEEQLQELERISGL---TAEEakEILLEKVEEEARHEAAVLIKEIEEE 181

                         170       180
                  ....*....|....*....|..
gi 1371986040 407 AKEadqlkqdlqearEAERRAK 428
Cdd:PRK12704  182 AKE------------EADKKAK 191
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 176-268 8.11e-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: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 176 YGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKisFPWNEIRNISYSDKEFTIKPLDKKIDV-FKFNSSklRVNKL 254
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVF--FRWEDIKNVINHKRTFSIECQNSEETVqFQFEDA--ETAKY 76

                          90
                  ....*....|....
gi 1371986040 255 ILQLCIGNHDLFMR 268
Cdd:cd13188    77 VWKLCVLQHKFYRQ 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 261-514 9.65e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 9.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  261 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 333
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  334 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 407
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  408 KEADQLKQDLQEAREAERRAKQKLLEIA----------TKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKrls 477
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIEslaaeieeleELIEELESELEALLNERASLEEALALLRSELEELSEELR--- 904

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1371986040  478 mEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 514
Cdd:TIGR02168  905 -ELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-85 1.06e-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: 46.66  E-value: 1.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371986040  24 VRIVTMDaEMEFNCEM--KWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVKKQI 85
Cdd:cd17106     4 CKVLLLD-GTEYTCEVekRAKGQVLFDKVCEHLNLLEKDYFGLTYRdAQDQKNWLDPAKEIKKQI 67
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 274-430 1.15e-06

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 50.61  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 274 SLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAtmANEALMRSEETADLLAEKAQITEEE 353
Cdd:TIGR02794  46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA--AAEKAAKQAEQAAKQAEEKQKQAEE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 354 AKLL----AQKAAEAEQEMQRIKATAIRTEEEKrlmeqkvleaevlALKMAEESERRAKEAD-QLKQDLQEAREAERRAK 428
Cdd:TIGR02794 124 AKAKqaaeAKAKAEAEAERKAKEEAAKQAEEEA-------------KAKAAAEAKKKAEEAKkKAEAEAKAKAEAEAKAK 190


                  ..
gi 1371986040 429 QK 430
Cdd:TIGR02794 191 AE 192
PTZ00121 PTZ00121
MAEBL; Provisional
 276-514 1.44e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  276 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAlmrseetadllAEKAQITEEEAK 355
Cdd:PTZ00121  1210 EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----------RRQAAIKAEEAR 1278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  356 llaqKAAEAEQEMQRIKATAIRTEEEKRLMEQkvleaevlALKMAEEserrAKEADQLKQDLQEAREAERRAKQKLLEIA 435
Cdd:PTZ00121  1279 ----KADELKKAEEKKKADEAKKAEEKKKADE--------AKKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAK 1342

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371986040  436 TKPTYPPMNPIPPPLPPDIPSFDIIADSlsfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 514
Cdd:PTZ00121  1343 KAAEAAKAEAEAAADEAEAAEEKAEAAE-----KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 268-539 2.00e-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: 50.89  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQM--------REEAERTR-DELERRLLQMKEEATMANEALMRSEE 338
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirqeerKRELERIRqEEIAMEISRMRELERLQMERQQKNER 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 339 TADLL--AEKAQITEEE------------AKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKvLEAEVLALKMAEESE 404
Cdd:pfam17380 394 VRQELeaARKVKILEEErqrkiqqqkvemEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE-RQQQVERLRQQEEER 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 405 RRAK-EADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADslsfdfkdtDMKRLSMEIEKE 483
Cdd:pfam17380 473 KRKKlELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE---------EERRREAEEERR 543

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1371986040 484 KVEYMEKSKHLQEQL---NELKTEIEALKlKERETALDVLHSESSDRGGPSSKHNTIKK 539
Cdd:pfam17380 544 KQQEMEERRRIQEQMrkaTEERSRLEAME-REREMMRQIVESEKARAEYEATTPITTIK 601
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-428 2.16e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  276 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 355
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371986040  356 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 428
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 269-429 2.29e-06

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 49.84  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 269 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 348
Cdd:TIGR02794  69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 349 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQDLQEAR---EAER 425
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKA-KAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAaaaEAER 227


                  ....
gi 1371986040 426 RAKQ 429
Cdd:TIGR02794 228 KADE 231
PTZ00121 PTZ00121
MAEBL; Provisional
 269-514 3.90e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 3.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllqmKEEATMANEALMRSEETADllAEKAQ 348
Cdd:PTZ00121  1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK-----AAEAKKKADEAKKAEEAKK--ADEAK 1528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  349 ITEEEAKLLAQKAAEAEQEMQRI-KATAIRTEEEKRLMEQKVLEAE--VLALKMAEES----ERRAKEADQLK------- 414
Cdd:PTZ00121  1529 KAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAkkaeEARIEEVMKLYeeekkmk 1608

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  415 -QDLQEAREAERRAKQ-------KLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSfdFKDTDMKRLSMEIEKEKVE 486
Cdd:PTZ00121  1609 aEEAKKAEEAKIKAEElkkaeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA--KKAEEDKKKAEEAKKAEED 1686

