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Conserved domains on  [gi|1024747630|gb|KZZ86796|]
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septin AspB [Ascosphaera apis ARSEF 7405]

Protein Classification

septin family protein( domain architecture ID 11472051)

septin family protein is a filament-forming cytoskeletal GTPase, whose activity is involved in various cellular processes, including cytoskeleton organization, cytokinesis, and membrane dynamics

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 701-1081 1.69e-165

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


:

Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 492.61  E-value: 1.69e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  701 TGYVGFANLPNQWHRKSVRKGFSFNVMVVGESGLGKSTLVNTLFNSSLYPPKEYSGPSNDILPKTVGIQSTSSDIEENGV 780
Cdd:COG5019      1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRAEGTSPTLEIKITKAELEEDGF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  781 RLRLTVVDTPGFGDFVNNDESWRPIVENIESRFDAYLEAENKVNR-MNIVDNRIHACIYFIQPTGHSLKPLDIQVMKLLH 859
Cdd:COG5019     81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  860 TKVNLIPVIAKSDTLTDEEVGNFKQRILADINYHRINIFESPRYELDDEETIAENQEIMSKVPFAVVGANTEVTTaDGRK 939
Cdd:COG5019    161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLEENQDLRSLIPFAIIGSNTEIEN-GGEQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  940 VRGRRYPWGVIEVDNEEHCDFVKLRQMLIRTHMEELKEQTNNVLYEDYRTEKLTQMGVTQDSSvfkevnpavkqeeERAL 1019
Cdd:COG5019    240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNSGEPS-------------LKEI 306

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024747630 1020 HEAKLAKMESEMKAVFQQKVHEKESKLKQSEDELYARHREMKEQLEKQRAELEEKKARIESG 1081
Cdd:COG5019    307 HEARLNEEERELKKKFTEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKL 368
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 161-389 2.87e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  161 PTSARNAASSPDTSINTAITTATSASSMQSSTVAAAMKNVAETK-------RVSAASSTTSNSTSTSTSNSNSTSSASAS 233
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPssppaepPPSTPPAAASPRPPRRSSPISASASSPAP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  234 MATASQKSSLTQSQSHYTSAMSREGTPSAIVTAAKDIAPGVTTTGSPDRTRGHgrdsiDEDGRGNGSGSGDTYDSASPTA 313
Cdd:PHA03307   223 APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGW-----NGPSSRPGPASSSSSPRERSPS 297

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024747630  314 SAAINSSTGAKSAvSASTSGFGSNSGSAGLESASGNESARHSVTTSSGSASSRPLNMGSRNPFSSGPGTSKRANAS 389
Cdd:PHA03307   298 PSPSSPGSGPAPS-SPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPS 372
 
Name Accession Description Interval E-value
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 701-1081 1.69e-165

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 492.61  E-value: 1.69e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  701 TGYVGFANLPNQWHRKSVRKGFSFNVMVVGESGLGKSTLVNTLFNSSLYPPKEYSGPSNDILPKTVGIQSTSSDIEENGV 780
Cdd:COG5019      1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRAEGTSPTLEIKITKAELEEDGF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  781 RLRLTVVDTPGFGDFVNNDESWRPIVENIESRFDAYLEAENKVNR-MNIVDNRIHACIYFIQPTGHSLKPLDIQVMKLLH 859
Cdd:COG5019     81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  860 TKVNLIPVIAKSDTLTDEEVGNFKQRILADINYHRINIFESPRYELDDEETIAENQEIMSKVPFAVVGANTEVTTaDGRK 939
Cdd:COG5019    161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLEENQDLRSLIPFAIIGSNTEIEN-GGEQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  940 VRGRRYPWGVIEVDNEEHCDFVKLRQMLIRTHMEELKEQTNNVLYEDYRTEKLTQMGVTQDSSvfkevnpavkqeeERAL 1019
Cdd:COG5019    240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNSGEPS-------------LKEI 306

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024747630 1020 HEAKLAKMESEMKAVFQQKVHEKESKLKQSEDELYARHREMKEQLEKQRAELEEKKARIESG 1081
Cdd:COG5019    307 HEARLNEEERELKKKFTEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKL 368
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 720-996 4.95e-161

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 477.04  E-value: 4.95e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  720 KGFSFNVMVVGESGLGKSTLVNTLFNSSLYPPKEYSGPSNDIlPKTVGIQSTSSDIEENGVRLRLTVVDTPGFGDFVNND 799
Cdd:cd01850      1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHI-TKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  800 ESWRPIVENIESRFDAYLEAENKVNRM-NIVDNRIHACIYFIQPTGHSLKPLDIQVMKLLHTKVNLIPVIAKSDTLTDEE 878
Cdd:cd01850     80 DCWKPIVDYIDDQFESYLREESRINRNrRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  879 VGNFKQRILADINYHRINIFESPRYElDDEETIAENQEIMSKVPFAVVGANTEVTTaDGRKVRGRRYPWGVIEVDNEEHC 958
Cdd:cd01850    160 LTEFKKRIMEDIEENNIKIYKFPEDE-EDEEEIEENKKLKSLIPFAIVGSNEEVEV-NGKKVRGRKYPWGVVEVENEEHC 237

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1024747630  959 DFVKLRQMLIRTHMEELKEQTNNVLYEDYRTEKLTQMG 996
Cdd:cd01850    238 DFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 721-993 1.46e-147

Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.


