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Conserved domains on  [gi|2244985390|ref|NP_001393994|]
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merlin isoform 19 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 38-134 1.54e-65

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: 204.04  E-value: 1.54e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  38 MYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 117
Cdd:cd13194     1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                          90
                  ....*....|....*..
gi 2244985390 118 ILQLCIGNHDLFMRRRK 134
Cdd:cd13194    81 ILDLCMGNHELYMRRRK 97
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 168-287 3.67e-20

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: 85.36  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 168 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 247
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2244985390 248 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 287
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
ERM_C super family cl38012
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 340-401 1.95e-17

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


The actual alignment was detected with superfamily member pfam00769:

Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 76.47  E-value: 1.95e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244985390 340 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSdRGGSSKHNTIKK 401
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENV-RQGRDKYKTLRK 61
B41 super family cl33382
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1-44 1.08e-10

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.


The actual alignment was detected with superfamily member smart00295:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 60.77  E-value: 1.08e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2244985390    1 MTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 44
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PLN03086 super family cl29366
PRLI-interacting factor K; Provisional
 129-189 2.71e-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: 39.86  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2244985390 129 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 189
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 ...
 38-134 1.54e-65

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: 204.04  E-value: 1.54e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  38 MYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 117
Cdd:cd13194     1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                          90
                  ....*....|....*..
gi 2244985390 118 ILQLCIGNHDLFMRRRK 134
Cdd:cd13194    81 ILDLCMGNHELYMRRRK 97
FERM_C pfam09380
FERM C-terminal PH-like domain;
48-133 2.92e-29

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 108.88  E-value: 2.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  48 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 126
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 2244985390 127 DLFMRRR 133
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 168-287 3.67e-20

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: 85.36  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 168 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 247
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2244985390 248 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 287
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 340-401 1.95e-17

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


Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 76.47  E-value: 1.95e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244985390 340 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSdRGGSSKHNTIKK 401
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENV-RQGRDKYKTLRK 61
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 132-298 5.62e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 5.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 132 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 211
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 212 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 291
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                  ....*..
gi 2244985390 292 QKLLEIA 298
Cdd:COG1196   435 EEEEEEE 441
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1-44 1.08e-10

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: 60.77  E-value: 1.08e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2244985390    1 MTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 44
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 140-300 1.95e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.05  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 140 VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKL 219
Cdd:PRK09510   61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAK 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 220 LAQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 298
Cdd:PRK09510  141 AAAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215


                  ..
gi 2244985390 299 TK 300
Cdd:PRK09510  216 KK 217
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 1-44 9.52e-09

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 53.04  E-value: 9.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2244985390   1 MTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 44
Cdd:pfam00373  74 MKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 139-300 1.52e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  139 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 218
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  219 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 298
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907


                   ..
gi 2244985390  299 TK 300
Cdd:TIGR02168  908 SK 909
PTZ00121 PTZ00121
MAEBL; Provisional
 132-377 1.99e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSLEVQQMKAQAREEkARKQMERQRLAREKQMREEAERTRDELERRllqmKEEATMANEALMRSEEtADLLAEKAQ 211
Cdd:PTZ00121  1430 KKKADEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKADEAKKKAEE-AKKKADEAK 1503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  212 ITEEEAKLL--------AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 283
Cdd:PTZ00121  1504 KAAEAKKKAdeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  284 REAERRAKQKLLEIAtkPTYPPMNPIPAPLPPDIPSFNLIGDSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNE 363
Cdd:PTZ00121  1584 EEAKKAEEARIEEVM--KLYEEEKKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          250
                   ....*....|....
gi 2244985390  364 LKTEIEALKLKERE 377
Cdd:PTZ00121  1659 NKIKAAEEAKKAEE 1672
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 1-36 8.49e-06

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: 44.16  E-value: 8.49e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2244985390   1 MTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDL 36
Cdd:cd14473    64 RKPEEWEKRIVELHKKLRGLSPAEAKLKYLKIARKL 99
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 124-385 3.59e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 3.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  124 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 196
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  197 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 270
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  271 KEADQLKQDLQEAREAERRAKQKLLEIATkpTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEY 350
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2244985390  351 MEKSKH-LQEQLNELKTEIEALKLKERETALDILHN 385
Cdd:TIGR02168  906 LESKRSeLRRELEELREKLAQLELRLEGLEVRIDNL 941
growth_prot_Scy NF041483
polarized growth protein Scy;
134-287 3.17e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.28  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  134 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 213
Cdd:NF041483   490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  214 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRL------MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 287
Cdd:NF041483   560 EETERAIAARQAEAAEELTR-----LHTEAEERLtaaeeaLADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
growth_prot_Scy NF041483
polarized growth protein Scy;
139-300 3.55e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  139 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 218
Cdd:NF041483   583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  219 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 293
Cdd:NF041483   660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                   ....*..
gi 2244985390  294 LLEIATK 300
Cdd:NF041483   740 LLASARK 746
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 129-371 8.06e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 129 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 208
Cdd:COG1196   565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 209 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAE---VLALKMAEESERRAKEADQLKQDLQEARE 285
Cdd:COG1196   645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEElelEEALLAEEEEERELAEAEEERLEEELEEE 724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 286 AERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPsfnligDSLSFDFKDTDMKRLSMEIEK-EKV------EY---MEKSK 355
Cdd:COG1196   725 ALEEQLEAEREELLEELLEEEELLEEEALEELP------EPPDLEELERELERLEREIEAlGPVnllaieEYeelEERYD 798

                         250
                  ....*....|....*.
gi 2244985390 356 HLQEQLNELKTEIEAL 371
Cdd:COG1196   799 FLSEQREDLEEARETL 814
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 129-189 2.71e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.86  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2244985390 129 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 189
Cdd:PLN03086    3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 151-236 4.36e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 151 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 229
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106


                  ....*..
gi 2244985390 230 EMQRIKA 236
Cdd:cd06503   107 EKEKALA 113
 
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 ...
 38-134 1.54e-65

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: 204.04  E-value: 1.54e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  38 MYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKL 117
Cdd:cd13194     1 MYGVNYFEIKNKKGTDLWLGVDALGLNIYEPDNKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYSPRLRINKR 80

                          90
                  ....*....|....*..
gi 2244985390 118 ILQLCIGNHDLFMRRRK 134
Cdd:cd13194    81 ILDLCMGNHELYMRRRK 97
FERM_C pfam09380
FERM C-terminal PH-like domain;
48-133 2.92e-29

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 108.88  E-value: 2.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  48 NKKGTELLLGVDALGLHIYDPENRLtpKISFPWNEIRNISYSDKEFTIKPLDKKI-DVFKFNSSKLRVNKLILQLCIGNH 126
Cdd:pfam09380   1 DKEGTDLWLGVSAKGILVYEDNNKI--LNLFPWREIRKISFKRKKFLIKLRDKSSeETLGFYTESSRACKYLWKLCVEQH 78


                  ....*..
gi 2244985390 127 DLFMRRR 133
Cdd:pfam09380  79 TFFRLRR 85
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 168-287 3.67e-20

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: 85.36  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 168 REEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL 247
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2244985390 248 MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 287
Cdd:pfam20492  81 LEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
ERM_C pfam00769
Ezrin/radixin/moesin family C terminal; This entry represents the C-terminal domain of the ERM ...
 340-401 1.95e-17

