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Conserved domains on  [gi|1034629014|ref|XP_016884298|]
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merlin isoform X1 [Homo sapiens]

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 ...
 178-274 2.58e-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: 202.12  E-value: 2.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 178 MYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 257
Cdd:cd13194     1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                          90
                  ....*....|....*..
gi 1034629014 258 ILQLCIGNHDLFMRRRK 274
Cdd:cd13194    81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1-184 1.78e-57

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: 190.58  E-value: 1.78e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014    1 MKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVLDHDVsKEEPVTFHFLAKFYPENaEEELVQEITQH 78
Cdd:smart00295  18 SSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVKFYPPD-PNQLKEDPTRL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014   79 -LFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINlyQMTPEMWEERITAWYAE 156
Cdd:smart00295  96 nLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD--SRKLKEWRERIVELHKE 173

                          170       180
                   ....*....|....*....|....*...
gi 1034629014  157 HRGRARDEAEMEYLKIAQDLEMYGVNYF 184
Cdd:smart00295 174 LIGLSPEEAKLKYLELARKLPTYGVELF 201
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 480-557 1.57e-25

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: 99.97  E-value: 1.57e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629014 480 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSdRGGSSKHNTIKKLTLQSAKSRVAFFEEL 557
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENV-RQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 308-427 1.83e-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: 98.45  E-value: 1.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 308 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 387
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034629014 388 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 427
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
PLN03086 super family cl29366
PRLI-interacting factor K; Provisional
 269-329 2.34e-03

PRLI-interacting factor K; Provisional


The actual alignment was detected with superfamily member PLN03086:

Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.63  E-value: 2.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629014 269 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 329
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 ...
 178-274 2.58e-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: 202.12  E-value: 2.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 178 MYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 257
Cdd:cd13194     1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                          90
                  ....*....|....*..
gi 1034629014 258 ILQLCIGNHDLFMRRRK 274
Cdd:cd13194    81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1-184 1.78e-57

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: 190.58  E-value: 1.78e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014    1 MKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVLDHDVsKEEPVTFHFLAKFYPENaEEELVQEITQH 78
Cdd:smart00295  18 SSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVKFYPPD-PNQLKEDPTRL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014   79 -LFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINlyQMTPEMWEERITAWYAE 156
Cdd:smart00295  96 nLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD--SRKLKEWRERIVELHKE 173

                          170       180
                   ....*....|....*....|....*...
gi 1034629014  157 HRGRARDEAEMEYLKIAQDLEMYGVNYF 184
Cdd:smart00295 174 LIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 1-65 6.24e-39

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: 137.13  E-value: 6.24e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629014   1 MKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPE 65
Cdd:cd17186    20 MKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQDVPKEEPVTFHFLAKFYPE 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 68-184 4.25e-34

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 125.07  E-value: 4.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  68 EEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWE 147
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034629014 148 ERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 184
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C pfam09380
FERM C-terminal PH-like domain;
188-273 6.18e-28

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.95  E-value: 6.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 188 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 266
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 1034629014 267 DLFMRRR 273
Cdd:pfam09380  79 TFFRLRR 85
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 480-557 1.57e-25

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: 99.97  E-value: 1.57e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629014 480 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSdRGGSSKHNTIKKLTLQSAKSRVAFFEEL 557
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENV-RQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 308-427 1.83e-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: 98.45  E-value: 1.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 308 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 387
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034629014 388 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 427
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-438 7.52e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.05  E-value: 7.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 272 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 351
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 352 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 431
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                  ....*..
gi 1034629014 432 QKLLEIA 438
Cdd:COG1196   435 EEEEEEE 441
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 281-440 1.58e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 62.90  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 281 QQMKAQAREEKARKQMERQRlAREKQMREEAErtrdelERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 360
Cdd:PRK09510   69 QQQKSAKRAEEQRKKKEQQQ-AEELQQKQAAE------QERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 361 AQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 439
Cdd:PRK09510  142 AAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216


                  .
gi 1034629014 440 K 440
Cdd:PRK09510  217 K 217
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 279-440 4.21e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 4.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  279 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 358
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  359 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 438
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907


                   ..
gi 1034629014  439 TK 440
Cdd:TIGR02168  908 SK 909
PTZ00121 PTZ00121
MAEBL; Provisional
 272-517 1.89e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQAREEkARKQMERQRLAREKQMREEAERTRDELERRllqmKEEATMANEALMRSEEtADLLAEKAQ 351
Cdd:PTZ00121  1430 KKKADEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKADEAKKKAEE-AKKKADEAK 1503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  352 ITEEEAKLL--------AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 423
Cdd:PTZ00121  1504 KAAEAKKKAdeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  424 REAERRAKQKLLEIAtkPTYPPMNPIPAPLPPDIPSFNLIGDSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNE 503
Cdd:PTZ00121  1584 EEAKKAEEARIEEVM--KLYEEEKKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          250
                   ....*....|....
gi 1034629014  504 LKTEIEALKLKERE 517
Cdd:PTZ00121  1659 NKIKAAEEAKKAEE 1672
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 264-525 3.08e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  264 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 336
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  337 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 410
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  411 KEADQLKQDLQEAREAERRAKQKLLEIATkpTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEY 490
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034629014  491 MEKSKH-LQEQLNELKTEIEALKLKERETALDILHN 525
Cdd:TIGR02168  906 LESKRSeLRRELEELREKLAQLELRLEGLEVRIDNL 941
growth_prot_Scy NF041483
polarized growth protein Scy;
274-427 6.19e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 49.44  E-value: 6.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  274 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 353
Cdd:NF041483   490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  354 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRLM--EQKV----LEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 427
Cdd:NF041483   560 EETERAIAARQAEAAEELTR-----LHTEAEERLTaaEEALadarAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
growth_prot_Scy NF041483
polarized growth protein Scy;
279-440 1.30e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 48.28  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  279 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 358
Cdd:NF041483   583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  359 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 433
Cdd:NF041483   660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                   ....*..
gi 1034629014  434 LLEIATK 440
Cdd:NF041483   740 LLASARK 746
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 269-511 9.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 9.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 269 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 348
Cdd:COG1196   565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 349 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAE---VLALKMAEESERRAKEADQLKQDLQEARE 425
Cdd:COG1196   645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEElelEEALLAEEEEERELAEAEEERLEEELEEE 724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 426 AERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPsfnligDSLSFDFKDTDMKRLSMEIEK-EKV------EY---MEKSK 495
Cdd:COG1196   725 ALEEQLEAEREELLEELLEEEELLEEEALEELP------EPPDLEELERELERLEREIEAlGPVnllaieEYeelEERYD 798

                         250
                  ....*....|....*.
gi 1034629014 496 HLQEQLNELKTEIEAL 511
Cdd:COG1196   799 FLSEQREDLEEARETL 814
growth_prot_Scy NF041483
polarized growth protein Scy;
295-436 3.54e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.66  E-value: 3.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  295 QMERQRLARE-KQMREEA----ERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAA--- 365
Cdd:NF041483   439 QEEARRLRGEaEQLRAEAvaegERIRGEARREAVQQIEEaARTAEELLTKAKADADELRSTATAESERVRTEAIERAttl 518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  366 --EAEQEMQRIKATA--IRTEEEKRLMEQKVlEAEVLALKMAEESE-----RRAKEADQLKQDLQEAREAERRAKQKLLE 436
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 ...
 291-382 7.97e-04

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.73  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 291 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 369
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106

                          90
                  ....*....|...
gi 1034629014 370 EMQRIKAtAIRTE 382
Cdd:cd06503   107 EKEKALA-ELRKE 118
growth_prot_Scy NF041483
polarized growth protein Scy;
283-428 2.24e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  283 MKAQARE--EKARKQMERQRlareKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAqiTEEEAKL- 359
Cdd:NF041483   518 LRRQAEEtlERTRAEAERLR----AEAEEQAEEVRAAAERAARELREETERAIAA--RQAEAAEELTRLH--TEAEERLt 589

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  360 -----LAQKAAEAE-------QEMQRIKATAirTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDL--QEARE 425
Cdd:NF041483   590 aaeeaLADARAEAErirreaaEETERLRTEA--AERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLrsEAAAE 667


                   ...
gi 1034629014  426 AER 428
Cdd:NF041483   668 AER 670
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 269-329 2.34e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.63  E-value: 2.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629014 269 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 329
Cdd:PLN03086    3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 267-459 4.32e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.00  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 267 DLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 346
Cdd:NF033838  189 ELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 347 AEKAQIT----EEEAKLLA----------------QKAAEAEQEMQRIKATAIRTEEEKRL----------------MEQ 390
Cdd:NF033838  269 VLGEPATpdkkENDAKSSDssvgeetlpspslkpeKKVAEAEKKVEEAKKKAKDQKEEDRRnyptntyktleleiaeSDV 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 391 KVLEAEVLALK--------------MAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLP-P 455
Cdd:NF033838  349 KVKEAELELVKeeakeprneekikqAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPqP 428


                  ....
gi 1034629014 456 DIPS 459
Cdd:NF033838  429 EKPA 432
 
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 ...
 178-274 2.58e-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: 202.12  E-value: 2.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 178 MYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 257
Cdd:cd13194     1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                          90
                  ....*....|....*..
gi 1034629014 258 ILQLCIGNHDLFMRRRK 274
Cdd:cd13194    81 ILDLCMGNHELYMRRRK 97
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1-184 1.78e-57

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: 190.58  E-value: 1.78e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014    1 MKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA--WLKMDKKVLDHDVsKEEPVTFHFLAKFYPENaEEELVQEITQH 78
Cdd:smart00295  18 SSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLrhWLDPAKTLLDQDV-KSEPLTLYFRVKFYPPD-PNQLKEDPTRL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014   79 -LFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVH-KRGFLAQEELLPKRVINlyQMTPEMWEERITAWYAE 156
Cdd:smart00295  96 nLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQLLD--SRKLKEWRERIVELHKE 173

                          170       180
                   ....*....|....*....|....*...
gi 1034629014  157 HRGRARDEAEMEYLKIAQDLEMYGVNYF 184
Cdd:smart00295 174 LIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_F1_Merlin cd17186
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in merlin and ...
 1-65 6.24e-39

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: 137.13  E-value: 6.24e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629014   1 MKWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPE 65
Cdd:cd17186    20 MKWKGKDLFDLVCRTIGLRETWYFGLQYTDsKGTVAWLKMDKKVLDQDVPKEEPVTFHFLAKFYPE 85
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 68-184 4.25e-34

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 125.07  E-value: 4.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  68 EEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWE 147
Cdd:pfam00373   3 ELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKELE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034629014 148 ERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 184
Cdd:pfam00373  81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 1-65 2.20e-33

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: 122.00  E-value: 2.20e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629014   1 MKWKGKDLFDLVCRTLGLRETWFFGLQYTIKD-TVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPE 65
Cdd:cd17097    18 PKAKGRELFDLVCRTIGLRETWYFGLQYENKKgRVAWLKPDKKVLTQDVSKNNTLKFFFLVKFYPE 83
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 76-176 4.34e-30