Pssm-ID: 395596  Cd Length: 272  Bit Score: 442.12  E-value: 1.46e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  721 GFSFNVMVVGESGLGKSTLVNTLFNSSLYPPKEYSGPSNDIlPKTVGIQSTSSDIEENGVRLRLTVVDTPGFGDFVNNDE 800
Cdd:pfam00735    1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKI-KKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  801 SWRPIVENIESRFDAYLEAENKVNRMNIVDNRIHACIYFIQPTGHSLKPLDIQVMKLLHTKVNLIPVIAKSDTLTDEEVG 880
Cdd:pfam00735   80 CWRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  881 NFKQRILADINYHRINIFESPRYELDDEETIAENQEIMSKVPFAVVGANTEVtTADGRKVRGRRYPWGVIEVDNEEHCDF 960
Cdd:pfam00735  160 RFKKRIREEIERQNIPIYHFPDEESDEDEEKELNEQLKSSIPFAIVGSNTVI-ENDGEKVRGRKYPWGVVEVENPSHCDF 238

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1024747630  961 VKLRQMLIRTHMEELKEQTNNVLYEDYRTEKLT 993
Cdd:pfam00735  239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLS 271
PTZ00121 PTZ00121
MAEBL; Provisional
 951-1090 2.57e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  951 EVDNEEHCDFVKLRQMLIRTHMEELKEQTNNVLYEDYRTEKLTQMGVTQDSSVFKEvnPAVKQEEERALHEAKLAKMESE 1030
Cdd:PTZ00121  1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--ELKKAEEEKKKVEQLKKKEAEE 1645

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1031 MKAVFQQKVHEKESKLKQSedELYARHREMKEQLEKQRAELEEKKARIESGRPVVEEKYK 1090
Cdd:PTZ00121  1646 KKKAEELKKAEEENKIKAA--EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 722-792 1.73e-03

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 42.63  E-value: 1.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024747630  722 FSFNVMVVGESGLGKSTLVNTLFNSSLYPPKEYSgpsndilPKTVGIQSTSSDIeeNGVRLRltVVDTPGF 792
Cdd:TIGR00993  117 FSLNILVLGKSGVGKSATINSIFGEVKFSTDAFG-------MGTTSVQEIEGLV--QGVKIR--VIDTPGL 176
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 161-389 2.87e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  161 PTSARNAASSPDTSINTAITTATSASSMQSSTVAAAMKNVAETK-------RVSAASSTTSNSTSTSTSNSNSTSSASAS 233
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPssppaepPPSTPPAAASPRPPRRSSPISASASSPAP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  234 MATASQKSSLTQSQSHYTSAMSREGTPSAIVTAAKDIAPGVTTTGSPDRTRGHgrdsiDEDGRGNGSGSGDTYDSASPTA 313
Cdd:PHA03307   223 APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGW-----NGPSSRPGPASSSSSPRERSPS 297

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024747630  314 SAAINSSTGAKSAvSASTSGFGSNSGSAGLESASGNESARHSVTTSSGSASSRPLNMGSRNPFSSGPGTSKRANAS 389
Cdd:PHA03307   298 PSPSSPGSGPAPS-SPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPS 372
 
Name Accession Description Interval E-value
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 701-1081 1.69e-165

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 492.61  E-value: 1.69e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  701 TGYVGFANLPNQWHRKSVRKGFSFNVMVVGESGLGKSTLVNTLFNSSLYPPKEYSGPSNDILPKTVGIQSTSSDIEENGV 780
Cdd:COG5019      1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIDDIRAEGTSPTLEIKITKAELEEDGF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  781 RLRLTVVDTPGFGDFVNNDESWRPIVENIESRFDAYLEAENKVNR-MNIVDNRIHACIYFIQPTGHSLKPLDIQVMKLLH 859
Cdd:COG5019     81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRnPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  860 TKVNLIPVIAKSDTLTDEEVGNFKQRILADINYHRINIFESPRYELDDEETIAENQEIMSKVPFAVVGANTEVTTaDGRK 939
Cdd:COG5019    161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLEENQDLRSLIPFAIIGSNTEIEN-GGEQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  940 VRGRRYPWGVIEVDNEEHCDFVKLRQMLIRTHMEELKEQTNNVLYEDYRTEKLTQMGVTQDSSvfkevnpavkqeeERAL 1019
Cdd:COG5019    240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNSGEPS-------------LKEI 306

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024747630 1020 HEAKLAKMESEMKAVFQQKVHEKESKLKQSEDELYARHREMKEQLEKQRAELEEKKARIESG 1081
Cdd:COG5019    307 HEARLNEEERELKKKFTEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKL 368
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 720-996 4.95e-161