                          250       260
                   ....*....|....*....|....*...
gi 1371986040  487 YMEKSKHLQEQLNElKTEIEALKLKERE 514
Cdd:PTZ00121  1687 EKKAAEALKKEAEE-AKKAEELKKKEAE 1713
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 276-433 4.94e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.03  E-value: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 276 EVQQMKAQAREEKaRKQMERQRLAREKQmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 355
Cdd:PRK09510  105 QLEKERLAAQEQK-KQAEEAAKQAALKQ-KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 356 LLAQKAAEAEQ---EMQRIKATAIRTEEEKRLMEQKvleAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 432
Cdd:PRK09510  183 AKKKAEAEAAAkaaAEAKKKAEAEAKKKAAAEAKKK---AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259


                  .
gi 1371986040 433 E 433
Cdd:PRK09510  260 D 260
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 184-268 5.09e-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: 45.38  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 184 RNKKGTE--LLLGVDALGLHIYDP-ENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRvNKLILQLCI 260
Cdd:cd13185    12 KSKKETPgsVLLGITAKGIQIYQEsDGEQQLLRTFPWSNIGKLSFDRKKFEIRPEGSLRKLTYYTSSDEK-SKYLLALCR 90


                  ....*...
gi 1371986040 261 GNHDLFMR 268
Cdd:cd13185    91 ETHQFSMA 98
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 30-85 7.39e-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: 44.18  E-value: 7.39e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371986040  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVKKQI 85
Cdd:cd17104    10 SVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTgPKGERLWLNLRNRISRQL 66
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
269-431 1.18e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEvqQMKAQARE-EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAEKA 347
Cdd:COG4913    248 REQIELLE--PIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL------ERLEARLD 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  348 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALKMAEESERRA-----KEADQLKQDLQEA 420
Cdd:COG4913    320 ALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRarLEALLAALGLPLPASAEEfaalrAEAAALLEALEEE 399

                          170
                   ....*....|.
gi 1371986040  421 REAERRAKQKL 431
Cdd:COG4913    400 LEALEEALAEA 410
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
268-439 1.24e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.11  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQARE-----EKARKQMERQRLARE--KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETA 340
Cdd:PRK02224  272 REREELAEEVRDLRERLEEleeerDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 341 DLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQ----- 415
Cdd:PRK02224  352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreael 431

                         170       180
                  ....*....|....*....|....*.
gi 1371986040 416 --DLQEAREAERRAkQKLLEIATKPT 439
Cdd:PRK02224  432 eaTLRTARERVEEA-EALLEAGKCPE 456
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
276-437 1.36e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 276 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEeatmANEALMRSEETADLLAEKAQITEEEAK 355
Cdd:COG4717    75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK----LLQLLPLYQELEALEAELAELPERLEE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 356 LLAQKA--AEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 432
Cdd:COG4717   151 LEERLEelRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                  ....*
gi 1371986040 433 EIATK 437
Cdd:COG4717   231 QLENE 235
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 176-233 1.49e-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: 1.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1371986040 176 YGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPwnEIRNISYSDKEFTIK 233
Cdd:cd13195     1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERIPYT--AIQMATSSGRVFTLT 56
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 184-272 1.49e-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: 43.85  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 184 RNKK--GTELLLGVDALGLHIYDPEN-RLTPKISFPWNEIRNISYSDKEFTIKP--LDKKIDVFKFNSSKlrVNKLILQL 258
Cdd:cd13187     9 REKKssTLSLWLGICSRGIIIYEEKNgARTPVLRFPWRETQKISFDKKKFTIESrgGSGIKHTFYTDSYK--KSQYLLQL 86

                          90
                  ....*....|....*.
gi 1371986040 259 CIGNH--DLFMRRRKA 272
Cdd:cd13187    87 CSAQHkfHIQMRSRQS 102
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 272-431 1.51e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.13  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  272 ADSLEVQQMKAQARE-EKARKQMERQRLARE--------KQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtADL 342
Cdd:PRK10929   104 TDALEQEILQVSSQLlEKSRQAQQEQDRAREisdslsqlPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQ-AES 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  343 LAEKAQITEEEaklLAQKAAEAEQEMQRIKATAIRTEEEK----------RLMEQKVLEAEvLALkmaEESERRAKEADQ 412
Cdd:PRK10929   183 AALKALVDELE---LAQLSANNRQELARLRSELAKKRSQQldaylqalrnQLNSQRQREAE-RAL---ESTELLAEQSGD 255

                          170
                   ....*....|....*....
gi 1371986040  413 LKQDLQEAREAERRAKQKL 431
Cdd:PRK10929   256 LPKSIVAQFKINRELSQAL 274
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 286-426 1.59e-05

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 45.03  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 286 EEKARKQMERQRLAREKQMREEAERTRDELERRLLQmKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAE 365
Cdd:pfam05672  10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRK-EELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEER 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1371986040 366 QEMQRikatairteEEKRLMEQKVLEAEVlalKMAEESERRAKEADQLKQDLQEAREAERR 426
Cdd:pfam05672  89 EQREQ---------EEQERLQKQKEEAEA---KAREEAERQRQEREKIMQQEEQERLERKK 137
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 42-85 1.88e-05

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: 43.00  E-value: 1.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1371986040  42 KGKDLFDLVCRTLGLRETWFFGLQYTikDTVA---WLKMDKKVKKQI 85
Cdd:cd17102    23 KGQFLLDYVCNYLNLLEKDYFGLRYV--DTEKqrhWLDPNKSIYKQL 67
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 268-429 2.43e-05