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


Pssm-ID: 271216  Cd Length: 99  Bit Score: 113.50  E-value: 4.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  76 TQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINlyQMTPEMWEERITAWYA 155
Cdd:cd14473     1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLK--QRKPEEWEKRIVELHK 78

                          90       100
                  ....*....|....*....|.
gi 1034629014 156 EHRGRARDEAEMEYLKIAQDL 176
Cdd:cd14473    79 KLRGLSPAEAKLKYLKIARKL 99
FERM_C pfam09380
FERM C-terminal PH-like domain;
188-273 6.18e-28

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 106.95  E-value: 6.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 188 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 266
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 1034629014 267 DLFMRRR 273
Cdd:pfam09380  79 TFFRLRR 85
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 480-557 1.57e-25

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: 99.97  E-value: 1.57e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629014 480 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSdRGGSSKHNTIKKLTLQSAKSRVAFFEEL 557
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENV-RQGRDKYKTLRKIRQGNTKQRVDFFEEL 77
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 308-427 1.83e-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: 98.45  E-value: 1.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 308 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 387
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034629014 388 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 427
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
FERM_F1_ERM cd17187
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 5-65 1.76e-23

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: 94.46  E-value: 1.76e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629014   5 GKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPE 65
Cdd:cd17187    22 GKQLFDQVVKTIGLREIWFFGLQYVdSKGYSTWLKLNKKVLSQDVKKENPLQFKFRAKFYPE 83
FERM_F1_Ezrin cd17239
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Ezrin and ...
 5-65 9.46e-19

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: 80.80  E-value: 9.46e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629014   5 GKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPE 65
Cdd:cd17239    24 GKQLFDQVVKTIGLREVWYFGLQYVdNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPE 85
FERM_F1_Moesin cd17237
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in moesin and ...
 5-65 2.27e-17

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: 77.09  E-value: 2.27e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629014   5 GKDLFDLVCRTLGLRETWFFGLQYtiKDTVA---WLKMDKKVLDHDVSKEEPVTFHFLAKFYPE 65
Cdd:cd17237    23 GKQLFDQVVKTIGLREVWFFGLQY--QDTKGfstWLKLNKKVTAQDVRKESPLLFKFRAKFYPE 84
FERM_F1_Radixin cd17238
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in radixin and ...
 5-65 3.55e-17

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: 76.31  E-value: 3.55e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629014   5 GKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPE 65
Cdd:cd17238    22 GKQLFDQVVKTVGLREVWFFGLQYVdSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPE 83
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 180-270 2.25e-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: 74.33  E-value: 2.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 180 GVNYFAIRNK--KGTELLLGVDALGLHIYDPENRlTPKISFPWNEIRNISYS-DKEFTIKPLDK-KIDVFKFNSSKlRVN 255
Cdd:cd00836     1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEdKQSKLLFQTPS-RQA 78

                          90
                  ....*....|....*
gi 1034629014 256 KLILQLCIGNHDLFM 270
Cdd:cd00836    79 KEIWKLIVGYHRFLL 93
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-438 7.52e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.05  E-value: 7.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 272 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 351
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 352 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 431
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                  ....*..
gi 1034629014 432 QKLLEIA 438
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 ...
 180-275 5.19e-14

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: 68.53  E-value: 5.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 180 GVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKK--------------IDVF 245
Cdd:cd13191     1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRrnshrsrrtfqsssVSVH 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034629014 246 KFNSSKLRVNKLILQLCIGNHDLFMRRRKA 275
Cdd:cd13191    81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQS 110
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 2-62 1.23e-12

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: 63.38  E-value: 1.23e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629014   2 KWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVLDHdVSKEEPVTFHFLAKF 62
Cdd:cd01765    20 KATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKhWLDLDKKISKQ-LKRSGPYQFYFRVKF 80
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-440 2.26e-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: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 350
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 351 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 430
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                         170
                  ....*....|
gi 1034629014 431 KQKLLEIATK 440
Cdd:COG1196   469 LEEAALLEAA 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 279-440 5.86e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 5.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 279 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 358
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 359 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 438
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399


                  ..
gi 1034629014 439 TK 440
Cdd:COG1196   400 AQ 401
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 267-438 9.34e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.04  E-value: 9.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 267 DLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 346
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 347 AEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREA 426
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         170
                  ....*....|..
gi 1034629014 427 ERRAKQKLLEIA 438
Cdd:COG1196   395 AAELAAQLEELE 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 278-440 1.77e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 278 LEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEA 357
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 358 KLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 437
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433


                  ...
gi 1034629014 438 ATK 440
Cdd:COG1196   434 EEE 436
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-440 2.03e-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: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 350
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 351 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 430
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         170
                  ....*....|
gi 1034629014 431 KQKLLEIATK 440
Cdd:COG1196   483 LEELAEAAAR 492
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-439 2.54e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.50  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 350
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 351 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 430
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412


                  ....*....
gi 1034629014 431 KQKLLEIAT 439
Cdd:COG1196   413 LERLERLEE 421
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-440 2.63e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.50  E-value: 2.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 272 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQmREEAErtRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 351
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLE-ELEEE--LAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 352 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 431
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441


                  ....*....
gi 1034629014 432 QKLLEIATK 440
Cdd:COG1196   442 EALEEAAEE 450
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-440 9.76e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 9.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREkqmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 350
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 351 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 430
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                         170
                  ....*....|
gi 1034629014 431 KQKLLEIATK 440
Cdd:COG1196   448 AEEEAELEEE 457
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-440 1.33e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.19  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 350
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 351 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 430
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                         170
                  ....*....|
gi 1034629014 431 KQKLLEIATK 440
Cdd:COG1196   462 LELLAELLEE 471
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 281-440 1.58e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 62.90  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 281 QQMKAQAREEKARKQMERQRlAREKQMREEAErtrdelERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 360
Cdd:PRK09510   69 QQQKSAKRAEEQRKKKEQQQ-AEELQQKQAAE------QERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 361 AQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 439
Cdd:PRK09510  142 AAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216


                  .
gi 1034629014 440 K 440
Cdd:PRK09510  217 K 217
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 6-66 2.97e-10

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: 56.82  E-value: 2.97e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629014   6 KDLFDLVCRTLGLRETWFFGLQYtIKDT--VAWLKMDKKVLDHDVSKEE-PVTFHFLAKFYPEN 66
Cdd:cd17200    26 RELLDLVASHFNLKEKEYFGITF-IDDTgqSNWLQLDHRVLDHDLPKKSgPVTLYFAVRFYIES 88
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 2-66 7.55e-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: 55.75  E-value: 7.55e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629014   2 KWKGKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHDVSK---EEPVTFHFLAKFYPEN 66
Cdd:cd17103    22 KLLAGDLLDLVASHFNLKEKEYFGLAYEDeTGHYNWLQLDKRVLDHEFPKkwsSGPLVLHFAVKFYVES 90
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 273-438 1.35e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 273 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQI 352
Cdd:COG1196   213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 353 TEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQ 432
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372


                  ....*.
gi 1034629014 433 KLLEIA 438
Cdd:COG1196   373 ELAEAE 378
PTZ00121 PTZ00121
MAEBL; Provisional
 272-517 1.85e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 1.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-EATMANEALMRSEETADLLAEKA 350
Cdd:PTZ00121  1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEA 1612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  351 QiTEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESeRRAKEADQLKQDLQEAREAERRA 430
Cdd:PTZ00121  1613 K-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-KKAEEDKKKAEEAKKAEEDEKKA 1690

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  431 KQKLLeiatkptyppmnpipaplppdipsfnligdslsfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEA 510
Cdd:PTZ00121  1691 AEALK------------------------------------KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734


                   ....*..
gi 1034629014  511 LKLKERE 517
Cdd:PTZ00121  1735 AKKEAEE 1741
PTZ00121 PTZ00121
MAEBL; Provisional
 272-433 3.39e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 3.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQARE----EKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 344
Cdd:PTZ00121  1277 ARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAA 1356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  345 LLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEADQLKQDLQEAR 424
Cdd:PTZ00121  1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAEEKKKAD 1434


                   ....*....
gi 1034629014  425 EAERRAKQK 433
Cdd:PTZ00121  1435 EAKKKAEEA 1443
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 271-433 3.56e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 58.66  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 350
Cdd:PRK09510   81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 351 QITEEEAKLLAQKAAEAEQEmQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 430
Cdd:PRK09510  161 KKAAAEAKKKAEAEAAKKAA-AEAKKKAEAEAAAKAAAEAKK-KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAA 238


                  ...
gi 1034629014 431 KQK 433
Cdd:PRK09510  239 EKA 241
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 270-440 8.85e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.51  E-value: 8.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 270 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMRSEETADLLAEK 349
Cdd:PRK09510   67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEEAAKQAALKQKQAEEAAAKAAAA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 350 AQI-TEEEAKLLAQKAAEAEQEMqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 428
Cdd:PRK09510  145 AKAkAEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA 221

                         170
                  ....*....|..
gi 1034629014 429 RAKQKLLEIATK 440
Cdd:PRK09510  222 EAKAAAAKAAAE 233
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 4-48 1.24e-08

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: 51.44  E-value: 1.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHDV 48
Cdd:pfam09379  18 TGQVLLDQVCNHLNLKEKDYFGLQFLdDNGEHRWLDLSKRLSKQAP 63
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 5-64 1.44e-08

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: 51.83  E-value: 1.44e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629014   5 GKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHdVSKEEPVTFHFLAKFYP 64
Cdd:cd17098    23 GEVLFDQVCKHLNLLESDYFGLEFTdPEGNKCWLDPEKPILRQ-VKRPKDVVFKFVVKFYT 82
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 178-269 2.91e-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: 51.54  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 178 MYGVNYFAIRNKKGTELLLGVDALGLHIYdpENRLtpKIS-FPWNEIRNISYSDKEFTI----KPLDKKIDVFKFNSSKL 252
Cdd:cd13189     1 LYGVELHSARDSNNLELQIGVSSAGILVF--QNGI--RINtFPWSKIVKISFKRKQFFIqlrrEPNESRDTILGFNMLSY 76

                          90
                  ....*....|....*..
gi 1034629014 253 RVNKLILQLCIGNHDLF 269
Cdd:cd13189    77 RACKNLWKSCVEHHTFF 93
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 279-440 4.21e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 4.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  279 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 358
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  359 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 438
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907


                   ..
gi 1034629014  439 TK 440
Cdd:TIGR02168  908 SK 909
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 4-66 4.81e-08

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: 50.80  E-value: 4.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQYTIKDT-VAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPEN 66
Cdd:cd17107    28 KGSVVLDVVFQHLNLLETDYFGLRYIDRQHqTHWLDPAKTLSEQLKLIGPPYTLYFGVKFYAED 91
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 179-269 6.44e-08