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 477.04  E-value: 4.95e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  720 KGFSFNVMVVGESGLGKSTLVNTLFNSSLYPPKEYSGPSNDIlPKTVGIQSTSSDIEENGVRLRLTVVDTPGFGDFVNND 799
Cdd:cd01850      1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHI-TKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  800 ESWRPIVENIESRFDAYLEAENKVNRM-NIVDNRIHACIYFIQPTGHSLKPLDIQVMKLLHTKVNLIPVIAKSDTLTDEE 878
Cdd:cd01850     80 DCWKPIVDYIDDQFESYLREESRINRNrRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  879 VGNFKQRILADINYHRINIFESPRYElDDEETIAENQEIMSKVPFAVVGANTEVTTaDGRKVRGRRYPWGVIEVDNEEHC 958
Cdd:cd01850    160 LTEFKKRIMEDIEENNIKIYKFPEDE-EDEEEIEENKKLKSLIPFAIVGSNEEVEV-NGKKVRGRKYPWGVVEVENEEHC 237

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1024747630  959 DFVKLRQMLIRTHMEELKEQTNNVLYEDYRTEKLTQMG 996
Cdd:cd01850    238 DFVKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 721-993 1.46e-147

Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.


Pssm-ID: 395596  Cd Length: 272  Bit Score: 442.12  E-value: 1.46e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  721 GFSFNVMVVGESGLGKSTLVNTLFNSSLYPPKEYSGPSNDIlPKTVGIQSTSSDIEENGVRLRLTVVDTPGFGDFVNNDE 800
Cdd:pfam00735    1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKI-KKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  801 SWRPIVENIESRFDAYLEAENKVNRMNIVDNRIHACIYFIQPTGHSLKPLDIQVMKLLHTKVNLIPVIAKSDTLTDEEVG 880
Cdd:pfam00735   80 CWRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  881 NFKQRILADINYHRINIFESPRYELDDEETIAENQEIMSKVPFAVVGANTEVtTADGRKVRGRRYPWGVIEVDNEEHCDF 960
Cdd:pfam00735  160 RFKKRIREEIERQNIPIYHFPDEESDEDEEKELNEQLKSSIPFAIVGSNTVI-ENDGEKVRGRKYPWGVVEVENPSHCDF 238

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1024747630  961 VKLRQMLIRTHMEELKEQTNNVLYEDYRTEKLT 993
Cdd:pfam00735  239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLS 271
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 728-879 1.60e-08

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 55.16  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  728 VVGESGLGKSTLVNTLFNSSLYPPKEYSGPsndilpkTVGIQSTSSDIEENGVRLRLtvVDTPGFGDFVNNDESWRPIve 807
Cdd:cd00882      2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGT-------TRDPDVYVKELDKGKVKLVL--VDTPGLDEFGGLGREELAR-- 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024747630  808 niesrfdayleaenkvnrmnIVDNRIHACIYFIQPTGHSLKP--LDIQVMKLLHTKVNLIPVIAKSDTLTDEEV 879
Cdd:cd00882     71 --------------------LLLRGADLILLVVDSTDRESEEdaKLLILRRLRKEGIPIILVGNKIDLLEEREV 124
YeeP COG3596
Predicted GTPase [General function prediction only];
724-800 3.50e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 56.70  E-value: 3.50e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024747630  724 FNVMVVGESGLGKSTLVNTLFNSSLyppkeysGPSNDILPKTVGIQSTssDIEENGVRLrLTVVDTPGFGDFVNNDE 800
Cdd:COG3596     40 PVIALVGKTGAGKSSLINALFGAEV-------AEVGVGRPCTREIQRY--RLESDGLPG-LVLLDTPGLGEVNERDR 106
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1010-1091 2.42e-06

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 48.92  E-value: 2.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1010 AVKQEEERALHEAKL----AKMESEMKAVFQQKVHEKESKLKQSEDElyarhremKEQLEKQRAELEEKKARIESGRPVV 1085
Cdd:pfam11600   33 AEKEEKERLKEEAKAekerAKEEARRKKEEEKELKEKERREKKEKDE--------KEKAEKLRLKEEKRKEKQEALEAKL 104


                   ....*.
gi 1024747630 1086 EEKYKR 1091
Cdd:pfam11600  105 EEKRKK 110
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 724-802 1.03e-05

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 47.16  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  724 FNVMVVGESGLGKSTLVNTLFNSslyppkeysgpsnDILPktVGIQSTSSDIEENGVRLR--LTVVDTPGFGDFVNNDES 801
Cdd:cd09912      1 FLLAVVGEFSAGKSTLLNALLGE-------------EVLP--TGVTPTTAVITVLRYGLLkgVVLVDTPGLNSTIEHHTE 65


                   .
gi 1024747630  802 W 802
Cdd:cd09912     66 I 66
PTZ00121 PTZ00121
MAEBL; Provisional
 951-1090 2.57e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  951 EVDNEEHCDFVKLRQMLIRTHMEELKEQTNNVLYEDYRTEKLTQMGVTQDSSVFKEvnPAVKQEEERALHEAKLAKMESE 1030
Cdd:PTZ00121  1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE--ELKKAEEEKKKVEQLKKKEAEE 1645