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.87  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 347
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 348 QitEEEAKLLAQKAAEAEQEMQRIKATAIR-TEEEKRLME----------QKVLEAEVLALKMAEESERRAKEADQLKQD 416
Cdd:pfam15709 433 Q--ELQRKKQQEEAERAEAEKQRQKELEMQlAEEQKRLMEmaeeerleyqRQKQEAEEKARLEAEERRQKEEEAARLALE 510

                         170
                  ....*....|...
gi 1371986040 417 lQEAREAERRAKQ 429
Cdd:pfam15709 511 -EAMKQAQEQARQ 522
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 27-85 3.04e-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: 42.65  E-value: 3.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371986040  27 VTMDAEMEFNC--EMKWKGKDLFDLVCRTLGLRETWFFGLQYTIK-DTVAWLKMDKKVKKQI 85
Cdd:cd17202     6 VTLLDGTEYSCdlEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSaNQKNWLDSTKEIKRQI 67
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 257-439 3.15e-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: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 257 QLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQR---LAREKQM----REEAERTRDELErrlLQMKEEATMA 329
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRleeQERQQQVerlrQQEEERKRKKLE---LEKEKRDRKR 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 330 NEALMRSEETADLLAEKAQITEEEAKllaQKAAEAEQEMQRikaTAIRTEEEKRLM-EQKVLEAEVLALKMAEESERRAK 408
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERK---RKLLEKEMEERQ---KAIYEEERRREAeEERRKQQEMEERRRIQEQMRKAT 562

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1371986040 409 EADQLKQDLQEARE-----AERRAKQKLLEIATKPT 439
Cdd:pfam17380 563 EERSRLEAMEREREmmrqiVESEKARAEYEATTPIT 598
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 268-427 3.36e-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: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQMER--QRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 345
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 346 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAE-----VLALKMAEESERRAKEADQLKQDLQEA 420
Cdd:COG1196   457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAY 536


                  ....*..
gi 1371986040 421 REAERRA 427
Cdd:COG1196   537 EAALEAA 543
PRK12705 PRK12705
hypothetical protein; Provisional
 254-427 3.67e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 46.24  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 254 LILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKarkqmERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAL 333
Cdd:PRK12705   12 LLIGLLLGVLVVLLKKRQRLAKEAERILQEAQKEA-----EEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 334 MRSEEtaDLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL--MEQKVLEAEVLALKMAEESERRAKEAD 411
Cdd:PRK12705   87 VQKEE--QLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVagLTPEQARKLLLKLLDAELEEEKAQRVK 164

                         170
                  ....*....|....*.
gi 1371986040 412 QLKQDLQEarEAERRA 427
Cdd:PRK12705  165 KIEEEADL--EAERKA 178
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 20-84 3.77e-05

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: 42.33  E-value: 3.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371986040  20 KTFTVRIVTMDaEMEFNCEMK------WKGKDLFDLVCRTLGLRETWFFGLQYTIKDT-VAWLKMDKKVKKQ 84
Cdd:cd17107     1 EEFYCEIVLLD-ESELILTIQqdgiksSKGSVVLDVVFQHLNLLETDYFGLRYIDRQHqTHWLDPAKTLSEQ 71
growth_prot_Scy NF041483
polarized growth protein Scy;
271-424 4.41e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 46.74  E-value: 4.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  271 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 350
Cdd:NF041483   490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  351 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRL------MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 424
Cdd:NF041483   560 EETERAIAARQAEAAEELTR-----LHTEAEERLtaaeeaLADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 268-420 6.23e-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: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDE--LERRLLQMKEEATMANEALMRSEETADLLAE 345
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErlEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371986040 346 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 420
Cdd:COG1196   451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 290-514 7.06e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 290 RKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMrsEETADLLAEKAQIteeeakllaqkAAEAEQEMQ 369
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERR--RKLEEAEKARQAEM--DRQAAIYAEQERM-----------AMERERELE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 370 RikataIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERraKQKLLEIATKPTYPPMNPIPPP 449
Cdd:pfam17380 352 R-----IRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR--KVKILEEERQRKIQQQKVEMEQ 424

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371986040 450 LPPDIPsfdiiadslsfDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 514
Cdd:pfam17380 425 IRAEQE-----------EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLE 478
growth_prot_Scy NF041483
polarized growth protein Scy;
276-437 7.24e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 45.97  E-value: 7.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  276 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 355
Cdd:NF041483   583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  356 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 430
Cdd:NF041483   660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                   ....*..
gi 1371986040  431 LLEIATK 437
Cdd:NF041483   740 LLASARK 746
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
276-435 7.36e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 45.25  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 276 EVQQMKAQAREEKARKQMERQ-RLAREKQMREEAERTRDELERRLLQMKEEATmanealmRSEETADLLAEKA-QITEEE 353
Cdd:COG2268   202 RIAEAEAERETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEER-------REAETARAEAEAAyEIAEAN 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 354 AKLLAQKAAEAEQEMQRIKATAIRTE-EEKRLMEQKVLEAEVLALKMA--EESERRAKEADQLKQdlQEAREAERRAKQK 430
Cdd:COG2268   275 AEREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEaeAEAEAEAIRAKGLAE--AEGKRALAEAWNK 352