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


Pssm-ID: 270005  Cd Length: 94  Bit Score: 50.40  E-value: 6.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 179 YGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK-------PLDKKIDvFKFNSSk 251
Cdd:cd13184     1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRIN---RFAWPKVLKISYKRNNFYIKirpgefeQYETTIG-FKLPNH- 75

                          90
                  ....*....|....*...
gi 1034629014 252 lRVNKLILQLCIGNHDLF 269
Cdd:cd13184    76 -RAAKRLWKVCVEHHTFF 92
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 273-445 7.24e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.84  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 273 RKADSLEVQQMKAQAREEKARKQMERQRlarekqmrEEAERTRDELERRLLQMKEEATMAN--EALMRSEETADLL---- 346
Cdd:COG3883    51 EEYNELQAELEALQAEIDKLQAEIAEAE--------AEIEERREELGERARALYRSGGSVSylDVLLGSESFSDFLdrls 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 347 -------AEKAQITE--EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLK 417
Cdd:COG3883   123 alskiadADADLLEElkADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202

                         170       180
                  ....*....|....*....|....*...
gi 1034629014 418 QDLQEAREAERRAKQKLLEIATKPTYPP 445
Cdd:COG3883   203 AELAAAEAAAAAAAAAAAAAAAAAAAAA 230
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 165-244 8.52e-08

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


Pssm-ID: 270013  Cd Length: 105  Bit Score: 50.47  E-value: 8.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 165 AEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTI---KPLDKK 241
Cdd:cd13192     1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFILhvmQKEEKK 77


                  ...
gi 1034629014 242 IDV 244
Cdd:cd13192    78 HTL 80
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 4-63 1.69e-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: 1.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQYTikDTVA---WLKMDKKVLDHdVSKEEPVTFHFLAKFY 63
Cdd:cd17102    23 KGQFLLDYVCNYLNLLEKDYFGLRYV--DTEKqrhWLDPNKSIYKQ-LKGVPPYVLCFRVKFY 82
PTZ00121 PTZ00121
MAEBL; Provisional
 272-517 1.89e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQAREEkARKQMERQRLAREKQMREEAERTRDELERRllqmKEEATMANEALMRSEEtADLLAEKAQ 351
Cdd:PTZ00121  1430 KKKADEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKADEAKKKAEE-AKKKADEAK 1503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  352 ITEEEAKLL--------AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 423
Cdd:PTZ00121  1504 KAAEAKKKAdeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  424 REAERRAKQKLLEIAtkPTYPPMNPIPAPLPPDIPSFNLIGDSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNE 503
Cdd:PTZ00121  1584 EEAKKAEEARIEEVM--KLYEEEKKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          250
                   ....*....|....
gi 1034629014  504 LKTEIEALKLKERE 517
Cdd:PTZ00121  1659 NKIKAAEEAKKAEE 1672
PTZ00121 PTZ00121
MAEBL; Provisional
 267-530 2.53e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  267 DLFMRRRKADSL---EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR-----LLQMKEEATMANEALMR 338
Cdd:PTZ00121  1575 DKNMALRKAEEAkkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkveqLKKKEAEEKKKAEELKK 1654

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  339 SEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQkVLEAEVLALKMAEESeRRAKEADQLK- 417
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEEL-KKAEEENKIKa 1732

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  418 -QDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDtdmKRLSMEIEKEKVEYMEKSKH 496
Cdd:PTZ00121  1733 eEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED---EKRRMEVDKKIKDIFDNFAN 1809

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1034629014  497 LQEQLNELKTEIEALKLKERETALDILHNENSDR 530
Cdd:PTZ00121  1810 IIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 277-433 3.59e-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: 52.54  E-value: 3.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 277 SLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAtmANEALMRSEETADLLAEKAQITEEE 356
Cdd:TIGR02794  46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA--AAEKAAKQAEQAAKQAEEKQKQAEE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 357 AKLL----AQKAAEAEQEMQRIKATAIRTEEEKrlmeqkvleaevlALKMAEESERRAKEAD-QLKQDLQEAREAERRAK 431
Cdd:TIGR02794 124 AKAKqaaeAKAKAEAEAERKAKEEAAKQAEEEA-------------KAKAAAEAKKKAEEAKkKAEAEAKAKAEAEAKAK 190


                  ..
gi 1034629014 432 QK 433
Cdd:TIGR02794 191 AE 192
PTZ00121 PTZ00121
MAEBL; Provisional
 272-432 3.69e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 3.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQAREEKARKQMERQRLA------REKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADl 345
Cdd:PTZ00121  1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeaakaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK- 1392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  346 lAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEARE 425
Cdd:PTZ00121  1393 -ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471


                   ....*..
gi 1034629014  426 AERRAKQ 432
Cdd:PTZ00121  1472 ADEAKKK 1478
PRK12704 PRK12704
phosphodiesterase; Provisional
 272-431 4.73e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.47  E-value: 4.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 272 RRKADSLEVQQMKAQARE--EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEET------- 342
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRilEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENldrklel 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 343 -----ADLLAEKAQITEEEAKLLAQKA------AEAEQEMQRIkatAIRTEEE--KRLMEQKVLEAEVLALKMAEESERR 409
Cdd:PRK12704  105 lekreEELEKKEKELEQKQQELEKKEEeleeliEEQLQELERI---SGLTAEEakEILLEKVEEEARHEAAVLIKEIEEE 181

                         170       180
                  ....*....|....*....|..
gi 1034629014 410 AKEadqlkqdlqearEAERRAK 431
Cdd:PRK12704  182 AKE------------EADKKAK 191
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 179-271 7.04e-07

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


Pssm-ID: 270009  Cd Length: 91  Bit Score: 47.28  E-value: 7.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 179 YGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKisFPWNEIRNISYSDKEFTIKPLDKKIDV-FKFNSSklRVNKL 257
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVF--FRWEDIKNVINHKRTFSIECQNSEETVqFQFEDA--ETAKY 76

                          90
                  ....*....|....
gi 1034629014 258 ILQLCIGNHDLFMR 271
Cdd:cd13188    77 VWKLCVLQHKFYRQ 90
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 272-432 7.76e-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: 7.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 272 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETAD--LLAEK 349
Cdd:TIGR02794  69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAErkAKEEA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 350 AQITEEEAKllAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQDLQEAR---EA 426
Cdd:TIGR02794 149 AKQAEEEAK--AKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKA-KAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAaaaEA 225


                  ....*.
gi 1034629014 427 ERRAKQ 432
Cdd:TIGR02794 226 ERKADE 231
PTZ00121 PTZ00121
MAEBL; Provisional
 272-433 9.68e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 9.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEvQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR---------LLQMKEEATMANEALMRSEET 342
Cdd:PTZ00121  1404 KKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeeakkaeeAKKKAEEAKKADEAKKKAEEA 1482

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  343 ADllAEKAQITEEEAKLLAQKAAEAEQEMQriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRaKEADQLKQdLQE 422
Cdd:PTZ00121  1483 KK--ADEAKKKAEEAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK-KKADELKK-AEE 1556

                          170
                   ....*....|...
gi 1034629014  423 AREAE--RRAKQK 433
Cdd:PTZ00121  1557 LKKAEekKKAEEA 1569
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 2-63 1.10e-06

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: 46.57  E-value: 1.10e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629014   2 KWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVlDHDVSKEEPVTFHFLAKFY 63
Cdd:cd17108    20 KAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQhWLDPTKKI-KKQVKIGPPYTLRFRVKFY 81
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 1-66 1.30e-06

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: 46.78  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014   1 MKWKGKDLFDLVCRTLGLRETWFFGLQYtIKDT-------------VA---WLKMDKKVLDHdvsKEEPVTFHFLAKFYP 64
Cdd:cd17101    20 VKTTVQDLFDQVCDHLGLQETELFGLAV-LKDGeyffldpdtklskYApkgWKSEAKKGLKG---GKPVFTLYFRVKFYV 95


                  ..
gi 1034629014  65 EN 66
Cdd:cd17101    96 DN 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 279-431 1.41e-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: 51.21  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  279 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 358
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629014  359 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 431
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 279-436 1.67e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.58  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 279 EVQQMKAQAREEKaRKQMERQRLAREKQmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 358
Cdd:PRK09510  105 QLEKERLAAQEQK-KQAEEAAKQAALKQ-KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 359 LLAQKAAEAEQ---EMQRIKATAIRTEEEKRLMEQKvleAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 435
Cdd:PRK09510  183 AKKKAEAEAAAkaaAEAKKKAEAEAKKKAAAEAKKK---AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259


                  .
gi 1034629014 436 E 436
Cdd:PRK09510  260 D 260
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 260-459 2.14e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.51  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 260 QLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQR---LAREKQM----REEAERTRDELErrlLQMKEEATMA 332
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRleeQERQQQVerlrQQEEERKRKKLE---LEKEKRDRKR 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 333 NEALMRSEETADLLAEKAQITEEEAKllaQKAAEAEQEMQRikaTAIRTEEEKRLM-EQKVLEAEVLALKMAEESERRAK 411
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERK---RKLLEKEMEERQ---KAIYEEERRREAeEERRKQQEMEERRRIQEQMRKAT 562

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629014 412 EADQLKQDLQEARE-----AERRAKQKLLEIATKPTypPMNPIPAP-----LPPDIPS 459
Cdd:pfam17380 563 EERSRLEAMEREREmmrqiVESEKARAEYEATTPIT--TIKPIYRPriseyQPPDVES 618
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 287-438 2.27e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 287 AREEKARKQME--RQRLAR--------EKQM---REEAERTR------DELERR-----LLQMKE-EATMANEALMRSEE 341
Cdd:COG1196   172 ERKEEAERKLEatEENLERledilgelERQLeplERQAEKAEryrelkEELKELeaellLLKLRElEAELEELEAELEEL 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 342 TADLLAEKAQITEEEAKL---------LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKE 412
Cdd:COG1196   252 EAELEELEAELAELEAELeelrleleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                         170       180
                  ....*....|....*....|....*.
gi 1034629014 413 ADQLKQDLQEAREAERRAKQKLLEIA 438
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAE 357
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 2-66 2.75e-06

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: 45.73  E-value: 2.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629014   2 KWKGKDLFDLVCRTLGLRETWFFGLQYTIKDT-VAWLKMDKKVLDHDVSKEE-PVTFHFLAKFYPEN 66
Cdd:cd17199    22 KLLAKELLDLVASHFNLKEKEYFGIAFTDETGhLNWLQLDRRVLEHDFPKKSgPVVLYFCVRFYIES 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 264-525 3.08e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  264 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 336
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  337 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 410
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  411 KEADQLKQDLQEAREAERRAKQKLLEIATkpTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEY 490
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034629014  491 MEKSKH-LQEQLNELKTEIEALKLKERETALDILHN 525
Cdd:TIGR02168  906 LESKRSeLRRELEELREKLAQLELRLEGLEVRIDNL 941
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-440 3.36e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 272 RRKADSLEVQqmKAQAREEKARKQMERQRLAREKQMR-EEAERTRDELERRLLQMKEEATMANEALmrSEETADLLAEKA 350
Cdd:COG1196   199 ERQLEPLERQ--AEKAERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAEL--AELEAELEELRL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 351 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvLALKMAEESERRAKEADQLKQDLQEAREAERRA 430
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         170
                  ....*....|
gi 1034629014 431 KQKLLEIATK 440
Cdd:COG1196   354 EEAEAELAEA 363
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 180-275 3.38e-06