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1031 MKAVFQQKVHEKESKLKQSedELYARHREMKEQLEKQRAELEEKKARIESGRPVVEEKYK 1090
Cdd:PTZ00121  1646 KKKAEELKKAEEENKIKAA--EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
726-895 2.63e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.13  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  726 VMVVGESGLGKSTLVNTLFNSSlYPPKEYSGpsndilpkTVGIQSTSSDIEENGVRLRLTVVDTPGFGDFvnndESWRPI 805
Cdd:COG1100      6 IVVVGTGGVGKTSLVNRLVGDI-FSLEKYLS--------TNGVTIDKKELKLDGLDVDLVIWDTPGQDEF----RETRQF 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  806 VENIESRFDAYLEaenkvnrmnIVDNRihaciyfIQPTGHSLKpLDIQVMKLLHTKVNLIPVIAKSDTLTDEEVGNfKQR 885
Cdd:COG1100     73 YARQLTGASLYLF---------VVDGT-------REETLQSLY-ELLESLRRLGKKSPIILVLNKIDLYDEEEIED-EER 134

                          170
                   ....*....|
gi 1024747630  886 ILADINYHRI 895
Cdd:COG1100    135 LKEALSEDNI 144
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 729-817 4.02e-05

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 44.64  E-value: 4.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  729 VGESGLGKSTLVNTLFNSSLyppkeysGPSNDILPKTVGIQSTSSDIEENGvrlrLTVVDTPGFGDFVNNDESWRPIVEN 808
Cdd:cd11383      3 MGKTGAGKSSLCNALFGTEV-------AAVGDRRPTTRAAQAYVWQTGGDG----LVLLDLPGVGERGRRDREYEELYRR 71


                   ....*....
gi 1024747630  809 IESRFDAYL 817
Cdd:cd11383     72 LLPEADLVL 80
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 729-900 4.76e-05

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 45.19  E-value: 4.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  729 VGESGLGKSTLVNTLFNsslyppkeysgpsNDILPKTvgiqstSS-----------DIEENgvrlrLTVVDTPGFGdF-- 795
Cdd:cd01876      5 AGRSNVGKSSLINALTN-------------RKKLART------SKtpgrtqlinffNVGDK-----FRLVDLPGYG-Yak 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  796 VNND--ESWRPIVENiesrfdaYLEaenkvNRMNI------VDNRihaciyfiqptgHSLKPLDIQVMKLL-HTKVNLIP 866
Cdd:cd01876     60 VSKEvrEKWGKLIEE-------YLE-----NRENLkgvvllIDAR------------HGPTPIDLEMLEFLeELGIPFLI 115

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1024747630  867 VIAKSDTLTDEEVGN----FKQRILADINYHRINIFES 900
Cdd:cd01876    116 VLTKADKLKKSELAKvlkkIKEELNLFNILPPVILFSS 153
iSH2_PIK3R1 cd12924
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
 962-1083 6.01e-05

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 1, PIK3R1, also called p85alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In addition, p85alpha, also called PIK3R1, contains N-terminal SH3 and GAP domains. p85alpha carry functions independent of its PI3K regulatory role. It can independently stimulate signaling pathways involved in cytoskeletal rearrangements. Insulin-sensitive tissues express splice variants of the PIK3R1 gene, p50alpha and p55alpha, which may play important roles in insulin signaling during lipid and glucose metabolism. Mice deficient with PIK3R1 die perinatally, indicating its importance in development.


Pssm-ID: 214017 [Multi-domain]  Cd Length: 161  Bit Score: 44.68  E-value: 6.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  962 KLRQMliRTHMEElKEQTNNVLYEDY-RTEKLTQMGVTqdssVFKEVNPAVKQEEERALHEAKLAKmesEMKAVFQQKVH 1040
Cdd:cd12924      9 KLHEY--NTQFQE-KSREYDRLYEEYtRTSQEIQMKRT----AIEAFNETIKIFEEQCQTQERYSK---EYIEKFKREGN 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1024747630 1041 EKE--------SKLKQSEDELYARHREMKEQLEKQRAELEEKKARIESGRP 1083
Cdd:cd12924     79 EKEiqrimhnyEKLKSRISEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKP 129
PLN03118 PLN03118
Rab family protein; Provisional
 722-791 9.94e-05

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 44.66  E-value: 9.94e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  722 FSFNVMVVGESGLGKSTLVNTLFNSSLyppkeysgpsNDILPkTVGIQSTSSDIEENGVRLRLTVVDTPG 791
Cdd:PLN03118    13 LSFKILLIGDSGVGKSSLLVSFISSSV----------EDLAP-TIGVDFKIKQLTVGGKRLKLTIWDTAG 71
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 725-868 1.39e-04

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 42.22  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  725 NVMVVGESGLGKSTLVNTLFNSSLYppkeysgpSNDILPKTVGIQstSSDIEENGVRLRLtvVDTPGFgdFVNNDESWRp 804
Cdd:pfam01926    1 RVALVGRPNVGKSTLINALTGAKAI--------VSDYPGTTRDPN--EGRLELKGKQIIL--VDTPGL--IEGASEGEG- 65