                  ....*
gi 1371986040 431 LLEIA 435
Cdd:COG2268   353 LGDAA 357
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
269-373 7.45e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.04  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 269 RRKADSLEVQQMKAQAREEKARKQMER-QRLARE----KQMREEAERTRDELERRLLQMKEEATMANEALmrsEETADLL 343
Cdd:COG1566   109 EAEIAAAEAQLAAAQAQLDLAQRELERyQALYKKgavsQQELDEARAALDAAQAQLEAAQAQLAQAQAGL---REEEELA 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 1371986040 344 AEKAQITEEEAKLlaqKAAEAEQEMQRIKA 373
Cdd:COG1566   186 AAQAQVAQAEAAL---AQAELNLARTTIRA 212
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 30-85 8.69e-05

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


Pssm-ID: 340620  Cd Length: 86  Bit Score: 41.14  E-value: 8.69e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQY----TIKDTVAWLKMDKKVKKQI 85
Cdd:cd17100    11 DTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFsddsPATDSMRWLDPLKPIRKQI 70
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-85 8.78e-05

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


Pssm-ID: 340723  Cd Length: 84  Bit Score: 41.46  E-value: 8.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371986040  25 RIVTMDAEmEFNCEM--KWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVKKQI 85
Cdd:cd17203     5 KVTLLDGS-EYTCEVekRSKGQVLFDKVCEHLNLLEKDYFGLTYRdSENQKNWLDPAKEIKKQI 67
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 42-85 9.01e-05

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: 41.34  E-value: 9.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1371986040  42 KGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVKKQI 85
Cdd:cd17204    22 KGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAhWLDHTKPIKKQI 66
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 30-85 9.24e-05

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


Pssm-ID: 340708  Cd Length: 86  Bit Score: 41.33  E-value: 9.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371986040  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQY-TIKDTVAWLKMDKKVKKQI 85
Cdd:cd17188    11 DSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFrNHAGNNVWLELLKPITKQI 67
PTZ00121 PTZ00121
MAEBL; Provisional
 276-514 9.58e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 9.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  276 EVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAQITEEEAK 355
Cdd:PTZ00121  1114 ARKAEEAKKKAEDARK-AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA--RKAEDAKKAEAARKAEEVRKA 1190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  356 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 435
Cdd:PTZ00121  1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371986040  436 TKPTYPPMNPIPPPLPPDIPSFDiiadslsfDFKDTDMKRLSMEIeKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 514
Cdd:PTZ00121  1271 AIKAEEARKADELKKAEEKKKAD--------EAKKAEEKKKADEA-KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 268-439 1.09e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 44.94  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEaertrdelerrllqmkeeatmanealmRSEETADLLAEKA 347
Cdd:PRK05035  432 RQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA---------------------------RHKKAAEARAAKD 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 348 Q--ITEEEAKLLAQKAAEAEQemqrikaTAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAer 425
Cdd:PRK05035  485 KdaVAAALARVKAKKAAATQP-------IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA-- 555

                         170
                  ....*....|....
gi 1371986040 426 RAKQKLLEIATKPT 439
Cdd:PRK05035  556 RAKAKKAAQQAANA 569
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 268-371 1.11e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 347
Cdd:COG1196   676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                          90       100
                  ....*....|....*....|....
gi 1371986040 348 QITEEEAKLLAQKAAEAEQEMQRI 371
Cdd:COG1196   756 LPEPPDLEELERELERLEREIEAL 779
PTZ00491 PTZ00491
major vault protein; Provisional
 279-410 1.11e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 45.01  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 279 QMKAQAREEKARKQMERQRLarekQMREEAERTRdeleRRLLQMKEEATmANEALMRSEETADLLAEKAQITEEeaklla 358
Cdd:PTZ00491  669 RHQAELLEQEARGRLERQKM----HDKAKAEEQR----TKLLELQAESA-AVESSGQSRAEALAEAEARLIEAE------ 733

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371986040 359 qkaAEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLAlKMAEESERRAKEA 410
Cdd:PTZ00491  734 ---AEVEQAELRAKALRIEAEAElEKLRKRQELELEYEQ-AQNELEIAKAKEL 782
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 264-436 1.32e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 264 DLFMRRRKADSLEVQQMKAQAREEKARkqmerQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 343
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALL-----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 344 AEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQK---------------------VLEAEVLALKMAEE 402
Cdd:COG1196   462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvkaalllaglrglagavaVLIGVEAAYEAALE 541

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1371986040 403 SERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 436
Cdd:COG1196   542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 287-433 1.33e-04

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: 44.50  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 287 EKARKQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEET-ADLLAEKAQITEEEAKLLAQKAAeae 365
Cdd:pfam07888  51 EAANRQREKEK-ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKyKELSASSEELSEEKDALLAQRAA--- 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371986040 366 qEMQRIKataiRTEEEKRLMEQKVLEAEVLALKMAEESERRAKeadQLKQDlqearEAERRAKQKLLE 433
Cdd:pfam07888 127 -HEARIR----ELEEDIKTLTQRVLERETELERMKERAKKAGA---QRKEE-----EAERKQLQAKLQ 181
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 27-85 1.33e-04

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


Pssm-ID: 340625  Cd Length: 83  Bit Score: 40.57  E-value: 1.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371986040  27 VTMDAEMEFNCEMK--WKGKDLFDLVCRTLGLRETWFFGLQ-YTIKDTVAWLKMDKKVKKQI 85
Cdd:cd17105     5 VSLLDDTVYECEVEkhAKGQDLFKKVCEHLNLLEEDYFGLAiWDSPTSKTWLDPAKEIKKQV 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 266-508 1.48e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 266 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 345
Cdd:COG1196   565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 346 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 425
Cdd:COG1196   645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 426 RAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADslsFDFKDTDMKRLSMEIEK-EKV------EY---MEKSKHLQ 495
Cdd:COG1196   725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD---LEELERELERLEREIEAlGPVnllaieEYeelEERYDFLS 801