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: 45.78  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 180 GVNYFAI-RNKK--GTELLLGVDALGLHIYDPEN-RLTPKISFPWNEIRNISYSDKEFTIKP--LDKKIDVFKFNSSKlr 253
Cdd:cd13187     1 GVHFHRVyREKKssTLSLWLGICSRGIIIYEEKNgARTPVLRFPWRETQKISFDKKKFTIESrgGSGIKHTFYTDSYK-- 78

                          90       100
                  ....*....|....*....|....
gi 1034629014 254 VNKLILQLCIGNH--DLFMRRRKA 275
Cdd:cd13187    79 KSQYLLQLCSAQHkfHIQMRSRQS 102
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 271-528 3.53e-06

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.74  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQM--------REEAERTR-DELERRLLQMKEEATMANEALMRSEE 341
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirqeerKRELERIRqEEIAMEISRMRELERLQMERQQKNER 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 342 TADLL--AEKAQITEEEAKllaQKAAEAEQEMQRIKATA--IRTEEEKRLMEQKVLEAEvlalKMAEESERRAKEADQLK 417
Cdd:pfam17380 394 VRQELeaARKVKILEEERQ---RKIQQQKVEMEQIRAEQeeARQREVRRLEEERAREME----RVRLEEQERQQQVERLR 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 418 QDLQEAR------EAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDT--DMKRLSMEIEKEKVE 489
Cdd:pfam17380 467 QQEEERKrkklelEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQ 546

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034629014 490 YMEKSKHLQEQL---NELKTEIEALKlKERETALDILHNENS 528
Cdd:pfam17380 547 EMEERRRIQEQMrkaTEERSRLEAME-REREMMRQIVESEKA 587
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 289-429 3.71e-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: 46.96  E-value: 3.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 289 EEKARKQMERQRLAREKQMREEAERTRDELERRLLQmKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAE 368
Cdd:pfam05672  10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRK-EELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEER 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629014 369 QEMQRikatairteEEKRLMEQKVLEAEVlalKMAEESERRAKEADQLKQDLQEAREAERR 429
Cdd:pfam05672  89 EQREQ---------EEQERLQKQKEEAEA---KAREEAERQRQEREKIMQQEEQERLERKK 137
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 177-271 4.01e-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: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 177 EMYGVNYFAIRNKK---GTELLLGVDALGLHIYDP-ENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKL 252
Cdd:cd13185     1 EDLNAHLYRLRKSKketPGSVLLGITAKGIQIYQEsDGEQQLLRTFPWSNIGKLSFDRKKFEIRPEGSLRKLTYYTSSDE 80

                          90
                  ....*....|....*....
gi 1034629014 253 RvNKLILQLCIGNHDLFMR 271
Cdd:cd13185    81 K-SKYLLALCRETHQFSMA 98
PTZ00121 PTZ00121
MAEBL; Provisional
 273-517 4.35e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 4.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  273 RKADslEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAlmrseetadllAEKAQI 352
Cdd:PTZ00121  1206 RKAE--EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA-----------RRQAAI 1272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  353 TEEEAKllaqKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKE----ADQLKQDLQEAREAER 428
Cdd:PTZ00121  1273 KAEEAR----KADELKKAEEKKKADEAKKAEEKKKADEAKKKAE--EAKKADEAKKKAEEakkkADAAKKKAEEAKKAAE 1346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  429 RAKQKLLEIATKPTYPPmnpipaplppdipsfnligDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEI 508
Cdd:PTZ00121  1347 AAKAEAEAAADEAEAAE-------------------EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407


                   ....*....
gi 1034629014  509 EALKLKERE 517
Cdd:PTZ00121  1408 DELKKAAAA 1416
PTZ00121 PTZ00121
MAEBL; Provisional
 272-517 4.86e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 4.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQARE------EKARKQMERQRLAREKQMREEAERTRDELERRL--LQMKEEATMANEALMRSEETA 343
Cdd:PTZ00121  1443 AKKADEAKKKAEEAKKAEeakkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAK 1522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  344 DllAEKAQITEEEAKLLAQKAAEAEQEMQRI-KATAIRTEEEKRLMEQKVLEAE--VLALKMAEES----ERRAKEADQL 416
Cdd:PTZ00121  1523 K--ADEAKKAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAkkaeEARIEEVMKL 1600

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  417 K--------QDLQEAREAERRAKQKLLEIATKPTYPPMNPipaplppdipsfnligdslsfdfKDTDMKRLSMEIEKEKV 488
Cdd:PTZ00121  1601 YeeekkmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK-----------------------KEAEEKKKAEELKKAEE 1657

                          250       260
                   ....*....|....*....|....*....
gi 1034629014  489 EYMEKSKHLQEQLNELKTEIEALKLKERE 517
Cdd:PTZ00121  1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
RA_FERM_F0_F1_like cd01768
Ras-associating (RA) domain, FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0/F1 ...
 5-60 5.35e-06

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: 45.62  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014   5 GKDLFDLVCRTLGLR-----------ETWFFGLQYTIKDTVA--------------WLKMDKKV----LDHDVSKEEPVT 55
Cdd:cd01768    26 ARELVAEALERYGLAgspgggpgessCVDAFALCDALGRPAAagvgsgewraehlrVLGDSERPllvqELWRARPGWARR 105


                  ....*
gi 1034629014  56 FHFLA 60
Cdd:cd01768   106 FELRG 110
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
271-442 5.80e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 5.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQARE-----EKARKQMERQRLARE--KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETA 343
Cdd:PRK02224  272 REREELAEEVRDLRERLEEleeerDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 344 DLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQ----- 418
Cdd:PRK02224  352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreael 431

                         170       180
                  ....*....|....*....|....*.
gi 1034629014 419 --DLQEAREAERRAkQKLLEIATKPT 442
Cdd:PRK02224  432 eaTLRTARERVEEA-EALLEAGKCPE 456
growth_prot_Scy NF041483
polarized growth protein Scy;
274-427 6.19e-06

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 49.44  E-value: 6.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  274 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 353
Cdd:NF041483   490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  354 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRLM--EQKV----LEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 427
Cdd:NF041483   560 EETERAIAARQAEAAEELTR-----LHTEAEERLTaaEEALadarAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
272-434 6.21e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 6.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEvqQMKAQARE-EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAEKA 350
Cdd:COG4913    248 REQIELLE--PIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL------ERLEARLD 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  351 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALKMAEESERRA-----KEADQLKQDLQEA 423
Cdd:COG4913    320 ALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRarLEALLAALGLPLPASAEEfaalrAEAAALLEALEEE 399

                          170
                   ....*....|.
gi 1034629014  424 REAERRAKQKL 434
Cdd:COG4913    400 LEALEEALAEA 410
PTZ00121 PTZ00121
MAEBL; Provisional
 272-440 6.50e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 6.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSL----EVQQMKAQAREEKARKQMERQRLAREKQ-----MREEAERTRDELERRllqmKEEATMANEALMRSEET 342
Cdd:PTZ00121  1328 KKKADAAkkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAeaaekKKEEAKKKADAAKKK----AEEKKKADEAKKKAEED 1403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  343 ADLLAEKAQitEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQE 422
Cdd:PTZ00121  1404 KKKADELKK--AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481

                          170
                   ....*....|....*...
gi 1034629014  423 AREAErRAKQKLLEIATK 440
Cdd:PTZ00121  1482 AKKAD-EAKKKAEEAKKK 1498
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
279-440 7.62e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 7.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 279 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEeatmANEALMRSEETADLLAEKAQITEEEAK 358
Cdd:COG4717    75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK----LLQLLPLYQELEALEAELAELPERLEE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 359 LLAQKA--AEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 435
Cdd:COG4717   151 LEERLEelRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                  ....*
gi 1034629014 436 EIATK 440
Cdd:COG4717   231 QLENE 235
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 271-432 1.01e-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: 48.41  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMR-----EEAERTRDELERRLLQMKEEATMANEALMRSEETADL 345
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRlrkqrLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 346 LAEKAQITEEEAKllaqkaaEAEQEMQRIKATAIR-TEEEKRLME----------QKVLEAEVLALKMAEESERRAKEAD 414
Cdd:pfam15709 433 QELQRKKQQEEAE-------RAEAEKQRQKELEMQlAEEQKRLMEmaeeerleyqRQKQEAEEKARLEAEERRQKEEEAA 505

                         170
                  ....*....|....*...
gi 1034629014 415 QLKQDlQEAREAERRAKQ 432
Cdd:pfam15709 506 RLALE-EAMKQAQEQARQ 522
growth_prot_Scy NF041483
polarized growth protein Scy;
279-440 1.30e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 48.28  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  279 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 358
Cdd:NF041483   583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  359 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 433
Cdd:NF041483   660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                   ....*..
gi 1034629014  434 LLEIATK 440
Cdd:NF041483   740 LLASARK 746
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 275-434 1.48e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.13  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  275 ADSLEVQQMKAQARE-EKARKQMERQRLARE--------KQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtADL 345
Cdd:PRK10929   104 TDALEQEILQVSSQLlEKSRQAQQEQDRAREisdslsqlPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQ-AES 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  346 LAEKAQITEEEaklLAQKAAEAEQEMQRIKATAIRTEEEK----------RLMEQKVLEAEvLALkmaEESERRAKEADQ 415
Cdd:PRK10929   183 AALKALVDELE---LAQLSANNRQELARLRSELAKKRSQQldaylqalrnQLNSQRQREAE-RAL---ESTELLAEQSGD 255

                          170
                   ....*....|....*....
gi 1034629014  416 LKQDLQEAREAERRAKQKL 434
Cdd:PRK10929   256 LPKSIVAQFKINRELSQAL 274
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
305-512 1.63e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  305 KQMREEAERTRDELERrLLQMKEEATmANEALMRSEETADLLAEKAQI--TEEEAKLLAQKAAEAEQEMQRIKATAIRTE 382
Cdd:COG4913    238 ERAHEALEDAREQIEL-LEPIRELAE-RYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  383 EEKRLMEQKVLEAEvlalkmAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKptyppMNPIPAPLPPDIPSFNL 462
Cdd:COG4913    316 ARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL-----LAALGLPLPASAEEFAA 384

