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Conserved domains on  [gi|356582398|ref|NP_001239180|]
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merlin isoform 1 [Mus musculus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 216-312 2.55e-63

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


:

Pssm-ID: 270015  Cd Length: 97  Bit Score: 202.89  E-value: 2.55e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 216 MYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 295
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 356582398 296 ILQLCIGNHDLFMRRRK 312
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 23-222 2.39e-60

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 199.06  E-value: 2.39e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398    23 TVRIVTMDAEM-EFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVLDHDVsKEEPVTFHFLAK 99
Cdd:smart00295   1 VLKVYLLDGTTlEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   100 FYPENaEEELVQEITQH-LFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINly 177
Cdd:smart00295  80 FYPPD-PNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD-- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 356582398   178 QMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 222
Cdd:smart00295 157 SRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 346-465 5.62e-24

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


:

Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 96.91  E-value: 5.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  346 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 425
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 356582398  426 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 465
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
ERM_C super family cl38012
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 518-580 1.31e-16

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


The actual alignment was detected with superfamily member pfam00769:

Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 74.54  E-value: 1.31e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582398  518 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGgpSSKHNTIKK 580
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQG--RDKYKTLRK 61
PLN03086 super family cl29366
PRLI-interacting factor K; Provisional
 307-367 3.15e-03

PRLI-interacting factor K; Provisional


The actual alignment was detected with superfamily member PLN03086:

Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.24  E-value: 3.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356582398 307 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 367
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 ...
 216-312 2.55e-63

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


Pssm-ID: 270015  Cd Length: 97  Bit Score: 202.89  E-value: 2.55e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 216 MYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 295
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 356582398 296 ILQLCIGNHDLFMRRRK 312
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 23-222 2.39e-60

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 199.06  E-value: 2.39e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398    23 TVRIVTMDAEM-EFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVLDHDVsKEEPVTFHFLAK 99
Cdd:smart00295   1 VLKVYLLDGTTlEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   100 FYPENaEEELVQEITQH-LFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINly 177
Cdd:smart00295  80 FYPPD-PNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD-- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 356582398   178 QMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 222
Cdd:smart00295 157 SRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 20-103 2.56e-53

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


Pssm-ID: 340706  Cd Length: 85  Bit Score: 176.42  E-value: 2.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  20 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHDVSKEEPVTFHFLA 98
Cdd:cd17186    1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQDVPKEEPVTFHFLA 80


                 ....*
gi 356582398  99 KFYPE 103
Cdd:cd17186   81 KFYPE 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 106-222 2.52e-33

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 123.15  E-value: 2.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  106 EEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWE 185
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 356582398  186 ERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 222
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-311 1.07e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.57  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  226 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 304
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 356582398  305 DLFMRRR 311
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 346-465 5.62e-24

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 96.91  E-value: 5.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  346 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 425
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 356582398  426 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 465
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 518-580 1.31e-16

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: 74.54  E-value: 1.31e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582398  518 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGgpSSKHNTIKK 580
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQG--RDKYKTLRK 61
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-476 9.01e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 9.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 310 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 389
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 390 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 469
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                 ....*..
gi 356582398 470 QKLLEIA 476
Cdd:COG1196  435 EEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 317-558 1.01e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 317 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 396
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 476
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 477 TKPTYPPMNPIPPPLPPDIPSFDIIADslsfdfkDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERET 556
Cdd:COG1196  400 AQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472


                 ..
gi 356582398 557 AL 558
Cdd:COG1196  473 AL 474
PTZ00121 PTZ00121
MAEBL; Provisional
 310-580 1.05e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.16  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEVQQMKAQARE----EKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 382
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAA 1356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  383 LLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEADQLKQDLQEAR 462
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAEEKKKAD 1434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  463 EAERRA--KQKLLEIATKPTYPPMNPIPPPLPPDIPSfdiiADSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLN 540
Cdd:PTZ00121 1435 EAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAK---KKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 356582398  541 ELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKK 580
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 319-478 2.57e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 62.52  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 319 QQMKAQAREEKARKQMERQRlAREKQMREEAErtrdelERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 398
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQ-AEELQQKQAAE------QERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 399 AQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 477
Cdd:PRK09510 142 AAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216


                 .
gi 356582398 478 K 478
Cdd:PRK09510 217 K 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-549 1.87e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   317 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 396
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 476
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   477 TKPTYPPMNPIPPPLPPDIPSFDI---------IADSLSFDFKDTdmkrlSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 547
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLeglevridnLQERLSEEYSLT-----LEEAEALENKIEDDEEEARRRLKRLENKIK 982


                   ..
gi 356582398   548 AL 549
Cdd:TIGR02168  983 EL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 302-555 4.84e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 4.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   302 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 374
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   375 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 448
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   449 KEADQLKQDLQEAREAERRAKQKLLEIA----------TKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKrls 518
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIEslaaeieeleELIEELESELEALLNERASLEEALALLRSELEELSEELR--- 904

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 356582398   519 mEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 555
Cdd:TIGR02168  905 -ELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
growth_prot_Scy NF041483
polarized growth protein Scy;
312-465 1.58e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 48.28  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  312 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 391
Cdd:NF041483  490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  392 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRL------MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 465
Cdd:NF041483  560 EETERAIAARQAEAAEELTR-----LHTEAEERLtaaeeaLADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
growth_prot_Scy NF041483
polarized growth protein Scy;
317-478 3.29e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.13  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  317 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 396
Cdd:NF041483  583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 471
Cdd:NF041483  660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                  ....*..
gi 356582398  472 LLEIATK 478
Cdd:NF041483  740 LLASARK 746
growth_prot_Scy NF041483
polarized growth protein Scy;
333-474 9.74e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.51  E-value: 9.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  333 QMERQRLARE-KQMREEA----ERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAA--- 403
Cdd:NF041483  439 QEEARRLRGEaEQLRAEAvaegERIRGEARREAVQQIEEaARTAEELLTKAKADADELRSTATAESERVRTEAIERAttl 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  404 --EAEQEMQRIKATA--IRTEEEKRLMEQKVlEAEVLALKMAEESE-----RRAKEADQLKQDLQEAREAERRAKQKLLE 474
Cdd:NF041483  519 rrQAEETLERTRAEAerLRAEAEEQAEEVRA-AAERAARELREETEraiaaRQAEAAEELTRLHTEAEERLTAAEEALAD 597
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 329-414 1.01e-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: 39.34  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 329 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 407
Cdd:cd06503   29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106


                 ....*..
gi 356582398 408 EMQRIKA 414
Cdd:cd06503  107 EKEKALA 113
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 307-367 3.15e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.24  E-value: 3.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356582398 307 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 367
Cdd:PLN03086   3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
growth_prot_Scy NF041483
polarized growth protein Scy;
321-466 6.31e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.81  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  321 MKAQARE--EKARKQMERQRlareKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAqiTEEEAKL- 397
Cdd:NF041483  518 LRRQAEEtlERTRAEAERLR----AEAEEQAEEVRAAAERAARELREETERAIAA--RQAEAAEELTRLH--TEAEERLt 589

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  398 -----LAQKAAEAE-------QEMQRIKATAirTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDL--QEARE 463
Cdd:NF041483  590 aaeeaLADARAEAErirreaaEETERLRTEA--AERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLrsEAAAE 667


                  ...
gi 356582398  464 AER 466
Cdd:NF041483  668 AER 670
 
Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 216-312 2.55e-63

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


Pssm-ID: 270015  Cd Length: 97  Bit Score: 202.89  E-value: 2.55e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 216 MYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 295
Cdd:cd13194    1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                         90
                 ....*....|....*..
gi 356582398 296 ILQLCIGNHDLFMRRRK 312
Cdd:cd13194   81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 23-222 2.39e-60

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 199.06  E-value: 2.39e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398    23 TVRIVTMDAEM-EFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVLDHDVsKEEPVTFHFLAK 99
Cdd:smart00295   1 VLKVYLLDGTTlEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   100 FYPENaEEELVQEITQH-LFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINly 177
Cdd:smart00295  80 FYPPD-PNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD-- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 356582398   178 QMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 222
Cdd:smart00295 157 SRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 20-103 2.56e-53

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


Pssm-ID: 340706  Cd Length: 85  Bit Score: 176.42  E-value: 2.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  20 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHDVSKEEPVTFHFLA 98
Cdd:cd17186    1 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQDVPKEEPVTFHFLA 80


                 ....*
gi 356582398  99 KFYPE 103
Cdd:cd17186   81 KFYPE 85
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 22-103 1.34e-42

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


Pssm-ID: 340617  Cd Length: 83  Bit Score: 147.43  E-value: 1.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  22 FTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKD-TVAWLKMDKKVLDHDVSKEEPVTFHFLAKF 100
Cdd:cd17097    1 INVRVTTMDAELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKgRVAWLKPDKKVLTQDVSKNNTLKFFFLVKF 80


                 ...
gi 356582398 101 YPE 103
Cdd:cd17097   81 YPE 83
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 106-222 2.52e-33

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 123.15  E-value: 2.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  106 EEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWE 185
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 356582398  186 ERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 222
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 23-103 2.97e-30

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


Pssm-ID: 340707 [Multi-domain]  Cd Length: 83  Bit Score: 113.33  E-value: 2.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  23 TVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFY 101
Cdd:cd17187    2 NVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREIWFFGLQYVdSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKFY 81


                 ..
gi 356582398 102 PE 103
Cdd:cd17187   82 PE 83
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 114-214 8.47e-30

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


Pssm-ID: 271216  Cd Length: 99  Bit Score: 112.72  E-value: 8.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 114 TQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWEERITAWYA 193
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLK--QRKPEEWEKRIVELHK 78

                         90       100
                 ....*....|....*....|.
gi 356582398 194 EHRGRARDEAEMEYLKIAQDL 214
Cdd:cd14473   79 KLRGLSPAEAKLKYLKIARKL 99
FERM_C pfam09380
FERM C-terminal PH-like domain;
226-311 1.07e-27