                         250
                  ....*....|...
gi 1371986040 496 EQLNELKTEIEAL 508
Cdd:COG1196   802 EQREDLEEARETL 814
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 23-92 1.50e-04

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


Pssm-ID: 340725  Cd Length: 86  Bit Score: 40.79  E-value: 1.50e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371986040  23 TVRIVTMDA-EMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVKKQILDEKVYC 92
Cdd:cd17205     4 TCRVSLLDGtDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAhWLDVTKSIKKQVKIGPPYC 75
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 266-433 1.63e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  266 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAE 345
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI------EELEEL 867

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  346 KAQITEEEAKLLAQKAaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAER 425
Cdd:TIGR02168  868 IEELESELEALLNERA-SLEEALALLRSELEELSEELRELESKRSELR-------RELEELREKLAQLELRLEGLEVRID 939


                   ....*...
gi 1371986040  426 RAKQKLLE 433
Cdd:TIGR02168  940 NLQERLSE 947
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 269-438 2.03e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 269 RRKADSLEVQQMKAQAREEKARKQMERQRlAREKQMREEAERTRDELERRLLQM--------------KEEATMANEALM 334
Cdd:COG4942    61 ERRIAALARRIRALEQELAALEAELAELE-KEIAELRAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQ 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 335 RSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLK 414
Cdd:COG4942   140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219

                         170       180
                  ....*....|....*....|....
gi 1371986040 415 QDLQEAREAERRAKQKLLEIATKP 438
Cdd:COG4942   220 QEAEELEALIARLEAEAAAAAERT 243
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 276-437 2.06e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.17  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 276 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEAL----MRSEETADLLAEKAQITE 351
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQL--ERAEKMREELELEQQRRFEEIRLRKQRLeeerQRQEEEERKQRLQLQAAQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 352 EEAKLLAQKAAEAEQEMQRIKAT--AIRTEEEKRL---MEQKVLEAEVLALKMAEES-----ERRAKEADQLKQDLQEAR 421
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRKKQQeeAERAEAEKQRqkeLEMQLAEEQKRLMEMAEEErleyqRQKQEAEEKARLEAEERR 498

                         170
                  ....*....|....*.
gi 1371986040 422 EAERRAKQKLLEIATK 437
Cdd:pfam15709 499 QKEEEAARLALEEAMK 514
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 268-430 2.45e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 268 RRRKADSLEVQQMKAQAREEKARKQM-ERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEalmrsEETADLLAEK 346
Cdd:TIGR02794  89 ARQKELEQRAAAEKAAKQAEQAAKQAeEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE-----EEAKAKAAAE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 347 AQITEEEAKLLAQKAAEAEQEMQRiKATAirtEEEKRLMEQKVLEAEVLALKMAE-ESERRAKEADQLKQDLQEAREAER 425
Cdd:TIGR02794 164 AKKKAEEAKKKAEAEAKAKAEAEA-KAKA---EEAKAKAEAAKAKAAAEAAAKAEaEAAAAAAAEAERKADEAELGDIFG 239


                  ....*
gi 1371986040 426 RAKQK 430
Cdd:TIGR02794 240 LASGS 244
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 169-233 2.89e-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: 2.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1371986040 169 IAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK 233
Cdd:cd13193     2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
264-434 3.96e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 264 DLFMRRRKADSLEVQQMKAQAREEKARKQmERQRLAREKQMREEAERTRDELERRLLQMKEEAtmanEALMRSEETADLL 343
Cdd:COG4717    57 ELFKPQGRKPELNLKELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREEL----EKLEKLLQLLPLY 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 344 AEKAQItEEEAKLLAQKAAEAEQEMQRIKataiRTEEEKRLMEQKVLEAE-VLALKMAEESERRAKEADQLKQDLQEARE 422
Cdd:COG4717   132 QELEAL-EAELAELPERLEELEERLEELR----ELEEELEELEAELAELQeELEELLEQLSLATEEELQDLAEELEELQQ 206

                         170
                  ....*....|..
gi 1371986040 423 AERRAKQKLLEI 434
Cdd:COG4717   207 RLAELEEELEEA 218
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 313-414 4.80e-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: 4.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 313 DELERRLLQMKEEAtmanEALMRSEETADllAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEA 392
Cdd:COG0542   414 DELERRLEQLEIEK----EALKKEQDEAS--FERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487

                          90       100
                  ....*....|....*....|..
gi 1371986040 393 EVLALKMAEESERRAKEADQLK 414
Cdd:COG0542   488 PELEKELAELEEELAELAPLLR 509
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 281-539 5.18e-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: 43.04  E-value: 5.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  281 KAQAREEKARKQMERQRLAR-----EKQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtadLLAEKAQITEEEAK 355
Cdd:pfam02463  171 KKEALKKLIEETENLAELIIdleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK---LNEERIDLLQELLR 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  356 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 435
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  436 TKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLnELKTEIEALKLKERET 515
Cdd:pfam02463  328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA-KLKEEELELKSEEEKE 406