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


Pssm-ID: 459932 [Multi-domain]  Cd Length: 77  Bit Score: 76.47  E-value: 1.95e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244985390 340 SMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSdRGGSSKHNTIKK 401
Cdd:pfam00769   1 SLEIEEERVTYAEKNKRLQEQLKELKSELAQARDETKQTALDILHEENV-RQGRDKYKTLRK 61
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 40-130 1.34e-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: 74.72  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  40 GVNYFAIRNK--KGTELLLGVDALGLHIYDPENRlTPKISFPWNEIRNISYS-DKEFTIKPLDK-KIDVFKFNSSKlRVN 115
Cdd:cd00836     1 GVEFFPVKDKskKGSPIILGVNPEGISVYDELTG-QPLVLFPWPNIKKISFSgAKKFTIVVADEdKQSKLLFQTPS-RQA 78

                          90
                  ....*....|....*
gi 2244985390 116 KLILQLCIGNHDLFM 130
Cdd:cd00836    79 KEIWKLIVGYHRFLL 93
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 40-135 1.62e-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: 69.30  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  40 GVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKK--------------IDVF 105
Cdd:cd13191     1 GVHYYEVKDKNGIPWWLGVSYKGIGQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRrnshrsrrtfqsssVSVH 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2244985390 106 KFNSSKLRVNKLILQLCIGNHDLFMRRRKA 135
Cdd:cd13191    81 VWYGQTPALCKTIWSMAIAQHQFYLDRKQS 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 132-298 5.62e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 5.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 132 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 211
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 212 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 291
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                  ....*..
gi 2244985390 292 QKLLEIA 298
Cdd:COG1196   435 EEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-300 1.49e-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: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 210
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 290
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                         170
                  ....*....|
gi 2244985390 291 KQKLLEIATK 300
Cdd:COG1196   469 LEEAALLEAA 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 139-300 3.59e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 139 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 218
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 219 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 298
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399


                  ..
gi 2244985390 299 TK 300
Cdd:COG1196   400 AQ 401
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 127-298 5.72e-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: 5.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 127 DLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLL 206
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 207 AEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREA 286
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                         170
                  ....*....|..
gi 2244985390 287 ERRAKQKLLEIA 298
Cdd:COG1196   395 AAELAAQLEELE 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 138-300 1.02e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 138 LEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEA 217
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 218 KLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 297
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433


                  ...
gi 2244985390 298 ATK 300
Cdd:COG1196   434 EEE 436
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 1-44 1.08e-10

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: 60.77  E-value: 1.08e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2244985390    1 MTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 44
Cdd:smart00295 158 RKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-300 1.11e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 210
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 290
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                         170
                  ....*....|
gi 2244985390 291 KQKLLEIATK 300
Cdd:COG1196   483 LEELAEAAAR 492
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-299 1.45e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 210
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 290
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412


                  ....*....
gi 2244985390 291 KQKLLEIAT 299
Cdd:COG1196   413 LERLERLEE 421
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 132-300 2.33e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 132 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQmREEAErtRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 211
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLE-ELEEE--LAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 212 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 291
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441


                  ....*....
gi 2244985390 292 QKLLEIATK 300
Cdd:COG1196   442 EALEEAAEE 450
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-300 6.51e-10

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: 6.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREkqmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 210
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 290
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                         170
                  ....*....|
gi 2244985390 291 KQKLLEIATK 300
Cdd:COG1196   448 AEEEAELEEE 457
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-300 6.81e-10

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: 6.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 210
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRA 290
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                         170
                  ....*....|
gi 2244985390 291 KQKLLEIATK 300
Cdd:COG1196   462 LELLAELLEE 471
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 140-300 1.95e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.05  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 140 VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKL 219
Cdd:PRK09510   61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAK 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 220 LAQKA-AEAEQEMQRIKATAIRTEEEKrlmeqKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 298
Cdd:PRK09510  141 AAAAAkAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215


                  ..
gi 2244985390 299 TK 300
Cdd:PRK09510  216 KK 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-298 6.57e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 6.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 133 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQI 212
Cdd:COG1196   213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 213 TEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQ 292
Cdd:COG1196   293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372


                  ....*.
gi 2244985390 293 KLLEIA 298
Cdd:COG1196   373 ELAEAE 378
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 1-44 9.52e-09

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


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 53.04  E-value: 9.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2244985390   1 MTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYF 44
Cdd:pfam00373  74 MKSKELEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 39-129 1.98e-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: 51.56  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  39 YGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK-------PLDKKIDvFKFNSSk 111
Cdd:cd13184     1 YGVDLHPAKDSEGVDIMLGVCSSGLLVYRDRLRIN---RFAWPKVLKISYKRNNFYIKirpgefeQYETTIG-FKLPNH- 75

                          90
                  ....*....|....*...
gi 2244985390 112 lRVNKLILQLCIGNHDLF 129
Cdd:cd13184    76 -RAAKRLWKVCVEHHTFF 92
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 38-129 2.01e-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: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  38 MYGVNYFAIRNKKGTELLLGVDALGLHIYdpENRLtpKIS-FPWNEIRNISYSDKEFTI----KPLDKKIDVFKFNSSKL 112
Cdd:cd13189     1 LYGVELHSARDSNNLELQIGVSSAGILVF--QNGI--RINtFPWSKIVKISFKRKQFFIqlrrEPNESRDTILGFNMLSY 76

                          90
                  ....*....|....*..
gi 2244985390 113 RVNKLILQLCIGNHDLF 129
Cdd:cd13189    77 RACKNLWKSCVEHHTFF 93
PTZ00121 PTZ00121
MAEBL; Provisional
 132-294 2.03e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 2.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-EATMANEALMRSEETADLLAEKA 210
Cdd:PTZ00121  1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEA 1612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  211 QiTEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESeRRAKEADQLKQDLQEAREAERRA 290
Cdd:PTZ00121  1613 K-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-KKAEEDKKKAEEAKKAEEDEKKA 1690


                   ....
gi 2244985390  291 KQKL 294
Cdd:PTZ00121  1691 AEAL 1694
PTZ00121 PTZ00121
MAEBL; Provisional
 132-293 2.23e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 2.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSLEVQQMKAQARE----EKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 204
Cdd:PTZ00121  1277 ARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAA 1356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  205 LLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEADQLKQDLQEAR 284
Cdd:PTZ00121  1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD--ELKKAAAAKKKADEAKKKAEEKKKAD 1434


                   ....*....
gi 2244985390  285 EAERRAKQK 293
Cdd:PTZ00121  1435 EAKKKAEEA 1443
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 131-298 2.61e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 55.58  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 210
Cdd:PRK09510   81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA--REAER 288
Cdd:PRK09510  161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEakAAAEK 240

                         170
                  ....*....|
gi 2244985390 289 RAKQKLLEIA 298
Cdd:PRK09510  241 AAAAKAAEKA 250
FERM_C_FRMD3_FRMD5 cd13192
FERM domain C-lobe of FERM domain-containing protein 3 and 5 (FRMD3 and 5); FRMD3 (also called ...
 25-104 6.02e-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: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  25 AEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTI---KPLDKK 101
Cdd:cd13192     1 AEDNFLRKAATLETYGVDPHPVKDHRGNQLYLGFTHTGIVTFQGGKRVH---HFRWNDITKFNYEGKMFILhvmQKEEKK 77