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.57  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  226 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 304
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 356582398  305 DLFMRRR 311
Cdd:pfam09380  79 TFFRLRR 85
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 20-103 7.57e-26

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


Pssm-ID: 340759  Cd Length: 85  Bit Score: 101.22  E-value: 7.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  20 KTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDVSKEEPVTFHFLA 98
Cdd:cd17239    1 KPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVdNKGFPTWLKLDKKVSAQEVRKENPLQFKFRA 80


                 ....*
gi 356582398  99 KFYPE 103
Cdd:cd17239   81 KFYPE 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 346-465 5.62e-24

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 96.91  E-value: 5.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  346 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 425
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 356582398  426 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 465
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 21-103 6.77e-24

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


Pssm-ID: 340757  Cd Length: 84  Bit Score: 95.58  E-value: 6.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  21 TFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYtiKDTVA---WLKMDKKVLDHDVSKEEPVTFHFL 97
Cdd:cd17237    1 TISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQY--QDTKGfstWLKLNKKVTAQDVRKESPLLFKFR 78


                 ....*.
gi 356582398  98 AKFYPE 103
Cdd:cd17237   79 AKFYPE 84
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 24-103 4.23e-23

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


Pssm-ID: 340758 [Multi-domain]  Cd Length: 83  Bit Score: 93.26  E-value: 4.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  24 VRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYP 102
Cdd:cd17238    3 VRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVdSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFP 82


                 .
gi 356582398 103 E 103
Cdd:cd17238   83 E 83
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 518-580 1.31e-16

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: 74.54  E-value: 1.31e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582398  518 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGgpSSKHNTIKK 580
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENVRQG--RDKYKTLRK 61
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 218-308 3.79e-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: 3.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 218 GVNYFTIRNK--KGTELLLGVDALGLHIYDPENRlTPKISFPWNEIRNISYS-DKEFTIKPLDK-KIDVFKFNSSKlRVN 293
Cdd:cd00836    1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEdKQSKLLFQTPS-RQA 78

                         90
                 ....*....|....*
gi 356582398 294 KLILQLCIGNHDLFM 308
Cdd:cd00836   79 KEIWKLIVGYHRFLL 93
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 22-100 6.96e-15

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


Pssm-ID: 340464  Cd Length: 80  Bit Score: 69.92  E-value: 6.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  22 FTVRIVTMD-AEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVLDHdVSKEEPVTFHFLAK 99
Cdd:cd01765    1 ISCRVRLLDgTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKhWLDLDKKISKQ-LKRSGPYQFYFRVK 79


                 .
gi 356582398 100 F 100
Cdd:cd01765   80 F 80
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-476 9.01e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 9.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 310 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 389
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 390 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 469
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                 ....*..
gi 356582398 470 QKLLEIA 476
Cdd:COG1196  435 EEEEEEE 441
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 218-313 1.58e-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: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 218 GVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKK--------------IDVF 283
Cdd:cd13191    1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRrnshrsrrtfqsssVSVH 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 356582398 284 KFNSSKLRVNKLILQLCIGNHDLFMRRRKA 313
Cdd:cd13191   81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQS 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 317-558 1.01e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 317 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 396
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 476
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 477 TKPTYPPMNPIPPPLPPDIPSFDIIADslsfdfkDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERET 556
Cdd:COG1196  400 AQLEELEEAEEALLERLERLEEELEEL-------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472


                 ..
gi 356582398 557 AL 558
Cdd:COG1196  473 AL 474
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-478 2.57e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 388
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 389 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 468
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                        170
                 ....*....|
gi 356582398 469 KQKLLEIATK 478
Cdd:COG1196  469 LEEAALLEAA 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 305-565 1.03e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 305 DLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 384
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 385 AEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREA 464
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 465 ERRAKQKLLEIATkptyPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKT 544
Cdd:COG1196  395 AAELAAQLEELEE----AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                        250       260
                 ....*....|....*....|.
gi 356582398 545 EIEALKLKERETALDVLHSES 565
Cdd:COG1196  471 EAALLEAALAELLEELAEAAA 491
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 30-104 1.87e-11

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


Pssm-ID: 340720  Cd Length: 89  Bit Score: 60.29  E-value: 1.87e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356582398  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYtIKDT--VAWLKMDKKVLDHDVSKEE-PVTFHFLAKFYPEN 104
Cdd:cd17200   12 DRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITF-IDDTgqSNWLQLDHRVLDHDLPKKSgPVTLYFAVRFYIES 88
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-478 2.32e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 388
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 389 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 468
Cdd:COG1196  403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        170
                 ....*....|
gi 356582398 469 KQKLLEIATK 478
Cdd:COG1196  483 LEELAEAAAR 492
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 26-86 4.57e-11

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


Pssm-ID: 430570  Cd Length: 63  Bit Score: 58.37  E-value: 4.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582398   26 IVTMDA-EMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDV 86
Cdd:pfam09379   1 VRLLDGtVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLdDNGEHRWLDLSKRLSKQAP 63
PTZ00121 PTZ00121
MAEBL; Provisional
 310-580 1.05e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.16  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEVQQMKAQARE----EKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 382
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAA 1356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  383 LLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEADQLKQDLQEAR 462
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAEEKKKAD 1434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  463 EAERRA--KQKLLEIATKPTYPPMNPIPPPLPPDIPSfdiiADSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLN 540
Cdd:PTZ00121 1435 EAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAK---KKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 356582398  541 ELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKK 580
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 30-102 1.81e-10

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


Pssm-ID: 340618  Cd Length: 85  Bit Score: 57.61  E-value: 1.81e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356582398  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHdVSKEEPVTFHFLAKFYP 102
Cdd:cd17098   10 DTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTdPEGNKCWLDPEKPILRQ-VKRPKDVVFKFVVKFYT 82
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 319-478 2.57e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 62.52  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 319 QQMKAQAREEKARKQMERQRlAREKQMREEAErtrdelERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 398
Cdd:PRK09510  69 QQQKSAKRAEEQRKKKEQQQ-AEELQQKQAAE------QERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 399 AQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 477
Cdd:PRK09510 142 AAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216


                 .
gi 356582398 478 K 478
Cdd:PRK09510 217 K 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 311-557 3.39e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 3.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 311 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQI 390
Cdd:COG1196  213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 391 TEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQ 470
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 471 KLLEIATKptyppmnpippPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 550
Cdd:COG1196  373 ELAEAEEE-----------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441


                 ....*..
gi 356582398 551 LKERETA 557
Cdd:COG1196  442 EALEEAA 448
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 30-104 4.11e-10

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


Pssm-ID: 340623  Cd Length: 91  Bit Score: 56.52  E-value: 4.11e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356582398  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHDVSK---EEPVTFHFLAKFYPEN 104
Cdd:cd17103   12 DRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDeTGHYNWLQLDKRVLDHEFPKkwsSGPLVLHFAVKFYVES 90
RA_FERM_F0_F1_like cd01768
Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 ...
 24-98 6.29e-10

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


Pssm-ID: 340467  Cd Length: 110  Bit Score: 56.79  E-value: 6.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  24 VRIVTM-----DAEMEFNCEMKWKGKDLFDLVCRTLGLR-----------ETWFFGLQYTIKDTVA-------------- 73
Cdd:cd01768    2 LKIFGAglasgANYKSVLATARSTARELVAEALERYGLAgspgggpgessCVDAFALCDALGRPAAagvgsgewraehlr 81

                         90       100
                 ....*....|....*....|....*....
gi 356582398  74 WLKMDKKV----LDHDVSKEEPVTFHFLA 98
Cdd:cd01768   82 VLGDSERPllvqELWRARPGWARRFELRG 110
PTZ00121 PTZ00121
MAEBL; Provisional
 310-555 9.42e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.08  E-value: 9.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-EATMANEALMRSEETADLLAEKA 388
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEA 1612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  389 QiTEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESeRRAKEADQLKQDLQEAREAERRA 468
Cdd:PTZ00121 1613 K-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-KKAEEDKKKAEEAKKAEEDEKKA 1690

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  469 KQKLLEIATKPTYPPMNPIppplppdipsfdiiadslsfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEA 548
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKK----------------------KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748


                  ....*..
gi 356582398  549 LKLKERE 555
Cdd:PTZ00121 1749 AKKDEEE 1755
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 309-471 4.95e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 58.66  E-value: 4.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 388
Cdd:PRK09510  81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 389 QITEEEAKLLAQKAAEAEQEmQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 468
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAA-AEAKKKAEAEAAAKAAAEAKK-KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAA 238


                 ...
gi 356582398 469 KQK 471
Cdd:PRK09510 239 EKA 241
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 20-104 6.16e-09

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


Pssm-ID: 340627  Cd Length: 91  Bit Score: 53.50  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  20 KTFTVRIVTMDaEMEFNCEMK------WKGKDLFDLVCRTLGLRETWFFGLQYTIKDT-VAWLKMDKKVLDHDVSKEEPV 92
Cdd:cd17107    1 EEFYCEIVLLD-ESELILTIQqdgiksSKGSVVLDVVFQHLNLLETDYFGLRYIDRQHqTHWLDPAKTLSEQLKLIGPPY 79

                         90
                 ....*....|..
gi 356582398  93 TFHFLAKFYPEN 104
Cdd:cd17107   80 TLYFGVKFYAED 91
PTZ00121 PTZ00121
MAEBL; Provisional
 310-555 6.28e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 6.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEVQQMKAQAREEkARKQMERQRLAREKQMREEAERTRDELERRllqmKEEATMANEALMRSEEtADLLAEKAQ 389
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKADEAKKKAEE-AKKKADEAK 1503

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  390 ITEEEAKLL--------AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 461
Cdd:PTZ00121 1504 KAAEAKKKAdeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  462 REAERRAKQKLLEIAtkPTYPPMNPIPPPLPPDIPSFDIIADSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNE 541
Cdd:PTZ00121 1584 EEAKKAEEARIEEVM--KLYEEEKKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                         250
                  ....*....|....
gi 356582398  542 LKTEIEALKLKERE 555
Cdd:PTZ00121 1659 NKIKAAEEAKKAEE 1672
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 32-104 7.84e-09