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034629014  463 IGDSLSfDFKDtDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 512
Cdd:COG4913    385 LRAEAA-ALLE-ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
PTZ00121 PTZ00121
MAEBL; Provisional
 277-517 1.89e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  277 SLEVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDEleRRLlqmkEEATMANEALMRSEETADllAEKAQITEEE 356
Cdd:PTZ00121  1184 AEEVRKAEELRKAEDARK-AEAARKAEEERKAEEARKAEDA--KKA----EAVKKAEEAKKDAEEAKK--AEEERNNEEI 1254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  357 AKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLA---LKMAEESERRAKE---ADQLKQDLQEAREAERRA 430
Cdd:PTZ00121  1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeeKKKADEAKKKAEEakkADEAKKKAEEAKKKADAA 1334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  431 KQKLLEIATKPTYPPMNPIPAplppdipsfnliGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEA 510
Cdd:PTZ00121  1335 KKKAEEAKKAAEAAKAEAEAA------------ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402


                   ....*..
gi 1034629014  511 LKLKERE 517
Cdd:PTZ00121  1403 DKKKADE 1409
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-430 1.90e-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: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMER--QRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 348
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 349 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAE-----VLALKMAEESERRAKEADQLKQDLQEA 423
Cdd:COG1196   457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAY 536


                  ....*..
gi 1034629014 424 REAERRA 430
Cdd:COG1196   537 EAALEAA 543
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 4-64 2.42e-05

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: 42.95  E-value: 2.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVLDHdvSKEEPVTFHFLAKFYP 64
Cdd:cd17201    23 RGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKnWLDPSKEIKKQ--IRSGPWHFAFTVKFYP 82
PTZ00121 PTZ00121
MAEBL; Provisional
 272-433 2.70e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLevqqmKAQAREEKaRKQMERQRLAREKQMREEAERTRDELER--RLLQMKEEATMANEALMRSEET--ADLLA 347
Cdd:PTZ00121  1390 KKKADEA-----KKKAEEDK-KKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAkkAEEAK 1463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  348 EKAQITE--EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlaLKMAEEserrAKEADQLKQdLQEARE 425
Cdd:PTZ00121  1464 KKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE---AKKAEE----AKKADEAKK-AEEAKK 1535

                          170
                   ....*....|
gi 1034629014  426 AE--RRAKQK 433
Cdd:PTZ00121  1536 ADeaKKAEEK 1545
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
279-438 2.74e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.79  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 279 EVQQMKAQAREEKARKQMERQ-RLAREKQMREEAERTRDELERRLLQMKEEATmanealmRSEETADLLAEKA-QITEEE 356
Cdd:COG2268   202 RIAEAEAERETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEER-------REAETARAEAEAAyEIAEAN 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 357 AKLLAQKAAEAEQEMQRIKATAIRTE-EEKRLMEQKVLEAEVLALKMA--EESERRAKEADQLKQdlQEAREAERRAKQK 433
Cdd:COG2268   275 AEREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEaeAEAEAEAIRAKGLAE--AEGKRALAEAWNK 352


                  ....*
gi 1034629014 434 LLEIA 438
Cdd:COG2268   353 LGDAA 357
PRK12705 PRK12705
hypothetical protein; Provisional
 257-430 2.80e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 46.63  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 257 LILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKarkqmERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAL 336
Cdd:PRK12705   12 LLIGLLLGVLVVLLKKRQRLAKEAERILQEAQKEA-----EEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 337 MRSEEtaDLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL--MEQKVLEAEVLALKMAEESERRAKEAD 414
Cdd:PRK12705   87 VQKEE--QLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVagLTPEQARKLLLKLLDAELEEEKAQRVK 164

                         170
                  ....*....|....*.
gi 1034629014 415 QLKQDLQEarEAERRA 430
Cdd:PRK12705  165 KIEEEADL--EAERKA 178
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 179-236 3.18e-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: 43.39  E-value: 3.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629014 179 YGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPwnEIRNISYSDKEFTIK 236
Cdd:cd13195     1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERIPYT--AIQMATSSGRVFTLT 56
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 2-63 3.38e-05

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: 42.26  E-value: 3.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629014   2 KWKGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMdKKVLDHDVSKEEPVTFHFLAKFY 63
Cdd:cd17104    20 KANGQECLDKVCQKLGIIEKDYFGLQYTgPKGERLWLNL-RNRISRQLPGPPPYRLRLRVKFF 81
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-423 3.78e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDE--LERRLLQMKEEATMANEALMRSEETADLLAE 348
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErlEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629014 349 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 423
Cdd:COG1196   451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
272-376 4.11e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.81  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 272 RRKADSLEVQQMKAQAREEKARKQMER-QRLARE----KQMREEAERTRDELERRLLQMKEEATMANEALmrsEETADLL 346
Cdd:COG1566   109 EAEIAAAEAQLAAAQAQLDLAQRELERyQALYKKgavsQQELDEARAALDAAQAQLEAAQAQLAQAQAGL---REEEELA 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034629014 347 AEKAQITEEEAKLlaqKAAEAEQEMQRIKA 376
Cdd:COG1566   186 AAQAQVAQAEAAL---AQAELNLARTTIRA 212
PTZ00121 PTZ00121
MAEBL; Provisional
 272-432 4.51e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQA----REEKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 344
Cdd:PTZ00121  1353 EAAADEAEAAEEKAEAaekkKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaaAAKKKADEAKKKAEEKKK 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  345 llAEKAQITEEEAKllaqKAAEAEQEMQRIKataiRTEEEKRLMEQKVLEAEvlaLKMAEESERRA----KEADQLKQDL 420
Cdd:PTZ00121  1433 --ADEAKKKAEEAK----KADEAKKKAEEAK----KAEEAKKKAEEAKKADE---AKKKAEEAKKAdeakKKAEEAKKKA 1499

                          170
                   ....*....|..
gi 1034629014  421 QEAREAERRAKQ 432
Cdd:PTZ00121  1500 DEAKKAAEAKKK 1511
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 290-436 5.72e-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: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 290 EKARKQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEET-ADLLAEKAQITEEEAKLLAQKAAeae 368
Cdd:pfam07888  51 EAANRQREKEK-ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKyKELSASSEELSEEKDALLAQRAA--- 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629014 369 qEMQRIKataiRTEEEKRLMEQKVLEAEVLALKMAEESERRAKeadQLKQDlqearEAERRAKQKLLE 436
Cdd:pfam07888 127 -HEARIR----ELEEDIKTLTQRVLERETELERMKERAKKAGA---QRKEE-----EAERKQLQAKLQ 181
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 272-452 6.59e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 272 RRKADSLEVQQMKAQAREEKARKQMERQRlAREKQMREEAERTRDELERRLLQM--------------KEEATMANEALM 337
Cdd:COG4942    61 ERRIAALARRIRALEQELAALEAELAELE-KEIAELRAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQ 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 338 RSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLalkMAEESERRAKEADQLK 417
Cdd:COG4942   140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELA 216

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034629014 418 QDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAP 452
Cdd:COG4942   217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 267-439 6.65e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 6.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 267 DLFMRRRKADSLEVQQMKAQAREEKARkqmerQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 346
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALL-----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 347 AEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQK---------------------VLEAEVLALKMAEE 405
Cdd:COG1196   462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvkaalllaglrglagavaVLIGVEAAYEAALE 541

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034629014 406 SERRAKEADQLKQDLQEAREAERRAKQKLLEIAT 439
Cdd:COG1196   542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-436 6.82e-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: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 350
Cdd:COG1196   676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 351 QITEEEAKLLAQKAAEAEQEMQRIKA---TAIrtEEekrlmeqkvleaevlalkMAEESERRAKEADQlKQDLQEAREA- 426
Cdd:COG1196   756 LPEPPDLEELERELERLEREIEALGPvnlLAI--EE------------------YEELEERYDFLSEQ-REDLEEARETl 814

                         170
                  ....*....|....*..
gi 1034629014 427 -------ERRAKQKLLE 436
Cdd:COG1196   815 eeaieeiDRETRERFLE 831
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 271-450 7.27e-05

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 45.71  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEaertrdelerrllqmkeeatmanealmRSEETADLLAEKA 350
Cdd:PRK05035  432 RQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA---------------------------RHKKAAEARAAKD 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 351 Q--ITEEEAKLLAQKAAEAEQemqrikaTAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAer 428
Cdd:PRK05035  485 KdaVAAALARVKAKKAAATQP-------IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA-- 555

                         170       180
                  ....*....|....*....|..
gi 1034629014 429 RAKQKLLEIATKPTYPPMNPIP 450
Cdd:PRK05035  556 RAKAKKAAQQAANAEAEEEVDP 577
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 172-236 8.51e-05

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: 42.33  E-value: 8.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629014 172 IAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK 236
Cdd:cd13193     2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 271-433 8.66e-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: 8.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQM-ERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEalmrsEETADLLAEK 349
Cdd:TIGR02794  89 ARQKELEQRAAAEKAAKQAEQAAKQAeEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE-----EEAKAKAAAE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 350 AQITEEEAKLLAQKAAEAEQEMQRiKATAirtEEEKRLMEQKVLEAEVLALKMAE-ESERRAKEADQLKQDLQEAREAER 428
Cdd:TIGR02794 164 AKKKAEEAKKKAEAEAKAKAEAEA-KAKA---EEAKAKAEAAKAKAAAEAAAKAEaEAAAAAAAEAERKADEAELGDIFG 239


                  ....*
gi 1034629014 429 RAKQK 433
Cdd:TIGR02794 240 LASGS 244
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 269-511 9.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 9.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 269 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 348
Cdd:COG1196   565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 349 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAE---VLALKMAEESERRAKEADQLKQDLQEARE 425
Cdd:COG1196   645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEElelEEALLAEEEEERELAEAEEERLEEELEEE 724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 426 AERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPsfnligDSLSFDFKDTDMKRLSMEIEK-EKV------EY---MEKSK 495
Cdd:COG1196   725 ALEEQLEAEREELLEELLEEEELLEEEALEELP------EPPDLEELERELERLEREIEAlGPVnllaieEYeelEERYD 798

                         250
                  ....*....|....*.
gi 1034629014 496 HLQEQLNELKTEIEAL 511
Cdd:COG1196   799 FLSEQREDLEEARETL 814
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 279-440 9.49e-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: 45.33  E-value: 9.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 279 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEAL----MRSEETADLLAEKAQITE 354
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQL--ERAEKMREELELEQQRRFEEIRLRKQRLeeerQRQEEEERKQRLQLQAAQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 355 EEAKLLAQKAAEAEQEMQRIKAT--AIRTEEEKRL---MEQKVLEAEVLALKMAEES-----ERRAKEADQLKQDLQEAR 424
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRKKQQeeAERAEAEKQRqkeLEMQLAEEQKRLMEMAEEErleyqRQKQEAEEKARLEAEERR 498

                         170
                  ....*....|....*.
gi 1034629014 425 EAERRAKQKLLEIATK 440
Cdd:pfam15709 499 QKEEEAARLALEEAMK 514
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 269-436 9.55e-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: 9.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  269 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAE 348
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI------EELEEL 867

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  349 KAQITEEEAKLLAQKAaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAER 428
Cdd:TIGR02168  868 IEELESELEALLNERA-SLEEALALLRSELEELSEELRELESKRSELR-------RELEELREKLAQLELRLEGLEVRID 939