                          250       260
                   ....*....|....*....|....
gi 1371986040  516 ALDVLHSESSDRGGPSSKHNTIKK 539
Cdd:pfam02463  407 AQLLLELARQLEDLLKEEKKEELE 430
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 271-525 5.52e-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: 43.13  E-value: 5.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  271 KADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQIT 350
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  351 EEEAKLLAQKAAEAEQEMQRIKATAIRTEE-----EKRLMEQKVLEAEVLALKMAEESER---RAKEADQLKQDLQEARE 422
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKE 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  423 AERRAKQKLLE--IATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDmKRLSmEIEKEKVEYMEKSKHLQEQLNE 500
Cdd:TIGR02169  830 YLEKEIQELQEqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE-SRLG-DLKKERDELEAQLRELERKIEE 907

                          250       260
                   ....*....|....*....|....*..
gi 1371986040  501 LKTEIEALK--LKERETALDVLHSESS 525
Cdd:TIGR02169  908 LEAQIEKKRkrLSELKAKLEALEEELS 934
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-432 5.68e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 269 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQM----REEAERTRDELERRLLQMKEEATMANEALmrsEETADLLA 344
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPlyqeLEALEAELAELPERLEELEERLEELRELE---EELEELEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 345 EKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAE 424
Cdd:COG4717   171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ-------EELEELEEELEQLENELEAAALEE 243


                  ....*...
gi 1371986040 425 RRAKQKLL 432
Cdd:COG4717   244 RLKEARLL 251
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 269-416 5.85e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.90  E-value: 5.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEA------ERTRDELERRLLQMKEEATMANEALmrsEETADL 342
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfartalKNARLDLRRLFDEKQSEKDKKNKAL---AERKDS 679

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371986040  343 LAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESER--RAKEADQLKQD 416
Cdd:pfam12128  680 ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRsgAKAELKALETW 755
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 276-418 6.28e-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: 6.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  276 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRD-------ELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 348
Cdd:TIGR02169  372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  349 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQ 418
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
282-434 7.73e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 282 AQAREEKARKQMERQRLAREKQMREEA-ERTRD--ELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLa 358
Cdd:PRK02224  471 EEDRERVEELEAELEDLEEEVEEVEERlERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL- 549

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371986040 359 qkaaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 434
Cdd:PRK02224  550 ----EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 274-434 8.54e-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: 42.43  E-value: 8.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 274 SLEVQQMkaqaREEKARKQMERQRLAREKQMREEAERTRDELERRLL-----QMKEEATMANEALMR------------- 335
Cdd:pfam07111 480 SLELEQL----REERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLsevaqQLEQELQRAQESLASvgqqlevarqgqq 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 336 --SEETADLLAEKAQITEEEAKLLAQKAAEAEQEM-QRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERrakeADQ 412
Cdd:pfam07111 556 esTEEAASLRQELTQQQEIYGQALQEKVAEVETRLrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER----NQE 631

                         170       180
                  ....*....|....*....|...
gi 1371986040 413 LKQDLQEAREAE-RRAKQKLLEI 434
Cdd:pfam07111 632 LRRLQDEARKEEgQRLARRVQEL 654
Rabaptin pfam03528
Rabaptin;
280-429 1.02e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 41.63  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 280 MKAQAREEKAR--KQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEaLMRSEETADLLAEKAQITEEEAKLL 357
Cdd:pfam03528 113 MKETVREYEVQfhRRLEQER-AQWNQYRESAEREIADLRRRLSEGQEEENLEDE-MKKAQEDAEKLRSVVMPMEKEIAAL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 358 AQKAAEAEQEMQRIKATAIRT-----EEEKRLMEQKVLEAEVLALK---MAEESERRAKEADQLKQDLQEAREAERRAKQ 429
Cdd:pfam03528 191 KAKLTEAEDKIKELEASKMKElnhylEAEKSCRTDLEMYVAVLNTQksvLQEDAEKLRKELHEVCHLLEQERQQHNQLKH 270
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 275-435 1.06e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  275 LEVQQMKAQAREEKARKQMERQRLAREKQMRE--EAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEE 352
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  353 EAKLLAQKAAEAEQEMQRIKATAIRTEEE----KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 428
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486


                   ....*..
gi 1371986040  429 QKLLEIA 435
Cdd:TIGR02169  487 KLQRELA 493
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 30-85 1.20e-03

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: 38.25  E-value: 1.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1371986040  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVKKQI 85
Cdd:cd17189    10 DTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDhRKVMVWLDLLKPIVKQI 66
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
248-427 1.39e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  248 KLRVNKLILQLCIGNHDLFMRRRKADSL--EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTR--------DELER 317
Cdd:COG4913    266 AARERLAELEYLRAALRLWFAQRRLELLeaELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLER 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  318 RLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMqrikatairtEEEKRLMEQKVLEAEVLAL 397
Cdd:COG4913    346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL----------EEELEALEEALAEAEAALR 415

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1371986040  398 KMAEESERRAKEADQLKQ-------DLQEAREAERRA 427
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 ...
 288-373 1.90e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.57  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 288 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 366
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106


                  ....*..
gi 1371986040 367 EMQRIKA 373
Cdd:cd06503   107 EKEKALA 113
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 269-527 2.09e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.11  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQAREEKARKQMERQRLA--REKQMREEAERTRDELERRLLQMKEEATMANEalMRSEETADLLAEK 346
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLaqVLKENKEEEKEKKLQEEELKLLAKEEEELKSE--LLKLERRKVDDEE 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  347 AQITEEEAKLLAQKAAEAEQEmqrIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERR 426
Cdd:pfam02463  315 KLKESEKEKKKAEKELKKEKE---EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  427 AKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 506
Cdd:pfam02463  392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471