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024747630  805 ivenIESRFDAYLEAEnkvnrmnivdnrihaCIYFIQPTGHSLKPLDIQVMKLLhtKVNLIPVI 868
Cdd:pfam01926   66 ----LGRAFLAIIEAD---------------LILFVVDSEEGITPLDEELLELL--RENKKPII 108
fliH PRK06669
flagellar assembly protein H; Validated
 985-1093 1.77e-04

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 44.62  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  985 EDYRTEKLTQMGVTQDSSVFKEVNPAVKQEEERALHEAklakmeSEMKAVFQQKVHEKeskLKQSEDELYARHREMKEQL 1064
Cdd:PRK06669    31 SIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDA------FEIVEAAEEEAKEE---LLKKTDEASSIIEKLQMQI 101

                           90       100       110
                   ....*....|....*....|....*....|
gi 1024747630 1065 EKQRAELEEKKAR-IESGRpvvEEKYKRGK 1093
Cdd:PRK06669   102 EREQEEWEEELERlIEEAK---AEGYEEGY 128
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
968-1094 3.94e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 3.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  968 IRTHMEELKEQtnnvlYEDY--RTEKLTQMGVTQD---SSVFKEVNPavKQEEERALhEAKLAKMESEMKAVFQQKV--- 1039
Cdd:PRK03918   170 VIKEIKRRIER-----LEKFikRTENIEELIKEKEkelEEVLREINE--ISSELPEL-REELEKLEKEVKELEELKEeie 241

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1040 --HEKESKLKQSEDELYARHREMKEQLEKQRA---ELEEKKARIESGRPVVEEKYKRGKF 1094
Cdd:PRK03918   242 elEKELESLEGSKRKLEEKIRELEERIEELKKeieELEEKVKELKELKEKAEEYIKLSEF 301
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
893-1091 4.01e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  893 HRINIFESPRYELDD-EETIAENQEIMSKVpfavvgantevttadgrKVRGRRypwgvIEVDNEEHCDFVKLRQML--IR 969
Cdd:PRK03918   449 HRKELLEEYTAELKRiEKELKEIEEKERKL-----------------RKELRE-----LEKVLKKESELIKLKELAeqLK 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  970 THMEELKEQTNNVL---YEDYRT--EKLTQMGvTQDSSVFKEVNPAVKQEEERALHEAKLAKMESEMKAVFQQ------- 1037
Cdd:PRK03918   507 ELEEKLKKYNLEELekkAEEYEKlkEKLIKLK-GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfe 585

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024747630 1038 -------------KVHEKESKLKQSEDELyarhREMKEQLEKQRAELEEKKARIESGRPVVEEKYKR 1091
Cdd:PRK03918   586 sveeleerlkelePFYNEYLELKDAEKEL----EREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
 724-897 5.35e-04

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 41.78  E-value: 5.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  724 FNVMVVGESGLGKSTLVNTLfnsslyppkeySGPSNDILP---KTVGIQStsSDIEENGvrLRLTVVDTPGFGDfvnnde 800
Cdd:cd01897      1 RTLVIAGYPNVGKSSLVNKL-----------TRAKPEVAPypfTTKSLFV--GHFDYKY--LRWQVIDTPGILD------ 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  801 swRPIVE--NIESRFDAYLeaenkvnrmnivdNRIHACI-YFIQPTGHSLKPLDIQVmKLLHT-----KVNLIPVIAKSD 872
Cdd:cd01897     60 --RPLEErnTIEMQAITAL-------------AHLRAAVlFFIDPSETCGYSIEEQL-SLFKEikplfNKPVIVVLNKID 123

                          170       180
                   ....*....|....*....|....*
gi 1024747630  873 TLTDEEVgNFKQRILADINYHRINI 897
Cdd:cd01897    124 LLTEEDL-SEIEKELEKEGEEVIKI 147
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
962-1094 5.79e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  962 KLRQmlIRTHMEELKEQtnnvLYEdyRTEKLTQMGVTQDSSVfKEVNpAVKQEEERAlhEAKLAKMESEMKAVfQQKVHE 1041
Cdd:COG4372     67 ELEQ--ARSELEQLEEE----LEE--LNEQLQAAQAELAQAQ-EELE-SLQEEAEEL--QEELEELQKERQDL-EQQRKQ 133

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1024747630 1042 KESKLKQSEDELYARHREmKEQLEKQRAELEEKKARIESGRPVVEEKYKRGKF 1094
Cdd:COG4372    134 LEAQIAELQSEIAEREEE-LKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
PRK12704 PRK12704
phosphodiesterase; Provisional
 1011-1090 5.89e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 5.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1011 VKQEEERALHEAKLAKMES-----EMKAVFQQKVHEKESKLKQSEDELyarhREMKEQLEKQRAELEEKKARIESGRPVV 1085
Cdd:PRK12704    44 LEEAKKEAEAIKKEALLEAkeeihKLRNEFEKELRERRNELQKLEKRL----LQKEENLDRKLELLEKREEELEKKEKEL 119