                  ...
gi 2244985390 102 IDV 104
Cdd:cd13192    78 HTL 80
PTZ00121 PTZ00121
MAEBL; Provisional
 132-297 7.40e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 7.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSL----EVQQMKAQAREEKARKQMERQRLA-REKQMREEAERTRDELERRLLQmkEEATMANEALmRSEETADLL 206
Cdd:PTZ00121  1545 KKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMAlRKAEEAKKAEEARIEEVMKLYE--EEKKMKAEEA-KKAEEAKIK 1621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  207 AEKAQITEEEAKLLAQKAAEAEQEMQRI-------KATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEadQLKQD 279
Cdd:PTZ00121  1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeEENKIKAAEEAKKAEEDKKKAE--EAKKAEEDEKKAAE--ALKKE 1697

                          170
                   ....*....|....*...
gi 2244985390  280 LQEAREAERRAKQKLLEI 297
Cdd:PTZ00121  1698 AEEAKKAEELKKKEAEEK 1715
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 130-300 9.74e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 53.66  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 130 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMRSEETADLLAEK 209
Cdd:PRK09510   67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEEAAKQAALKQKQAEEAAAKAAAA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 210 AQI-TEEEAKLLAQKAAEAEQEMqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 288
Cdd:PRK09510  145 AKAkAEAEAKRAAAAAKKAAAEA---KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA 221

                         170
                  ....*....|..
gi 2244985390 289 RAKQKLLEIATK 300
Cdd:PRK09510  222 EAKAAAAKAAAE 233
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 139-300 1.52e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  139 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 218
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  219 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIA 298
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907


                   ..
gi 2244985390  299 TK 300
Cdd:TIGR02168  908 SK 909
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 39-131 2.87e-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: 48.05  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  39 YGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKisFPWNEIRNISYSDKEFTIKPLDKKIDV-FKFNSSklRVNKL 117
Cdd:cd13188     1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRPPVF--FRWEDIKNVINHKRTFSIECQNSEETVqFQFEDA--ETAKY 76

                          90
                  ....*....|....
gi 2244985390 118 ILQLCIGNHDLFMR 131
Cdd:cd13188    77 VWKLCVLQHKFYRQ 90
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 133-305 1.39e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 133 RKADSLEVQQMKAQAREEKARKQMERQRlarekqmrEEAERTRDELERRLLQMKEEATMAN--EALMRSEETADLL---- 206
Cdd:COG3883    51 EEYNELQAELEALQAEIDKLQAEIAEAE--------AEIEERREELGERARALYRSGGSVSylDVLLGSESFSDFLdrls 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 207 -------AEKAQITE--EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLK 277
Cdd:COG3883   123 alskiadADADLLEElkADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202

                         170       180
                  ....*....|....*....|....*...
gi 2244985390 278 QDLQEAREAERRAKQKLLEIATKPTYPP 305
Cdd:COG3883   203 AELAAAEAAAAAAAAAAAAAAAAAAAAA 230
PTZ00121 PTZ00121
MAEBL; Provisional
 132-292 1.66e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSLEVQQMKAQAREEKARKQMERQRLA------REKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADl 205
Cdd:PTZ00121  1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAaeaakaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK- 1392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  206 lAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEARE 285
Cdd:PTZ00121  1393 -ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471


                   ....*..
gi 2244985390  286 AERRAKQ 292
Cdd:PTZ00121  1472 ADEAKKK 1478
PRK12704 PRK12704
phosphodiesterase; Provisional
 132-291 1.92e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 132 RRKADSLEVQQMKAQARE--EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETadlLAEK 209
Cdd:PRK12704   25 RKKIAEAKIKEAEEEAKRilEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN---LDRK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 210 AQITEEEAKLLAQKAAEAEQEMQRIK-----ATAIRTEEEKRLMEQKVL---EAEVLALKMAEEsERRAKEADQLKQDLQ 281
Cdd:PRK12704  102 LELLEKREEELEKKEKELEQKQQELEkkeeeLEELIEEQLQELERISGLtaeEAKEILLEKVEE-EARHEAAVLIKEIEE 180

                         170
                  ....*....|.
gi 2244985390 282 EARE-AERRAK 291
Cdd:PRK12704  181 EAKEeADKKAK 191
PTZ00121 PTZ00121
MAEBL; Provisional
 132-377 1.99e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSLEVQQMKAQAREEkARKQMERQRLAREKQMREEAERTRDELERRllqmKEEATMANEALMRSEEtADLLAEKAQ 211
Cdd:PTZ00121  1430 KKKADEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKADEAKKK----AEEAKKADEAKKKAEE-AKKKADEAK 1503

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  212 ITEEEAKLL--------AQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 283
Cdd:PTZ00121  1504 KAAEAKKKAdeakkaeeAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  284 REAERRAKQKLLEIAtkPTYPPMNPIPAPLPPDIPSFNLIGDSLSfdfKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNE 363
Cdd:PTZ00121  1584 EEAKKAEEARIEEVM--KLYEEEKKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          250
                   ....*....|....
gi 2244985390  364 LKTEIEALKLKERE 377
Cdd:PTZ00121  1659 NKIKAAEEAKKAEE 1672
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 40-135 2.21e-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: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  40 GVNYFAI-RNKK--GTELLLGVDALGLHIYDPEN-RLTPKISFPWNEIRNISYSDKEFTIKP--LDKKIDVFKFNSSKlr 113
Cdd:cd13187     1 GVHFHRVyREKKssTLSLWLGICSRGIIIYEEKNgARTPVLRFPWRETQKISFDKKKFTIESrgGSGIKHTFYTDSYK-- 78

                          90       100
                  ....*....|....*....|....
gi 2244985390 114 VNKLILQLCIGNH--DLFMRRRKA 135
Cdd:cd13187    79 KSQYLLQLCSAQHkfHIQMRSRQS 102
FERM_C_FRMD1_FRMD6 cd13185
FERM domain C-lobe of FERM domain containing 1 and 6 proteins; FRMD6 (also called willin and ...
 47-131 2.35e-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: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  47 RNKKGTE--LLLGVDALGLHIYDP-ENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRvNKLILQLCI 123
Cdd:cd13185    12 KSKKETPgsVLLGITAKGIQIYQEsDGEQQLLRTFPWSNIGKLSFDRKKFEIRPEGSLRKLTYYTSSDEK-SKYLLALCR 90


                  ....*...
gi 2244985390 124 GNHDLFMR 131
Cdd:cd13185    91 ETHQFSMA 98
PTZ00121 PTZ00121
MAEBL; Provisional
 127-390 2.54e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  127 DLFMRRRKADSL---EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR-----LLQMKEEATMANEALMR 198
Cdd:PTZ00121  1575 DKNMALRKAEEAkkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkveqLKKKEAEEKKKAEELKK 1654

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  199 SEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQkVLEAEVLALKMAEESeRRAKEADQLK- 277
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEEL-KKAEEENKIKa 1732

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  278 -QDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDtdmKRLSMEIEKEKVEYMEKSKH 356
Cdd:PTZ00121  1733 eEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED---EKRRMEVDKKIKDIFDNFAN 1809