                          250       260
                   ....*....|....*....|.
gi 1371986040  507 ALKLKERETALDVLHSESSDR 527
Cdd:pfam02463  472 DLLKETQLVKLQEQLELLLSR 492
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
281-518 2.17e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 281 KAQAREEKARKQMERQRlAREKQMREEAERTRDELERR---LLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 357
Cdd:COG4372    35 KALFELDKLQEELEQLR-EELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 358 AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATK 437
Cdd:COG4372   114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 438 PTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETAL 517
Cdd:COG4372   194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273


                  .
gi 1371986040 518 D 518
Cdd:COG4372   274 E 274
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
262-437 2.50e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 40.35  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 262 NHDLFMRRRKAdslevqqmkAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAT--MANEALMRSEET 339
Cdd:PRK07735    4 EKDLEDLKKEA---------ARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 340 ADLLAEKAQITEEEAKLLAQKAAEAEQemqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQE 419
Cdd:PRK07735   75 AKQKREGTEEVTEEEKAKAKAKAAAAA-----KAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREG 149

                         170
                  ....*....|....*...
gi 1371986040 420 AREAERRAKQKLLEIATK 437
Cdd:PRK07735  150 TEEVTEEEEETDKEKAKA 167
growth_prot_Scy NF041483
polarized growth protein Scy;
292-433 2.57e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  292 QMERQRLARE-KQMREEA----ERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAA--- 362
Cdd:NF041483   439 QEEARRLRGEaEQLRAEAvaegERIRGEARREAVQQIEEaARTAEELLTKAKADADELRSTATAESERVRTEAIERAttl 518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  363 --EAEQEMQRIKATA--IRTEEEKRLMEQKVlEAEVLALKMAEESE-----RRAKEADQLKQDLQEAREAERRAKQKLLE 433
Cdd:NF041483   519 rrQAEETLERTRAEAerLRAEAEEQAEEVRA-AAERAARELREETEraiaaRQAEAAEELTRLHTEAEERLTAAEEALAD 597
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 270-423 2.63e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 40.37  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 270 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERtrdelerrllqMKEEATMANEALMRSEETADLLAEKAQI 349
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK-----------QQEAKNLPKPADTSSPKEDKQVAENQKR 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371986040 350 TEEEAKLLAQKAAEAEQEMQRIKATAIRTE--EEKRLMEQKVLEAEVLALKMAEESERRAKEAD-QLKQDLQEAREA 423
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQEskASEKEAEDKELEAQKKREPVAEDLQKTKPQVEaQPTSLNEDAIDS 358
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 266-326 2.77e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.63  E-value: 2.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371986040 266 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 326
Cdd:PLN03086    3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
284-427 3.27e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  284 AREEKARKQMERQRLAREkqmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKL------- 356
Cdd:COG4913    608 NRAKLAALEAELAELEEE---LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerldass 684

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371986040  357 -----LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLalkmAEESERRAKEADQLKQDLQEAREAERRA 427
Cdd:COG4913    685 ddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFA 756
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 272-404 3.88e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 272 ADSLEVQQMKAQArEEKARKQmeRQRLAREKQMREEAERTRDELERRLLQMKEEatmanEALMRSEetadlLAEKAQITE 351
Cdd:PRK00409  513 EDKEKLNELIASL-EELEREL--EQKAEEAEALLKEAEKLKEELEEKKEKLQEE-----EDKLLEE-----AEKEAQQAI 579

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1371986040 352 EEAKLLAQKAAEAEQEMQRIKATAIR---TEEEKRLMEQKVLEAEVLALKMAEESE 404
Cdd:PRK00409  580 KEAKKEADEIIKELRQLQKGGYASVKaheLIEARKRLNKANEKKEKKKKKQKEKQE 635
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 269-517 4.41e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMR---------------------------EEAERTRDELERRLLQ 321
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqallkekreyegyellkekealerqkEAIERQLASLEEELEK 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  322 MKEEATMANEALMRSEETADLLAEKAQ-ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVL----- 395
Cdd:TIGR02169  256 LTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEidkll 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  396 --ALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDM 473
Cdd:TIGR02169  336 aeIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1371986040  474 KRLSMEIEKEKveymEKSKHLQEQLNELKTEIE--ALKLKERETAL 517
Cdd:TIGR02169  416 QRLSEELADLN----AAIAGIEAKINELEEEKEdkALEIKKQEWKL 457
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 292-434 4.74e-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: 39.55  E-value: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 292 QMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQemqri 371
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQ----- 401

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371986040 372 kataiRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 434
Cdd:pfam15709 402 -----RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEM 459
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 267-425 4.99e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.13  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 267 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRseETADLLAEK 346
Cdd:pfam13868  30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ--EREQMDEIV 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371986040 347 AQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 425
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 285-434 5.05e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.95  E-value: 5.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  285 REEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQI--TEEEAKLLAQKA 361
Cdd:TIGR00618  368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLAHAKKQQelQQRYAELCAAAI 447

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1371986040  362 AEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 434
Cdd:TIGR00618  448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 271-554 5.55e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 5.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  271 KADSLE-VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRlLQMKEEATMA-NEALMRSEETADLLAEKAQ 348
Cdd:pfam15921  456 KNESLEkVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS-LQEKERAIEAtNAEITKLRSRVDLKLQELQ 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  349 ITEEEAKLLAQKAAEAE----QEMQRIKATAIRTEEEKRLMeQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 424
Cdd:pfam15921  535 HLKNEGDHLRNVQTECEalklQMAEKDKVIEILRQQIENMT-QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILK 613