                   ....*
gi 1024747630 1086 EEKYK 1090
Cdd:PRK12704   120 EQKQQ 124
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 1014-1091 6.02e-04

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: 40.67  E-value: 6.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1014 EEERALHEAKLAKMESEMKAV------FQQKVHEKESKLKQSE---DELYARHREM-----------------KEQLEKQ 1067
Cdd:pfam20492    5 EREKQELEERLKQYEEETKKAqeeleeSEETAEELEEERRQAEeeaERLEQKRQEAeeekerleesaemeaeeKEQLEAE 84

                           90       100
                   ....*....|....*....|....
gi 1024747630 1068 RAELEEKKARIEsgrpvvEEKYKR 1091
Cdd:pfam20492   85 LAEAQEEIARLE------EEVERK 102
Enkurin pfam13864
Calmodulin-binding; This is a family of apparent calmodulin-binding proteins found at high ...
 1011-1080 7.49e-04

Calmodulin-binding; This is a family of apparent calmodulin-binding proteins found at high levels in the testis and vomeronasal organ and at lower levels in certain other tissues. Enkurin is a scaffold protein that binds PI3 kinase to sperm transient receptor potential (canonical) (TRPC) channels. The mammalian transient receptor potential (canonical) channels are the primary candidates for the Ca(2+) entry pathway activated by the hormones, growth factors, and neurotransmitters that exert their effect through activation of PLC. Calmodulin binds to the C-terminus of all TRPC channels, and dissociation of calmodulin from TRPC4 results in profound activation of the channel.


Pssm-ID: 464004 [Multi-domain]  Cd Length: 92  Bit Score: 39.86  E-value: 7.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1011 VKQEEERA-LHEAKLAKMESEMKAVFQQKVHEKESKLKQSEDELY------------ARHREMKEQLEKQRAELEEKKAR 1077
Cdd:pfam13864   10 RKEELEKEeEEYEEYVREEEERRLLSEEERQELLDGLKKNWDELNkeyqklplkidtLSKKRRKEELEKELAQLEKDIKK 89


                   ...
gi 1024747630 1078 IES 1080
Cdd:pfam13864   90 LER 92
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 722-792 1.41e-03

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 41.53  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  722 FSFNVMVVGESGLGKSTLVNTLFN------SSLYP----PKEYSGpsndilpkTVgiqstssdieeNGVrlRLTVVDTPG 791
Cdd:cd01853     30 FSLTILVLGKTGVGKSSTINSIFGerkvsvSAFQSetlrPREVSR--------TV-----------DGF--KLNIIDTPG 88


                   .
gi 1024747630  792 F 792
Cdd:cd01853     89 L 89
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 949-1088 1.47e-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: 42.80  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  949 VIEVDNEEHCDFVKLRQMLIRTHMEELKEQTnnvlyEDYRTEKLTQMGVTQDSSVFKEVNPAVKQEEeraLHEAKLAKME 1028
Cdd:pfam17380  439 RLEEERAREMERVRLEEQERQQQVERLRQQE-----EERKRKKLELEKEKRDRKRAEEQRRKILEKE---LEERKQAMIE 510

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1029 SEMKavfqQKVHEKESKLKQSEDELYARHREMKEQLEKQRaELEEKKARIESGRPVVEEK 1088
Cdd:pfam17380  511 EERK----RKLLEKEMEERQKAIYEEERRREAEEERRKQQ-EMEERRRIQEQMRKATEER 565
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 722-792 1.73e-03

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 42.63  E-value: 1.73e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024747630  722 FSFNVMVVGESGLGKSTLVNTLFNSSLYPPKEYSgpsndilPKTVGIQSTSSDIeeNGVRLRltVVDTPGF 792
Cdd:TIGR00993  117 FSLNILVLGKSGVGKSATINSIFGEVKFSTDAFG-------MGTTSVQEIEGLV--QGVKIR--VIDTPGL 176
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1005-1097 1.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1005 KEVNPAVKQEEERALHEAKLAKMESEMKAV---FQQKVHEKESKLKQSEDELYARHREMKEQLEKQRAEL--------EE 1073
Cdd:PRK03918   623 KLEEELDKAFEELAETEKRLEELRKELEELekkYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIkktleklkEE 702

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1024747630 1074 KKAR---------IESGRPVVE---EKYKRGKFSLR 1097
Cdd:PRK03918   703 LEERekakkelekLEKALERVEelrEKVKKYKALLK 738
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 973-1081 1.83e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  973 EELKEQTNNVLYEDYRTEKLTQMGVTQDSSVFKEVNPAVKQEEERALHE-------AKLAKMESEMKAVFQQKVHEKESK 1045
Cdd:pfam01576  896 EELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLErqnkelkAKLQEMEGTVKSKFKSSIAALEAK 975

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1024747630 1046 LKQSEDELYARHRE--------------MKE---QLEKQRAELEEKKARIESG 1081
Cdd:pfam01576  976 IAQLEEQLEQESRErqaanklvrrtekkLKEvllQVEDERRHADQYKDQAEKG 1028
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 1010-1081 1.89e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 42.35  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1010 AVKQEEERALHEAKLAK-MESE-MKAVFQQKVHEKESKLKQSEDELYARHR----------EMKEQLEKQRAELEEKKAR 1077
Cdd:pfam05911   63 NVKEEQEQKIHDVVLKKtKEWEkIKAELEAKLVETEQELLRAAAENDALSRslqerenllmKLSEEKSQAEAEIEALKSR 142