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2244985390  357 LQEQLNELKTEIEALKLKERETALDILHNENSDR 390
Cdd:PTZ00121  1810 IIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 139-291 4.38e-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: 48.90  E-value: 4.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  139 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 218
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244985390  219 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 291
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 1-36 8.49e-06

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: 44.16  E-value: 8.49e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2244985390   1 MTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDL 36
Cdd:cd14473    64 RKPEEWEKRIVELHKKLRGLSPAEAKLKYLKIARKL 99
PTZ00121 PTZ00121
MAEBL; Provisional
 132-291 9.60e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 9.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSLEvQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERR---------LLQMKEEATMANEALMRSEET 202
Cdd:PTZ00121  1404 KKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeeakkaeeAKKKAEEAKKADEAKKKAEEA 1482

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  203 ADllAEKAQITEEEAKLLAQKAAEAEQEMQriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRaKEADQLKQdLQE 282
Cdd:PTZ00121  1483 KK--ADEAKKKAEEAKKKADEAKKAAEAKK--KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK-KKADELKK-AEE 1556


                   ....*....
gi 2244985390  283 AREAERRAK 291
Cdd:PTZ00121  1557 LKKAEEKKK 1565
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 137-293 1.48e-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: 46.76  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 137 SLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAtmANEALMRSEETADLLAEKAQITEEE 216
Cdd:TIGR02794  46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA--AAEKAAKQAEQAAKQAEEKQKQAEE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 217 AKLL----AQKAAEAEQEMQRIKATAIRTEEEKrlmeqkvleaevlALKMAEESERRAKEAD-QLKQDLQEAREAERRAK 291
Cdd:TIGR02794 124 AKAKqaaeAKAKAEAEAERKAKEEAAKQAEEEA-------------KAKAAAEAKKKAEEAKkKAEAEAKAKAEAEAKAK 190


                  ..
gi 2244985390 292 QK 293
Cdd:TIGR02794 191 AE 192
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 132-292 1.51e-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: 46.76  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 132 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 211
Cdd:TIGR02794  69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 212 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVlEAEVLALKMAEESERRAKEADQLKQDLQEAR---EAER 288
Cdd:TIGR02794 149 AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKA-KAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAaaaEAER 227


                  ....
gi 2244985390 289 RAKQ 292
Cdd:TIGR02794 228 KADE 231
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 139-296 1.61e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.72  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 139 EVQQMKAQAREEKaRKQMERQRLAREKQmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 218
Cdd:PRK09510  105 QLEKERLAAQEQK-KQAEEAAKQAALKQ-KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 219 LLAQKAAEAEQ---EMQRIKATAIRTEEEKRLMEQKvleAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 295
Cdd:PRK09510  183 AKKKAEAEAAAkaaAEAKKKAEAEAKKKAAAEAKKK---AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259


                  .
gi 2244985390 296 E 296
Cdd:PRK09510  260 D 260
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 135-294 1.73e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.97  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  135 ADSLEVQQMKAQAR-EEKARKQMERQRLARE--------KQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtADL 205
Cdd:PRK10929   104 TDALEQEILQVSSQlLEKSRQAQQEQDRAREisdslsqlPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQ-AES 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  206 LAEKAQITEEEaklLAQKAAEAEQEMQRIKATAIRTEEEK----------RLMEQKVLEAEvLALkmaEESERRAKEADQ 275
Cdd:PRK10929   183 AALKALVDELE---LAQLSANNRQELARLRSELAKKRSQQldaylqalrnQLNSQRQREAE-RAL---ESTELLAEQSGD 255

                          170
                   ....*....|....*....
gi 2244985390  276 LKQDLQEAREAERRAKQKL 294
Cdd:PRK10929   256 LPKSIVAQFKINRELSQAL 274
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
132-294 2.13e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSLEvqQMKAQARE-EKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAEKA 210
Cdd:COG4913    248 REQIELLE--PIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL------ERLEARLD 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  211 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKM-------AEESERRAKEADQLKQDLQEA 283
Cdd:COG4913    320 ALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEE 399

                          170
                   ....*....|.
gi 2244985390  284 REAERRAKQKL 294
Cdd:COG4913    400 LEALEEALAEA 410
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 39-96 2.26e-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: 2.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2244985390  39 YGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPwnEIRNISYSDKEFTIK 96
Cdd:cd13195     1 YGVEFFEVRNIEGQKLLIGVGPHGITICNDDFEVIERIPYT--AIQMATSSGRVFTLT 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 132-300 2.45e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 132 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMRE-EAERTRDELERRLLQMKEEATMANEAlmrsEETADLLAEKA 210
Cdd:COG1196   199 ERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRElEAELEELEAELEELEAELEELEAELA----ELEAELEELRL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvLALKMAEESERRAKEADQLKQDLQEAREAERRA 290
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE-LEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         170
                  ....*....|
gi 2244985390 291 KQKLLEIATK 300
Cdd:COG1196   354 EEAEAELAEA 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 124-385 3.59e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 3.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  124 GNHDLFMRRRKADSLE--VQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKE-----EATMANEAL 196
Cdd:TIGR02168  668 TNSSILERRREIEELEekIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  197 MRSEETADLLAEKAQITEEEAKL--LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKV--LEAEVLALK--MAEESERRA 270
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEIEELEAQIEQLKEELKALREALdeLRAELTLLNeeAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  271 KEADQLKQDLQEAREAERRAKQKLLEIATkpTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEY 350
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIES--LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2244985390  351 MEKSKH-LQEQLNELKTEIEALKLKERETALDILHN 385
Cdd:TIGR02168  906 LESKRSeLRRELEELREKLAQLELRLEGLEVRIDNL 941
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-298 4.22e-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: 4.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 147 AREEKARKQME--RQRLAR--------EKQM---REEAERTR------DELERR-----LLQMKE-EATMANEALMRSEE 201
Cdd:COG1196   172 ERKEEAERKLEatEENLERledilgelERQLeplERQAEKAEryrelkEELKELeaellLLKLRElEAELEELEAELEEL 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 202 TADLLAEKAQITEEEAKL---------LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKE 272
Cdd:COG1196   252 EAELEELEAELAELEAELeelrleleeLELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                         170       180
                  ....*....|....*....|....*.
gi 2244985390 273 ADQLKQDLQEAREAERRAKQKLLEIA 298
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAE 357
PTZ00121 PTZ00121
MAEBL; Provisional
 139-377 4.31e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 4.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  139 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 218
Cdd:PTZ00121  1210 EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  219 LLAQKAAEAEqEMQRIKATAIRTEEEKRLMEQKVLEAEvlALKMAEESERRAKEadqlKQDLQEAREAERRAKQKLLEIA 298
Cdd:PTZ00121  1290 KKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEE--AKKKADAAKKKAEE----AKKAAEAAKAEAEAAADEAEAA 1362

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2244985390  299 TKPTyppmnpipaplppdipsfnligdslSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERE 377
Cdd:PTZ00121  1363 EEKA-------------------------EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
PTZ00121 PTZ00121
MAEBL; Provisional
 132-300 4.50e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSL----EVQQMKAQAREEKARKQMERQRLAREKQ-----MREEAERTRDELERRllqmKEEATMANEALMRSEET 202
Cdd:PTZ00121  1328 KKKADAAkkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAeaaekKKEEAKKKADAAKKK----AEEKKKADEAKKKAEED 1403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  203 ADLLAEKAQitEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQE 282
Cdd:PTZ00121  1404 KKKADELKK--AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481