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


Pssm-ID: 340621  Cd Length: 97  Bit Score: 53.33  E-value: 7.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  32 EMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYtIKDT-------------VA---WLKMDKKVLDHdvsKEEPVTFH 95
Cdd:cd17101   13 RLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAV-LKDGeyffldpdtklskYApkgWKSEAKKGLKG---GKPVFTLY 88


                 ....*....
gi 356582398  96 FLAKFYPEN 104
Cdd:cd17101   89 FRVKFYVDN 97
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 308-478 1.34e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.12  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 308 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMRSEETADLLAEK 387
Cdd:PRK09510  67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEEAAKQAALKQKQAEEAAAKAAAA 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 388 AQI-TEEEAKLLAQKAAEAEQEMqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 466
Cdd:PRK09510 145 AKAkAEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA 221

                        170
                 ....*....|..
gi 356582398 467 RAKQKLLEIATK 478
Cdd:PRK09510 222 EAKAAAAKAAAE 233
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 216-307 1.65e-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: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 216 MYGVNYFTIRNKKGTELLLGVDALGLHIYdpENRLtpKIS-FPWNEIRNISYSDKEFTI----KPLDKKIDVFKFNSSKL 290
Cdd:cd13189    1 LYGVELHSARDSNNLELQIGVSSAGILVF--QNGI--RINtFPWSKIVKISFKRKQFFIqlrrEPNESRDTILGFNMLSY 76

                         90
                 ....*....|....*..
gi 356582398 291 RVNKLILQLCIGNHDLF 307
Cdd:cd13189   77 RACKNLWKSCVEHHTFF 93
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-549 1.87e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.76  E-value: 1.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   317 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 396
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 476
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   477 TKPTYPPMNPIPPPLPPDIPSFDI---------IADSLSFDFKDTdmkrlSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 547
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLeglevridnLQERLSEEYSLT-----LEEAEALENKIEDDEEEARRRLKRLENKIK 982


                   ..
gi 356582398   548 AL 549
Cdd:TIGR02168  983 EL 984
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 217-307 7.35e-08

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


Pssm-ID: 270005  Cd Length: 94  Bit Score: 50.40  E-value: 7.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 217 YGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK-------PLDKKIDvFKFNSSk 289
Cdd:cd13184    1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRIN---RFAWPKVLKISYKRNNFYIKirpgefeQYETTIG-FKLPNH- 75

                         90
                 ....*....|....*...
gi 356582398 290 lRVNKLILQLCIGNHDLF 307
Cdd:cd13184   76 -RAAKRLWKVCVEHHTFF 92
PTZ00121 PTZ00121
MAEBL; Provisional
 310-555 7.54e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 7.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEvQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR---------LLQMKEEATMANEALMRSEET 380
Cdd:PTZ00121 1404 KKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeeakkaeeAKKKAEEAKKADEAKKKAEEA 1482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  381 ADllAEKAQITEEEAKLLAQKAAEAEQEMQriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRaKEADQLKQdLQE 460
Cdd:PTZ00121 1483 KK--ADEAKKKAEEAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK-KKADELKK-AEE 1556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  461 AREAE--RRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRlsMEIEKEKVEYMEKSKHLQEQ 538
Cdd:PTZ00121 1557 LKKAEekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKK 1634

                         250
                  ....*....|....*..
gi 356582398  539 LNELKTEIEALKLKERE 555
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEE 1651
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 203-282 1.06e-07

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: 50.08  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 203 AEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTI---KPLDKK 279
Cdd:cd13192    1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFILhvmQKEEKK 77


                 ...
gi 356582398 280 IDV 282
Cdd:cd13192   78 HTL 80
PTZ00121 PTZ00121
MAEBL; Provisional
 305-568 1.21e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  305 DLFMRRRKADSL---EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR-----LLQMKEEATMANEALMR 376
Cdd:PTZ00121 1575 DKNMALRKAEEAkkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkveqLKKKEAEEKKKAEELKK 1654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  377 SEETADLLAEKAQITEEEAKLLAQKAAEAEQEmQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEE----SERRAKEAD 452
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElkkaEEENKIKAE 1733

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  453 QLKQDLQEAREAERRAKQKLLEiATKPTYPPMNPIPPPLPPDIPSFDIIADSLsfdfKDTDMKRlSMEIEKEKVEYMEKS 532
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEEL----DEEDEKR-RMEVDKKIKDIFDNF 1807

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 356582398  533 KHLQEQLNELKTEIEALKLKERETALDVLHSESSDR 568
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 311-471 1.52e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.68  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 311 RKADSLEVQQMKAQAREEKARKQMERQRlarekqmrEEAERTRDELERRLLQMKEEATMAN--EALMRSEETADLL---- 384
Cdd:COG3883   51 EEYNELQAELEALQAEIDKLQAEIAEAE--------AEIEERREELGERARALYRSGGSVSylDVLLGSESFSDFLdrls 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 385 -------AEKAQITE--EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLK 455
Cdd:COG3883  123 alskiadADADLLEElkADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202

                        170
                 ....*....|....*.
gi 356582398 456 QDLQEAREAERRAKQK 471
Cdd:COG3883  203 AELAAAEAAAAAAAAA 218
PTZ00121 PTZ00121
MAEBL; Provisional
 310-555 1.67e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAE-----------RTRDELERRLLQMKEEATMANEALMRSE 378
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkadeakkaeeaKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  379 ETADllAEKAQITEEEAKLLAQKAAEAEQ--------------EMQRIKATAIRTEEEKRLMEQKVLEAE-----VLALK 439
Cdd:PTZ00121 1562 EKKK--AEEAKKAEEDKNMALRKAEEAKKaeearieevmklyeEEKKMKAEEAKKAEEAKIKAEELKKAEeekkkVEQLK 1639

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  440 MAEESERRakEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSfdiiadslsfdfKDTDMKRLSM 519
Cdd:PTZ00121 1640 KKEAEEKK--KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK------------KEAEEAKKAE 1705

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 356582398  520 EIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 555
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 42-101 1.97e-07

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


Pssm-ID: 340622  Cd Length: 82  Bit Score: 48.78  E-value: 1.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582398  42 KGKDLFDLVCRTLGLRETWFFGLQYTikDTVA---WLKMDKKVLDHdVSKEEPVTFHFLAKFY 101
Cdd:cd17102   23 KGQFLLDYVCNYLNLLEKDYFGLRYV--DTEKqrhWLDPNKSIYKQ-LKGVPPYVLCFRVKFY 82
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 309-581 2.09e-07

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 53.97  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQM--------REEAERTR-DELERRLLQMKEEATMANEALMRSEE 379
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirqeerKRELERIRqEEIAMEISRMRELERLQMERQQKNER 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  380 TADLL--AEKAQITEEE------------AKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKvLEAEVLALKMAEESE 445
Cdd:pfam17380 394 VRQELeaARKVKILEEErqrkiqqqkvemEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE-RQQQVERLRQQEEER 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  446 RRAK-EADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADslsfdfkdtDMKRLSMEIEKE 524
Cdd:pfam17380 473 KRKKlELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE---------EERRREAEEERR 543

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  525 KVEYMEKSKHLQEQL---NELKTEIEALKlKERETALDVLHSESSDRGGPSSKHNTIKKP 581
Cdd:pfam17380 544 KQQEMEERRRIQEQMrkaTEERSRLEAME-REREMMRQIVESEKARAEYEATTPITTIKP 602
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 325-568 2.46e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 325 AREEKARKQME--RQRLAR--------EKQM---REEAERTR------DELERR-----LLQMKE-EATMANEALMRSEE 379
Cdd:COG1196  172 ERKEEAERKLEatEENLERledilgelERQLeplERQAEKAEryrelkEELKELeaellLLKLRElEAELEELEAELEEL 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 380 TADLLAEKAQITEEEAKL---------LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKE 450
Cdd:COG1196  252 EAELEELEAELAELEAELeelrleleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 451 ADQLKQDLQEAREAERRAKQKLLEIATKptypPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYME 530
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 356582398 531 KSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDR 568
Cdd:COG1196  408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 30-104 2.65e-07

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


Pssm-ID: 340719  Cd Length: 89  Bit Score: 48.81  E-value: 2.65e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356582398  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDT-VAWLKMDKKVLDHDVSKEE-PVTFHFLAKFYPEN 104
Cdd:cd17199   12 DRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGhLNWLQLDRRVLEHDFPKKSgPVVLYFCVRFYIES 88
PTZ00121 PTZ00121
MAEBL; Provisional
 315-555 3.33e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  315 SLEVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLlAEKAQITEEE 394
Cdd:PTZ00121 1184 AEEVRKAEELRKAEDARK-AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN-EEIRKFEEAR 1261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  395 AKLLAQKAAEAEQEMQRiKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLE 474
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEAR-KADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  475 IATKPTYPPMNPIPPplppdipsfdiiADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKER 554
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAA------------ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408


                  .
gi 356582398  555 E 555
Cdd:PTZ00121 1409 E 1409
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 315-471 4.13e-07

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 52.16  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  315 SLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAtmANEALMRSEETADLLAEKAQITEEE 394
Cdd:TIGR02794  46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA--AAEKAAKQAEQAAKQAEEKQKQAEE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  395 AKLL----AQKAAEAEQEMQRIKATAIRTEEEKrlmeqkvleaevlALKMAEESERRAKEAD-QLKQDLQEAREAERRAK 469
Cdd:TIGR02794 124 AKAKqaaeAKAKAEAEAERKAKEEAAKQAEEEA-------------KAKAAAEAKKKAEEAKkKAEAEAKAKAEAEAKAK 190


                  ..
gi 356582398  470 QK 471
Cdd:TIGR02794 191 AE 192
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-101 4.13e-07