                   ....*...
gi 1034629014  429 RAKQKLLE 436
Cdd:TIGR02168  940 NLQERLSE 947
PTZ00491 PTZ00491
major vault protein; Provisional
 282-413 1.17e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 45.01  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 282 QMKAQAREEKARKQMERQRLarekQMREEAERTRdeleRRLLQMKEEATmANEALMRSEETADLLAEKAQITEEeaklla 361
Cdd:PTZ00491  669 RHQAELLEQEARGRLERQKM----HDKAKAEEQR----TKLLELQAESA-AVESSGQSRAEALAEAEARLIEAE------ 733

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034629014 362 qkaAEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLAlKMAEESERRAKEA 413
Cdd:PTZ00491  734 ---AEVEQAELRAKALRIEAEAElEKLRKRQELELEYEQ-AQNELEIAKAKEL 782
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 293-436 1.53e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 293 RKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMrsEETADLLAEKAQIteeeakllaqkAAEAEQEMQ 372
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERR--RKLEEAEKARQAEM--DRQAAIYAEQERM-----------AMERERELE 351

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629014 373 RikataIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERraKQKLLE 436
Cdd:pfam17380 352 R-----IRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR--KVKILE 408
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
267-437 2.10e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 267 DLFMRRRKADSLEVQQMKAQAREEKARKQmERQRLAREKQMREEAERTRDELERRLLQMKEEAtmanEALMRSEETADLL 346
Cdd:COG4717    57 ELFKPQGRKPELNLKELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREEL----EKLEKLLQLLPLY 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 347 AEKAQItEEEAKLLAQKAAEAEQEMQRIKataiRTEEEKRLMEQKVLEAE-VLALKMAEESERRAKEADQLKQDLQEARE 425
Cdd:COG4717   132 QELEAL-EAELAELPERLEELEERLEELR----ELEEELEELEAELAELQeELEELLEQLSLATEEELQDLAEELEELQQ 206

                         170
                  ....*....|..
gi 1034629014 426 AERRAKQKLLEI 437
Cdd:COG4717   207 RLAELEEELEEA 218
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 277-437 3.09e-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: 43.59  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 277 SLEVQQMkaqaREEKARKQMERQRLAREKQMREEAERTRDELERRLL-----QMKEEATMANEALMR------------- 338
Cdd:pfam07111 480 SLELEQL----REERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLsevaqQLEQELQRAQESLASvgqqlevarqgqq 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 339 --SEETADLLAEKAQITEEEAKLLAQKAAEAEQEM-QRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERrakeADQ 415
Cdd:pfam07111 556 esTEEAASLRQELTQQQEIYGQALQEKVAEVETRLrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER----NQE 631

                         170       180
                  ....*....|....*....|...
gi 1034629014 416 LKQDLQEAREAE-RRAKQKLLEI 437
Cdd:pfam07111 632 LRRLQDEARKEEgQRLARRVQEL 654
growth_prot_Scy NF041483
polarized growth protein Scy;
295-436 3.54e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.66  E-value: 3.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  295 QMERQRLARE-KQMREEA----ERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAA--- 365
Cdd:NF041483   439 QEEARRLRGEaEQLRAEAvaegERIRGEARREAVQQIEEaARTAEELLTKAKADADELRSTATAESERVRTEAIERAttl 518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  366 --EAEQEMQRIKATA--IRTEEEKRLMEQKVlEAEVLALKMAEESE-----RRAKEADQLKQDLQEAREAERRAKQKLLE 436
Cdd:NF041483   519 rrQAEETLERTRAEAerLRAEAEEQAEEVRA-AAERAARELREETEraiaaRQAEAAEELTRLHTEAEERLTAAEEALAD 597
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
279-435 3.62e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 279 EVQQMKAQAREEKARKQMERQRLAREKQM------REEAERTRDELERRLLQMKEEATMANEALmrsEETADLLAEKAQI 352
Cdd:COG4717    99 ELEEELEELEAELEELREELEKLEKLLQLlplyqeLEALEAELAELPERLEELEERLEELRELE---EELEELEAELAEL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 353 TEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAERRAKQ 432
Cdd:COG4717   176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ-------EELEELEEELEQLENELEAAALEERLKEA 248


                  ...
gi 1034629014 433 KLL 435
Cdd:COG4717   249 RLL 251
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 279-421 3.68e-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: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  279 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRD-------ELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 351
Cdd:TIGR02169  372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  352 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQ 421
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
PTZ00121 PTZ00121
MAEBL; Provisional
 279-517 3.80e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  279 EVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAQITEEEAK 358
Cdd:PTZ00121  1114 ARKAEEAKKKAEDARK-AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA--RKAEDAKKAEAARKAEEVRKA 1190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  359 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKvleaevlalKMAEEserrAKEADQLKQDLQEAREAErraKQKLLEIA 438
Cdd:PTZ00121  1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDA---------KKAEA----VKKAEEAKKDAEEAKKAE---EERNNEEI 1254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  439 TKPTYPPMNPIPAPLPPDIPSFNLIGDSL--SFDFKDTDMKRLSMEIE-----KEKVEYMEKSKHLQEQLNELKTEIEAL 511
Cdd:PTZ00121  1255 RKFEEARMAHFARRQAAIKAEEARKADELkkAEEKKKADEAKKAEEKKkadeaKKKAEEAKKADEAKKKAEEAKKKADAA 1334


                   ....*.
gi 1034629014  512 KLKERE 517
Cdd:PTZ00121  1335 KKKAEE 1340
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 272-419 3.80e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.67  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEA------ERTRDELERRLLQMKEEATMANEALmrsEETADL 345
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfartalKNARLDLRRLFDEKQSEKDKKNKAL---AERKDS 679

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629014  346 LAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESER--RAKEADQLKQD 419
Cdd:pfam12128  680 ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRsgAKAELKALETW 755
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 4-63 3.85e-04

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


Pssm-ID: 340724  Cd Length: 84  Bit Score: 39.42  E-value: 3.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDKKVlDHDVSKEEPVTFHFLAKFY 63
Cdd:cd17204    22 KGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAhWLDHTKPI-KKQIKIGPPYTLHFRIKYY 81
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 4-45 4.05e-04

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: 39.52  E-value: 4.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQYTIKDTVA-WLKMDK---KVLD 45
Cdd:cd17099    25 TGQDCLEYVAQRLELREIEYFGLRYVNKKGQLrWVDLEKplkKQLD 70
Rabaptin pfam03528
Rabaptin;
283-432 4.20e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 43.17  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 283 MKAQAREEKAR--KQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEaLMRSEETADLLAEKAQITEEEAKLL 360
Cdd:pfam03528 113 MKETVREYEVQfhRRLEQER-AQWNQYRESAEREIADLRRRLSEGQEEENLEDE-MKKAQEDAEKLRSVVMPMEKEIAAL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 361 AQKAAEAEQEMQRIKATAIRT-----EEEKRLMEQKVLEAEVLALK---MAEESERRAKEADQLKQDLQEAREAERRAKQ 432
Cdd:pfam03528 191 KAKLTEAEDKIKELEASKMKElnhylEAEKSCRTDLEMYVAVLNTQksvLQEDAEKLRKELHEVCHLLEQERQQHNQLKH 270
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
285-437 4.30e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 285 AQAREEKARKQMERQRLAREKQMREEA-ERTRD--ELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLa 361
Cdd:PRK02224  471 EEDRERVEELEAELEDLEEEVEEVEERlERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL- 549

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629014 362 qkaaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 437
Cdd:PRK02224  550 ----EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 316-417 4.39e-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: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 316 DELERRLLQMKEEAtmanEALMRSEETADllAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEA 395
Cdd:COG0542   414 DELERRLEQLEIEK----EALKKEQDEAS--FERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487

                          90       100
                  ....*....|....*....|..
gi 1034629014 396 EVLALKMAEESERRAKEADQLK 417
Cdd:COG0542   488 PELEKELAELEEELAELAPLLR 509
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 284-437 4.54e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.42  E-value: 4.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  284 KAQAREEKARKQMERQRLAR-----EKQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtadLLAEKAQITEEEAK 358
Cdd:pfam02463  171 KKEALKKLIEETENLAELIIdleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK---LNEERIDLLQELLR 247

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629014  359 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 437
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 278-438 5.74e-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: 5.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  278 LEVQQMKAQAREEKARKQMERQRLAREKQMRE--EAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEE 355
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  356 EAKLLAQKAAEAEQEMQRIKATAIRTEEE----KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 431
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486


                   ....*..
gi 1034629014  432 QKLLEIA 438
Cdd:TIGR02169  487 KLQRELA 493
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 4-64 7.08e-04

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: 38.80  E-value: 7.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQYTIK-DTVAWLKMDKKVLDHdvSKEEPVTFHFLAKFYP 64
Cdd:cd17202    23 KGQVLFDKVCEHLNLLEKDYFGLLYQVSaNQKNWLDSTKEIKRQ--IRRLPWLFTFNVKFYP 82
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 291-382 7.97e-04

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.73  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 291 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 369
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106

                          90
                  ....*....|...
gi 1034629014 370 EMQRIKAtAIRTE 382
Cdd:cd06503   107 EKEKALA-ELRKE 118
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-430 8.52e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 8.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  251 KLRVNKLILQLCIGNHDLFMRRRKADSL--EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTR--------DELER 320
Cdd:COG4913    266 AARERLAELEYLRAALRLWFAQRRLELLeaELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLER 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  321 RLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMqrikatairtEEEKRLMEQKVLEAEVLAL 400
Cdd:COG4913    346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL----------EEELEALEEALAEAEAALR 415

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034629014  401 KMAEESERRAKEADQLKQ-------DLQEAREAERRA 430
Cdd:COG4913    416 DLRRELRELEAEIASLERrksnipaRLLALRDALAEA 452
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 270-428 1.03e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 270 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRseETADLLAEK 349
Cdd:pfam13868  30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ--EREQMDEIV 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629014 350 AQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 428
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 277-528 1.04e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  277 SLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAL-----MRSEETADLLAEKAQ 351
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELS 801

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  352 ITEEEAKLLAQKAAEAEQEMQRIkatairtEEEKRLMEQKV--LEAEVLALKMAEESERRAKEADQLKQDLQEAREAERR 429
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQKLNRL-------TLEKEYLEKEIqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  430 AKQKLLEiatkptyppmnpipaplppdipsfnligdslsfdfkdtdmKRLSmEIEKEKVEYMEKSKHLQEQLNELKTEIE 509
Cdd:TIGR02169  875 AALRDLE----------------------------------------SRLG-DLKKERDELEAQLRELERKIEELEAQIE 913