                          170
                   ....*....|....*...
gi 2244985390  283 AREAErRAKQKLLEIATK 300
Cdd:PTZ00121  1482 AKKAD-EAKKKAEEAKKK 1498
PTZ00121 PTZ00121
MAEBL; Provisional
 132-377 4.50e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSL----EVQQMKAQAREEKARKQMERQRLAREKQMREEAE-----RTRDELERRLLQMKEEATMANEALMRSEET 202
Cdd:PTZ00121  1496 KKKADEAkkaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeekKKADELKKAEELKKAEEKKKAEEAKKAEED 1575

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  203 ADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEadqlKQDLQE 282
Cdd:PTZ00121  1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE----KKKAEE 1651

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  283 AREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSfnligDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLN 362
Cdd:PTZ00121  1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-----KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726

                          250
                   ....*....|....*
gi 2244985390  363 ELKTEIEALKLKERE 377
Cdd:PTZ00121  1727 ENKIKAEEAKKEAEE 1741
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 32-96 4.96e-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: 42.72  E-value: 4.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2244985390  32 IAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTpkiSFPWNEIRNISYSDKEFTIK 96
Cdd:cd13193     2 TARRCELYGIRLHPAKDREGVKLNLAVAHMGILVFQGFTKIN---TFSWAKIRKLSFKRKRFLIK 63
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
139-300 5.19e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 139 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEeatmANEALMRSEETADLLAEKAQITEEEAK 218
Cdd:COG4717    75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK----LLQLLPLYQELEALEAELAELPERLEE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 219 LLAQKA--AEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLL 295
Cdd:COG4717   151 LEERLEelRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230


                  ....*
gi 2244985390 296 EIATK 300
Cdd:COG4717   231 QLENE 235
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
131-302 5.72e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLArekQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 210
Cdd:PRK02224  282 RDLRERLEELEEERDDLLAEAGLDDADAEAVE---ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 QITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQ-------DLQEA 283
Cdd:PRK02224  359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREreaeleaTLRTA 438

                         170
                  ....*....|....*....
gi 2244985390 284 REAERRAkQKLLEIATKPT 302
Cdd:PRK02224  439 RERVEEA-EALLEAGKCPE 456
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-372 5.76e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 5.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  165 KQMREEAERTRDELERrLLQMKEEATmANEALMRSEETADLLAEKAQI--TEEEAKLLAQKAAEAEQEMQRIKATAIRTE 242
Cdd:COG4913    238 ERAHEALEDAREQIEL-LEPIRELAE-RYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  243 EEKRLMEQKVLEAEvlalkmAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKptyppMNPIPAPLPPDIPSFNL 322
Cdd:COG4913    316 ARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEAL-----LAALGLPLPASAEEFAA 384

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2244985390  323 IGDSLSfDFKDtDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALK 372
Cdd:COG4913    385 LRAEAA-ALLE-ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
PRK12705 PRK12705
hypothetical protein; Provisional
 117-290 7.56e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 44.70  E-value: 7.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 117 LILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKarkqmERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAL 196
Cdd:PRK12705   12 LLIGLLLGVLVVLLKKRQRLAKEAERILQEAQKEA-----EEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 197 MRSEEtaDLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRL--MEQKVLEAEVLALKMAEESERRAKEAD 274
Cdd:PRK12705   87 VQKEE--QLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVagLTPEQARKLLLKLLDAELEEEKAQRVK 164

                         170
                  ....*....|....*.
gi 2244985390 275 QLKQDLQEarEAERRA 290
Cdd:PRK12705  165 KIEEEADL--EAERKA 178
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
132-236 9.03e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.27  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 132 RRKADSLEVQQMKAQAREEKARKQMER-QRLARE----KQMREEAERTRDELERRLLQMKEEATMANEALmrsEETADLL 206
Cdd:COG1566   109 EAEIAAAEAQLAAAQAQLDLAQRELERyQALYKKgavsQQELDEARAALDAAQAQLEAAQAQLAQAQAGL---REEEELA 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 2244985390 207 AEKAQITEEEAKLlaqKAAEAEQEMQRIKA 236
Cdd:COG1566   186 AAQAQVAQAEAAL---AQAELNLARTTIRA 212
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-290 9.95e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 9.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMER--QRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 208
Cdd:COG1196   377 AEEELEELAEELLEALRAAAELAAQLEEleEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 209 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAE-----VLALKMAEESERRAKEADQLKQDLQEA 283
Cdd:COG1196   457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegVKAALLLAGLRGLAGAVAVLIGVEAAY 536


                  ....*..
gi 2244985390 284 REAERRA 290
Cdd:COG1196   537 EAALEAA 543
PTZ00491 PTZ00491
major vault protein; Provisional
 142-273 1.47e-04

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 44.24  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 142 QMKAQAREEKARKQMERQRLarekQMREEAERTRdeleRRLLQMKEEATmANEALMRSEETADLLAEKAQITEEeaklla 221
Cdd:PTZ00491  669 RHQAELLEQEARGRLERQKM----HDKAKAEEQR----TKLLELQAESA-AVESSGQSRAEALAEAEARLIEAE------ 733

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2244985390 222 qkaAEAEQEMQRIKATAIRTEEE-KRLMEQKVLEAEVLAlKMAEESERRAKEA 273
Cdd:PTZ00491  734 ---AEVEQAELRAKALRIEAEAElEKLRKRQELELEYEQ-AQNELEIAKAKEL 782
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-283 1.56e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDE--LERRLLQMKEEATMANEALMRSEETADLLAE 208
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErlEEELEELEEALAELEEEEEEEEEALEEAAEE 450

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2244985390 209 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEA 283
Cdd:COG1196   451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
PTZ00121 PTZ00121
MAEBL; Provisional
 137-377 1.90e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  137 SLEVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDElerrllQMKEEATMANEALMRSEETADllAEKAQITEEE 216
Cdd:PTZ00121  1184 AEEVRKAEELRKAEDARK-AEAARKAEEERKAEEARKAEDA------KKAEAVKKAEEAKKDAEEAKK--AEEERNNEEI 1254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  217 AKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLA---LKMAEESERRAKE---ADQLKQDLQEAREAERRA 290
Cdd:PTZ00121  1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeeKKKADEAKKKAEEakkADEAKKKAEEAKKKADAA 1334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  291 KQKLLEIATKPTYPPMNPIPAplppdipsfnliGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEA 370
Cdd:PTZ00121  1335 KKKAEEAKKAAEAAKAEAEAA------------ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402


                   ....*..
gi 2244985390  371 LKLKERE 377
Cdd:PTZ00121  1403 DKKKADE 1409
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 131-234 2.11e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 210
Cdd:COG1196   676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755