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


Pssm-ID: 340628  Cd Length: 81  Bit Score: 47.73  E-value: 4.13e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356582398  25 RIVTMD-AEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVlDHDVSKEEPVTFHFLAKFY 101
Cdd:cd17108    4 KVILLDgTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQhWLDPTKKI-KKQVKIGPPYTLRFRVKFY 81
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 302-555 4.84e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 4.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   302 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 374
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   375 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 448
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   449 KEADQLKQDLQEAREAERRAKQKLLEIA----------TKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKrls 518
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIEslaaeieeleELIEELESELEALLNERASLEEALALLRSELEELSEELR--- 904

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 356582398   519 mEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 555
Cdd:TIGR02168  905 -ELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-102 4.91e-07

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


Pssm-ID: 340721  Cd Length: 84  Bit Score: 47.57  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  25 RIVTMDAEmEFNCEM--KWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVLDHdvSKEEPVTFHFLAKFY 101
Cdd:cd17201    5 KVTLLDGS-EYECEVekHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKnWLDPSKEIKKQ--IRSGPWHFAFTVKFY 81


                 .
gi 356582398 102 P 102
Cdd:cd17201   82 P 82
PRK12704 PRK12704
phosphodiesterase; Provisional
 310-469 5.51e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.47  E-value: 5.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 310 RRKADSLEVQQMKAQARE--EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEET------- 380
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKRilEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENldrklel 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 381 -----ADLLAEKAQITEEEAKLLAQKA------AEAEQEMQRIkatAIRTEEE--KRLMEQKVLEAEVLALKMAEESERR 447
Cdd:PRK12704 105 lekreEELEKKEKELEQKQQELEKKEEeleeliEEQLQELERI---SGLTAEEakEILLEKVEEEARHEAAVLIKEIEEE 181

                        170       180
                 ....*....|....*....|..
gi 356582398 448 AKEadqlkqdlqearEAERRAK 469
Cdd:PRK12704 182 AKE------------EADKKAK 191
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 310-470 8.68e-07

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 51.38  E-value: 8.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETAD--LLAEK 387
Cdd:TIGR02794  69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAErkAKEEA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  388 AQITEEEAKllAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQDLQEAR---EA 464
Cdd:TIGR02794 149 AKQAEEEAK--AKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKA-KAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAaaaEA 225


                  ....*.
gi 356582398  465 ERRAKQ 470
Cdd:TIGR02794 226 ERKADE 231
PTZ00121 PTZ00121
MAEBL; Provisional
 311-555 8.95e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 8.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  311 RKADslEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAlmrseetadllAEKAQI 390
Cdd:PTZ00121 1206 RKAE--EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----------RRQAAI 1272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  391 TEEEAKllaqKAAEAEQEMQRIKATAIRTEEEKRLMEQkvleaevlALKMAEEserrAKEADQLKQDLQEAREAERRAKQ 470
Cdd:PTZ00121 1273 KAEEAR----KADELKKAEEKKKADEAKKAEEKKKADE--------AKKKAEE----AKKADEAKKKAEEAKKKADAAKK 1336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  471 KLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSlsfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 550
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE-----KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411


                  ....*
gi 356582398  551 LKERE 555
Cdd:PTZ00121 1412 KAAAA 1416
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 217-309 9.67e-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: 46.90  E-value: 9.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 217 YGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKisFPWNEIRNISYSDKEFTIKPLDKKIDV-FKFNSSklRVNKL 295
Cdd:cd13188    1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVF--FRWEDIKNVINHKRTFSIECQNSEETVqFQFEDA--ETAKY 76

                         90
                 ....*....|....
gi 356582398 296 ILQLCIGNHDLFMR 309
Cdd:cd13188   77 VWKLCVLQHKFYRQ 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 317-469 1.44e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   317 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 396
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582398   397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 469
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 22-83 1.47e-06

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


Pssm-ID: 340619  Cd Length: 85  Bit Score: 46.46  E-value: 1.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356582398  22 FTVRIVTMDAE-MEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDK---KVLD 83
Cdd:cd17099    4 FVVRIQLLDNTvLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLrWVDLEKplkKQLD 70
PTZ00121 PTZ00121
MAEBL; Provisional
 310-555 2.06e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEVQQMKAQARE------EKARKQMERQRLAREKQMREEAERTRDELERRL--LQMKEEATMANEALMRSEETA 381
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEeakkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAK 1522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  382 DllAEKAQITEEEAKLLAQKAAEAEQEMQRI-KATAIRTEEEKRLMEQKVLEAE--VLALKMAEES----ERRAKEADQL 454
Cdd:PTZ00121 1523 K--ADEAKKAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAkkaeEARIEEVMKL 1600

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  455 K--------QDLQEAREAERRAKQ-------KLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSfdFKDTDMKRLSM 519
Cdd:PTZ00121 1601 YeeekkmkaEEAKKAEEAKIKAEElkkaeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA--KKAEEDKKKAE 1678

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 356582398  520 EIEKEKVEYMEKSKHLQEQLNElKTEIEALKLKERE 555
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAE 1713
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 317-474 2.19e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.19  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 317 EVQQMKAQAREEKaRKQMERQRLAREKQmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 396
Cdd:PRK09510 105 QLEKERLAAQEQK-KQAEEAAKQAALKQ-KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 397 LLAQKAAEAEQ---EMQRIKATAIRTEEEKRLMEQKvleAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 473
Cdd:PRK09510 183 AKKKAEAEAAAkaaAEAKKKAEAEAKKKAAAEAKKK---AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259


                 .
gi 356582398 474 E 474
Cdd:PRK09510 260 D 260
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 24-102 4.64e-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: 45.12  E-value: 4.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  24 VRIVTMDaEMEFNCEM--KWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWL---KMDKKVLdhdvsKEEPVTFHFL 97
Cdd:cd17106    4 CKVLLLD-GTEYTCEVekRAKGQVLFDKVCEHLNLLEKDYFGLTYRdAQDQKNWLdpaKEIKKQI-----RSGPWLFSFN 77


                 ....*
gi 356582398  98 AKFYP 102
Cdd:cd17106   78 VKFYP 82
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 225-309 4.67e-06

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


Pssm-ID: 270006  Cd Length: 107  Bit Score: 45.76  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 225 RNKKGTE--LLLGVDALGLHIYDP-ENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRvNKLILQLCI 301
Cdd:cd13185   12 KSKKETPgsVLLGITAKGIQIYQEsDGEQQLLRTFPWSNIGKLSFDRKKFEIRPEGSLRKLTYYTSSDEK-SKYLLALCR 90


                 ....*...
gi 356582398 302 GNHDLFMR 309
Cdd:cd13185   91 ETHQFSMA 98
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 30-101 5.50e-06

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


Pssm-ID: 340624  Cd Length: 81  Bit Score: 44.57  E-value: 5.50e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582398  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMdKKVLDHDVSKEEPVTFHFLAKFY 101
Cdd:cd17104   10 SVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTgPKGERLWLNL-RNRISRQLPGPPPYRLRLRVKFF 81
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 327-467 6.29e-06

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 46.57  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  327 EEKARKQMERQRLAREKQMREEAERTRDELERRLLQmKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAE 406
Cdd:pfam05672  10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRK-EELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEER 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356582398  407 QEMQRikatairteEEKRLMEQKVLEAEVlalKMAEESERRAKEADQLKQDLQEAREAERR 467
Cdd:pfam05672  89 EQREQ---------EEQERLQKQKEEAEA---KAREEAERQRQEREKIMQQEEQERLERKK 137
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
309-480 6.90e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 309 RRRKADSLEVQQMKAQARE-----EKARKQMERQRLARE--KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETA 381
Cdd:PRK02224 272 REREELAEEVRDLRERLEEleeerDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 382 DLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQ----- 456
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreael 431

                        170       180
                 ....*....|....*....|....*.
gi 356582398 457 --DLQEAREAERRAkQKLLEIATKPT 480
Cdd:PRK02224 432 eaTLRTARERVEEA-EALLEAGKCPE 456
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
317-478 7.37e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 7.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 317 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEeatmANEALMRSEETADLLAEKAQITEEEAK 396
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK----LLQLLPLYQELEALEAELAELPERLEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 397 LLAQKA--AEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 473
Cdd:COG4717  151 LEERLEelRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                 ....*
gi 356582398 474 EIATK 478
Cdd:COG4717  231 QLENE 235
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
310-472 8.26e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 8.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEvqQMKAQARE-EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAEKA 388
Cdd:COG4913   248 REQIELLE--PIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL------ERLEARLD 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  389 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALKMAEESERRA-----KEADQLKQDLQEA 461
Cdd:COG4913   320 ALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRarLEALLAALGLPLPASAEEfaalrAEAAALLEALEEE 399

                         170
                  ....*....|.
gi 356582398  462 REAERRAKQKL 472
Cdd:COG4913   400 LEALEEALAEA 410
PTZ00121 PTZ00121
MAEBL; Provisional
 310-582 1.16e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLevqqmKAQAREEKaRKQMERQRLAREKQMREEAERTRDELER--RLLQMKEEATMANEALMRSEET--ADLLA 385
Cdd:PTZ00121 1390 KKKADEA-----KKKAEEDK-KKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAkkAEEAK 1463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  386 EKAQITE--EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlaLKMAEESER--------RAKEADQLK 455
Cdd:PTZ00121 1464 KKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE---AKKAEEAKKadeakkaeEAKKADEAK 1540

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  456 QdLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSfDFKDTDMKRLSMEIEKEKVEYMEKSKHL 535
Cdd:PTZ00121 1541 K-AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEA 1618

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 356582398  536 QEQLNELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKKPQ 582
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 313-472 1.34e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.51  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  313 ADSLEVQQMKAQAR-EEKARKQMERQRLARE--------KQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtADL 383
Cdd:PRK10929  104 TDALEQEILQVSSQlLEKSRQAQQEQDRAREisdslsqlPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQ-AES 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  384 LAEKAQITEEEaklLAQKAAEAEQEMQRIKATAIRTEEEK----------RLMEQKVLEAEvLALkmaEESERRAKEADQ 453
Cdd:PRK10929  183 AALKALVDELE---LAQLSANNRQELARLRSELAKKRSQQldaylqalrnQLNSQRQREAE-RAL---ESTELLAEQSGD 255