                          250       260
                   ....*....|....*....|.
gi 1034629014  510 ALK--LKERETALDILHNENS 528
Cdd:TIGR02169  914 KKRkrLSELKAKLEALEEELS 934
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
265-440 1.21e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 41.50  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 265 NHDLFMRRRKAdslevqqmkAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAT--MANEALMRSEET 342
Cdd:PRK07735    4 EKDLEDLKKEA---------ARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 343 ADLLAEKAQITEEEAKLLAQKAAEAEQemqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQE 422
Cdd:PRK07735   75 AKQKREGTEEVTEEEKAKAKAKAAAAA-----KAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREG 149

                         170
                  ....*....|....*...
gi 1034629014 423 AREAERRAKQKLLEIATK 440
Cdd:PRK07735  150 TEEVTEEEEETDKEKAKA 167
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 273-426 1.31e-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: 41.53  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 273 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERtrdelerrllqMKEEATMANEALMRSEETADLLAEKAQI 352
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK-----------QQEAKNLPKPADTSSPKEDKQVAENQKR 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629014 353 TEEEAKLLAQKAAEAEQEMQRIKATAIRTE--EEKRLMEQKVLEAEVLALKMAEESERRAKEAD-QLKQDLQEAREA 426
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQEskASEKEAEDKELEAQKKREPVAEDLQKTKPQVEaQPTSLNEDAIDS 358
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 268-550 1.40e-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: 41.58  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  268 LFMRRRKADSLEVQQMKAQAREEK--ARKQMERQRLARE-KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETAD 344
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAERYKELkaELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  345 LLAE-KAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQ 421
Cdd:TIGR02168  275 EVSElEEEIEELQKELyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  422 EAREAERRAKQKLLEiatkptyppmnpipaplppdipsfnligdslsfdfkdtdMKRLSMEIEKEKVEYMEKSKHLQEQL 501
Cdd:TIGR02168  355 SLEAELEELEAELEE---------------------------------------LESRLEELEEQLETLRSKVAQLELQI 395

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034629014  502 NELKTEIEALK--LKERETALDILHNENSDRGGSSKHNTIKKLTLQSAKSR 550
Cdd:TIGR02168  396 ASLNNEIERLEarLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 4-64 1.56e-03

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: 37.81  E-value: 1.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWL---KMDKKVLdhdvsKEEPVTFHFLAKFYP 64
Cdd:cd17106    23 KGQVLFDKVCEHLNLLEKDYFGLTYRdAQDQKNWLdpaKEIKKQI-----RSGPWLFSFNVKFYP 82
growth_prot_Scy NF041483
polarized growth protein Scy;
283-428 2.24e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  283 MKAQARE--EKARKQMERQRlareKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAqiTEEEAKL- 359
Cdd:NF041483   518 LRRQAEEtlERTRAEAERLR----AEAEEQAEEVRAAAERAARELREETERAIAA--RQAEAAEELTRLH--TEAEERLt 589

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  360 -----LAQKAAEAE-------QEMQRIKATAirTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDL--QEARE 425
Cdd:NF041483   590 aaeeaLADARAEAErirreaaEETERLRTEA--AERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLrsEAAAE 667


                   ...
gi 1034629014  426 AER 428
Cdd:NF041483   668 AER 670
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 4-63 2.29e-03

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: 37.29  E-value: 2.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQY----TIKDTVAWLKMDKKvLDHDVSKEEPVTFHFLAKFY 63
Cdd:cd17100    23 KGQVLLDKVFNHLELVEKDYFGLQFsddsPATDSMRWLDPLKP-IRKQIKGGPPYYLNFRVKFY 85
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
287-430 2.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  287 AREEKARKQMERQRLAREkqmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKL------- 359
Cdd:COG4913    608 NRAKLAALEAELAELEEE---LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerldass 684

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629014  360 -----LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLalkmAEESERRAKEADQLKQDLQEAREAERRA 430
Cdd:COG4913    685 ddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFA 756
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 269-329 2.34e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 40.63  E-value: 2.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629014 269 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 329
Cdd:PLN03086    3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 272-516 2.39e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTR-DELERRLLQMKEEATMANEALMRSeETADLLAEKA 350
Cdd:TIGR02169  176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEkREYEGYELLKEKEALERQKEAIER-QLASLEEELE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  351 QIT---EEEAKLLAQKAAEAEQEMQRIKAtaiRTEEEKRLMEQKV--LEAEVLALKMA-EESERRAKEADQLKQDLQEAR 424
Cdd:TIGR02169  255 KLTeeiSELEKRLEEIEQLLEELNKKIKD---LGEEEQLRVKEKIgeLEAEIASLERSiAEKERELEDAEERLAKLEAEI 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  425 EAERRAKQKLLEiatkptyppmnpipaplppDIPSFNLIGDSLSFDFKDTDMKRLSM-----EIEKEKVEYMEKSKHLQE 499
Cdd:TIGR02169  332 DKLLAEIEELER-------------------EIEEERKRRDKLTEEYAELKEELEDLraeleEVDKEFAETRDELKDYRE 392

                          250
                   ....*....|....*..
gi 1034629014  500 QLNELKTEIEALKLKER 516
Cdd:TIGR02169  393 KLEKLKREINELKRELD 409
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 295-437 2.76e-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: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 295 QMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQemqri 374
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQ----- 401

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629014 375 kataiRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 437
Cdd:pfam15709 402 -----RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEM 459
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
278-444 3.06e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 278 LEVQQMKAQAREEKARKQMERQRLA----REKQMREEAERTRDELERRLLQMKEEATMANEALMRseetadLLAEKAQIT 353
Cdd:COG3206   231 ARAELAEAEARLAALRAQLGSGPDAlpelLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA------LRAQIAALR 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 354 EEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAE-ESERRAKEA--DQLKQDLQEAR--EAER 428
Cdd:COG3206   305 AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEVARElyESLLQRLEEARlaEALT 384

                         170
                  ....*....|....*.
gi 1034629014 429 RAKQKLLEIATKPTYP 444
Cdd:COG3206   385 VGNVRVIDPAVVPLKP 400
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 5-64 3.17e-03

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


Pssm-ID: 340709  Cd Length: 85  Bit Score: 36.71  E-value: 3.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629014   5 GKDLFDLVCRTLGLRETWFFGLQYTI-KDTVAWLKMDKKVLDHdVSKEEPVTFHFLAKFYP 64
Cdd:cd17189    23 GKVLLDAVCSHLNLVEGDYFGLEFQDhRKVMVWLDLLKPIVKQ-IRRPKHVVLRFVVKFFP 82
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 284-425 3.25e-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: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 284 KAQAREEKARkQMERQrLAREKQMREEAERTRDELERRLlqmkeeaTMANEALMRSEETADLLAEKAQITEEEAKLLAQK 363
Cdd:pfam00261  86 RALKDEEKME-ILEAQ-LKEAKEIAEEADRKYEEVARKL-------VVVEGDLERAEERAELAESKIVELEEELKVVGNN 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629014 364 AAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalKMAEESERRA----KEADQLKQDLQEARE 425
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAE----TRAEFAERSVqkleKEVDRLEDELEAEKE 218
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 276-418 3.37e-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: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 276 DSLEVQQMKAQAREEKARKQMERQR-----LAREKQMREEAERTRDELERRLLQMKEEATMANEAL-----------MRS 339
Cdd:pfam00529  61 DSAEAQLAKAQAQVARLQAELDRLQaleseLAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLarrrvlapiggISR 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 340 EEtadLLAEKAQITEEEAKLLAqkaaeAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEvlaLKMAEESERRAKEADQLKQ 418
Cdd:pfam00529 141 ES---LVTAGALVAQAQANLLA-----TVAQLDQIYVQITQSAAEnQAEVRSELSGAQ---LQIAEAEAELKLAKLDLER 209
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
276-437 3.42e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 276 DSLEVQQMKAQAREEKARKQMERQRLARE------------KQMREEAERTRDELERRLLQMKEEATMANEALMRSEETA 343
Cdd:PRK02224  223 ERYEEQREQARETRDEADEVLEEHEERREeletleaeiedlRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 344 DLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEE-KRLMEQkvleaevlALKMAEESERRAKEADQLKQDLQE 422
Cdd:PRK02224  303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaESLRED--------ADDLEERAEELREEAAELESELEE 374

                         170
                  ....*....|....*
gi 1034629014 423 AREAERRAKQKLLEI 437
Cdd:PRK02224  375 AREAVEDRREEIEEL 389
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 288-437 3.48e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  288 REEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEE-ATMANEALMRSEETADLLAEKAQI--TEEEAKLLAQKA 364
Cdd:TIGR00618  368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLAHAKKQQelQQRYAELCAAAI 447

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629014  365 AEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 437
Cdd:TIGR00618  448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 275-407 3.93e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 275 ADSLEVQQMKAQArEEKARKQmeRQRLAREKQMREEAERTRDELERRLLQMKEEatmanEALMRSEetadlLAEKAQITE 354
Cdd:PRK00409  513 EDKEKLNELIASL-EELEREL--EQKAEEAEALLKEAEKLKEELEEKKEKLQEE-----EDKLLEE-----AEKEAQQAI 579

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629014 355 EEAKLLAQKAAEAEQEMQRIKATAIR---TEEEKRLMEQKVLEAEVLALKMAEESE 407
Cdd:PRK00409  580 KEAKKEADEIIKELRQLQKGGYASVKaheLIEARKRLNKANEKKEKKKKKQKEKQE 635
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 267-459 4.32e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 40.00  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 267 DLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 346
Cdd:NF033838  189 ELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 347 AEKAQIT----EEEAKLLA----------------QKAAEAEQEMQRIKATAIRTEEEKRL----------------MEQ 390
Cdd:NF033838  269 VLGEPATpdkkENDAKSSDssvgeetlpspslkpeKKVAEAEKKVEEAKKKAKDQKEEDRRnyptntyktleleiaeSDV 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 391 KVLEAEVLALK--------------MAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLP-P 455
Cdd:NF033838  349 KVKEAELELVKeeakeprneekikqAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPqP 428


                  ....
gi 1034629014 456 DIPS 459
Cdd:NF033838  429 EKPA 432
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
284-521 4.57e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 284 KAQAREEKARKQMERQRlAREKQMREEAERTRDELERR---LLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLL 360
Cdd:COG4372    35 KALFELDKLQEELEQLR-EELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 361 AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATK 440
Cdd:COG4372   114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 441 PTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETAL 520
Cdd:COG4372   194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273


                  .
gi 1034629014 521 D 521
Cdd:COG4372   274 E 274
Caldesmon pfam02029
Caldesmon;
271-437 4.86e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.47  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQM--------------KEEATMANEAL 336
Cdd:pfam02029 168 EVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTtkrrqgglsqsqerEEEAEVFLEAE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 337 MRSEETADLLAEKAqitEEEAKLLAQKAAEAEQEMQRIKataiRTEEEKRlmeqKVLEAEVLALKmAEESERRAKEAD-- 414
Cdd:pfam02029 248 QKLEELRRRRQEKE---SEEFEKLRQKQQEAELELEELK----KKREERR----KLLEEEEQRRK-QEEAERKLREEEek 315