                          90       100
                  ....*....|....*....|....
gi 2244985390 211 QITEEEAKLLAQKAAEAEQEMQRI 234
Cdd:COG1196   756 LPEPPDLEELERELERLEREIEAL 779
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 131-310 2.28e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 43.40  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEaertrdelerrllqmkeeatmanealmRSEETADLLAEKA 210
Cdd:PRK05035  432 RQAKAEIRAIEQEKKKAEEAKARFEARQARLEREKAAREA---------------------------RHKKAAEARAAKD 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 Q--ITEEEAKLLAQKAAEAEQemqrikaTAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAer 288
Cdd:PRK05035  485 KdaVAAALARVKAKKAAATQP-------IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIA-- 555

                         170       180
                  ....*....|....*....|..
gi 2244985390 289 RAKQKLLEIATKPTYPPMNPIP 310
Cdd:PRK05035  556 RAKAKKAAQQAANAEAEEEVDP 577
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 120-319 2.58e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.19  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 120 QLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQR---LAREKQM----REEAERTRDELErrlLQMKEEATMA 192
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRleeQERQQQVerlrQQEEERKRKKLE---LEKEKRDRKR 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 193 NEALMRSEETADLLAEKAQITEEEAKllaQKAAEAEQEMQRikaTAIRTEEEKRLM-EQKVLEAEVLALKMAEESERRAK 271
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERK---RKLLEKEMEERQ---KAIYEEERRREAeEERRKQQEMEERRRIQEQMRKAT 562

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2244985390 272 EADQLKQDLQEARE-----AERRAKQKLLEIATKPTypPMNPIPAP-----LPPDIPS 319
Cdd:pfam17380 563 EERSRLEAMEREREmmrqiVESEKARAEYEATTPIT--TIKPIYRPriseyQPPDVES 618
PTZ00121 PTZ00121
MAEBL; Provisional
 130-293 3.13e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  130 MRRRKADSLEVQQMKAQAREEKaRKQMERQRLAREKQMREEAERTRDELER--RLLQMKEEATMANEALMRSEET--ADL 205
Cdd:PTZ00121  1383 AKKKAEEKKKADEAKKKAEEDK-KKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAkkAEE 1461

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  206 LAEKAQITE--EEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlaLKMAEEserrAKEADQLKQdLQEA 283
Cdd:PTZ00121  1462 AKKKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE---AKKAEE----AKKADEAKK-AEEA 1533

                          170
                   ....*....|..
gi 2244985390  284 REAE--RRAKQK 293
Cdd:PTZ00121  1534 KKADeaKKAEEK 1545
growth_prot_Scy NF041483
polarized growth protein Scy;
134-287 3.17e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.28  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  134 KADSLEVQQmKAQAREEKARKQMERQRLAREKQMREEAERTRDELERrllQMKEEATMANEALMRSEETAdllaekAQIT 213
Cdd:NF041483   490 KADADELRS-TATAESERVRTEAIERATTLRRQAEETLERTRAEAER---LRAEAEEQAEEVRAAAERAA------RELR 559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  214 EEEAKLLAQKAAEAEQEMQRikataIRTEEEKRL------MEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAE 287
Cdd:NF041483   560 EETERAIAARQAEAAEELTR-----LHTEAEERLtaaeeaLADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQE 634
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
139-298 3.18e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.55  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 139 EVQQMKAQAREEKARKQMERQ-RLAREKQMREEAERTRDELERRLLQMKEEATmanealmRSEETADLLAEKA-QITEEE 216
Cdd:COG2268   202 RIAEAEAERETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEER-------REAETARAEAEAAyEIAEAN 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 217 AKLLAQKAAEAEQEMQRIKATAIRTE-EEKRLMEQKVLEAEVLALKMA--EESERRAKEADQLKQdlQEAREAERRAKQK 293
Cdd:COG2268   275 AEREVQRQLEIAEREREIELQEKEAErEEAELEADVRKPAEAEKQAAEaeAEAEAEAIRAKGLAE--AEGKRALAEAWNK 352


                  ....*
gi 2244985390 294 LLEIA 298
Cdd:COG2268   353 LGDAA 357
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 139-300 3.50e-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: 42.80  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 139 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAK 218
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 219 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQkvlEAEVLALKMAEESERRAKEADQLKQDLQEareaERRAKQKLLEIA 298
Cdd:pfam17380 489 AEEQRRKILEKELEERKQAMIEEERKRKLLEK---EMEERQKAIYEEERRREAEEERRKQQEME----ERRRIQEQMRKA 561


                  ..
gi 2244985390 299 TK 300
Cdd:pfam17380 562 TE 563
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 132-312 3.50e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 132 RRKADSLEVQQMKAQAREEKARKQMERQRlAREKQMREEAERTRDELERRLLQM--------------KEEATMANEALM 197
Cdd:COG4942    61 ERRIAALARRIRALEQELAALEAELAELE-KEIAELRAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQ 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 198 RSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLalkMAEESERRAKEADQLK 277
Cdd:COG4942   140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELA 216

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2244985390 278 QDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAP 312
Cdd:COG4942   217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
growth_prot_Scy NF041483
polarized growth protein Scy;
139-300 3.55e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  139 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEALmRSEETADLLAEKAQITEEEAK 218
Cdd:NF041483   583 EAEERLTAAEEALADARAEAERIRREAA--EETERLRTEAAERIRTLQAQAEQEAERL-RTEAAADASAARAEGENVAVR 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  219 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMA-EESERRAKEADQL----KQDLQEAREAERRAKQK 293
Cdd:NF041483   660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAqEEAARRRREAEETlgsaRAEADQERERAREQSEE 739


                   ....*..
gi 2244985390  294 LLEIATK 300
Cdd:NF041483   740 LLASARK 746
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 129-296 4.55e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 4.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  129 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALmrseetADLLAE 208
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI------EELEEL 867

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  209 KAQITEEEAKLLAQKAaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAER 288
Cdd:TIGR02168  868 IEELESELEALLNERA-SLEEALALLRSELEELSEELRELESKRSELR-------RELEELREKLAQLELRLEGLEVRID 939


                   ....*...
gi 2244985390  289 RAKQKLLE 296
Cdd:TIGR02168  940 NLQERLSE 947
PTZ00121 PTZ00121
MAEBL; Provisional
 132-292 4.68e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 4.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSLEVQQMKAQA----REEKARKQMERQRLAREKQMREEAERTRDELERRLLQMK---EEATMANEALMRSEETAD 204
Cdd:PTZ00121  1353 EAAADEAEAAEEKAEAaekkKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaaAAKKKADEAKKKAEEKKK 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  205 llAEKAQITEEEAKllaqKAAEAEQEMQRIKataiRTEEEKRLMEQKVLEAEvlaLKMAEESERRA----KEADQLKQDL 280
Cdd:PTZ00121  1433 --ADEAKKKAEEAK----KADEAKKKAEEAK----KAEEAKKKAEEAKKADE---AKKKAEEAKKAdeakKKAEEAKKKA 1499

                          170
                   ....*....|..
gi 2244985390  281 QEAREAERRAKQ 292
Cdd:PTZ00121  1500 DEAKKAAEAKKK 1511
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 131-292 5.25e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 42.25  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKA 210
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKL 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 211 QitEEEAKLLAQKAAEAEQEMQRIKATAIR-TEEEKRLME----------QKVLEAEVLALKMAEESERRAKEADQLKQD 279
Cdd:pfam15709 433 Q--ELQRKKQQEEAERAEAEKQRQKELEMQlAEEQKRLMEmaeeerleyqRQKQEAEEKARLEAEERRQKEEEAARLALE 510