                         170
                  ....*....|....*....
gi 356582398  454 LKQDLQEAREAERRAKQKL 472
Cdd:PRK10929  256 LPKSIVAQFKINRELSQAL 274
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 309-470 1.42e-05

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 48.02  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMR-----EEAERTRDELERRLLQMKEEATMANEALMRSEETADL 383
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRlrkqrLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  384 LAEKAQITEEEAKllaqkaaEAEQEMQRIKATAIR-TEEEKRLME----------QKVLEAEVLALKMAEESERRAKEAD 452
Cdd:pfam15709 433 QELQRKKQQEEAE-------RAEAEKQRQKELEMQlAEEQKRLMEmaeeerleyqRQKQEAEEKARLEAEERRQKEEEAA 505

                         170
                  ....*....|....*...
gi 356582398  453 QLKQDlQEAREAERRAKQ 470
Cdd:pfam15709 506 RLALE-EAMKQAQEQARQ 522
growth_prot_Scy NF041483
polarized growth protein Scy;
312-465 1.58e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 48.28  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  312 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 391
Cdd:NF041483  490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  392 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRL------MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 465
Cdd:NF041483  560 EETERAIAARQAEAAEELTR-----LHTEAEERLtaaeeaLADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 217-274 1.59e-05

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


Pssm-ID: 270016  Cd Length: 111  Bit Score: 44.16  E-value: 1.59e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 356582398 217 YGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPwnEIRNISYSDKEFTIK 274
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 ...
 225-313 1.71e-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: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 225 RNKK--GTELLLGVDALGLHIYDPEN-RLTPKISFPWNEIRNISYSDKEFTIKP--LDKKIDVFKFNSSKlrVNKLILQL 299
Cdd:cd13187    9 REKKssTLSLWLGICSRGIIIYEEKNgARTPVLRFPWRETQKISFDKKKFTIESrgGSGIKHTFYTDSYK--KSQYLLQL 86

                         90
                 ....*....|....*.
gi 356582398 300 CIGNH--DLFMRRRKA 313
Cdd:cd13187   87 CSAQHkfHIQMRSRQS 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-468 2.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 309 RRRKADSLEVQQMKAQAREEKARKQMER--QRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 386
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 387 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAE-----VLALKMAEESERRAKEADQLKQDLQEA 461
Cdd:COG1196  457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAY 536


                 ....*..
gi 356582398 462 REAERRA 468
Cdd:COG1196  537 EAALEAA 543
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 298-480 2.28e-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: 47.43  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  298 QLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQR---LAREKQM----REEAERTRDELErrlLQMKEEATMA 370
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRleeQERQQQVerlrQQEEERKRKKLE---LEKEKRDRKR 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  371 NEALMRSEETADLLAEKAQITEEEAKllaQKAAEAEQEMQRikaTAIRTEEEKRLM-EQKVLEAEVLALKMAEESERRAK 449
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERK---RKLLEKEMEERQ---KAIYEEERRREAeEERRKQQEMEERRRIQEQMRKAT 562

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 356582398  450 EADQLKQDLQEARE-----AERRAKQKLLEIATKPT 480
Cdd:pfam17380 563 EERSRLEAMEREREmmrqiVESEKARAEYEATTPIT 598
PRK12705 PRK12705
hypothetical protein; Provisional
 295-468 2.81e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.01  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 295 LILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKarkqmERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAL 374
Cdd:PRK12705  12 LLIGLLLGVLVVLLKKRQRLAKEAERILQEAQKEA-----EEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 375 MRSEEtaDLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL--MEQKVLEAEVLALKMAEESERRAKEAD 452
Cdd:PRK12705  87 VQKEE--QLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVagLTPEQARKLLLKLLDAELEEEKAQRVK 164

                        170
                 ....*....|....*.
gi 356582398 453 QLKQDLQEarEAERRA 468
Cdd:PRK12705 165 KIEEEADL--EAERKA 178
growth_prot_Scy NF041483
polarized growth protein Scy;
317-478 3.29e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.13  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  317 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 396
Cdd:NF041483  583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 471
Cdd:NF041483  660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                  ....*..
gi 356582398  472 LLEIATK 478
Cdd:NF041483  740 LLASARK 746
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 27-102 3.70e-05

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


Pssm-ID: 340722  Cd Length: 84  Bit Score: 42.27  E-value: 3.70e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356582398  27 VTMDAEMEFNC--EMKWKGKDLFDLVCRTLGLRETWFFGLQYTIK-DTVAWLKMDKKVLDHdvSKEEPVTFHFLAKFYP 102
Cdd:cd17202    6 VTLLDGTEYSCdlEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSaNQKNWLDSTKEIKRQ--IRRLPWLFTFNVKFYP 82
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
317-476 4.15e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 317 EVQQMKAQAREEKARKQMERQ-RLAREKQMREEAERTRDELERRLLQMKEEATmanealmRSEETADLLAEKA-QITEEE 394
Cdd:COG2268  202 RIAEAEAERETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEER-------REAETARAEAEAAyEIAEAN 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 395 AKLLAQKAAEAEQEMQRIKATAIRTE-EEKRLMEQKVLEAEVLALKMAEESErraKEADQLKQDLQ---EAREAERRAKQ 470
Cdd:COG2268  275 AEREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEAEAE---AEAEAIRAKGLaeaEGKRALAEAWN 351


                 ....*.
gi 356582398 471 KLLEIA 476
Cdd:COG2268  352 KLGDAA 357
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-461 4.22e-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: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDE--LERRLLQMKEEATMANEALMRSEETADLLAE 386
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErlEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356582398 387 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 461
Cdd:COG1196  451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 331-555 5.34e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.27  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  331 RKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMrsEETADLLAEKAQIteeeakllaqkAAEAEQEMQ 410
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERR--RKLEEAEKARQAEM--DRQAAIYAEQERM-----------AMERERELE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  411 RikataIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERraKQKLLEIATKPTYPPMNPIPPP 490
Cdd:pfam17380 352 R-----IRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR--KVKILEEERQRKIQQQKVEMEQ 424

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356582398  491 LPPDIPsfdiiadslsfDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 555
Cdd:pfam17380 425 IRAEQE-----------EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLE 478
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
310-414 5.56e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.42  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 310 RRKADSLEVQQMKAQAREEKARKQMER-QRLARE----KQMREEAERTRDELERRLLQMKEEATMANEALmrsEETADLL 384
Cdd:COG1566  109 EAEIAAAEAQLAAAQAQLDLAQRELERyQALYKKgavsQQELDEARAALDAAQAQLEAAQAQLAQAQAGL---REEEELA 185

                         90       100       110
                 ....*....|....*....|....*....|
gi 356582398 385 AEKAQITEEEAKLlaqKAAEAEQEMQRIKA 414
Cdd:COG1566  186 AAQAQVAQAEAAL---AQAELNLARTTIRA 212
PTZ00121 PTZ00121
MAEBL; Provisional
 317-555 5.98e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 5.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  317 EVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAQITEEEAK 396
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARK-AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA--RKAEDAKKAEAARKAEEVRKA 1190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 476
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356582398  477 TKPTYPPMNPIPPPLPPDIPSFDiiadslsfDFKDTDMKRLSMEIeKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 555
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEEKKKAD--------EAKKAEEKKKADEA-KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE 1340
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 328-474 6.73e-05

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 45.66  E-value: 6.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  328 EKARKQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEET-ADLLAEKAQITEEEAKLLAQKAAeae 406
Cdd:pfam07888  51 EAANRQREKEK-ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKyKELSASSEELSEEKDALLAQRAA--- 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356582398  407 qEMQRIKataiRTEEEKRLMEQKVLEAEVLALKMAEESERRAKeadQLKQDlqearEAERRAKQKLLE 474
Cdd:pfam07888 127 -HEARIR----ELEEDIKTLTQRVLERETELERMKERAKKAGA---QRKEE-----EAERKQLQAKLQ 181
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 309-474 7.69e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 7.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 388
Cdd:COG1196  676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 389 QITEEEAKLLAQKAAEAEQEMQRIKA---TAIrtEEekrlmeqkvleaevlalkMAEESERRAKEADQlKQDLQEAREA- 464
Cdd:COG1196  756 LPEPPDLEELERELERLEREIEALGPvnlLAI--EE------------------YEELEERYDFLSEQ-REDLEEARETl 814

                        170
                 ....*....|....*..
gi 356582398 465 -------ERRAKQKLLE 474
Cdd:COG1196  815 eeaieeiDRETRERFLE 831
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 305-477 7.82e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 7.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 305 DLFMRRRKADSLEVQQMKAQAREEKARkqmerQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 384
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALL-----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 385 AEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQK---------------------VLEAEVLALKMAEE 443
Cdd:COG1196  462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvkaalllaglrglagavaVLIGVEAAYEAALE 541

                        170       180       190
                 ....*....|....*....|....*....|....
gi 356582398 444 SERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 477
Cdd:COG1196  542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 307-549 8.82e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 8.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 307 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 386
Cdd:COG1196  565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 387 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 466
Cdd:COG1196  645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 467 RAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADslsFDFKDTDMKRLSMEIEK-EKV------EY---MEKSKHLQ 536
Cdd:COG1196  725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD---LEELERELERLEREIEAlGPVnllaieEYeelEERYDFLS 801

                        250
                 ....*....|...
gi 356582398 537 EQLNELKTEIEAL 549
Cdd:COG1196  802 EQREDLEEARETL 814
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 309-471 9.64e-05