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  425 RRAKQKLLEIATKPT---YPPMNPIPPPLPPDIPSFDIIA--DSLSFDFKDT--DMKRLSMEIEKEKVEYMEKSKHLQEQ 497
Cdd:pfam15921  614 DKKDAKIRELEARVSdleLEKVKLVNAGSERLRAVKDIKQerDQLLNEVKTSrnELNSLSEDYEVLKRNFRNKSEEMETT 693

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371986040  498 LNELKTEIEALKLKERETALDVLHSESSDRGGPS-----SKHNTIKKLTLQSAKSRVAFFEE 554
Cdd:pfam15921  694 TNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKvamgmQKQITAKRGQIDALQSKIQFLEE 755
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 269-437 5.90e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  269 RRKADSLEVQQMKAQAREEKARKQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 348
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELS-EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  349 ITEEEAKLLAQKAAEAEQEMQRikatairteEEKRLMEQKVLEAEV--LALKMAEESERRAKEADQLKQDLQEAREAERR 426
Cdd:TIGR02168  951 LTLEEAEALENKIEDDEEEARR---------RLKRLENKIKELGPVnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021

                          170
                   ....*....|.
gi 1371986040  427 AKQKLLEIATK 437
Cdd:TIGR02168 1022 AIEEIDREARE 1032
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
273-434 6.15e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 6.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 273 DSLEVQQMKAQAREEKARKQMERQRLARE------------KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETA 340
Cdd:PRK02224  223 ERYEEQREQARETRDEADEVLEEHEERREeletleaeiedlRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 341 DLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEE-KRLMEQkvleaevlALKMAEESERRAKEADQLKQDLQE 419
Cdd:PRK02224  303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaESLRED--------ADDLEERAEELREEAAELESELEE 374

                         170
                  ....*....|....*
gi 1371986040 420 AREAERRAKQKLLEI 434
Cdd:PRK02224  375 AREAVEDRREEIEEL 389
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 273-415 7.01e-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: 38.94  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 273 DSLEVQQMKAQAREEKARKQMERQR-----LAREKQMREEAERTRDELERRLLQMKEEATMANEAL-----------MRS 336
Cdd:pfam00529  61 DSAEAQLAKAQAQVARLQAELDRLQaleseLAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLarrrvlapiggISR 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 337 EEtadLLAEKAQITEEEAKLLAqkaaeAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEvlaLKMAEESERRAKEADQLKQ 415
Cdd:pfam00529 141 ES---LVTAGALVAQAQANLLA-----TVAQLDQIYVQITQSAAEnQAEVRSELSGAQ---LQIAEAEAELKLAKLDLER 209
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 265-527 7.37e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 7.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  265 LFMRRRKADSLEVQQMKAQAREEK--ARKQMERQRLARE-KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETAD 341
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAERYKELkaELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  342 LLAEkaqiteeeaklLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAR 421
Cdd:TIGR02168  275 EVSE-----------LEEEIEELQKELYALANEISRLEQQKQILRERLANLE-------RQLEELEAQLEELESKLDELA 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  422 EAERRAKQKLLEIATKPT-----YPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTdmkRLSMEIEKEKVEYMEKSK-HLQ 495
Cdd:TIGR02168  337 EELAELEEKLEELKEELEsleaeLEELEAELEELESRLEELEEQLETLRSKVAQL---ELQIASLNNEIERLEARLeRLE 413

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1371986040  496 EQLNELKTEIEALKLKERETALDVLHSESSDR 527
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAELKELQAELEEL 445
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 284-415 8.00e-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: 39.17  E-value: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  284 AREEKARKQMER--QRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLaeKAQITEEEAK----LL 357
Cdd:COG3096    529 RQQQNAERLLEEfcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL--RARIKELAARapawLA 606

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040  358 AQKAAE--AEQEMQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQ 415
Cdd:COG3096    607 AQDALErlREQSGEALADSQEVTAAMQQLLERER-EATVERDELAARKQALESQIERLSQ 665
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 269-437 8.52e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 269 RRKADSLEVQQMKAQAREEKARKQME--RQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALM-RSEETADLLAE 345
Cdd:COG4942    33 QQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEaQKEELAELLRA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 346 ---KAQITEEEAKLLAQKAAEAEQEMQRIKatAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAR- 421
Cdd:COG4942   113 lyrLGRQPPLALLLSPEDFLDAVRRLQYLK--YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAl 190

                         170
                  ....*....|....*.
gi 1371986040 422 EAERRAKQKLLEIATK 437
Cdd:COG4942   191 EALKAERQKLLARLEK 206
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 273-433 9.71e-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: 38.83  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 273 DSLEVQQMKAQAREEKARKQMERQRLAREKQMR-EEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITE 351
Cdd:pfam05262 175 DSISDKKVVEALREDNEKGVNFRRDMTDLKEREsQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371986040 352 EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVL------ALKMAEESERRAKEADQLKQDLQEAREAER 425
Cdd:pfam05262 255 QEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALkakdhkAFDLKQESKASEKEAEDKELEAQKKREPVA 334


                  ....*...
gi 1371986040 426 RAKQKLLE 433
Cdd:pfam05262 335 EDLQKTKP 342
 
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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