                         170
                  ....*....|...
gi 2244985390 280 lQEAREAERRAKQ 292
Cdd:pfam15709 511 -EAMKQAQEQARQ 522
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 176-277 5.26e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 176 DELERRLLQMKEEAtmanEALMRSEETADllAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEA 255
Cdd:COG0542   414 DELERRLEQLEIEK----EALKKEQDEAS--FERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487

                          90       100
                  ....*....|....*....|..
gi 2244985390 256 EVLALKMAEESERRAKEADQLK 277
Cdd:COG0542   488 PELEKELAELEEELAELAPLLR 509
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 131-388 6.70e-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: 42.03  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 131 RRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQM--------REEAERTR-DELERRLLQMKEEATMANEALMRSEE 201
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerirqeerKRELERIRqEEIAMEISRMRELERLQMERQQKNER 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 202 TADLL--AEKAQITEEEAKllaQKAAEAEQEMQRIKATA--IRTEEEKRLMEQKVLEAEvlalKMAEESERRAKEADQLK 277
Cdd:pfam17380 394 VRQELeaARKVKILEEERQ---RKIQQQKVEMEQIRAEQeeARQREVRRLEEERAREME----RVRLEEQERQQQVERLR 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 278 QDLQEAR------EAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDT--DMKRLSMEIEKEKVE 349
Cdd:pfam17380 467 QQEEERKrkklelEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQ 546

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2244985390 350 YMEKSKHLQEQL---NELKTEIEALKlKERETALDILHNENS 388
Cdd:pfam17380 547 EMEERRRIQEQMrkaTEERSRLEAME-REREMMRQIVESEKA 587
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 129-371 8.06e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 129 FMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAE 208
Cdd:COG1196   565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 209 KAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAE---VLALKMAEESERRAKEADQLKQDLQEARE 285
Cdd:COG1196   645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEElelEEALLAEEEEERELAEAEEERLEEELEEE 724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 286 AERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPsfnligDSLSFDFKDTDMKRLSMEIEK-EKV------EY---MEKSK 355
Cdd:COG1196   725 ALEEQLEAEREELLEELLEEEELLEEEALEELP------EPPDLEELERELERLEREIEAlGPVnllaieEYeelEERYD 798

                         250
                  ....*....|....*.
gi 2244985390 356 HLQEQLNELKTEIEAL 371
Cdd:COG1196   799 FLSEQREDLEEARETL 814
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 132-279 1.18e-03

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: 41.36  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  132 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEA------ERTRDELERRLLQMKEEATMANEALmrsEETADL 205
Cdd:pfam12128  603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETfartalKNARLDLRRLFDEKQSEKDKKNKAL---AERKDS 679

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2244985390  206 LAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESER--RAKEADQLKQD 279
Cdd:pfam12128  680 ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRsgAKAELKALETW 755
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 150-284 1.28e-03

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: 41.03  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 150 EKARKQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEET-ADLLAEKAQITEEEAKLLAQKAA--- 225
Cdd:pfam07888  51 EAANRQREKEK-ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKyKELSASSEELSEEKDALLAQRAAhea 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2244985390 226 ---EAEQEMQRIKATAIRTEEEKRLMEQKVLEAevLALKMAEESERRA---------KEADQLKQDLQEAR 284
Cdd:pfam07888 130 rirELEEDIKTLTQRVLERETELERMKERAKKA--GAQRKEEEAERKQlqaklqqteEELRSLSKEFQELR 198
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 139-281 1.30e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  139 EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRD-------ELERRLLQMKEEATMANEALMRSEETADLLAEKAQ 211
Cdd:TIGR02169  372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  212 ITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQ 281
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 149-271 1.36e-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: 38.87  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 149 EEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAE 228
Cdd:pfam05672  10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEERE 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2244985390 229 QEMQRIKATAIRTEEE-----KRLMEQKVLEAEVLALKMAEESERRAK 271
Cdd:pfam05672  90 QREQEEQERLQKQKEEaeakaREEAERQRQEREKIMQQEEQERLERKK 137
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
127-297 1.78e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 127 DLFMRRRKADSLEVQQMKAQAREEKARKQmERQRLAREKQMREEAERTRDELERRLLQMKEEAtmanEALMRSEETADLL 206
Cdd:COG4717    57 ELFKPQGRKPELNLKELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREEL----EKLEKLLQLLPLY 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 207 AEKAQItEEEAKLLAQKAAEAEQEMQRIKataiRTEEEKRLMEQKVLEAE-VLALKMAEESERRAKEADQLKQDLQEARE 285
Cdd:COG4717   132 QELEAL-EAELAELPERLEELEERLEELR----ELEEELEELEAELAELQeELEELLEQLSLATEEELQDLAEELEELQQ 206

                         170
                  ....*....|..
gi 2244985390 286 AERRAKQKLLEI 297
Cdd:COG4717   207 RLAELEEELEEA 218
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
132-295 2.23e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 132 RRKADSLEVQQMKAQAREEKARKQMERQRLAREKQM----REEAERTRDELERRLLQMKEEATMANEALmrsEETADLLA 207
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPlyqeLEALEAELAELPERLEELEERLEELRELE---EELEELEA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 208 EKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEvlalkmaEESERRAKEADQLKQDLQEAREAE 287
Cdd:COG4717   171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ-------EELEELEEELEQLENELEAAALEE 243


                  ....*...
gi 2244985390 288 RRAKQKLL 295
Cdd:COG4717   244 RLKEARLL 251
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 138-298 2.26e-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: 40.44  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  138 LEVQQMKAQAREEKARKQMERQRLAREKQMRE--EAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEE 215
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  216 EAKLLAQKAAEAEQEMQRIKATAIRTEEE----KRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAK 291
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486


                   ....*..
gi 2244985390  292 QKLLEIA 298
Cdd:TIGR02169  487 KLQRELA 493
Rabaptin pfam03528
Rabaptin;
149-292 2.62e-03

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 39.70  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 149 EEKARKQMERQRlAREKQMREEAERTRDELERRLLQMKEEATMANEaLMRSEETADLLAEKAQITEEEAKLLAQKAAEAE 228
Cdd:pfam03528 121 EVQFHRRLEQER-AQWNQYRESAEREIADLRRRLSEGQEEENLEDE-MKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAE 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2244985390 229 QEMQRIKATAIRT-----EEEKRLMEQKVLEAEVLALK---MAEESERRAKEADQLKQDLQEAREAERRAKQ 292
Cdd:pfam03528 199 DKIKELEASKMKElnhylEAEKSCRTDLEMYVAVLNTQksvLQEDAEKLRKELHEVCHLLEQERQQHNQLKH 270
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
145-297 2.69e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 145 AQAREEKARKQMERQRLAREKQMREEA-ERTRD--ELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLa 221
Cdd:PRK02224  471 EEDRERVEELEAELEDLEEEVEEVEERlERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL- 549

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2244985390 222 qkaaEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 297
Cdd:PRK02224  550 ----EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 129-189 2.71e-03