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.84  E-value: 9.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  309 RRRKADSLEVQQMKAQAREEKARKQM-ERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEalmrsEETADLLAEK 387
Cdd:TIGR02794  89 ARQKELEQRAAAEKAAKQAEQAAKQAeEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE-----EEAKAKAAAE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  388 AQITEEEAKLLAQKAAEAEQEMQRiKATAirtEEEKRLMEQKVLEAEVLALKMAE-ESERRAKEADQLKQDLQEAREAER 466
Cdd:TIGR02794 164 AKKKAEEAKKKAEAEAKAKAEAEA-KAKA---EEAKAKAEAAKAKAAAEAAAKAEaEAAAAAAAEAERKADEAELGDIFG 239


                  ....*
gi 356582398  467 RAKQK 471
Cdd:TIGR02794 240 LASGS 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 307-474 9.88e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 9.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   307 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAE 386
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI------EELEEL 867

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   387 KAQITEEEAKLLAQKAaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAER 466
Cdd:TIGR02168  868 IEELESELEALLNERA-SLEEALALLRSELEELSEELRELESKRSELR-------RELEELREKLAQLELRLEGLEVRID 939


                   ....*...
gi 356582398   467 RAKQKLLE 474
Cdd:TIGR02168  940 NLQERLSE 947
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 310-479 1.09e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 310 RRKADSLEVQQMKAQAREEKARKQMERQRlAREKQMREEAERTRDELERRLLQM--------------KEEATMANEALM 375
Cdd:COG4942   61 ERRIAALARRIRALEQELAALEAELAELE-KEIAELRAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQ 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 376 RSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLK 455
Cdd:COG4942  140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219

                        170       180
                 ....*....|....*....|....
gi 356582398 456 QDLQEAREAERRAKQKLLEIATKP 479
Cdd:COG4942  220 QEAEELEALIARLEAEAAAAAERT 243
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 309-480 1.13e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 45.32  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEaertrdelerrllqmkeeatmanealmRSEETADLLAEKA 388
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA---------------------------RHKKAAEARAAKD 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 389 Q--ITEEEAKLLAQKAAEAEQemqrikaTAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAer 466
Cdd:PRK05035 485 KdaVAAALARVKAKKAAATQP-------IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA-- 555

                        170
                 ....*....|....
gi 356582398 467 RAKQKLLEIATKPT 480
Cdd:PRK05035 556 RAKAKKAAQQAANA 569
PTZ00491 PTZ00491
major vault protein; Provisional
 320-451 1.26e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 45.01  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 320 QMKAQAREEKARKQMERQRLarekQMREEAERTRdeleRRLLQMKEEATmANEALMRSEETADLLAEKAQITEEeaklla 399
Cdd:PTZ00491 669 RHQAELLEQEARGRLERQKM----HDKAKAEEQR----TKLLELQAESA-AVESSGQSRAEALAEAEARLIEAE------ 733

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 356582398 400 qkaAEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLAlKMAEESERRAKEA 451
Cdd:PTZ00491 734 ---AEVEQAELRAKALRIEAEAElEKLRKRQELELEYEQ-AQNELEIAKAKEL 782
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 317-478 1.30e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.94  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  317 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEAL----MRSEETADLLAEKAQITE 392
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQL--ERAEKMREELELEQQRRFEEIRLRKQRLeeerQRQEEEERKQRLQLQAAQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  393 EEAKLLAQKAAEAEQEMQRIKAT--AIRTEEEKRL---MEQKVLEAEVLALKMAEES-----ERRAKEADQLKQDLQEAR 462
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRKKQQeeAERAEAEKQRqkeLEMQLAEEQKRLMEMAEEErleyqRQKQEAEEKARLEAEERR 498

                         170
                  ....*....|....*.
gi 356582398  463 EAERRAKQKLLEIATK 478
Cdd:pfam15709 499 QKEEEAARLALEEAMK 514
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 322-580 1.95e-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: 44.58  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   322 KAQAREEKARKQMERQRLAR-----EKQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtadLLAEKAQITEEEAK 396
Cdd:pfam02463  171 KKEALKKLIEETENLAELIIdleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK---LNEERIDLLQELLR 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 476
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   477 TKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLnELKTEIEALKLKERET 556
Cdd:pfam02463  328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA-KLKEEELELKSEEEKE 406

                          250       260
                   ....*....|....*....|....
gi 356582398   557 ALDVLHSESSDRGGPSSKHNTIKK 580
Cdd:pfam02463  407 AQLLLELARQLEDLLKEEKKEELE 430
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
305-475 2.10e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 305 DLFMRRRKADSLEVQQMKAQAREEKARKQmERQRLAREKQMREEAERTRDELERRLLQMKEEAtmanEALMRSEETADLL 384
Cdd:COG4717   57 ELFKPQGRKPELNLKELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREEL----EKLEKLLQLLPLY 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 385 AEKAQItEEEAKLLAQKAAEAEQEMQRIKataiRTEEEKRLMEQKVLEAE-VLALKMAEESERRAKEADQLKQDLQEARE 463
Cdd:COG4717  132 QELEAL-EAELAELPERLEELEERLEELR----ELEEELEELEAELAELQeELEELLEQLSLATEEELQDLAEELEELQQ 206

                        170
                 ....*....|..
gi 356582398 464 AERRAKQKLLEI 475
Cdd:COG4717  207 RLAELEEELEEA 218
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 312-566 2.89e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   312 KADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQIT 391
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   392 EEEAKLLAQKAAEAEQEMQRIKATAIRTEE-----EKRLMEQKVLEAEVLALKMAEESER---RAKEADQLKQDLQEARE 463
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKE 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   464 AERRAKQKLLE--IATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDmKRLSmEIEKEKVEYMEKSKHLQEQLNE 541
Cdd:TIGR02169  830 YLEKEIQELQEqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE-SRLG-DLKKERDELEAQLRELERKIEE 907

                          250       260
                   ....*....|....*....|....*..
gi 356582398   542 LKTEIEALK--LKERETALDVLHSESS 566
Cdd:TIGR02169  908 LEAQIEKKRkrLSELKAKLEALEEELS 934
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 210-274 2.95e-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: 2.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356582398 210 IAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK 274
Cdd:cd13193    2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
310-473 3.34e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 310 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQM----REEAERTRDELERRLLQMKEEATMANEALmrsEETADLLA 385
Cdd:COG4717   94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPlyqeLEALEAELAELPERLEELEERLEELRELE---EELEELEA 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 386 EKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAE 465
Cdd:COG4717  171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ-------EELEELEEELEQLENELEAAALEE 243


                 ....*...
gi 356582398 466 RRAKQKLL 473
Cdd:COG4717  244 RLKEARLL 251
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 42-101 3.44e-04

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


Pssm-ID: 340724  Cd Length: 84  Bit Score: 39.80  E-value: 3.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356582398  42 KGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVlDHDVSKEEPVTFHFLAKFY 101
Cdd:cd17204   22 KGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAhWLDHTKPI-KKQIKIGPPYTLHFRIKYY 81
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 30-102 4.03e-04

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


Pssm-ID: 340709  Cd Length: 85  Bit Score: 39.40  E-value: 4.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356582398  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHdVSKEEPVTFHFLAKFYP 102
Cdd:cd17189   10 DTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDhRKVMVWLDLLKPIVKQ-IRRPKHVVLRFVVKFFP 82
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 317-459 4.32e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   317 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRD-------ELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 389
Cdd:TIGR02169  372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   390 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQ 459
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 30-101 4.45e-04

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


Pssm-ID: 340620  Cd Length: 86  Bit Score: 39.21  E-value: 4.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356582398  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQY----TIKDTVAWLKMDKKvLDHDVSKEEPVTFHFLAKFY 101
Cdd:cd17100   11 DTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFsddsPATDSMRWLDPLKP-IRKQIKGGPPYYLNFRVKFY 85
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 354-455 4.45e-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: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 354 DELERRLLQMKEEAtmanEALMRSEETADllAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEA 433
Cdd:COG0542  414 DELERRLEQLEIEK----EALKKEQDEAS--FERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487

                         90       100
                 ....*....|....*....|..
gi 356582398 434 EVLALKMAEESERRAKEADQLK 455
Cdd:COG0542  488 PELEKELAELEEELAELAPLLR 509
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 310-457 4.46e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.29  E-value: 4.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   310 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEA------ERTRDELERRLLQMKEEATMANEALmrsEETADL 383
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfartalKNARLDLRRLFDEKQSEKDKKNKAL---AERKDS 679

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356582398   384 LAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESER--RAKEADQLKQD 457
Cdd:pfam12128  680 ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRsgAKAELKALETW 755
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 27-102 4.53e-04

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


Pssm-ID: 340625  Cd Length: 83  Bit Score: 39.41  E-value: 4.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356582398  27 VTMDAEMEFNCEMK--WKGKDLFDLVCRTLGLRETWFFGLQ-YTIKDTVAWLKMDKKVLDHdvSKEEPVTFHFLAKFYP 102
Cdd:cd17105    5 VSLLDDTVYECEVEkhAKGQDLFKKVCEHLNLLEEDYFGLAiWDSPTSKTWLDPAKEIKKQ--VHGGPWEFTFNVKFYP 81
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
322-559 4.85e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 4.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 322 KAQAREEKARKQMERQRlAREKQMREEAERTRDELERR---LLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 398
Cdd:COG4372   35 KALFELDKLQEELEQLR-EELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 399 AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATK 478
Cdd:COG4372  114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 479 PTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETAL 558
Cdd:COG4372  194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273


                 .
gi 356582398 559 D 559
Cdd:COG4372  274 E 274
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 315-475 4.98e-04

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.20  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  315 SLEVQQMkaqaREEKARKQMERQRLAREKQMREEAERTRDELERRLL-----QMKEEATMANEALMR------------- 376
Cdd:pfam07111 480 SLELEQL----REERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLsevaqQLEQELQRAQESLASvgqqlevarqgqq 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  377 --SEETADLLAEKAQITEEEAKLLAQKAAEAEQEM-QRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERrakeADQ 453
Cdd:pfam07111 556 esTEEAASLRQELTQQQEIYGQALQEKVAEVETRLrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER----NQE 631