                         170       180
                  ....*....|....*....|....*.
gi 1034629014 415 -QLKQDLQEAR--EAERRakQKLLEI 437
Cdd:pfam02029 316 rRMKEEIERRRaeAAEKR--QKLPED 339
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 270-436 4.89e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.52  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 270 MRRRKADSLEVQQMKAQAREEKARKQMERQR-LAREKQMREEAERTRDELERRLLQMKEEATMANEALMrseetaDLLAE 348
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEkLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL------EYLKE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 349 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQ---KVLEAEVLA---LKMAEESERRAKEADQLKQDLQE 422
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDElraKLYQEEQERkerQKEREEAEKKARQRQELQQAREE 243

                         170
                  ....*....|....
gi 1034629014 423 AREAERRAKQKLLE 436
Cdd:pfam13868 244 QIELKERRLAEEAE 257
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 291-380 5.39e-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: 37.84  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 291 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAtmaneALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQE 370
Cdd:COG0711    30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEA-----AEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAE 104

                          90
                  ....*....|
gi 1034629014 371 MQRIKATAIR 380
Cdd:COG0711   105 IEQERAKALA 114
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 287-418 5.43e-03

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.94  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  287 AREEKARKQMER--QRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLaeKAQITEEEAK----LL 360
Cdd:COG3096    529 RQQQNAERLLEEfcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL--RARIKELAARapawLA 606

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  361 AQKAAE--AEQEMQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQ 418
Cdd:COG3096    607 AQDALErlREQSGEALADSQEVTAAMQQLLERER-EATVERDELAARKQALESQIERLSQ 665
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 276-436 5.56e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 39.60  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 276 DSLEVQQMKAQAREEKARKQMERQRLAREKQMR-EEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITE 354
Cdd:pfam05262 175 DSISDKKVVEALREDNEKGVNFRRDMTDLKEREsQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQ 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 355 EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVL------ALKMAEESERRAKEADQLKQDLQEAREAER 428
Cdd:pfam05262 255 QEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALkakdhkAFDLKQESKASEKEAEDKELEAQKKREPVA 334


                  ....*...
gi 1034629014 429 RAKQKLLE 436
Cdd:pfam05262 335 EDLQKTKP 342
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
272-437 5.59e-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: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  272 RRKADSLEVQQMKAQAREEKARKQME--RQRLAREKQMRE---------EAERTRDELERRLlqmkEEATMANEALMRSE 340
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDalQERREALQRLAEyswdeidvaSAEREIAELEAEL----ERLDASSDDLAALE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  341 ETADLL-AEKAQITEEEAKL------LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLAlkmAEESERRAKEA 413
Cdd:COG4913    692 EQLEELeAELEELEEELDELkgeigrLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA---ALGDAVERELR 768

                          170       180
                   ....*....|....*....|....
gi 1034629014  414 DQLKQDLQEAREAERRAKQKLLEI 437
Cdd:COG4913    769 ENLEERIDALRARLNRAEEELERA 792
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 270-381 6.26e-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: 37.71  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 270 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEK 349
Cdd:pfam05672  35 LEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEA 114

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034629014 350 AQITEEEAKLLAQKAAEAEQEMQRIKATAIRT 381
Cdd:pfam05672 115 ERQRQEREKIMQQEEQERLERKKRIEEIMKRT 146
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 4-64 7.09e-03

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: 36.07  E-value: 7.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629014   4 KGKDLFDLVCRTLGLRETWFFGLQYT-IKDTVAWLKMDKKVLDHdvSKEEPVTFHFLAKFYP 64
Cdd:cd17203    23 KGQVLFDKVCEHLNLLEKDYFGLTYRdSENQKNWLDPAKEIKKQ--IRSGAWQFSFNVKFYP 82
COG5022 COG5022
Myosin heavy chain [General function prediction only];
238-543 7.24e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 39.29  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  238 LDKKIDVFKFNSSKLRVNKLILQLcigNHDLFMRR--RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTR 315
Cdd:COG5022    904 LESEIIELKKSLSSDLIENLEFKT---ELIARLKKllNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKS 980

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  316 DELERRLLQMKEEATMANEAL-MRSEETADLLAEKAQITEEEAKLlaqkaAEAEQEMQRIKAT----AIRTEEEK----R 386
Cdd:COG5022    981 TILVREGNKANSELKNFKKELaELSKQYGALQESTKQLKELPVEV-----AELQSASKIISSEstelSILKPLQKlkglL 1055

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  387 LMEQKVLEAEVLALKMAEESERRakEADQLKQdLQEAREAERRAKQKLLEIATKPTYPPMNPIPApLPPDIPSFNLIGDS 466
Cdd:COG5022   1056 LLENNQLQARYKALKLRRENSLL--DDKQLYQ-LESTENLLKTINVKDLEVTNRNLVKPANVLQF-IVAQMIKLNLLQEI 1131

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  467 LSF------DFKDTDMKRLSMEIEKEKV---------------------------EYMEKSKHLQEQLNELKTEIEALKL 513
Cdd:COG5022   1132 SKFlsqlvnTLEPVFQKLSVLQLELDGLfweanlealpspppfaalsekrlyqsaLYDEKSKLSSSEVNDLKNELIALFS 1211

                          330       340       350
                   ....*....|....*....|....*....|
gi 1034629014  514 KERETALDILHNENSDRGGSSKHNTIKKLT 543
Cdd:COG5022   1212 KIFSGWPRGDKLKKLISEGWVPTEYSTSLK 1241
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 270-371 7.28e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 7.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 270 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKqmrEEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEK 349
Cdd:COG3883   135 LEELKADKAELEAKKAELEAKLAELEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211

                          90       100
                  ....*....|....*....|..
gi 1034629014 350 AQITEEEAKLLAQKAAEAEQEM 371
Cdd:COG3883   212 AAAAAAAAAAAAAAAAAAAAAA 233
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 287-376 7.32e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 37.45  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 287 AREEKARKQME---RQRLAREKQMREEAERTRDELERRLLQMKEEAtmanealmrseetadllaeKAQITEEEAKLLAQK 363
Cdd:PRK05759   45 AAAERAKKELElaqAKYEAQLAEARAEAAEIIEQAKKRAAQIIEEA-------------------KAEAEAEAARIKAQA 105

                          90
                  ....*....|...
gi 1034629014 364 AAEAEQEMQRIKA 376
Cdd:PRK05759  106 QAEIEQERKRARE 118
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 285-438 7.57e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 39.24  E-value: 7.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 285 AQAREEKARKQMERqrLARE-KQMREEAErtrdelerrllQMKEEATMANEALMRSEETADLlaEKAQITEEEAKLLA-Q 362
Cdd:pfam05701 368 VQAKEKEAREKMVE--LPKQlQQAAQEAE-----------EAKSLAQAAREELRKAKEEAEQ--AKAAASTVESRLEAvL 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 363 KAAEAEQEMQRIKATAIR----TEEEKRLMEQKVLEAEV-LALKMAEESERRAKEADQLKQD--------LQEAREAERR 429
Cdd:pfam05701 433 KEIEAAKASEKLALAAIKalqeSESSAESTNQEDSPRGVtLSLEEYYELSKRAHEAEELANKrvaeavsqIEEAKESELR 512


                  ....*....
gi 1034629014 430 AKQKLLEIA 438
Cdd:pfam05701 513 SLEKLEEVN 521
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 321-433 7.73e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.63  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 321 RLLQMKEEATMANEALMRSEET-ADLLAEKAQITEEEAKLLAQKAaEAEQEMQRIKATAIR--TEEEKRLMEQKVLEAEV 397
Cdd:PRK09510   66 RQQQQQKSAKRAEEQRKKKEQQqAEELQQKQAAEQERLKQLEKER-LAAQEQKKQAEEAAKqaALKQKQAEEAAAKAAAA 144

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034629014 398 LALKMAEESERRAKEADQLKQDLQEAREAERRAKQK 433
Cdd:PRK09510  145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAA 180
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 299-441 7.87e-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: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 299 QRLAREKQMREEAERTRDELERRLLQMKEEATmanealmrseetADLLAEKAQITEEEAKLLAQKAA-EAEQEMQRIKat 377
Cdd:TIGR02794  50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAE------------KQRAAEQARQKELEQRAAAEKAAkQAEQAAKQAE-- 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629014 378 airtEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKP 441
Cdd:TIGR02794 116 ----EKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA 175
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
279-523 8.20e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 8.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 279 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 358
Cdd:COG4372    46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 359 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALKMAEESERRAKEADQLKQDLQEAREA----ERRAKQ 432
Cdd:COG4372   126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLesLQEELAALEQELQALSEAEAEQALDELLKEANRNaekeEELAEA 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 433 KLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 512
Cdd:COG4372   206 EKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285

                         250
                  ....*....|.
gi 1034629014 513 LKERETALDIL 523
Cdd:COG4372   286 EALEEAALELK 296
rne PRK10811
ribonuclease E; Reviewed
 279-455 8.25e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 39.25  E-value: 8.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  279 EVQQMKAQAREEKARKQMERqRLAREKQMREEAER--TRDELERRLLQMKEEATMANealmRSEETADLLAEKAQITEEE 356
Cdd:PRK10811   587 KPQEQPAPKAEAKPERQQDR-RKPRQNNRRDRNERrdTRDNRTRREGRENREENRRN----RRQAQQQTAETRESQQAEV 661

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014  357 AKllAQKAAEAEQEMQRiKATAIRTEEEKRL--MEQKVLEAEVLALKMAEESERRA-----KEADQLKQD--LQEAREAE 427
Cdd:PRK10811   662 TE--KARTQDEQQQAPR-RERQRRRNDEKRQaqQEAKALNVEEQSVQETEQEERVQqvqprRKQRQLNQKvrIEQSVAEE 738

                          170       180
                   ....*....|....*....|....*...
gi 1034629014  428 RRAKQKLLEIATKPTYPPMNPIPAPLPP 455
Cdd:PRK10811   739 AVAPVVEETVAAEPVVQEVPAPRTELVK 766
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 271-374 8.27e-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: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 271 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 350
Cdd:pfam09756   1 KKLGAKKRAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEKLKS 80

                          90       100
                  ....*....|....*....|....
gi 1034629014 351 QITEEEAKLLAQKAAEAEQEMQRI 374
Cdd:pfam09756  81 QFVVEEEGTDKLSAEDESQLLEDF 104
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 302-436 9.99e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 38.65  E-value: 9.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629014 302 AREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEetadlLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRT 381
Cdd:pfam10174 517 SKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPE-----INDRIRLLEQEVARYKEESGKAQAEVERLLGILREV 591

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629014 382 EEEKRLMEQKVLEAEVLALKMAEE------------SERRAKEADQLKQDLQEAREAERRAKQKLLE 436
Cdd:pfam10174 592 ENEKNDKDKKIAELESLTLRQMKEqnkkvanikhgqQEMKKKGAQLLEEARRREDNLADNSQQLQLE 658
 
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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