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 39.86  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2244985390 129 FMRRRKADSLEvqqmkaqaREEKARKQMERQRLAREKQMREEAERTRDELE-----RRL--LQMKEEA 189
Cdd:PLN03086    3 FELRRAREKLE--------REQRERKQRAKLKLERERKAKEEAAKQREAIEaaqrsRRLdaIEAQIKA 62
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-290 2.72e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  111 KLRVNKLILQLCIGNHDLFMRRRKADSL--EVQQMKAQAREEKARKQMERQRLAREKQMREEAERTR--------DELER 180
Cdd:COG4913    266 AARERLAELEYLRAALRLWFAQRRLELLeaELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLER 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  181 RLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMqrikatairtEEEKRLMEQKVLEAEVLAL 260
Cdd:COG4913    346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL----------EEELEALEEALAEAEAALR 415

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2244985390  261 KMAEESERRAKEADQLKQ-------DLQEAREAERRA 290
Cdd:COG4913    416 DLRRELRELEAEIASLERrksnipaRLLALRDALAEA 452
PTZ00121 PTZ00121
MAEBL; Provisional
 139-377 3.54e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  139 EVQQMKAQAREEKARKqMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEAlmRSEETADLLAEKAQITEEEAK 218
Cdd:PTZ00121  1114 ARKAEEAKKKAEDARK-AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA--RKAEDAKKAEAARKAEEVRKA 1190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  219 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKvleaevlalKMAEEserrAKEADQLKQDLQEAREAErraKQKLLEIA 298
Cdd:PTZ00121  1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDA---------KKAEA----VKKAEEAKKDAEEAKKAE---EERNNEEI 1254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  299 TKPTYPPMNPIPAPLPPDIPSFNLIGDSL--SFDFKDTDMKRLSMEIE-----KEKVEYMEKSKHLQEQLNELKTEIEAL 371
Cdd:PTZ00121  1255 RKFEEARMAHFARRQAAIKAEEARKADELkkAEEKKKADEAKKAEEKKkadeaKKKAEEAKKADEAKKKAEEAKKKADAA 1334


                   ....*.
gi 2244985390  372 KLKERE 377
Cdd:PTZ00121  1335 KKKAEE 1340
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 144-297 4.20e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.57  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  144 KAQAREEKARKQMERQRLAR-----EKQMREEAERTRDELERRLLQMKEEATMANEALMRSEEtadLLAEKAQITEEEAK 218
Cdd:pfam02463  171 KKEALKKLIEETENLAELIIdleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK---LNEERIDLLQELLR 247

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2244985390  219 LLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEI 297
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 151-236 4.36e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 151 KARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEA-TMANEALMRSEETADLLAEKAQitEEEAKLLAQKAAEAEQ 229
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAqEIIEEARKEAEKIKEEILAEAK--EEAERILEQAKAEIEQ 106


                  ....*..
gi 2244985390 230 EMQRIKA 236
Cdd:cd06503   107 EKEKALA 113
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 133-286 4.36e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 39.22  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 133 RKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERtrdelerrllqMKEEATMANEALMRSEETADLLAEKAQI 212
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK-----------QQEAKNLPKPADTSSPKEDKQVAENQKR 281

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2244985390 213 TEEEAKLLAQKAAEAEQEMQRIKATAIRTE--EEKRLMEQKVLEAEVLALKMAEESERRAKEAD-QLKQDLQEAREA 286
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQEskASEKEAEDKELEAQKKREPVAEDLQKTKPQVEaQPTSLNEDAIDS 358
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 130-288 4.38e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.75  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 130 MRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRseETADLLAEK 209
Cdd:pfam13868  30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ--EREQMDEIV 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2244985390 210 AQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAER 288
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 153-296 4.83e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 153 RKQMERQRLAREKQMREEAERTRDELERRllQMKEEATMANEALMrsEETADLLAEKAQIteeeakllaqkAAEAEQEMQ 232
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERR--RKLEEAEKARQAEM--DRQAAIYAEQERM-----------AMERERELE 351

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2244985390 233 RikataIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERraKQKLLE 296
Cdd:pfam17380 352 R-----IRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR--KVKILE 408
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 139-300 5.37e-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: 38.78  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 139 EVQQMKAQAREEKARKQMERQRLAREKQmrEEAERTRDELERRLLQMKEEATMANEAL----MRSEETADLLAEKAQITE 214
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQL--ERAEKMREELELEQQRRFEEIRLRKQRLeeerQRQEEEERKQRLQLQAAQ 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 215 EEAKLLAQKAAEAEQEMQRIKAT--AIRTEEEKRL---MEQKVLEAEVLALKMAEES-----ERRAKEADQLKQDLQEAR 284
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRKKQQeeAERAEAEKQRqkeLEMQLAEEQKRLMEMAEEErleyqRQKQEAEEKARLEAEERR 498

                         170
                  ....*....|....*.
gi 2244985390 285 EAERRAKQKLLEIATK 300
Cdd:pfam15709 499 QKEEEAARLALEEAMK 514
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 135-267 5.39e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 135 ADSLEVQQMKAQArEEKARKQmeRQRLAREKQMREEAERTRDELERRLLQMKEEatmanEALMRSEetadlLAEKAQITE 214
Cdd:PRK00409  513 EDKEKLNELIASL-EELEREL--EQKAEEAEALLKEAEKLKEELEEKKEKLQEE-----EDKLLEE-----AEKEAQQAI 579

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2244985390 215 EEAKLLAQKAAEAEQEMQRIKATAIR---TEEEKRLMEQKVLEAEVLALKMAEESE 267
Cdd:PRK00409  580 KEAKKEADEIIKELRQLQKGGYASVKaheLIEARKRLNKANEKKEKKKKKQKEKQE 635
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
147-290 5.46e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 5.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390  147 AREEKARKQMERQRLAREkqmREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKL------- 219
Cdd:COG4913    608 NRAKLAALEAELAELEEE---LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELerldass 684

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2244985390  220 -----LAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLalkmAEESERRAKEADQLKQDLQEAREAERRA 290
Cdd:COG4913    685 ddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFA 756
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 137-297 6.70e-03

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: 38.58  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 137 SLEVQQMkaqaREEKARKQMERQRLAREKQMREEAERTRDELERRLL-----QMKEEATMANEALMR------------- 198
Cdd:pfam07111 480 SLELEQL----REERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLsevaqQLEQELQRAQESLASvgqqlevarqgqq 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 199 --SEETADLLAEKAQITEEEAKLLAQKAAEAEQEM-QRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERrakeADQ 275
Cdd:pfam07111 556 esTEEAASLRQELTQQQEIYGQALQEKVAEVETRLrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER----NQE 631

                         170       180
                  ....*....|....*....|...
gi 2244985390 276 LKQDLQEAREAE-RRAKQKLLEI 297
Cdd:pfam07111 632 LRRLQDEARKEEgQRLARRVQEL 654
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
125-300 6.97e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 38.42  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 125 NHDLFMRRRKAdslevqqmkAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEAT--MANEALMRSEET 202
Cdd:PRK07735    4 EKDLEDLKKEA---------ARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244985390 203 ADLLAEKAQITEEEAKLLAQKAAEAEQemqriKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQE 282
Cdd:PRK07735   75 AKQKREGTEEVTEEEKAKAKAKAAAAA-----KAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREG 149

                         170
                  ....*....|....*...
gi 2244985390 283 AREAERRAKQKLLEIATK 300
Cdd:PRK07735  150 TEEVTEEEEETDKEKAKA 167
 
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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