                         170       180
                  ....*....|....*....|...
gi 356582398  454 LKQDLQEAREAE-RRAKQKLLEI 475
Cdd:pfam07111 632 LRRLQDEARKEEgQRLARRVQEL 654
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
323-475 5.31e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 323 AQAREEKARKQMERQRLAREKQMREEA-ERTRD--ELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLa 399
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERlERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL- 549

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356582398 400 qkaaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 475
Cdd:PRK02224 550 ----EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 30-102 6.16e-04

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


Pssm-ID: 340708  Cd Length: 86  Bit Score: 39.02  E-value: 6.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356582398  30 DAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQY-TIKDTVAWLKMDKKVLDHdVSKEEPVTFHFLAKFYP 102
Cdd:cd17188   11 DSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFrNHAGNNVWLELLKPITKQ-IKNPKELIFKFTVKFFP 83
Rabaptin pfam03528
Rabaptin;
321-470 6.38e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 42.40  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  321 MKAQAREEKAR--KQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEaLMRSEETADLLAEKAQITEEEAKLL 398
Cdd:pfam03528 113 MKETVREYEVQfhRRLEQER-AQWNQYRESAEREIADLRRRLSEGQEEENLEDE-MKKAQEDAEKLRSVVMPMEKEIAAL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  399 AQKAAEAEQEMQRIKATAIRT-----EEEKRLMEQKVLEAEVLALK---MAEESERRAKEADQLKQDLQEAREAERRAKQ 470
Cdd:pfam03528 191 KAKLTEAEDKIKELEASKMKElnhylEAEKSCRTDLEMYVAVLNTQksvLQEDAEKLRKELHEVCHLLEQERQQHNQLKH 270
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 316-476 6.46e-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: 6.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   316 LEVQQMKAQAREEKARKQMERQRLAREKQMRE--EAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEE 393
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   394 EAKLLAQKAAEAEQEMQRIKATAIRTEEE----KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 469
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486


                   ....*..
gi 356582398   470 QKLLEIA 476
Cdd:TIGR02169  487 KLQRELA 493
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-102 6.91e-04

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


Pssm-ID: 340723  Cd Length: 84  Bit Score: 38.77  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  25 RIVTMDAEmEFNCEM--KWKGKDLFDLVCRTLGLRETWFFGLQY-TIKDTVAWLKMDKKVLDHdvSKEEPVTFHFLAKFY 101
Cdd:cd17203    5 KVTLLDGS-EYTCEVekRSKGQVLFDKVCEHLNLLEKDYFGLTYrDSENQKNWLDPAKEIKKQ--IRSGAWQFSFNVKFY 81


                 .
gi 356582398 102 P 102
Cdd:cd17203   82 P 82
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 310-568 8.74e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.27  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   310 RRKADSLEVQQMKAQAREEKARKQMERQRLA--REKQMREEAERTRDELERRLLQMKEEATMANEalMRSEETADLLAEK 387
Cdd:pfam02463  237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLaqVLKENKEEEKEKKLQEEELKLLAKEEEELKSE--LLKLERRKVDDEE 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   388 AQITEEEAKLLAQKAAEAEQEmqrIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERR 467
Cdd:pfam02463  315 KLKESEKEKKKAEKELKKEKE---EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   468 AKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIE 547
Cdd:pfam02463  392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471

                          250       260
                   ....*....|....*....|.
gi 356582398   548 ALKLKERETALDVLHSESSDR 568
Cdd:pfam02463  472 DLLKETQLVKLQEQLELLLSR 492
growth_prot_Scy NF041483
polarized growth protein Scy;
333-474 9.74e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.51  E-value: 9.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  333 QMERQRLARE-KQMREEA----ERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAA--- 403
Cdd:NF041483  439 QEEARRLRGEaEQLRAEAvaegERIRGEARREAVQQIEEaARTAEELLTKAKADADELRSTATAESERVRTEAIERAttl 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  404 --EAEQEMQRIKATA--IRTEEEKRLMEQKVlEAEVLALKMAEESE-----RRAKEADQLKQDLQEAREAERRAKQKLLE 474
Cdd:NF041483  519 rrQAEETLERTRAEAerLRAEAEEQAEEVRA-AAERAARELREETEraiaaRQAEAAEELTRLHTEAEERLTAAEEALAD 597
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 329-414 1.01e-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: 39.34  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 329 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 407
Cdd:cd06503   29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106


                 ....*..
gi 356582398 408 EMQRIKA 414
Cdd:cd06503  107 EKEKALA 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
289-468 1.03e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  289 KLRVNKLILQLCIGNHDLFMRRRKADSL--EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTR--------DELER 358
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQRRLELLeaELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLER 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  359 RLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMqrikatairtEEEKRLMEQKVLEAEVLAL 438
Cdd:COG4913   346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL----------EEELEALEEALAEAEAALR 415

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 356582398  439 KMAEESERRAKEADQLKQ-------DLQEAREAERRA 468
Cdd:COG4913   416 DLRRELRELEAEIASLERrksnipaRLLALRDALAEA 452
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
303-478 1.31e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 41.50  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 303 NHDLFMRRRKAdslevqqmkAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAT--MANEALMRSEET 380
Cdd:PRK07735   4 EKDLEDLKKEA---------ARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 381 ADLLAEKAQITEEEAKLLAQKAAEAEQemqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQE 460
Cdd:PRK07735  75 AKQKREGTEEVTEEEKAKAKAKAAAAA-----KAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREG 149

                        170
                 ....*....|....*...
gi 356582398 461 AREAERRAKQKLLEIATK 478
Cdd:PRK07735 150 TEEVTEEEEETDKEKAKA 167
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 311-464 1.59e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.14  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  311 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERtrdelerrllqMKEEATMANEALMRSEETADLLAEKAQI 390
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK-----------QQEAKNLPKPADTSSPKEDKQVAENQKR 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356582398  391 TEEEAKLLAQKAAEAEQEMQRIKATAIRTE--EEKRLMEQKVLEAEVLALKMAEESERRAKEAD-QLKQDLQEAREA 464
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQEskASEKEAEDKELEAQKKREPVAEDLQKTKPQVEaQPTSLNEDAIDS 358
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 308-466 1.77e-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: 40.67  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  308 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRseETADLLAEK 387
Cdd:pfam13868  30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ--EREQMDEIV 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356582398  388 AQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 466
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 310-554 2.36e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   310 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKqmreeAERTRDelerrLLQMKEEAtmanEALMRSEETADLLAEKAQ 389
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREK-----AERYQA-----LLKEKREY----EGYELLKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   390 ITEEEAKL---LAQKAAEAEQEMQRIKATAIRTEE-EKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 465
Cdd:TIGR02169  242 IERQLASLeeeLEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   466 RRAKQKLLEI-ATKPTYPPMNPIPPPLPPDIPSFDIIADSLsfdfKDTDMKRLS--MEIEKEKVEYMEKSKHLQEQLNEL 542
Cdd:TIGR02169  322 ERLAKLEAEIdKLLAEIEELEREIEEERKRRDKLTEEYAEL----KEELEDLRAelEEVDKEFAETRDELKDYREKLEKL 397

                          250
                   ....*....|..
gi 356582398   543 KTEIEALKLKER 554
Cdd:TIGR02169  398 KREINELKRELD 409
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
325-468 2.74e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  325 AREEKARKQMERQRLAREkqmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKL------- 397
Cdd:COG4913   608 NRAKLAALEAELAELEEE---LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerldass 684

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356582398  398 -----LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLalkmAEESERRAKEADQLKQDLQEAREAERRA 468
Cdd:COG4913   685 ddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFA 756
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 23-101 2.82e-03

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


Pssm-ID: 340725  Cd Length: 86  Bit Score: 37.33  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  23 TVRIVTMDA-EMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVlDHDVSKEEPVTFHFLAKF 100
Cdd:cd17205    4 TCRVSLLDGtDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAhWLDVTKSI-KKQVKIGPPYCLHLRVKF 82


                 .
gi 356582398 101 Y 101
Cdd:cd17205   83 Y 83
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 307-367 3.15e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.24  E-value: 3.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356582398 307 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 367
Cdd:PLN03086   3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 313-445 3.35e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 313 ADSLEVQQMKAQArEEKARKQmeRQRLAREKQMREEAERTRDELERRLLQMKEEatmanEALMRSEetadlLAEKAQITE 392
Cdd:PRK00409 513 EDKEKLNELIASL-EELEREL--EQKAEEAEALLKEAEKLKEELEEKKEKLQEE-----EDKLLEE-----AEKEAQQAI 579

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 356582398 393 EEAKLLAQKAAEAEQEMQRIKATAIR---TEEEKRLMEQKVLEAEVLALKMAEESE 445
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKaheLIEARKRLNKANEKKEKKKKKQKEKQE 635
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 333-475 3.40e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  333 QMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQemqri 412
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQ----- 401

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582398  413 kataiRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 475
Cdd:pfam15709 402 -----RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEM 459
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 310-478 3.47e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   310 RRKADSLEVQQMKAQAREEKARKQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 389
Cdd:TIGR02168  872 ESELEALLNERASLEEALALLRSELEELS-EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   390 ITEEEAKLLAQKAAEAEQEMQRikatairteEEKRLMEQKVLEAEV--LALKMAEESERRAKEADQLKQDLQEAREAERR 467
Cdd:TIGR02168  951 LTLEEAEALENKIEDDEEEARR---------RLKRLENKIKELGPVnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021

                          170
                   ....*....|.
gi 356582398   468 AKQKLLEIATK 478
Cdd:TIGR02168 1022 AIEEIDREARE 1032
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
314-475 4.00e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 314 DSLEVQQMKAQAREEKARKQMERQRLARE------------KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETA 381
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREeletleaeiedlRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 382 DLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEE-KRLMEQkvleaevlALKMAEESERRAKEADQLKQDLQE 460
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaESLRED--------ADDLEERAEELREEAAELESELEE 374