                   ....
gi 1024747630 1078 IESG 1081
Cdd:pfam05911  143 LESC 146
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 962-1077 1.93e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  962 KLRQMLIRTHMEELKEQTnnvlyEDYRTEKLTQmgvtqdssvfkevnpAVKQEEERALHEAKLAKMESEMKAVFQQKvHE 1041
Cdd:pfam13868   65 EERKEERKRYRQELEEQI-----EEREQKRQEE---------------YEEKLQEREQMDEIVERIQEEDQAEAEEK-LE 123

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1024747630 1042 KESKLKQSEDELYARHREMKEQlEKQRAELEEKKAR 1077
Cdd:pfam13868  124 KQRQLREEIDEFNEEQAEWKEL-EKEEEREEDERIL 158
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 973-1088 2.21e-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: 42.36  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  973 EELKEQTNNvLYEDYRTEKLTQMGvtqdssvfKEVNpavKQEEERALHEAKLAKMESEMkavfqQKVHEKESKLKQSEDE 1052
Cdd:TIGR02169  775 HKLEEALND-LEARLSHSRIPEIQ--------AELS---KLEEEVSRIEARLREIEQKL-----NRLTLEKEYLEKEIQE 837

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1024747630 1053 LYARHREMKEQLEKQRAELEEKKARIESGRPVVEEK 1088
Cdd:TIGR02169  838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1012-1092 2.54e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1012 KQEEERALHEAKL-------AKMESEMKAV---FQQKVHEK---ESKLkQSEDELYARHREMKEQLEKQRAELEEKKARI 1078
Cdd:pfam01576    2 RQEEEMQAKEEELqkvkerqQKAESELKELekkHQQLCEEKnalQEQL-QAETELCAEAEEMRARLAARKQELEEILHEL 80

                           90
                   ....*....|....
gi 1024747630 1079 ESgRpvVEEKYKRG 1092
Cdd:pfam01576   81 ES-R--LEEEEERS 91
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1012-1091 2.56e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1012 KQEEERALHEAKLAKMESEMKAV-----FQQKVHEKES-KLKQSE------------DELYARHREMKEQLEKQRAELEE 1073
Cdd:COG1579     63 RLELEIEEVEARIKKYEEQLGNVrnnkeYEALQKEIESlKRRISDledeilelmeriEELEEELAELEAELAELEAELEE 142

                           90
                   ....*....|....*...
gi 1024747630 1074 KKARIESGRPVVEEKYKR 1091
Cdd:COG1579    143 KKAELDEELAELEAELEE 160
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 161-389 2.87e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  161 PTSARNAASSPDTSINTAITTATSASSMQSSTVAAAMKNVAETK-------RVSAASSTTSNSTSTSTSNSNSTSSASAS 233
Cdd:PHA03307   143 SPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPssppaepPPSTPPAAASPRPPRRSSPISASASSPAP 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  234 MATASQKSSLTQSQSHYTSAMSREGTPSAIVTAAKDIAPGVTTTGSPDRTRGHgrdsiDEDGRGNGSGSGDTYDSASPTA 313
Cdd:PHA03307   223 APGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGW-----NGPSSRPGPASSSSSPRERSPS 297

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024747630  314 SAAINSSTGAKSAvSASTSGFGSNSGSAGLESASGNESARHSVTTSSGSASSRPLNMGSRNPFSSGPGTSKRANAS 389
Cdd:PHA03307   298 PSPSSPGSGPAPS-SPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPS 372
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 999-1096 3.48e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 39.10  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  999 QDSSVFKEVNPAVKQEEERAlhEAKLAKMESE---MKAVFQQKVHEKESKLKQSEDELYARHREMKEQLEKQRAELEEKK 1075
Cdd:pfam03938   12 EESPEGKAAQAQLEKKFKKR--QAELEAKQKElqkLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQ 89

                           90       100
                   ....*....|....*....|....*.
gi 1024747630 1076 ARI-----ESGRPVVEEKYKRGKFSL 1096
Cdd:pfam03938   90 QELlqpiqDKINKAIKEVAKEKGYDL 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1012-1096 3.77e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1012 KQEEERALHEAKLAKMESEMKAVfQQKVHEKESKLKQSEDELYARHREMK------EQLEKQRAELEEKKARIESGRPVV 1085
Cdd:COG4372     56 QAREELEQLEEELEQARSELEQL-EEELEELNEQLQAAQAELAQAQEELEslqeeaEELQEELEELQKERQDLEQQRKQL 134

                           90
                   ....*....|.
gi 1024747630 1086 EEKYKRGKFSL 1096
Cdd:COG4372    135 EAQIAELQSEI 145
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
959-1082 3.93e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  959 DFVKLRQMliRTHMEELKEQTNnVL------YEDYRtEKLTQMGVTQDssvFKEVNPAVKQEEERALHEAKLAKMESEMK 1032
Cdd:COG4913    233 HFDDLERA--HEALEDAREQIE-LLepirelAERYA-AARERLAELEY---LRAALRLWFAQRRLELLEAELEELRAELA 305

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1024747630 1033 AVfQQKVHEKESKLKQSEDELYARHREM-------KEQLEKQRAELEEKKARIESGR 1082
Cdd:COG4913    306 RL-EAELERLEARLDALREELDELEAQIrgnggdrLEQLEREIERLERELEERERRR 361
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 961-1078 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: 40.67  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  961 VKLRQMLiRTHMEElKEQTNNVLYEDYRTEKLtQMgvtqdssvfKEVNPAVkQEEERALHEAKLAKMESEMKAVF----- 1035
Cdd:pfam13868   72 KRYRQEL-EEQIEE-REQKRQEEYEEKLQERE-QM---------DEIVERI-QEEDQAEAEEKLEKQRQLREEIDefnee 138

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1024747630 1036 QQKVHEKESKLKQSEDELYARHREMKEQLEK----QRAELEEKKARI 1078
Cdd:pfam13868  139 QAEWKELEKEEEREEDERILEYLKEKAEREEereaEREEIEEEKERE 185
PRK12704 PRK12704
phosphodiesterase; Provisional
 1005-1090 4.85e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1005 KEVNPAVKQE--EERALHEAKLAKMESEMKAVfQQKVHEKESKLKQSEDELYARhremKEQLEKQRAELEEKKARIESGR 1082
Cdd:PRK12704    56 KEALLEAKEEihKLRNEFEKELRERRNELQKL-EKRLLQKEENLDRKLELLEKR----EEELEKKEKELEQKQQELEKKE 130


                   ....*...
gi 1024747630 1083 PVVEEKYK 1090
Cdd:PRK12704   131 EELEELIE 138
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 1014-1068 4.90e-03

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 38.75  E-value: 4.90e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024747630 1014 EEERALHEAKLAKMESEMK---AVFQQKVHEKESKLKQSEDELYARHREM----KEQLEKQR 1068
Cdd:pfam09744   88 EQETKDLLSQVESLEEENRrleADHVSRLEEKEAELKKEYSKLHERETEVlrklKEVVDRQR 149
iSH2_PI3K_IA_R cd12923
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
 962-1091 5.21e-03

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.


Pssm-ID: 214016 [Multi-domain]  Cd Length: 152  Bit Score: 38.74  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630  962 KLRQMLIRTHmEELKEQTN--NVLYEDY-RTEKLTQMgVTQDSSVFKEvnpAVKQ-EEERALHEaklaKMESEMKAvfqq 1037
Cdd:cd12923      5 KLAKKLKEIN-KEYLDKSReyDELYEKYnKLSQEIQL-KRQALEAFEE---AVKMfEEQLRTQE----KFQKEAQP---- 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024747630 1038 kvHEKES------KLKQSEDELYARHREMKEQLEKQRAELEEKKARIESGRPVVEEKYKR 1091
Cdd:cd12923     72 --HEKQRlmenneLLKSRLKELEESKEQLEEDLRKQVAYNRELEREMNSLKPELMQLRKQ 129
Remorin_C pfam03763
Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. ...
 1013-1088 5.69e-03

Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.


Pssm-ID: 427493 [Multi-domain]  Cd Length: 106  Bit Score: 37.55  E-value: 5.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024747630 1013 QEEERALHEAKLAKMESEMKAVFQQKVHEKESKLKQSEdelyarhremkEQLEKQRAELEEK-KARIESGRPVVEEK 1088
Cdd:pfam03763   10 EEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIE-----------EKLEKKRAEALEKmKNKLARIHKKAEEK 75
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1005-1079 6.78e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 6.78e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024747630 1005 KEVNpAVKQEEERAlhEAKLAKMESEMKAVfQQKVHEKESKLKQSEDELyarhREMKEQLEKQRAELEEKKARIE 1079
Cdd:COG1579     89 KEYE-ALQKEIESL--KRRISDLEDEILEL-MERIEELEEELAELEAEL----AELEAELEEKKAELDEELAELE 155
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1014-1087 8.08e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 8.08e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024747630 1014 EEERALHEAKLAKMESEMKAVfqQKVHEKESKLKQSEDELyARHREMKEQLEK----QRAELEEKKARIESGRPVVEE 1087
Cdd:PRK02224   474 RERVEELEAELEDLEEEVEEV--EERLERAEDLVEAEDRI-ERLEERREDLEEliaeRRETIEEKRERAEELRERAAE 548
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 725-792 8.39e-03

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 38.78  E-value: 8.39e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024747630  725 NVMVVGESGLGKSTLVNTLFnsslyppKEYSGPSNDILPKTVGIQS----TSSDIEENGVRLRLTVVDTPGF 792
Cdd:cd01855    127 DVYVVGATNVGKSTLINALL-------KSNGGKVQAQALVQRLTVSpipgTTLGLIKIPLGEGKKLYDTPGI 191
 
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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