                        170
                 ....*....|....*
gi 356582398 461 AREAERRAKQKLLEI 475
Cdd:PRK02224 375 AREAVEDRREEIEEL 389
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 326-475 4.00e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   326 REEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQI--TEEEAKLLAQKA 402
Cdd:TIGR00618  368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLAHAKKQQelQQRYAELCAAAI 447

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356582398   403 AEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 475
Cdd:TIGR00618  448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 306-568 4.34e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 4.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   306 LFMRRRKADSLEVQQMKAQAREEK--ARKQMERQRLARE-KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETAD 382
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAERYKELkaELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   383 LLAEkaqiteeeaklLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAR 462
Cdd:TIGR02168  275 EVSE-----------LEEEIEELQKELYALANEISRLEQQKQILRERLANLE-------RQLEELEAQLEELESKLDELA 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398   463 EAERRAKQKLLEIATKPT-----YPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTdmkRLSMEIEKEKVEYMEKSK-HLQ 536
Cdd:TIGR02168  337 EELAELEEKLEELKEELEsleaeLEELEAELEELESRLEELEEQLETLRSKVAQL---ELQIASLNNEIERLEARLeRLE 413

                          250       260       270
                   ....*....|....*....|....*....|..
gi 356582398   537 EQLNELKTEIEALKLKERETALDVLHSESSDR 568
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAELKELQAELEEL 445
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 314-456 4.41e-03

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


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 39.71  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  314 DSLEVQQMKAQAREEKARKQMERQR-----LAREKQMREEAERTRDELERRLLQMKEEATMANEAL-----------MRS 377
Cdd:pfam00529  61 DSAEAQLAKAQAQVARLQAELDRLQaleseLAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLarrrvlapiggISR 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  378 EEtadLLAEKAQITEEEAKLLAqkaaeAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEvlaLKMAEESERRAKEADQLKQ 456
Cdd:pfam00529 141 ES---LVTAGALVAQAQANLLA-----TVAQLDQIYVQITQSAAEnQAEVRSELSGAQ---LQIAEAEAELKLAKLDLER 209
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 322-463 4.47e-03

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


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 39.24  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  322 KAQAREEKARkQMERQrLAREKQMREEAERTRDELERRLlqmkeeaTMANEALMRSEETADLLAEKAQITEEEAKLLAQK 401
Cdd:pfam00261  86 RALKDEEKME-ILEAQ-LKEAKEIAEEADRKYEEVARKL-------VVVEGDLERAEERAELAESKIVELEEELKVVGNN 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356582398  402 AAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalKMAEESERRA----KEADQLKQDLQEARE 463
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAE----TRAEFAERSVqkleKEVDRLEDELEAEKE 218
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
317-559 5.78e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 317 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 396
Cdd:COG4372   46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 397 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALKMAEESERRAKEADQLKQDLQEAREA----ERRAKQ 470
Cdd:COG4372  126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLesLQEELAALEQELQALSEAEAEQALDELLKEANRNaekeEELAEA 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 471 KLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 550
Cdd:COG4372  206 EKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285


                 ....*....
gi 356582398 551 LKERETALD 559
Cdd:COG4372  286 EALEEAALE 294
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 325-456 6.24e-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: 39.55  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  325 AREEKARKQMER--QRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLaeKAQITEEEAK----LL 398
Cdd:COG3096   529 RQQQNAERLLEEfcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL--RARIKELAARapawLA 606

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  399 AQKAAE--AEQEMQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQ 456
Cdd:COG3096   607 AQDALErlREQSGEALADSQEVTAAMQQLLERER-EATVERDELAARKQALESQIERLSQ 665
growth_prot_Scy NF041483
polarized growth protein Scy;
321-466 6.31e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.81  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  321 MKAQARE--EKARKQMERQRlareKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAqiTEEEAKL- 397
Cdd:NF041483  518 LRRQAEEtlERTRAEAERLR----AEAEEQAEEVRAAAERAARELREETERAIAA--RQAEAAEELTRLH--TEAEERLt 589

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  398 -----LAQKAAEAE-------QEMQRIKATAirTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDL--QEARE 463
Cdd:NF041483  590 aaeeaLADARAEAErirreaaEETERLRTEA--AERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLrsEAAAE 667


                  ...
gi 356582398  464 AER 466
Cdd:NF041483  668 AER 670
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 329-418 6.84e-03

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


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 37.46  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 329 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAtmaneALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQE 408
Cdd:COG0711   30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEA-----AEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAE 104

                         90
                 ....*....|
gi 356582398 409 MQRIKATAIR 418
Cdd:COG0711  105 IEQERAKALA 114
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
310-475 6.94e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  310 RRKADSLEVQQMKAQAREEKARKQME--RQRLAREKQMRE---------EAERTRDELERRLlqmkEEATMANEALMRSE 378
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDalQERREALQRLAEyswdeidvaSAEREIAELEAEL----ERLDASSDDLAALE 691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  379 ETADLL-AEKAQITEEEAKL------LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLAlkmAEESERRAKEA 451
Cdd:COG4913   692 EQLEELeAELEELEEELDELkgeigrLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA---ALGDAVERELR 768

                         170       180
                  ....*....|....*....|....
gi 356582398  452 DQLKQDLQEAREAERRAKQKLLEI 475
Cdd:COG4913   769 ENLEERIDALRARLNRAEEELERA 792
Caldesmon pfam02029
Caldesmon;
309-475 7.05e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.08  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQM--------------KEEATMANEAL 374
Cdd:pfam02029 168 EVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTtkrrqgglsqsqerEEEAEVFLEAE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  375 MRSEETADLLAEKAqitEEEAKLLAQKAAEAEQEMQRIKataiRTEEEKRlmeqKVLEAEVLALKmAEESERRAKEAD-- 452
Cdd:pfam02029 248 QKLEELRRRRQEKE---SEEFEKLRQKQQEAELELEELK----KKREERR----KLLEEEEQRRK-QEEAERKLREEEek 315

                         170       180
                  ....*....|....*....|....*.
gi 356582398  453 -QLKQDLQEAR--EAERRakQKLLEI 475
Cdd:pfam02029 316 rRMKEEIERRRaeAAEKR--QKLPED 339
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 314-474 7.27e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 39.22  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  314 DSLEVQQMKAQAREEKARKQMERQRLAREKQMR-EEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITE 392
Cdd:pfam05262 175 DSISDKKVVEALREDNEKGVNFRRDMTDLKEREsQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  393 EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVL------ALKMAEESERRAKEADQLKQDLQEAREAER 466
Cdd:pfam05262 255 QEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALkakdhkAFDLKQESKASEKEAEDKELEAQKKREPVA 334


                  ....*...
gi 356582398  467 RAKQKLLE 474
Cdd:pfam05262 335 EDLQKTKP 342
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 308-419 8.49e-03

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.33  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  308 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEK 387
Cdd:pfam05672  35 LEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEA 114

                          90       100       110
                  ....*....|....*....|....*....|..
gi 356582398  388 AQITEEEAKLLAQKAAEAEQEMQRIKATAIRT 419
Cdd:pfam05672 115 ERQRQEREKIMQQEEQERLERKKRIEEIMKRT 146
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 337-479 8.50e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 38.67  E-value: 8.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  337 QRLAREKQMREEAERTRDELERRLLQMKEEATmanealmrseetADLLAEKAQITEEEAKLLAQKAA-EAEQEMQRIKat 415
Cdd:TIGR02794  50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAE------------KQRAAEQARQKELEQRAAAEKAAkQAEQAAKQAE-- 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356582398  416 airtEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKP 479
Cdd:TIGR02794 116 ----EKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA 175
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 325-414 9.21e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 37.06  E-value: 9.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 325 AREEKARKQME---RQRLAREKQMREEAERTRDELERRLLQMKEEAtmanealmrseetadllaeKAQITEEEAKLLAQK 401
Cdd:PRK05759  45 AAAERAKKELElaqAKYEAQLAEARAEAAEIIEQAKKRAAQIIEEA-------------------KAEAEAEAARIKAQA 105

                         90
                 ....*....|...
gi 356582398 402 AAEAEQEMQRIKA 414
Cdd:PRK05759 106 QAEIEQERKRARE 118
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 308-409 9.60e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 9.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 308 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKqmrEEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEK 387
Cdd:COG3883  135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211

                         90       100
                 ....*....|....*....|..
gi 356582398 388 AQITEEEAKLLAQKAAEAEQEM 409
Cdd:COG3883  212 AAAAAAAAAAAAAAAAAAAAAA 233
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
316-465 9.61e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 9.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398 316 LEVQQMKAQAREEKARKQMERQRLA----REKQMREEAERTRDELERRLLQMKEEATMANEALMRseetadLLAEKAQIT 391
Cdd:COG3206  231 ARAELAEAEARLAALRAQLGSGPDAlpelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA------LRAQIAALR 304

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356582398 392 EEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAE-ESERRAKEA--DQLKQDLQEAREAE 465
Cdd:COG3206  305 AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEVARElyESLLQRLEEARLAE 381
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 309-412 9.74e-03

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


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 37.71  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  309 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 388
Cdd:pfam09756   1 KKLGAKKRAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEKLKS 80

                          90       100
                  ....*....|....*....|....
gi 356582398  389 QITEEEAKLLAQKAAEAEQEMQRI 412
Cdd:pfam09756  81 QFVVEEEGTDKLSAEDESQLLEDF 104
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 308-474 9.83e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.36  E-value: 9.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  308 MRRRKADSLEVQQMKAQAREEKARKQMERQR-LAREKQMREEAERTRDELERRLLQMKEEATMANEALMrseetaDLLAE 386
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEkLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL------EYLKE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582398  387 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQ---KVLEAEVLA---LKMAEESERRAKEADQLKQDLQE 460
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDElraKLYQEEQERkerQKEREEAEKKARQRQELQQAREE 243

                         170
                  ....*....|....
gi 356582398  461 AREAERRAKQKLLE 474
Cdd:pfam13868 244 QIELKERRLAEEAE 257
 
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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